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Database: PDB
Entry: 1S70
LinkDB: 1S70
Original site: 1S70 
HEADER    HYDROLASE                               28-JAN-04   1S70              
TITLE     COMPLEX BETWEEN PROTEIN SER/THR PHOSPHATASE-1 (DELTA) AND THE MYOSIN  
TITLE    2 PHOSPHATASE TARGETING SUBUNIT 1 (MYPT1)                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE PROTEIN PHOSPHATASE PP1-BETA (OR DELTA)   
COMPND   3 CATALYTIC SUBUNIT;                                                   
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: PP-1B;                                                      
COMPND   6 EC: 3.1.3.16;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: 130 KDA MYOSIN-BINDING SUBUNIT OF SMOOTH MUSCLE MYOSIN     
COMPND  11 PHOPHATASE (M130);                                                   
COMPND  12 CHAIN: B;                                                            
COMPND  13 FRAGMENT: N-TERMINAL AA 1 TO 299;                                    
COMPND  14 EC: 3.1.3.53;                                                        
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PPP1CB;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PTYB12 IMPACT;                            
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE  12 ORGANISM_COMMON: CHICKEN;                                            
SOURCE  13 ORGANISM_TAXID: 9031;                                                
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  17 EXPRESSION_SYSTEM_PLASMID: PACYC184-T7                               
KEYWDS    MYOSIN PHOSPHATASE, MYPT1, PP1, MYOSIN REGULATION, DEPOSPHORYLATION,  
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.KERFF,M.TERRAK,R.DOMINGUEZ                                          
REVDAT   8   23-AUG-23 1S70    1       REMARK                                   
REVDAT   7   27-OCT-21 1S70    1       REMARK SEQADV LINK                       
REVDAT   6   24-FEB-09 1S70    1       VERSN                                    
REVDAT   5   05-DEC-06 1S70    1       REMARK                                   
REVDAT   4   02-AUG-05 1S70    1       AUTHOR KEYWDS                            
REVDAT   3   25-JAN-05 1S70    1       AUTHOR KEYWDS REMARK                     
REVDAT   2   20-JUL-04 1S70    1       AUTHOR                                   
REVDAT   1   22-JUN-04 1S70    0                                                
JRNL        AUTH   M.TERRAK,F.KERFF,K.LANGSETMO,T.TAO,R.DOMINGUEZ               
JRNL        TITL   STRUCTURAL BASIS OF PROTEIN PHOSPHATASE 1 REGULATION         
JRNL        REF    NATURE                        V. 429   780 2004              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   15164081                                                     
JRNL        DOI    10.1038/NATURE02582                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.67                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2713055.140                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 18135                          
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) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.293                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 927                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 5                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.91                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 63.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2302                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3930                       
REMARK   3   BIN FREE R VALUE                    : 0.4210                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 6.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 151                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.034                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4743                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 227                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 59.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 78.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -23.22000                                            
REMARK   3    B22 (A**2) : -23.22000                                            
REMARK   3    B33 (A**2) : 46.44000                                             
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) : 0.42                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.79                            
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) : 0.59                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.84                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.770                           
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) : 5.020 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 7.420 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 7.260 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 9.670 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 81.20                                                
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  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : PEG.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : PEG.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1S70 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000021446.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-AUG-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : BENT GE(111) MONOCHROMATOR         
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18135                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.1                               
REMARK 200  DATA REDUNDANCY                : 13.60                              
REMARK 200  R MERGE                    (I) : 0.09300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.91                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 65.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: 1FJM FOR MOLECULE 1 AND 3 ANKYRIN REPEATS FROM       
REMARK 200  1IHB FOR MOLECULE 2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 5000 MONOMETHYLETHER, GLYCEROL,      
REMARK 280  NH4CL, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
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   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      120.87650            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       37.59400            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       37.59400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      181.31475            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       37.59400            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       37.59400            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       60.43825            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       37.59400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       37.59400            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      181.31475            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       37.59400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       37.59400            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       60.43825            
