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Database: PDB
Entry: 5BZX
LinkDB: 5BZX
Original site: 5BZX 
HEADER    HYDROLASE                               11-JUN-15   5BZX              
TITLE     CRYSTAL STRUCTURE OF HUMAN PHOSPHATASE PTEN TREATED WITH A            
TITLE    2 BISPEROXOVANADIUM COMPLEX                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE 3-PHOSPHATASE AND 
COMPND   3 DUAL-SPECIFICITY PROTEIN PHOSPHATASE PTEN;                           
COMPND   4 CHAIN: A, B, C, D;                                                   
COMPND   5 FRAGMENT: PTEN WT 7-353 DELTA 286-309;                               
COMPND   6 SYNONYM: MUTATED IN MULTIPLE ADVANCED CANCERS 1,PHOSPHATASE AND      
COMPND   7 TENSIN HOMOLOG;                                                      
COMPND   8 EC: 3.1.3.16,3.1.3.48,3.1.3.67;                                      
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PTEN, MMAC1, TEP1;                                             
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFH1                                      
KEYWDS    PHOSPHATASE, C2 DOMAIN, DISULFIDE, OXIDIZED, VANADATE, HYDROLASE      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.-U.LEE,D.BIER,S.HENNIG,T.N.GROSSMANN                                
REVDAT   2   11-NOV-15 5BZX    1       JRNL                                     
REVDAT   1   07-OCT-15 5BZX    0                                                
JRNL        AUTH   C.U.LEE,G.HAHNE,J.HANSKE,T.BANGE,D.BIER,C.RADEMACHER,        
JRNL        AUTH 2 S.HENNIG,T.N.GROSSMANN                                       
JRNL        TITL   REDOX MODULATION OF PTEN PHOSPHATASE ACTIVITY BY HYDROGEN    
JRNL        TITL 2 PEROXIDE AND BISPEROXIDOVANADIUM COMPLEXES.                  
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  54 13796 2015              
JRNL        REFN                   ESSN 1521-3773                               
JRNL        PMID   26418532                                                     
JRNL        DOI    10.1002/ANIE.201506338                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.29                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 62095                          
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) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.204                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3297                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4369                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.27                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3420                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 231                          
REMARK   3   BIN FREE R VALUE                    : 0.3730                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10310                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 880                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 56.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.84                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -33.11000                                            
REMARK   3    B22 (A**2) : -30.39000                                            
REMARK   3    B33 (A**2) : 63.50000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.076         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.047         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.111         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.673         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10650 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  9820 ; 0.006 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14409 ; 1.538 ; 1.952       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 22568 ; 1.451 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1252 ;12.460 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   543 ;31.762 ;23.499       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1772 ;18.237 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    62 ;22.534 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1488 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12052 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2672 ; 0.005 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5020 ; 3.550 ; 6.109       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  5019 ; 3.549 ; 6.108       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6268 ; 5.666 ; 9.163       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.501                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : K, H, -L                                        
REMARK   3      TWIN FRACTION : 0.499                                           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 5BZX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000210556.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-SEP-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.77119                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 65393                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.293                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 12.91                              
REMARK 200  R MERGE                    (I) : 0.11800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.4300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.55200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.530                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.6                                          
REMARK 200 STARTING MODEL: 1D5R                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 1.25 M L-TARTRAT,      
REMARK 280  7.5% GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.83500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       43.83500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000      103.53000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      103.45000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000      103.53000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      103.45000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       43.83500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000      103.53000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      103.45000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       43.83500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000      103.53000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      103.45000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 510  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 522  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 624  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C 620  LIES ON A SPECIAL POSITION.                          
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  14    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  40    CG   CD   OE1  OE2                                  
REMARK 470     VAL A  45    CG1  CG2                                            
REMARK 470     TYR A  46    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A  62    CG   CD   CE   NZ                                   
REMARK 470     ARG A  74    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  80    CG   CD   CE   NZ                                   
