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Database: PDB
Entry: 1U32
LinkDB: 1U32
Original site: 1U32 
HEADER    HYDROLASE                               20-JUL-04   1U32              
TITLE     CRYSTAL STRUCTURE OF A PROTEIN PHOSPHATASE-1: CALCINEURIN             
TITLE    2 HYBRID BOUND TO OKADAIC ACID                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE PROTEIN PHOSPHATASE PP1-GAMMA             
COMPND   3 CATALYTIC SUBUNIT;                                                   
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: RESIDUES 6-298;                                            
COMPND   6 SYNONYM: PROTEIN PHOSPHATASE-1: CALCINEURIN HYBRID, PP-1G,           
COMPND   7 PROTEIN PHOSPHATASE 1C CATALYTIC SUBUNIT;                            
COMPND   8 EC: 3.1.3.16;                                                        
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PPP1CC;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.T.MAYNES,K.R.PERREAULT,M.M.CHERNEY,H.A.LUU,M.N.G.JAMES,             
AUTHOR   2 C.F.B.HOLMES                                                         
REVDAT   3   24-FEB-09 1U32    1       VERSN                                    
REVDAT   2   19-OCT-04 1U32    1       JRNL                                     
REVDAT   1   17-AUG-04 1U32    0                                                
JRNL        AUTH   J.T.MAYNES,K.R.PERREAULT,M.M.CHERNEY,H.A.LUU,                
JRNL        AUTH 2 M.N.G.JAMES,C.F.B.HOLMES                                     
JRNL        TITL   CRYSTAL STRUCTURE AND MUTAGENESIS OF A PROTEIN               
JRNL        TITL 2 PHOSPHATASE-1:CALCINEURIN HYBRID ELUCIDATE THE               
JRNL        TITL 3 ROLE OF THE {BETA}12-{BETA}13 LOOP IN INHIBITOR              
JRNL        TITL 4 BINDING                                                      
JRNL        REF    J.BIOL.CHEM.                  V. 279 43198 2004              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   15280359                                                     
JRNL        DOI    10.1074/JBC.M407184200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.01                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1946384.850                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 21272                          
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 SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1250                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3254                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2320                       
REMARK   3   BIN FREE R VALUE                    : 0.2730                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 199                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.019                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2371                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 71                                      
REMARK   3   SOLVENT ATOMS            : 89                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : 0.04000                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.12                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.29                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.20                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.79                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.380 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.110 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.080 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.060 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 37.25                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : BME.PARAM                                      
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : DAM.PARAM                                      
REMARK   3  PARAMETER FILE  5  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : BME.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : DAM.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1U32 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JUL-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB023182.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JUL-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH3R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : OSMIC MIRRORS                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21304                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.07600                            
REMARK 200  R SYM                      (I) : 0.05700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.36000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.020                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ID 1JK7                                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM SULFATE, TRIS, PEG 400,          
REMARK 280  MERCAPTOETHANOL, PH 8.0, VAPOR DIFFUSION, HANGING DROP,             
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2                        
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+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