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      120.87650            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5740 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     LEU A   310                                                      
REMARK 465     ASN A   311                                                      
REMARK 465     SER A   312                                                      
REMARK 465     GLY A   313                                                      
REMARK 465     ARG A   314                                                      
REMARK 465     PRO A   315                                                      
REMARK 465     VAL A   316                                                      
REMARK 465     THR A   317                                                      
REMARK 465     PRO A   318                                                      
REMARK 465     PRO A   319                                                      
REMARK 465     ARG A   320                                                      
REMARK 465     THR A   321                                                      
REMARK 465     ALA A   322                                                      
REMARK 465     ASN A   323                                                      
REMARK 465     PRO A   324                                                      
REMARK 465     PRO A   325                                                      
REMARK 465     LYS A   326                                                      
REMARK 465     LYS A   327                                                      
REMARK 465     ARG A   328                                                      
REMARK 465     SER B   292                                                      
REMARK 465     GLU B   293                                                      
REMARK 465     LYS B   294                                                      
REMARK 465     ARG B   295                                                      
REMARK 465     GLU B   296                                                      
REMARK 465     LYS B   297                                                      
REMARK 465     LYS B   298                                                      
REMARK 465     SER B   299                                                      
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 B   391     O    HOH B   391     7466     1.92            
REMARK 500   O    HOH B   320     O    HOH B   320     8665     2.10            
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    PRO B  26   C   -  N   -  CA  ANGL. DEV. =  15.0 DEGREES          
REMARK 500    PRO B  26   C   -  N   -  CD  ANGL. DEV. = -13.4 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    MET A   2      149.68    -23.21                                   
REMARK 500    ALA A   3     -141.91     85.93                                   
REMARK 500    ASP A   4     -170.97     60.45                                   
REMARK 500    ASP A  92       71.43     52.91                                   
REMARK 500    ASP A  95      148.71     72.74                                   
REMARK 500    ARG A  96      -72.08     74.82                                   
REMARK 500    GLU A 126       41.88   -108.17                                   
REMARK 500    PHE A 144     -111.61   -147.98                                   
REMARK 500    ASP A 166       27.98     41.37                                   
REMARK 500    CYS A 172      147.29   -171.67                                   
REMARK 500    PRO A 178        4.52    -66.93                                   
REMARK 500    ARG A 188       32.45    -87.02                                   
REMARK 500    SER A 207      161.41    -35.63                                   
REMARK 500    SER A 224     -159.61     52.53                                   
REMARK 500    PHE A 225     -150.47   -127.98                                   
REMARK 500    ALA A 247     -124.06   -128.79                                   
REMARK 500    HIS A 248      -34.62     77.26                                   
REMARK 500    LYS A 260       60.27     69.84                                   
REMARK 500    ARG A 261       18.40     57.01                                   
REMARK 500    MET A 282      117.13   -167.59                                   
REMARK 500    LEU A 289       27.95     86.32                                   
REMARK 500    GLU A 300       17.34     54.40                                   
REMARK 500    LYS A 301       62.47   -106.11                                   
REMARK 500    ASP B   5      -90.32    -36.99                                   
REMARK 500    GLU B  12       16.41    -60.00                                   
REMARK 500    SER B  20     -179.24    -53.37                                   
REMARK 500    GLU B  21       50.67    -68.76                                   
REMARK 500    LEU B  24      108.46    -56.12                                   
REMARK 500    GLU B  25      102.94    -26.31                                   
REMARK 500    PRO B  26       25.44    -68.80                                   
REMARK 500    PRO B  27     -104.26    -94.80                                   
REMARK 500    VAL B  28      -46.65   -134.90                                   
REMARK 500    LYS B  30       91.74    -40.02                                   
REMARK 500    LYS B  32       28.19    -79.06                                   
REMARK 500    ASP B  52       65.92    -68.85                                   
REMARK 500    ASN B  67       46.37    -89.14                                   
REMARK 500    ASN B  70     -171.11    -63.73                                   
REMARK 500    ASN B 104        6.57    -64.62                                   
REMARK 500    ASN B 186      -76.08    -56.43                                   
REMARK 500    ARG B 194      133.87    -38.38                                   
REMARK 500    ALA B 196      -38.63    -27.88                                   
REMARK 500    LYS B 197      -79.92    -84.61                                   
REMARK 500    ASP B 224      105.76    -44.31                                   
REMARK 500    PRO B 235       -3.41    -57.22                                   
REMARK 500    GLU B 245      -73.90    -38.41                                   
REMARK 500    ASP B 257       93.83    -57.88                                   
REMARK 500    ASP B 270      -73.81    -60.69                                   
REMARK 500    ALA B 272       27.54    -73.27                                   
REMARK 500    ASP B 273      -27.95    -23.35                                   
REMARK 500    ASP B 275      -89.09     20.09                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      55 RAMACHANDRAN OUTLIERS.                        