REMARK 470     ASN A  82    CG   OD1  ND2                                       
REMARK 470     HIS A 185    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASN A 311    CG   OD1  ND2                                       
REMARK 470     ASP A 312    CG   OD1  OD2                                       
REMARK 470     LYS A 349    CG   CD   CE   NZ                                   
REMARK 470     ARG B  14    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  40    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  62    CG   CD   CE   NZ                                   
REMARK 470     ASP B 116    CG   OD1  OD2                                       
REMARK 470     LYS B 183    CG   CD   CE   NZ                                   
REMARK 470     LYS B 221    CG   CD   CE   NZ                                   
REMARK 470     LYS B 260    CG   CD   CE   NZ                                   
REMARK 470     ASN B 262    CG   OD1  ND2                                       
REMARK 470     LEU B 265    CG   CD1  CD2                                       
REMARK 470     LYS B 266    CG   CD   CE   NZ                                   
REMARK 470     ASN B 311    CG   OD1  ND2                                       
REMARK 470     ASP B 312    CG   OD1  OD2                                       
REMARK 470     GLU B 314    CG   CD   OE1  OE2                                  
REMARK 470     ARG C  14    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C  47    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  80    CG   CD   CE   NZ                                   
REMARK 470     LYS C 221    CG   CD   CE   NZ                                   
REMARK 470     LYS C 260    CG   CD   CE   NZ                                   
REMARK 470     GLN C 261    CG   CD   OE1  NE2                                  
REMARK 470     MET C 264    CG   SD   CE                                        
REMARK 470     LEU C 265    CG   CD1  CD2                                       
REMARK 470     LYS C 266    CG   CD   CE   NZ                                   
REMARK 470     GLU C 284    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 285    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 310    CG   OD1  OD2                                       
REMARK 470     ARG D  14    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D  40    CG   CD   OE1  OE2                                  
REMARK 470     TYR D  46    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS D  62    CG   CD   CE   NZ                                   
REMARK 470     GLU D  91    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 221    CG   CD   CE   NZ                                   
REMARK 470     GLN D 261    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 263    CG   CD   CE   NZ                                   
REMARK 470     MET D 264    CG   SD   CE                                        
REMARK 470     LEU D 265    CG   CD1  CD2                                       
REMARK 470     LYS D 266    CG   CD   CE   NZ                                   
REMARK 470     GLU D 285    CG   CD   OE1  OE2                                  
REMARK 470     ASP D 310    CG   OD1  OD2                                       
REMARK 470     ASP D 312    CG   OD1  OD2                                       
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 B   683     O    HOH B   688              0.35            
REMARK 500   O    HOH D   596     O    HOH D   646              0.86            
REMARK 500   O    HOH D   506     O    HOH D   539              1.81            
REMARK 500   O    HOH B   597     O    HOH B   636              1.87            
REMARK 500   SG   CYS C   218     O    HOH C   675              1.88            
REMARK 500   OD1  ASP B    24     O    HOH B   501              1.94            
REMARK 500   OD1  ASP B    92     O    HOH B   502              1.94            
REMARK 500   O    ASP A   312     N    LYS C   266              1.97            
REMARK 500   O41  TLA B   401     O    HOH B   503              1.98            
REMARK 500   NH2  ARG B    15     O    TYR B    27              1.99            
REMARK 500   SG   CYS A   218     O    HOH A   599              1.99            
REMARK 500   O    HOH A   582     O    HOH A   602              2.00            
REMARK 500   O    LEU C   220     O    HOH C   501              2.00            
REMARK 500   O    ASP A   312     CB   LEU C   265              2.01            
REMARK 500   N    LYS D   327     O    HOH D   501              2.01            
REMARK 500   O    HOH A   601     O    HOH A   628              2.02            
REMARK 500   O    HOH C   507     O    HOH C   639              2.02            
REMARK 500   O    HOH D   665     O    HOH D   697              2.05            
REMARK 500   O    HOH A   647     O    HOH A   666              2.07            
REMARK 500   O    HOH C   508     O    HOH C   627              2.08            
REMARK 500   O    GLY D   127     NH1  ARG D   159              2.08            
REMARK 500   NH2  ARG C    55     O    HOH C   502              2.09            
REMARK 500   O    HOH C   562     O    HOH C   636              2.09            
REMARK 500   O    HOH C   543     O    HOH C   560              2.10            
REMARK 500   O4   TLA D   401     O    HOH D   502              2.10            
REMARK 500   O    HOH A   572     O    HOH A   603              2.11            
REMARK 500   O    HOH D   677     O    HOH D   705              2.12            
REMARK 500   NZ   LYS C   237     O    HOH C   503              2.13            
REMARK 500   ND2  ASN A    49     OD2  ASP A    52              2.13            
REMARK 500   SG   CYS A   250     O    HOH A   519              2.13            
REMARK 500   O    HOH A   566     O    HOH A   614              2.14            
REMARK 500   O    HOH C   632     O    HOH C   653              2.14            
REMARK 500   O    CYS A   250     O    HOH A   501              2.14            
REMARK 500   O    HOH B   636     O    HOH B   670              2.14            
REMARK 500   O    HOH C   525     O    HOH C   600              2.15            
REMARK 500   O    HOH D   684     O    HOH D   687              2.15            
REMARK 500   O    HOH C   657     O    HOH C   672              2.15            
REMARK 500   N    LYS B   327     O    HOH B   504              2.15            
REMARK 500   OE2  GLU C    43     O    HOH C   504              2.16            
REMARK 500   O    HOH A   575     O    HOH A   655              2.16            
REMARK 500   O    ASP A   326     O    HOH A   502              2.16            
REMARK 500   NE2  GLN A    87     O    HOH A   503              2.16            
REMARK 500   O    PRO A    95     O    HOH A   504              2.16            
REMARK 500   O    HOH B   609     O    HOH B   634              2.16            
REMARK 500   NH2  ARG D    84     O    HOH D   503              2.16            
REMARK 500   SG   CYS B   250     O    HOH B   526              2.16            
REMARK 500   O    HOH A   504     O    HOH A   537              2.17            
REMARK 500   O    ASN D   117     O    HOH D   504              2.18            
REMARK 500   O    HOH A   546     O    HOH A   614              2.18            