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,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       49.37950            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       49.37950            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       31.09000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       49.37950            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       49.37950            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       31.09000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       49.37950            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       49.37950            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       31.09000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       49.37950            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       49.37950            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       31.09000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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   O    HOH A   585     O    HOH A   585     8666     1.20            
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    ASP A 194   N   -  CA  -  C   ANGL. DEV. = -17.7 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    ASP A  95      148.60     80.78                                   
REMARK 500    ARG A  96      -48.94     71.31                                   
REMARK 500    GLU A 126       50.54    -94.35                                   
REMARK 500    TYR A 144     -110.44   -136.62                                   
REMARK 500    GLU A 167       15.85     54.90                                   
REMARK 500    SER A 224     -156.53     62.65                                   
REMARK 500    ALA A 247     -123.19   -135.24                                   
REMARK 500    HIS A 248      -28.46     73.46                                   
REMARK 500    ASP A 274       -2.58     64.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 400  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  92   OD2                                                    
REMARK 620 2 ASN A 124   OD1 100.9                                              
REMARK 620 3 HIS A 248   ND1 159.9  97.3                                        
REMARK 620 4 HIS A 173   NE2  81.2  89.3  90.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  64   OD2                                                    
REMARK 620 2 HIS A  66   NE2 107.4                                              
REMARK 620 3 ASP A  92   OD2  91.9  98.9                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 400                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 401                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OKA A 501                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 301                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 302                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 303                 
DBREF  1U32 A    6   298  UNP    P36873   PP1G_HUMAN       6    298             
SEQADV 1U32 LEU A  273  UNP  P36873    CYS   273 ENGINEERED                     
SEQADV 1U32 ASP A  274  UNP  P36873    GLY   274 ENGINEERED                     
SEQADV 1U32 VAL A  275  UNP  P36873    GLU   275 ENGINEERED                     
SEQADV 1U32 TYR A  276  UNP  P36873    PHE   276 ENGINEERED                     
SEQADV 1U32 ASN A  277  UNP  P36873    ASP   277 ENGINEERED                     
SEQRES   1 A  293  LYS LEU ASN ILE ASP SER ILE ILE GLN ARG LEU LEU GLU          
SEQRES   2 A  293  VAL ARG GLY SER LYS PRO GLY LYS ASN VAL GLN LEU GLN          
SEQRES   3 A  293  GLU ASN GLU ILE ARG GLY LEU CYS LEU LYS SER ARG GLU          
SEQRES   4 A  293  ILE PHE LEU SER GLN PRO ILE LEU LEU GLU LEU GLU ALA          
SEQRES   5 A  293  PRO LEU LYS ILE CYS GLY ASP ILE HIS GLY GLN TYR TYR          
SEQRES   6 A  293  ASP LEU LEU ARG LEU PHE GLU TYR GLY GLY PHE PRO PRO          
SEQRES   7 A  293  GLU SER ASN TYR LEU PHE LEU GLY ASP TYR VAL ASP ARG          
SEQRES   8 A  293  GLY LYS GLN SER LEU GLU THR ILE CYS LEU LEU LEU ALA          
SEQRES   9 A  293  TYR LYS ILE LYS TYR PRO GLU ASN PHE PHE LEU LEU ARG          
SEQRES  10 A  293  GLY ASN HIS GLU CYS ALA SER ILE ASN ARG ILE TYR GLY          
SEQRES  11 A  293  PHE TYR ASP GLU CYS LYS ARG ARG TYR ASN ILE LYS LEU          
SEQRES  12 A  293  TRP LYS THR PHE THR ASP CYS PHE ASN CYS LEU PRO ILE          
SEQRES  13 A  293  ALA ALA ILE VAL ASP GLU LYS ILE PHE CYS CYS HIS GLY          
SEQRES  14 A  293  GLY LEU SER PRO ASP LEU GLN SER MET GLU GLN ILE ARG          
SEQRES  15 A  293  ARG ILE MET ARG PRO THR ASP VAL PRO ASP GLN GLY LEU          
SEQRES  16 A  293  LEU CYS ASP LEU LEU TRP SER ASP PRO ASP LYS ASP VAL          
SEQRES  17 A  293  LEU GLY TRP GLY GLU ASN ASP ARG GLY VAL SER PHE THR          
SEQRES  18 A  293  PHE GLY ALA GLU VAL VAL ALA LYS PHE LEU HIS LYS HIS          
SEQRES  19 A  293  ASP LEU ASP LEU ILE CYS ARG ALA HIS GLN VAL VAL GLU          
SEQRES  20 A  293  ASP GLY TYR GLU PHE PHE ALA LYS ARG GLN LEU VAL THR          
SEQRES  21 A  293  LEU PHE SER ALA PRO ASN TYR LEU ASP VAL TYR ASN ASN          
SEQRES  22 A  293  ALA GLY ALA MET MET SER VAL ASP GLU THR LEU MET CYS          
SEQRES  23 A  293  SER PHE GLN ILE LEU LYS PRO                                  
HET     MN  A 400       1                                                       