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 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  64   OD1                                                    
REMARK 620 2 HIS A  66   NE2  77.1                                              
REMARK 620 3 ASP A  92   OD2  72.2  77.5                                        
REMARK 620 N                    1     2                                         
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  88.9                                              
REMARK 620 3 HIS A 173   NE2  81.8  69.0                                        
REMARK 620 4 HIS A 248   ND1 158.2  88.2  77.0                                  
REMARK 620 N                    1     2     3                                   
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                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 331                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FJM   RELATED DB: PDB                                   
REMARK 900 PROTEIN SER/THR PHOSPHATASE-1 (ALPHA) COMPLEXED WITH MICROCYSTIN-LR  
REMARK 900 TOXIN                                                                
REMARK 900 RELATED ID: 1IT6   RELATED DB: PDB                                   
REMARK 900 PROTEIN SER/THR PHOSPHATASE-1 (GAMMA) COMPLEXED WITH CALICULIN A     
REMARK 900 RELATED ID: 1JK7   RELATED DB: PDB                                   
REMARK 900 PROTEIN SER/THR PHOSPHATASE-1 (GAMMA) COMPLEXED WITH THE TUMOR-      
REMARK 900 PROMOTER OKADAIC ACID                                                
DBREF  1S70 A    2   328  UNP    P62140   PP1B_HUMAN       1    327             
DBREF  1S70 B    1   299  UNP    Q90624   Q90624_CHICK     1    299             
SEQADV 1S70 ALA A   -1  UNP  P62140              ENGINEERED MUTATION            
SEQADV 1S70 GLY A    0  UNP  P62140              ENGINEERED MUTATION            
SEQADV 1S70 HIS A    1  UNP  P62140              ENGINEERED MUTATION            
SEQRES   1 A  330  ALA GLY HIS MET ALA ASP GLY GLU LEU ASN VAL ASP SER          
SEQRES   2 A  330  LEU ILE THR ARG LEU LEU GLU VAL ARG GLY CYS ARG PRO          
SEQRES   3 A  330  GLY LYS ILE VAL GLN MET THR GLU ALA GLU VAL ARG GLY          
SEQRES   4 A  330  LEU CYS ILE LYS SER ARG GLU ILE PHE LEU SER GLN PRO          
SEQRES   5 A  330  ILE LEU LEU GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY          
SEQRES   6 A  330  ASP ILE HIS GLY GLN TYR THR ASP LEU LEU ARG LEU PHE          
SEQRES   7 A  330  GLU TYR GLY GLY PHE PRO PRO GLU ALA ASN TYR LEU PHE          
SEQRES   8 A  330  LEU GLY ASP TYR VAL ASP ARG GLY LYS GLN SER LEU GLU          
SEQRES   9 A  330  THR ILE CYS LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO          
SEQRES  10 A  330  GLU ASN PHE PHE LEU LEU ARG GLY ASN HIS GLU CYS ALA          
SEQRES  11 A  330  SER ILE ASN ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS          
SEQRES  12 A  330  ARG ARG PHE ASN ILE LYS LEU TRP LYS THR PHE THR ASP          
SEQRES  13 A  330  CYS PHE ASN CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU          
SEQRES  14 A  330  LYS ILE PHE CYS CYS HIS GLY GLY LEU SER PRO ASP LEU          
SEQRES  15 A  330  GLN SER MET GLU GLN ILE ARG ARG ILE MET ARG PRO THR          
SEQRES  16 A  330  ASP VAL PRO ASP THR GLY LEU LEU CYS ASP LEU LEU TRP          
SEQRES  17 A  330  SER ASP PRO ASP LYS ASP VAL GLN GLY TRP GLY GLU ASN          
SEQRES  18 A  330  ASP ARG GLY VAL SER PHE THR PHE GLY ALA ASP VAL VAL          
SEQRES  19 A  330  SER LYS PHE LEU ASN ARG HIS ASP LEU ASP LEU ILE CYS          
SEQRES  20 A  330  ARG ALA HIS GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE          