REMARK 500   OE1  GLU C    73     O    HOH C   505              2.19            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      54 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CB   GLU D    43     O    HOH B   512     1554     1.92            
REMARK 500   OE2  GLU C   150     NH1  ARG C   161     3556     2.15            
REMARK 500   O    HOH D   692     O    HOH D   692     4555     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B  74   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG C  74   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    PRO C 281   C   -  N   -  CA  ANGL. DEV. =  11.2 DEGREES          
REMARK 500    PRO C 281   C   -  N   -  CD  ANGL. DEV. = -13.3 DEGREES          
REMARK 500    ARG D  41   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 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      -55.25   -140.69                                   
REMARK 500    ARG A  47      -82.20   -155.68                                   
REMARK 500    HIS A  61       53.43   -148.07                                   
REMARK 500    CYS A 124     -105.38   -129.29                                   
REMARK 500    LYS A 125      -79.89    -93.77                                   
REMARK 500    LYS A 128      -92.27   -116.09                                   
REMARK 500    LEU A 220     -135.17     59.01                                   
REMARK 500    ASP A 236     -108.80     60.41                                   
REMARK 500    ASN A 262       -0.73     71.50                                   
REMARK 500    MET A 270      -63.73    -94.49                                   
REMARK 500    ASN A 340       -2.96     76.68                                   
REMARK 500    TYR B  16      -52.63   -142.50                                   
REMARK 500    PHE B  21       12.37   -144.77                                   
REMARK 500    ASP B  22       93.62    -10.32                                   
REMARK 500    HIS B  61       53.53   -147.83                                   
REMARK 500    PHE B  81       31.11    -96.40                                   
REMARK 500    ASN B  82       29.85     49.46                                   
REMARK 500    CYS B 124     -105.68   -129.03                                   
REMARK 500    LYS B 125      -80.22    -94.77                                   
REMARK 500    LYS B 128      -92.79   -115.30                                   
REMARK 500    LEU B 220     -136.07     58.89                                   
REMARK 500    SER B 229      133.61    -38.38                                   
REMARK 500    ASP B 236     -110.48     60.33                                   
REMARK 500    MET B 270      -63.78    -93.25                                   
REMARK 500    ASN B 340       -8.34     79.97                                   
REMARK 500    GLU C  43     -106.58    -85.34                                   
REMARK 500    VAL C  45        7.82    -30.22                                   
REMARK 500    HIS C  61       53.48   -148.41                                   
REMARK 500    PHE C  81       31.43    -96.66                                   
REMARK 500    CYS C 124     -105.13   -128.25                                   
REMARK 500    LYS C 125      -79.12    -95.27                                   
REMARK 500    LYS C 128      -92.47   -115.76                                   
REMARK 500    LEU C 220     -136.26     58.78                                   
REMARK 500    ASP C 236     -106.96     62.73                                   
REMARK 500    ASN C 262       -7.65     73.13                                   
REMARK 500    LEU C 265     -122.36     58.72                                   
REMARK 500    MET C 270      -63.35    -94.48                                   
REMARK 500    GLU C 284      116.58     32.11                                   
REMARK 500    ASN C 340       -2.71     76.93                                   
REMARK 500    LEU D  42     -115.98     58.77                                   
REMARK 500    TYR D  46      114.61     78.30                                   
REMARK 500    HIS D  61       53.65   -148.03                                   
REMARK 500    PHE D  81       31.06    -96.14                                   
REMARK 500    ASN D  82       29.93     49.25                                   
REMARK 500    CYS D 124     -105.10   -129.31                                   
REMARK 500    LYS D 125      -79.66    -95.29                                   
REMARK 500    LYS D 128      -92.83   -115.78                                   
REMARK 500    LEU D 220     -136.11     59.74                                   
REMARK 500    ASP D 236     -111.55     61.77                                   
REMARK 500    MET D 270      -63.33    -93.14                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      55 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   19     GLY A   20                  129.48                    
REMARK 500 GLU A   40     ARG A   41                  133.74                    
REMARK 500 ARG A   41     LEU A   42                 -143.07                    
REMARK 500 LEU A   42     GLU A   43                  133.79                    
REMARK 500 HIS A  123     CYS A  124                  142.17                    
REMARK 500 MET A  264     LEU A  265                 -122.87                    
REMARK 500 LEU A  265     LYS A  266                 -146.68                    
REMARK 500 ILE A  280     PRO A  281                   49.73                    
REMARK 500 GLY A  282     PRO A  283                 -118.76                    
REMARK 500 GLU A  285     ASP A  310                 -138.05                    
REMARK 500 ASP A  312     LYS A  313                  -79.36                    
REMARK 500 LYS A  313     GLU A  314                  146.66                    
REMARK 500 ASP B   19     GLY B   20                  129.19                    
REMARK 500 GLY B   20     PHE B   21                 -134.06                    
REMARK 500 PHE B   21     ASP B   22                 -132.13                    
REMARK 500 HIS B  123     CYS B  124                  142.59                    
REMARK 500 ILE B  280     PRO B  281                  -76.07                    
REMARK 500 GLU B  284     GLU B  285                 -122.52                    
REMARK 500 ASN B  311     ASP B  312                 -147.38                    
REMARK 500 ASP C   19     GLY C   20                  129.10                    
REMARK 500 ARG C   41     LEU C   42                 -149.49                    
REMARK 500 LEU C   42     GLU C   43                 -142.16                    
REMARK 500 GLY C   44     VAL C   45                 -115.17                    
REMARK 500 TYR C   46     ARG C   47                 -147.14                    
REMARK 500 HIS C  123     CYS C  124                  141.88                    
REMARK 500 ILE C  280     PRO C  281                 -109.18                    
REMARK 500 GLY C  282     PRO C  283                 -147.09                    
REMARK 500 PRO C  283     GLU C  284                  144.92                    
REMARK 500 ASP C  310     ASN C  311                 -113.59                    
REMARK 500 ASP C  312     LYS C  313                 -128.43                    
REMARK 500 ASP D   19     GLY D   20                  129.08                    
REMARK 500 HIS D  123     CYS D  124                  141.85                    