HET     MN  A 401       1                                                       
HET    OKA  A 501      57                                                       
HET    BME  A 301       4                                                       
HET    BME  A 302       4                                                       
HET    BME  A 303       4                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     OKA OKADAIC ACID                                                     
HETNAM     BME BETA-MERCAPTOETHANOL                                             
HETSYN     OKA 9,10-DEEPITHIO-9,10-DIDEHYDROACANTHIFOLICIN                      
FORMUL   2   MN    2(MN 2+)                                                     
FORMUL   4  OKA    C44 H68 O13                                                  
FORMUL   5  BME    3(C2 H6 O S)                                                 
FORMUL   8  HOH   *89(H2 O)                                                     
HELIX    1   1 ASN A    8  GLU A   18  1                                  11    
HELIX    2   2 GLN A   31  GLN A   49  1                                  19    
HELIX    3   3 GLN A   68  GLY A   80  1                                  13    
HELIX    4   4 GLN A   99  TYR A  114  1                                  16    
HELIX    5   5 CYS A  127  ARG A  132  1                                   6    
HELIX    6   6 GLY A  135  TYR A  144  1                                  10    
HELIX    7   7 ASN A  145  ASN A  157  1                                  13    
HELIX    8   8 SER A  182  ARG A  188  1                                   7    
HELIX    9   9 GLY A  199  SER A  207  1                                   9    
HELIX   10  10 GLY A  228  HIS A  239  1                                  12    
HELIX   11  11 ASN A  271  VAL A  275  5                                   5    
SHEET    1   A 6 LEU A  52  LEU A  55  0                                        
SHEET    2   A 6 ALA A 162  VAL A 165  1  O  ILE A 164   N  LEU A  53           
SHEET    3   A 6 ILE A 169  CYS A 171 -1  O  CYS A 171   N  ALA A 163           
SHEET    4   A 6 LEU A 243  ARG A 246  1  O  CYS A 245   N  PHE A 170           
SHEET    5   A 6 LEU A 263  LEU A 266  1  O  LEU A 266   N  ARG A 246           
SHEET    6   A 6 TYR A 255  PHE A 258 -1  N  GLU A 256   O  THR A 265           
SHEET    1   B 5 PHE A 118  LEU A 120  0                                        
SHEET    2   B 5 TYR A  87  PHE A  89  1  N  TYR A  87   O  PHE A 119           
SHEET    3   B 5 LEU A  59  CYS A  62  1  N  CYS A  62   O  LEU A  88           
SHEET    4   B 5 GLY A 280  VAL A 285 -1  O  MET A 283   N  ILE A  61           
SHEET    5   B 5 CYS A 291  LEU A 296 -1  O  LEU A 296   N  GLY A 280           
SHEET    1   C 3 ASP A 208  PRO A 209  0                                        
SHEET    2   C 3 PHE A 225  PHE A 227  1  O  PHE A 227   N  ASP A 208           
SHEET    3   C 3 TRP A 216  GLU A 218 -1  N  GLY A 217   O  THR A 226           
LINK        MN    MN A 400                 OD2 ASP A  92     1555   1555  2.20  
LINK        MN    MN A 400                 OD1 ASN A 124     1555   1555  2.17  
LINK        MN    MN A 401                 OD2 ASP A  64     1555   1555  2.09  
LINK         SG  CYS A 127                 S2  BME A 303     1555   1555  2.03  
LINK         SG  CYS A 202                 S2  BME A 301     1555   1555  2.04  
LINK         SG  CYS A 291                 S2  BME A 302     1555   1555  2.03  
LINK        MN    MN A 400                 ND1 HIS A 248     1555   1555  2.27  
LINK        MN    MN A 400                 NE2 HIS A 173     1555   1555  2.26  
LINK        MN    MN A 401                 NE2 HIS A  66     1555   1555  2.28  
LINK        MN    MN A 401                 OD2 ASP A  92     1555   1555  2.22  
CISPEP   1 ALA A   57    PRO A   58          0        -0.28                     
CISPEP   2 PRO A   82    PRO A   83          0         0.21                     
CISPEP   3 ARG A  191    PRO A  192          0         0.23                     
SITE     1 AC1  6 ASP A  92  ASN A 124  HIS A 173  HIS A 248                    
SITE     2 AC1  6  MN A 401  HOH A 505                                          
SITE     1 AC2  4 ASP A  64  HIS A  66  ASP A  92   MN A 400                    
SITE     1 AC3 15 ARG A  96  HIS A 125  ILE A 130  TYR A 134                    
SITE     2 AC3 15 GLN A 181  ARG A 188  ARG A 221  LYS A 234                    
SITE     3 AC3 15 HIS A 237  TYR A 272  LEU A 273  TYR A 276                    
SITE     4 AC3 15 BME A 301  HOH A 556  HOH A 566                               
SITE     1 AC4  6 VAL A 195  CYS A 202  TRP A 206  HIS A 237                    
SITE     2 AC4  6 BME A 303  OKA A 501                                          
SITE     1 AC5  3 ILE A 169  LEU A 289  CYS A 291                               
SITE     1 AC6  5 ARG A 122  CYS A 127  VAL A 195  TRP A 206                    
SITE     2 AC6  5 BME A 301                                                     
CRYST1   98.759   98.759   62.180  90.00  90.00  90.00 P 42 21 2     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      0.010126  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010126  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016082        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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