REMARK 500 LYS D  263     MET D  264                  141.46                    
REMARK 500 PRO D  281     GLY D  282                  113.12                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ILE A 280         11.52                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 678        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH A 679        DISTANCE =  5.91 ANGSTROMS                       
REMARK 525    HOH A 680        DISTANCE =  6.09 ANGSTROMS                       
REMARK 525    HOH A 681        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH A 682        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH A 683        DISTANCE =  6.18 ANGSTROMS                       
REMARK 525    HOH A 684        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH A 685        DISTANCE =  6.59 ANGSTROMS                       
REMARK 525    HOH A 686        DISTANCE =  7.03 ANGSTROMS                       
REMARK 525    HOH A 687        DISTANCE =  7.24 ANGSTROMS                       
REMARK 525    HOH A 688        DISTANCE =  7.38 ANGSTROMS                       
REMARK 525    HOH A 689        DISTANCE =  7.39 ANGSTROMS                       
REMARK 525    HOH A 690        DISTANCE =  7.67 ANGSTROMS                       
REMARK 525    HOH A 691        DISTANCE =  7.74 ANGSTROMS                       
REMARK 525    HOH A 692        DISTANCE =  8.47 ANGSTROMS                       
REMARK 525    HOH A 693        DISTANCE =  8.65 ANGSTROMS                       
REMARK 525    HOH A 694        DISTANCE =  8.73 ANGSTROMS                       
REMARK 525    HOH A 695        DISTANCE =  8.99 ANGSTROMS                       
REMARK 525    HOH A 696        DISTANCE = 10.00 ANGSTROMS                       
REMARK 525    HOH A 697        DISTANCE = 10.21 ANGSTROMS                       
REMARK 525    HOH A 698        DISTANCE = 10.21 ANGSTROMS                       
REMARK 525    HOH A 699        DISTANCE = 10.45 ANGSTROMS                       
REMARK 525    HOH A 700        DISTANCE = 10.56 ANGSTROMS                       
REMARK 525    HOH A 701        DISTANCE = 10.99 ANGSTROMS                       
REMARK 525    HOH A 702        DISTANCE = 12.50 ANGSTROMS                       
REMARK 525    HOH A 703        DISTANCE = 12.51 ANGSTROMS                       
REMARK 525    HOH B 684        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH B 685        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH B 686        DISTANCE =  5.88 ANGSTROMS                       
REMARK 525    HOH B 687        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH B 688        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH B 689        DISTANCE =  6.31 ANGSTROMS                       
REMARK 525    HOH B 690        DISTANCE =  6.34 ANGSTROMS                       
REMARK 525    HOH B 691        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH B 692        DISTANCE =  6.54 ANGSTROMS                       
REMARK 525    HOH B 693        DISTANCE =  6.62 ANGSTROMS                       
REMARK 525    HOH B 694        DISTANCE =  6.66 ANGSTROMS                       
REMARK 525    HOH B 695        DISTANCE =  6.71 ANGSTROMS                       
REMARK 525    HOH B 696        DISTANCE =  7.22 ANGSTROMS                       
REMARK 525    HOH B 697        DISTANCE =  7.40 ANGSTROMS                       
REMARK 525    HOH B 698        DISTANCE =  7.59 ANGSTROMS                       
REMARK 525    HOH B 699        DISTANCE =  7.66 ANGSTROMS                       
REMARK 525    HOH B 700        DISTANCE =  7.78 ANGSTROMS                       
REMARK 525    HOH B 701        DISTANCE =  7.83 ANGSTROMS                       
REMARK 525    HOH B 702        DISTANCE =  7.91 ANGSTROMS                       
REMARK 525    HOH B 703        DISTANCE =  8.53 ANGSTROMS                       
REMARK 525    HOH B 704        DISTANCE =  8.59 ANGSTROMS                       
REMARK 525    HOH B 705        DISTANCE =  8.83 ANGSTROMS                       
REMARK 525    HOH B 706        DISTANCE =  8.84 ANGSTROMS                       
REMARK 525    HOH B 707        DISTANCE =  8.90 ANGSTROMS                       
REMARK 525    HOH B 708        DISTANCE =  9.10 ANGSTROMS                       
REMARK 525    HOH B 709        DISTANCE =  9.90 ANGSTROMS                       
REMARK 525    HOH B 710        DISTANCE = 10.24 ANGSTROMS                       
REMARK 525    HOH B 711        DISTANCE = 10.79 ANGSTROMS                       
REMARK 525    HOH B 712        DISTANCE = 11.12 ANGSTROMS                       
REMARK 525    HOH B 713        DISTANCE = 11.15 ANGSTROMS                       
REMARK 525    HOH B 714        DISTANCE = 11.34 ANGSTROMS                       
REMARK 525    HOH B 715        DISTANCE = 11.69 ANGSTROMS                       
REMARK 525    HOH B 716        DISTANCE = 11.85 ANGSTROMS                       
REMARK 525    HOH B 717        DISTANCE = 12.94 ANGSTROMS                       
REMARK 525    HOH B 718        DISTANCE = 13.28 ANGSTROMS                       
REMARK 525    HOH B 719        DISTANCE = 13.36 ANGSTROMS                       
REMARK 525    HOH B 720        DISTANCE = 13.96 ANGSTROMS                       
REMARK 525    HOH B 721        DISTANCE = 16.18 ANGSTROMS                       
REMARK 525    HOH B 722        DISTANCE = 16.50 ANGSTROMS                       
REMARK 525    HOH B 723        DISTANCE = 18.02 ANGSTROMS                       
REMARK 525    HOH B 724        DISTANCE = 20.37 ANGSTROMS                       
REMARK 525    HOH C 689        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH C 690        DISTANCE =  6.45 ANGSTROMS                       
REMARK 525    HOH C 691        DISTANCE =  6.60 ANGSTROMS                       
REMARK 525    HOH C 692        DISTANCE =  6.61 ANGSTROMS                       
REMARK 525    HOH C 693        DISTANCE =  7.04 ANGSTROMS                       
REMARK 525    HOH C 694        DISTANCE =  7.21 ANGSTROMS                       
REMARK 525    HOH C 695        DISTANCE =  7.24 ANGSTROMS                       
REMARK 525    HOH C 696        DISTANCE =  7.69 ANGSTROMS                       
REMARK 525    HOH C 697        DISTANCE =  7.83 ANGSTROMS                       
REMARK 525    HOH C 698        DISTANCE =  8.24 ANGSTROMS                       
REMARK 525    HOH C 699        DISTANCE =  8.24 ANGSTROMS                       
REMARK 525    HOH C 700        DISTANCE =  8.51 ANGSTROMS                       
REMARK 525    HOH C 701        DISTANCE =  9.06 ANGSTROMS                       
REMARK 525    HOH C 702        DISTANCE =  9.33 ANGSTROMS                       
REMARK 525    HOH C 703        DISTANCE = 11.30 ANGSTROMS                       
REMARK 525    HOH C 704        DISTANCE = 11.57 ANGSTROMS                       
REMARK 525    HOH C 705        DISTANCE = 12.43 ANGSTROMS                       
REMARK 525    HOH C 706        DISTANCE = 13.11 ANGSTROMS                       
REMARK 525    HOH C 707        DISTANCE = 15.47 ANGSTROMS                       
REMARK 525    HOH C 708        DISTANCE = 16.40 ANGSTROMS                       
REMARK 525    HOH C 709        DISTANCE = 19.63 ANGSTROMS                       
REMARK 525    HOH D 717        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH D 718        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH D 719        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH D 720        DISTANCE =  6.30 ANGSTROMS                       
REMARK 525    HOH D 721        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH D 722        DISTANCE =  6.44 ANGSTROMS                       
REMARK 525    HOH D 723        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH D 724        DISTANCE =  6.88 ANGSTROMS                       
REMARK 525    HOH D 725        DISTANCE =  6.96 ANGSTROMS                       
REMARK 525    HOH D 726        DISTANCE =  7.46 ANGSTROMS                       
REMARK 525    HOH D 727        DISTANCE =  7.70 ANGSTROMS                       
REMARK 525    HOH D 728        DISTANCE =  7.83 ANGSTROMS                       
REMARK 525    HOH D 729        DISTANCE =  7.90 ANGSTROMS                       
REMARK 525    HOH D 730        DISTANCE =  8.31 ANGSTROMS                       
REMARK 525    HOH D 731        DISTANCE =  8.40 ANGSTROMS                       
REMARK 525    HOH D 732        DISTANCE =  8.55 ANGSTROMS                       
REMARK 525    HOH D 733        DISTANCE =  8.74 ANGSTROMS                       
REMARK 525    HOH D 734        DISTANCE =  8.88 ANGSTROMS                       
REMARK 525    HOH D 735        DISTANCE =  9.05 ANGSTROMS                       
REMARK 525    HOH D 736        DISTANCE =  9.18 ANGSTROMS                       
REMARK 525    HOH D 737        DISTANCE =  9.28 ANGSTROMS                       
REMARK 525    HOH D 738        DISTANCE =  9.69 ANGSTROMS                       
REMARK 525    HOH D 739        DISTANCE = 10.18 ANGSTROMS                       
REMARK 525    HOH D 740        DISTANCE = 10.54 ANGSTROMS                       
REMARK 525    HOH D 741        DISTANCE = 10.84 ANGSTROMS                       
REMARK 525    HOH D 742        DISTANCE = 11.31 ANGSTROMS                       
REMARK 525    HOH D 743        DISTANCE = 12.90 ANGSTROMS                       
REMARK 525    HOH D 744        DISTANCE = 13.43 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             VO4 C 402   V                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TLA C 401   O2                                                     
REMARK 620 2 VO4 C 402   O1   68.0                                              
REMARK 620 3 VO4 C 402   O2   98.7 111.2                                        
REMARK 620 4 VO4 C 402   O3   48.2 107.9 108.3                                  
REMARK 620 5 VO4 C 402   O4  149.8 110.1 109.3 110.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue VO4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TLA B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TLA D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues TLA C 401 and VO4 C      
REMARK 800  402                                                                 
DBREF  5BZX A   14   351  UNP    P60484   PTEN_HUMAN      14    351             
DBREF  5BZX B   14   351  UNP    P60484   PTEN_HUMAN      14    351             
DBREF  5BZX C   14   351  UNP    P60484   PTEN_HUMAN      14    351             
DBREF  5BZX D   14   351  UNP    P60484   PTEN_HUMAN      14    351             
SEQADV 5BZX     A       UNP  P60484    THR   286 DELETION                       
SEQADV 5BZX     A       UNP  P60484    SER   287 DELETION                       
SEQADV 5BZX     A       UNP  P60484    GLU   288 DELETION                       
SEQADV 5BZX     A       UNP  P60484    LYS   289 DELETION                       
SEQADV 5BZX     A       UNP  P60484    VAL   290 DELETION                       
SEQADV 5BZX     A       UNP  P60484    GLU   291 DELETION                       
SEQADV 5BZX     A       UNP  P60484    ASN   292 DELETION                       
SEQADV 5BZX     A       UNP  P60484    GLY   293 DELETION                       
SEQADV 5BZX     A       UNP  P60484    SER   294 DELETION                       
SEQADV 5BZX     A       UNP  P60484    LEU   295 DELETION                       
SEQADV 5BZX     A       UNP  P60484    CYS   296 DELETION                       
SEQADV 5BZX     A       UNP  P60484    ASP   297 DELETION                       
SEQADV 5BZX     A       UNP  P60484    GLN   298 DELETION                       
SEQADV 5BZX     A       UNP  P60484    GLU   299 DELETION                       
SEQADV 5BZX     A       UNP  P60484    ILE   300 DELETION                       
SEQADV 5BZX     A       UNP  P60484    ASP   301 DELETION                       
SEQADV 5BZX     A       UNP  P60484    SER   302 DELETION                       
SEQADV 5BZX     A       UNP  P60484    ILE   303 DELETION                       
SEQADV 5BZX     A       UNP  P60484    CYS   304 DELETION                       
SEQADV 5BZX     A       UNP  P60484    SER   305 DELETION                       
SEQADV 5BZX     A       UNP  P60484    ILE   306 DELETION                       
SEQADV 5BZX     A       UNP  P60484    GLU   307 DELETION                       
SEQADV 5BZX     A       UNP  P60484    ARG   308 DELETION                       
SEQADV 5BZX     A       UNP  P60484    ALA   309 DELETION                       
SEQADV 5BZX     B       UNP  P60484    THR   286 DELETION                       
SEQADV 5BZX     B       UNP  P60484    SER   287 DELETION                       
SEQADV 5BZX     B       UNP  P60484    GLU   288 DELETION                       
SEQADV 5BZX     B       UNP  P60484    LYS   289 DELETION                       
SEQADV 5BZX     B       UNP  P60484    VAL   290 DELETION                       
SEQADV 5BZX     B       UNP  P60484    GLU   291 DELETION                       
SEQADV 5BZX     B       UNP  P60484    ASN   292 DELETION                       
SEQADV 5BZX     B       UNP  P60484    GLY   293 DELETION                       
SEQADV 5BZX     B       UNP  P60484    SER   294 DELETION                       
SEQADV 5BZX     B       UNP  P60484    LEU   295 DELETION                       
SEQADV 5BZX     B       UNP  P60484    CYS   296 DELETION                       
SEQADV 5BZX     B       UNP  P60484    ASP   297 DELETION                       
SEQADV 5BZX     B       UNP  P60484    GLN   298 DELETION                       
SEQADV 5BZX     B       UNP  P60484    GLU   299 DELETION                       
SEQADV 5BZX     B       UNP  P60484    ILE   300 DELETION                       
SEQADV 5BZX     B       UNP  P60484    ASP   301 DELETION                       
SEQADV 5BZX     B       UNP  P60484    SER   302 DELETION                       
SEQADV 5BZX     B       UNP  P60484    ILE   303 DELETION                       
SEQADV 5BZX     B       UNP  P60484    CYS   304 DELETION                       
SEQADV 5BZX     B       UNP  P60484    SER   305 DELETION                       
SEQADV 5BZX     B       UNP  P60484    ILE   306 DELETION                       
SEQADV 5BZX     B       UNP  P60484    GLU   307 DELETION                       
SEQADV 5BZX     B       UNP  P60484    ARG   308 DELETION                       
SEQADV 5BZX     B       UNP  P60484    ALA   309 DELETION                       
SEQADV 5BZX     C       UNP  P60484    THR   286 DELETION                       
SEQADV 5BZX     C       UNP  P60484    SER   287 DELETION                       
SEQADV 5BZX     C       UNP  P60484    GLU   288 DELETION                       
SEQADV 5BZX     C       UNP  P60484    LYS   289 DELETION                       
SEQADV 5BZX     C       UNP  P60484    VAL   290 DELETION                       
SEQADV 5BZX     C       UNP  P60484    GLU   291 DELETION                       
SEQADV 5BZX     C       UNP  P60484    ASN   292 DELETION                       
SEQADV 5BZX     C       UNP  P60484    GLY   293 DELETION                       
SEQADV 5BZX     C       UNP  P60484    SER   294 DELETION                       
SEQADV 5BZX     C       UNP  P60484    LEU   295 DELETION                       
SEQADV 5BZX     C       UNP  P60484    CYS   296 DELETION                       
SEQADV 5BZX     C       UNP  P60484    ASP   297 DELETION                       
SEQADV 5BZX     C       UNP  P60484    GLN   298 DELETION                       
SEQADV 5BZX     C       UNP  P60484    GLU   299 DELETION                       
SEQADV 5BZX     C       UNP  P60484    ILE   300 DELETION                       
SEQADV 5BZX     C       UNP  P60484    ASP   301 DELETION                       
SEQADV 5BZX     C       UNP  P60484    SER   302 DELETION                       
SEQADV 5BZX     C       UNP  P60484    ILE   303 DELETION                       
SEQADV 5BZX     C       UNP  P60484    CYS   304 DELETION                       
SEQADV 5BZX     C       UNP  P60484    SER   305 DELETION                       
SEQADV 5BZX     C       UNP  P60484    ILE   306 DELETION                       
SEQADV 5BZX     C       UNP  P60484    GLU   307 DELETION                       
SEQADV 5BZX     C       UNP  P60484    ARG   308 DELETION                       
SEQADV 5BZX     C       UNP  P60484    ALA   309 DELETION                       
SEQADV 5BZX     D       UNP  P60484    THR   286 DELETION                       
SEQADV 5BZX     D       UNP  P60484    SER   287 DELETION                       
SEQADV 5BZX     D       UNP  P60484    GLU   288 DELETION                       
SEQADV 5BZX     D       UNP  P60484    LYS   289 DELETION                       
SEQADV 5BZX     D       UNP  P60484    VAL   290 DELETION                       
SEQADV 5BZX     D       UNP  P60484    GLU   291 DELETION                       
SEQADV 5BZX     D       UNP  P60484    ASN   292 DELETION                       
SEQADV 5BZX     D       UNP  P60484    GLY   293 DELETION                       
SEQADV 5BZX     D       UNP  P60484    SER   294 DELETION                       
SEQADV 5BZX     D       UNP  P60484    LEU   295 DELETION                       
SEQADV 5BZX     D       UNP  P60484    CYS   296 DELETION                       
SEQADV 5BZX     D       UNP  P60484    ASP   297 DELETION                       
SEQADV 5BZX     D       UNP  P60484    GLN   298 DELETION                       
SEQADV 5BZX     D       UNP  P60484    GLU   299 DELETION                       
SEQADV 5BZX     D       UNP  P60484    ILE   300 DELETION                       
SEQADV 5BZX     D       UNP  P60484    ASP   301 DELETION                       
SEQADV 5BZX     D       UNP  P60484    SER   302 DELETION                       
SEQADV 5BZX     D       UNP  P60484    ILE   303 DELETION                       
SEQADV 5BZX     D       UNP  P60484    CYS   304 DELETION                       
SEQADV 5BZX     D       UNP  P60484    SER   305 DELETION                       
SEQADV 5BZX     D       UNP  P60484    ILE   306 DELETION                       
SEQADV 5BZX     D       UNP  P60484    GLU   307 DELETION                       
SEQADV 5BZX     D       UNP  P60484    ARG   308 DELETION                       
SEQADV 5BZX     D       UNP  P60484    ALA   309 DELETION                       
SEQRES   1 A  314  ARG ARG TYR GLN GLU ASP GLY PHE ASP LEU ASP LEU THR          
SEQRES   2 A  314  TYR ILE TYR PRO ASN ILE ILE ALA MET GLY PHE PRO ALA          
SEQRES   3 A  314  GLU ARG LEU GLU GLY VAL TYR ARG ASN ASN ILE ASP ASP          
SEQRES   4 A  314  VAL VAL ARG PHE LEU ASP SER LYS HIS LYS ASN HIS TYR          
SEQRES   5 A  314  LYS ILE TYR ASN LEU CYS ALA GLU ARG HIS TYR ASP THR          
SEQRES   6 A  314  ALA LYS PHE ASN CYS ARG VAL ALA GLN TYR PRO PHE GLU          
SEQRES   7 A  314  ASP HIS ASN PRO PRO GLN LEU GLU LEU ILE LYS PRO PHE          
SEQRES   8 A  314  CYS GLU ASP LEU ASP GLN TRP LEU SER GLU ASP ASP ASN          
SEQRES   9 A  314  HIS VAL ALA ALA ILE HIS CYS LYS ALA GLY LYS GLY ARG          
SEQRES  10 A  314  THR GLY VAL MET ILE CYS ALA TYR LEU LEU HIS ARG GLY          
SEQRES  11 A  314  LYS PHE LEU LYS ALA GLN GLU ALA LEU ASP PHE TYR GLY          
SEQRES  12 A  314  GLU VAL ARG THR ARG ASP LYS LYS GLY VAL THR ILE PRO          
SEQRES  13 A  314  SER GLN ARG ARG TYR VAL TYR TYR TYR SER TYR LEU LEU          
SEQRES  14 A  314  LYS ASN HIS LEU ASP TYR ARG PRO VAL ALA LEU LEU PHE          
SEQRES  15 A  314  HIS LYS MET MET PHE GLU THR ILE PRO MET PHE SER GLY          
SEQRES  16 A  314  GLY THR CYS ASN PRO GLN PHE VAL VAL CYS GLN LEU LYS          
SEQRES  17 A  314  VAL LYS ILE TYR SER SER ASN SER GLY PRO THR ARG ARG          
SEQRES  18 A  314  GLU ASP LYS PHE MET TYR PHE GLU PHE PRO GLN PRO LEU          
SEQRES  19 A  314  PRO VAL CYS GLY ASP ILE LYS VAL GLU PHE PHE HIS LYS          
SEQRES  20 A  314  GLN ASN LYS MET LEU LYS LYS ASP LYS MET PHE HIS PHE          
SEQRES  21 A  314  TRP VAL ASN THR PHE PHE ILE PRO GLY PRO GLU GLU ASP          
SEQRES  22 A  314  ASN ASP LYS GLU TYR LEU VAL LEU THR LEU THR LYS ASN          
SEQRES  23 A  314  ASP LEU ASP LYS ALA ASN LYS ASP LYS ALA ASN ARG TYR          
SEQRES  24 A  314  PHE SER PRO ASN PHE LYS VAL LYS LEU TYR PHE THR LYS          
SEQRES  25 A  314  THR VAL                                                      
SEQRES   1 B  314  ARG ARG TYR GLN GLU ASP GLY PHE ASP LEU ASP LEU THR          
SEQRES   2 B  314  TYR ILE TYR PRO ASN ILE ILE ALA MET GLY PHE PRO ALA          
SEQRES   3 B  314  GLU ARG LEU GLU GLY VAL TYR ARG ASN ASN ILE ASP ASP          
SEQRES   4 B  314  VAL VAL ARG PHE LEU ASP SER LYS HIS LYS ASN HIS TYR          
SEQRES   5 B  314  LYS ILE TYR ASN LEU CYS ALA GLU ARG HIS TYR ASP THR          
SEQRES   6 B  314  ALA LYS PHE ASN CYS ARG VAL ALA GLN TYR PRO PHE GLU          
SEQRES   7 B  314  ASP HIS ASN PRO PRO GLN LEU GLU LEU ILE LYS PRO PHE          
SEQRES   8 B  314  CYS GLU ASP LEU ASP GLN TRP LEU SER GLU ASP ASP ASN          
SEQRES   9 B  314  HIS VAL ALA ALA ILE HIS CYS LYS ALA GLY LYS GLY ARG          
SEQRES  10 B  314  THR GLY VAL MET ILE CYS ALA TYR LEU LEU HIS ARG GLY          
SEQRES  11 B  314  LYS PHE LEU LYS ALA GLN GLU ALA LEU ASP PHE TYR GLY          
SEQRES  12 B  314  GLU VAL ARG THR ARG ASP LYS LYS GLY VAL THR ILE PRO          
SEQRES  13 B  314  SER GLN ARG ARG TYR VAL TYR TYR TYR SER TYR LEU LEU          
SEQRES  14 B  314  LYS ASN HIS LEU ASP TYR ARG PRO VAL ALA LEU LEU PHE          
SEQRES  15 B  314  HIS LYS MET MET PHE GLU THR ILE PRO MET PHE SER GLY          
SEQRES  16 B  314  GLY THR CYS ASN PRO GLN PHE VAL VAL CYS GLN LEU LYS          
SEQRES  17 B  314  VAL LYS ILE TYR SER SER ASN SER GLY PRO THR ARG ARG          
SEQRES  18 B  314  GLU ASP LYS PHE MET TYR PHE GLU PHE PRO GLN PRO LEU          
SEQRES  19 B  314  PRO VAL CYS GLY ASP ILE LYS VAL GLU PHE PHE HIS LYS          
SEQRES  20 B  314  GLN ASN LYS MET LEU LYS LYS ASP LYS MET PHE HIS PHE          
SEQRES  21 B  314  TRP VAL ASN THR PHE PHE ILE PRO GLY PRO GLU GLU ASP          
SEQRES  22 B  314  ASN ASP LYS GLU TYR LEU VAL LEU THR LEU THR LYS ASN          
SEQRES  23 B  314  ASP LEU ASP LYS ALA ASN LYS ASP LYS ALA ASN ARG TYR          
SEQRES  24 B  314  PHE SER PRO ASN PHE LYS VAL LYS LEU TYR PHE THR LYS          
SEQRES  25 B  314  THR VAL                                                      
SEQRES   1 C  314  ARG ARG TYR GLN GLU ASP GLY PHE ASP LEU ASP LEU THR          
SEQRES   2 C  314  TYR ILE TYR PRO ASN ILE ILE ALA MET GLY PHE PRO ALA          
SEQRES   3 C  314  GLU ARG LEU GLU GLY VAL TYR ARG ASN ASN ILE ASP ASP          
SEQRES   4 C  314  VAL VAL ARG PHE LEU ASP SER LYS HIS LYS ASN HIS TYR          
SEQRES   5 C  314  LYS ILE TYR ASN LEU CYS ALA GLU ARG HIS TYR ASP THR          
SEQRES   6 C  314  ALA LYS PHE ASN CYS ARG VAL ALA GLN TYR PRO PHE GLU          
SEQRES   7 C  314  ASP HIS ASN PRO PRO GLN LEU GLU LEU ILE LYS PRO PHE          
SEQRES   8 C  314  CYS GLU ASP LEU ASP GLN TRP LEU SER GLU ASP ASP ASN          
SEQRES   9 C  314  HIS VAL ALA ALA ILE HIS CYS LYS ALA GLY LYS GLY ARG          
SEQRES  10 C  314  THR GLY VAL MET ILE CYS ALA TYR LEU LEU HIS ARG GLY          
SEQRES  11 C  314  LYS PHE LEU LYS ALA GLN GLU ALA LEU ASP PHE TYR GLY          
SEQRES  12 C  314  GLU VAL ARG THR ARG ASP LYS LYS GLY VAL THR ILE PRO          
SEQRES  13 C  314  SER GLN ARG ARG TYR VAL TYR TYR TYR SER TYR LEU LEU          
SEQRES  14 C  314  LYS ASN HIS LEU ASP TYR ARG PRO VAL ALA LEU LEU PHE          
SEQRES  15 C  314  HIS LYS MET MET PHE GLU THR ILE PRO MET PHE SER GLY          
SEQRES  16 C  314  GLY THR CYS ASN PRO GLN PHE VAL VAL CYS GLN LEU LYS          
SEQRES  17 C  314  VAL LYS ILE TYR SER SER ASN SER GLY PRO THR ARG ARG          
SEQRES  18 C  314  GLU ASP LYS PHE MET TYR PHE GLU PHE PRO GLN PRO LEU          
SEQRES  19 C  314  PRO VAL CYS GLY ASP ILE LYS VAL GLU PHE PHE HIS LYS          
SEQRES  20 C  314  GLN ASN LYS MET LEU LYS LYS ASP LYS MET PHE HIS PHE          
SEQRES  21 C  314  TRP VAL ASN THR PHE PHE ILE PRO GLY PRO GLU GLU ASP          
SEQRES  22 C  314  ASN ASP LYS GLU TYR LEU VAL LEU THR LEU THR LYS ASN          
SEQRES  23 C  314  ASP LEU ASP LYS ALA ASN LYS ASP LYS ALA ASN ARG TYR          
SEQRES  24 C  314  PHE SER PRO ASN PHE LYS VAL LYS LEU TYR PHE THR LYS          
SEQRES  25 C  314  THR VAL                                                      
SEQRES   1 D  314  ARG ARG TYR GLN GLU ASP GLY PHE ASP LEU ASP LEU THR          
SEQRES   2 D  314  TYR ILE TYR PRO ASN ILE ILE ALA MET GLY PHE PRO ALA          
SEQRES   3 D  314  GLU ARG LEU GLU GLY VAL TYR ARG ASN ASN ILE ASP ASP          
SEQRES   4 D  314  VAL VAL ARG PHE LEU ASP SER LYS HIS LYS ASN HIS TYR          
SEQRES   5 D  314  LYS ILE TYR ASN LEU CYS ALA GLU ARG HIS TYR ASP THR          
SEQRES   6 D  314  ALA LYS PHE ASN CYS ARG VAL ALA GLN TYR PRO PHE GLU          
SEQRES   7 D  314  ASP HIS ASN PRO PRO GLN LEU GLU LEU ILE LYS PRO PHE          
SEQRES   8 D  314  CYS GLU ASP LEU ASP GLN TRP LEU SER GLU ASP ASP ASN          
SEQRES   9 D  314  HIS VAL ALA ALA ILE HIS CYS LYS ALA GLY LYS GLY ARG          
SEQRES  10 D  314  THR GLY VAL MET ILE CYS ALA TYR LEU LEU HIS ARG GLY          
SEQRES  11 D  314  LYS PHE LEU LYS ALA GLN GLU ALA LEU ASP PHE TYR GLY          
SEQRES  12 D  314  GLU VAL ARG THR ARG ASP LYS LYS GLY VAL THR ILE PRO          
SEQRES  13 D  314  SER GLN ARG ARG TYR VAL TYR TYR TYR SER TYR LEU LEU          
SEQRES  14 D  314  LYS ASN HIS LEU ASP TYR ARG PRO VAL ALA LEU LEU PHE          
SEQRES  15 D  314  HIS LYS MET MET PHE GLU THR ILE PRO MET PHE SER GLY          
SEQRES  16 D  314  GLY THR CYS ASN PRO GLN PHE VAL VAL CYS GLN LEU LYS          
SEQRES  17 D  314  VAL LYS ILE TYR SER SER ASN SER GLY PRO THR ARG ARG          
SEQRES  18 D  314  GLU ASP LYS PHE MET TYR PHE GLU PHE PRO GLN PRO LEU          
SEQRES  19 D  314  PRO VAL CYS GLY ASP ILE LYS VAL GLU PHE PHE HIS LYS          
SEQRES  20 D  314  GLN ASN LYS MET LEU LYS LYS ASP LYS MET PHE HIS PHE          
SEQRES  21 D  314  TRP VAL ASN THR PHE PHE ILE PRO GLY PRO GLU GLU ASP          
SEQRES  22 D  314  ASN ASP LYS GLU TYR LEU VAL LEU THR LEU THR LYS ASN          
SEQRES  23 D  314  ASP LEU ASP LYS ALA ASN LYS ASP LYS ALA ASN ARG TYR          
SEQRES  24 D  314  PHE SER PRO ASN PHE LYS VAL LYS LEU TYR PHE THR LYS          
SEQRES  25 D  314  THR VAL                                                      
HET    VO4  A 401       5                                                       
HET    TLA  B 401      10                                                       
HET    TLA  C 401      10                                                       
HET    VO4  C 402       5                                                       
HET    TLA  D 401      10                                                       
HETNAM     VO4 VANADATE ION                                                     
HETNAM     TLA L(+)-TARTARIC ACID                                               
FORMUL   5  VO4    2(O4 V 3-)                                                   
FORMUL   6  TLA    3(C4 H6 O6)                                                  
FORMUL  10  HOH   *880(H2 O)                                                    
HELIX    1 AA1 ASN A   49  LYS A   62  1                                  14    
HELIX    2 AA2 ASP A   77  ASN A   82  5                                   6    
HELIX    3 AA3 GLN A   97  GLU A   99  5                                   3    
HELIX    4 AA4 LEU A  100  ASP A  115  1                                  16    
HELIX    5 AA5 LYS A  128  ARG A  142  1                                  15    
HELIX    6 AA6 LYS A  147  THR A  160  1                                  14    
HELIX    7 AA7 ILE A  168  ASN A  184  1                                  17    
HELIX    8 AA8 PHE A  278  ILE A  280  5                                   3    
HELIX    9 AA9 ASN A  323  LEU A  325  5                                   3    
HELIX   10 AB1 LYS A  327  ASP A  331  5                                   5    
HELIX   11 AB2 ILE B   50  LYS B   62  1                                  13    
HELIX   12 AB3 ASP B   77  ASN B   82  5                                   6    
HELIX   13 AB4 GLN B   97  GLU B   99  5                                   3    
HELIX   14 AB5 LEU B  100  ASP B  115  1                                  16    
HELIX   15 AB6 LYS B  128  ARG B  142  1                                  15    
HELIX   16 AB7 LYS B  147  THR B  160  1                                  14    
HELIX   17 AB8 ILE B  168  ASN B  184  1                                  17    
HELIX   18 AB9 PHE B  278  ILE B  280  5                                   3    
HELIX   19 AC1 ASN B  323  LEU B  325  5                                   3    
HELIX   20 AC2 LYS B  327  ASP B  331  5                                   5    
HELIX   21 AC3 ASN C   49  LYS C   62  1                                  14    
HELIX   22 AC4 ASP C   77  ASN C   82  5                                   6    
HELIX   23 AC5 GLN C   97  GLU C   99  5                                   3    
HELIX   24 AC6 LEU C  100  ASP C  115  1                                  16    
HELIX   25 AC7 LYS C  128  ARG C  142  1                                  15    
HELIX   26 AC8 LYS C  147  THR C  160  1                                  14    
HELIX   27 AC9 ILE C  168  ASN C  184  1                                  17    
HELIX   28 AD1 PHE C  278  ILE C  280  5                                   3    
HELIX   29 AD2 ASN C  323  LEU C  325  5                                   3    
HELIX   30 AD3 LYS C  327  ASP C  331  5                                   5    
HELIX   31 AD4 ASN D   49  LYS D   62  1                                  14    
HELIX   32 AD5 ASP D   77  ASN D   82  5                                   6    
HELIX   33 AD6 GLN D   97  GLU D   99  5                                   3    
HELIX   34 AD7 LEU D  100  ASP D  115  1                                  16    
HELIX   35 AD8 LYS D  128  ARG D  142  1                                  15    
HELIX   36 AD9 LYS D  147  THR D  160  1                                  14    
HELIX   37 AE1 ILE D  168  ASN D  184  1                                  17    
HELIX   38 AE2 PHE D  278  ILE D  280  5                                   3    
HELIX   39 AE3 ASN D  323  LEU D  325  5                                   3    
HELIX   40 AE4 LYS D  327  ASP D  331  5                                   5    
SHEET    1 AA1 5 LEU A  25  TYR A  29  0                                        
SHEET    2 AA1 5 ILE A  32  MET A  35 -1  O  ALA A  34   N  THR A  26           
SHEET    3 AA1 5 VAL A 119  HIS A 123  1  O  ALA A 120   N  ILE A  33           
SHEET    4 AA1 5 TYR A  65  ASN A  69  1  N  LYS A  66   O  ALA A 121           
SHEET    5 AA1 5 VAL A  85  GLN A  87  1  O  ALA A  86   N  ASN A  69           
SHEET    1 AA2 5 ARG A 233  GLU A 235  0                                        
SHEET    2 AA2 5 PHE A 238  CYS A 250 -1  O  TYR A 240   N  ARG A 233           
SHEET    3 AA2 5 ALA A 192  PHE A 200 -1  N  PHE A 195   O  LEU A 247           
SHEET    4 AA2 5 LYS A 342  LYS A 349 -1  O  THR A 348   N  LEU A 194           
SHEET    5 AA2 5 LEU A 316  THR A 321 -1  N  LEU A 316   O  PHE A 347           
SHEET    1 AA3 4 VAL A 222  SER A 226  0                                        
SHEET    2 AA3 4 PRO A 213  GLN A 219 -1  N  GLN A 219   O  VAL A 222           
SHEET    3 AA3 4 ASP A 252  HIS A 259 -1  O  PHE A 258   N  GLN A 214           
SHEET    4 AA3 4 ASP A 268  ASN A 276 -1  O  PHE A 271   N  PHE A 257           
SHEET    1 AA4 5 LEU B  25  TYR B  29  0                                        
SHEET    2 AA4 5 ILE B  32  MET B  35 -1  O  ALA B  34   N  THR B  26           
SHEET    3 AA4 5 VAL B 119  HIS B 123  1  O  ALA B 120   N  ILE B  33           
SHEET    4 AA4 5 TYR B  65  ASN B  69  1  N  LYS B  66   O  ALA B 121           
SHEET    5 AA4 5 VAL B  85  GLN B  87  1  O  ALA B  86   N  ASN B  69           
SHEET    1 AA5 2 PRO B  38  ALA B  39  0                                        
SHEET    2 AA5 2 ASN B  48  ASN B  49  1  O  ASN B  48   N  ALA B  39           
SHEET    1 AA6 5 ARG B 233  GLU B 235  0                                        
SHEET    2 AA6 5 PHE B 238  CYS B 250 -1  O  TYR B 240   N  ARG B 233           
SHEET    3 AA6 5 ALA B 192  PHE B 200 -1  N  PHE B 195   O  LEU B 247           
SHEET    4 AA6 5 LYS B 342  LYS B 349 -1  O  THR B 348   N  LEU B 194           
SHEET    5 AA6 5 LEU B 316  THR B 321 -1  N  LEU B 316   O  PHE B 347           
SHEET    1 AA7 4 VAL B 222  SER B 226  0                                        
SHEET    2 AA7 4 PRO B 213  GLN B 219 -1  N  GLN B 219   O  VAL B 222           
SHEET    3 AA7 4 ASP B 252  GLN B 261 -1  O  PHE B 258   N  GLN B 214           
SHEET    4 AA7 4 MET B 264  ASN B 276 -1  O  MET B 264   N  GLN B 261           
SHEET    1 AA8 5 LEU C  25  TYR C  29  0                                        
SHEET    2 AA8 5 ILE C  32  MET C  35 -1  O  ALA C  34   N  THR C  26           
SHEET    3 AA8 5 VAL C 119  HIS C 123  1  O  ALA C 120   N  ILE C  33           
SHEET    4 AA8 5 TYR C  65  ASN C  69  1  N  LYS C  66   O  ALA C 121           
SHEET    5 AA8 5 VAL C  85  GLN C  87  1  O  ALA C  86   N  ASN C  69           
SHEET    1 AA9 5 ARG C 233  GLU C 235  0                                        
SHEET    2 AA9 5 PHE C 238  CYS C 250 -1  O  TYR C 240   N  ARG C 233           
SHEET    3 AA9 5 ALA C 192  PHE C 200 -1  N  PHE C 195   O  LEU C 247           
SHEET    4 AA9 5 LYS C 342  LYS C 349 -1  O  THR C 348   N  LEU C 194           
SHEET    5 AA9 5 LEU C 316  THR C 321 -1  N  LEU C 316   O  PHE C 347           
SHEET    1 AB1 4 VAL C 222  SER C 226  0                                        
SHEET    2 AB1 4 PRO C 213  GLN C 219 -1  N  GLN C 219   O  VAL C 222           
SHEET    3 AB1 4 ASP C 252  HIS C 259 -1  O  PHE C 258   N  GLN C 214           
SHEET    4 AB1 4 ASP C 268  ASN C 276 -1  O  PHE C 271   N  PHE C 257           
SHEET    1 AB2 5 LEU D  25  TYR D  29  0                                        
SHEET    2 AB2 5 ILE D  32  MET D  35 -1  O  ALA D  34   N  THR D  26           
SHEET    3 AB2 5 VAL D 119  HIS D 123  1  O  ALA D 120   N  ILE D  33           
SHEET    4 AB2 5 TYR D  65  ASN D  69  1  N  LYS D  66   O  ALA D 121           
SHEET    5 AB2 5 VAL D  85  GLN D  87  1  O  ALA D  86   N  ASN D  69           
SHEET    1 AB3 5 ARG D 233  GLU D 235  0                                        
SHEET    2 AB3 5 PHE D 238  CYS D 250 -1  O  TYR D 240   N  ARG D 233           
SHEET    3 AB3 5 ALA D 192  PHE D 200 -1  N  PHE D 195   O  LEU D 247           
SHEET    4 AB3 5 LYS D 342  LYS D 349 -1  O  THR D 348   N  LEU D 194           
SHEET    5 AB3 5 LEU D 316  THR D 321 -1  N  LEU D 316   O  PHE D 347           
SHEET    1 AB4 4 VAL D 222  SER D 226  0                                        
SHEET    2 AB4 4 PRO D 213  GLN D 219 -1  N  GLN D 219   O  VAL D 222           
SHEET    3 AB4 4 ASP D 252  HIS D 259 -1  O  PHE D 258   N  GLN D 214           
SHEET    4 AB4 4 ASP D 268  ASN D 276 -1  O  PHE D 271   N  PHE D 257           
SSBOND   1 CYS A   71    CYS A  124                          1555   1555  2.04  
SSBOND   2 CYS B   71    CYS B  124                          1555   1555  2.05  
SSBOND   3 CYS C   71    CYS C  124                          1555   1555  2.05  
SSBOND   4 CYS D   71    CYS D  124                          1555   1555  2.04  
LINK         C2  TLA C 401                 O1  VO4 C 402     1555   1555  1.20  
LINK         O2  TLA C 401                 V   VO4 C 402     1555   1555  2.37  
SITE     1 AC1 10 CYS A 124  LYS A 125  ALA A 126  GLY A 127                    
SITE     2 AC1 10 LYS A 128  GLY A 129  ARG A 130  THR A 131                    
SITE     3 AC1 10 HOH A 507  HOH A 563                                          
SITE     1 AC2 13 ASP B  92  HIS B  93  CYS B 124  LYS B 125                    
SITE     2 AC2 13 ALA B 126  GLY B 127  LYS B 128  GLY B 129                    
SITE     3 AC2 13 ARG B 130  THR B 131  HOH B 502  HOH B 503                    
SITE     4 AC2 13 HOH B 521                                                     
SITE     1 AC3 13 ASP D  92  HIS D  93  CYS D 124  LYS D 125                    
SITE     2 AC3 13 ALA D 126  GLY D 127  LYS D 128  GLY D 129                    
SITE     3 AC3 13 ARG D 130  THR D 131  HOH D 502  HOH D 510                    
SITE     4 AC3 13 HOH D 521                                                     
SITE     1 AC4 12 ASP C  92  HIS C  93  CYS C 124  LYS C 125                    
SITE     2 AC4 12 ALA C 126  GLY C 127  LYS C 128  GLY C 129                    
SITE     3 AC4 12 ARG C 130  THR C 131  GLN C 171  HOH C 542                    
CRYST1  207.060  206.900   87.670  90.00  90.00  90.00 C 2 2 21     32          
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      0.004830  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004833  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011406        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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