SEQRES  21 A  330  ALA LYS ARG GLN LEU VAL THR LEU PHE SER ALA PRO ASN          
SEQRES  22 A  330  TYR CYS GLY GLU PHE ASP ASN ALA GLY GLY MET MET SER          
SEQRES  23 A  330  VAL ASP GLU THR LEU MET CYS SER PHE GLN ILE LEU LYS          
SEQRES  24 A  330  PRO SER GLU LYS LYS ALA LYS TYR GLN TYR GLY GLY LEU          
SEQRES  25 A  330  ASN SER GLY ARG PRO VAL THR PRO PRO ARG THR ALA ASN          
SEQRES  26 A  330  PRO PRO LYS LYS ARG                                          
SEQRES   1 B  299  MET LYS MET ALA ASP ALA LYS GLN LYS ARG ASN GLU GLN          
SEQRES   2 B  299  LEU LYS ARG TRP ILE GLY SER GLU THR ASP LEU GLU PRO          
SEQRES   3 B  299  PRO VAL VAL LYS ARG LYS LYS THR LYS VAL LYS PHE ASP          
SEQRES   4 B  299  ASP GLY ALA VAL PHE LEU ALA ALA CYS SER SER GLY ASP          
SEQRES   5 B  299  THR GLU GLU VAL LEU ARG LEU LEU GLU ARG GLY ALA ASP          
SEQRES   6 B  299  ILE ASN TYR ALA ASN VAL ASP GLY LEU THR ALA LEU HIS          
SEQRES   7 B  299  GLN ALA CYS ILE ASP ASP ASN VAL ASP MET VAL LYS PHE          
SEQRES   8 B  299  LEU VAL GLU ASN GLY ALA ASN ILE ASN GLN PRO ASP ASN          
SEQRES   9 B  299  GLU GLY TRP ILE PRO LEU HIS ALA ALA ALA SER CYS GLY          
SEQRES  10 B  299  TYR LEU ASP ILE ALA GLU TYR LEU ILE SER GLN GLY ALA          
SEQRES  11 B  299  HIS VAL GLY ALA VAL ASN SER GLU GLY ASP THR PRO LEU          
SEQRES  12 B  299  ASP ILE ALA GLU GLU GLU ALA MET GLU GLU LEU LEU GLN          
SEQRES  13 B  299  ASN GLU VAL ASN ARG GLN GLY VAL ASP ILE GLU ALA ALA          
SEQRES  14 B  299  ARG LYS GLU GLU GLU ARG ILE MET LEU ARG ASP ALA ARG          
SEQRES  15 B  299  GLN TRP LEU ASN SER GLY HIS ILE ASN ASP VAL ARG HIS          
SEQRES  16 B  299  ALA LYS SER GLY GLY THR ALA LEU HIS VAL ALA ALA ALA          
SEQRES  17 B  299  LYS GLY TYR THR GLU VAL LEU LYS LEU LEU ILE GLN ALA          
SEQRES  18 B  299  ARG TYR ASP VAL ASN ILE LYS ASP TYR ASP GLY TRP THR          
SEQRES  19 B  299  PRO LEU HIS ALA ALA ALA HIS TRP GLY LYS GLU GLU ALA          
SEQRES  20 B  299  CYS ARG ILE LEU VAL GLU ASN LEU CYS ASP MET GLU ALA          
SEQRES  21 B  299  VAL ASN LYS VAL GLY GLN THR ALA PHE ASP VAL ALA ASP          
SEQRES  22 B  299  GLU ASP ILE LEU GLY TYR LEU GLU GLU LEU GLN LYS LYS          
SEQRES  23 B  299  GLN ASN LEU LEU HIS SER GLU LYS ARG GLU LYS LYS SER          
HET     MN  A 400       1                                                       
HET     MN  A 401       1                                                       
HET    PGE  A 331      10                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     PGE TRIETHYLENE GLYCOL                                               
FORMUL   3   MN    2(MN 2+)                                                     
FORMUL   5  PGE    C6 H14 O4                                                    
FORMUL   6  HOH   *227(H2 O)                                                    
HELIX    1   1 ASN A    8  GLU A   18  1                                  11    
HELIX    2   2 THR A   31  LEU A   47  1                                  17    
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  PHE A  144  1                                  10    
HELIX    7   7 ASN A  145  ASN A  157  1                                  13    
HELIX    8   8 MET A  183  ARG A  188  1                                   6    
HELIX    9   9 GLY A  199  SER A  207  1                                   9    
HELIX   10  10 GLY A  228  ASP A  240  1                                  13    
HELIX   11  11 ASN A  271  GLU A  275  5                                   5    
HELIX   12  12 MET B    3  SER B   20  1                                  18    
HELIX   13  13 ASP B   39  GLY B   51  1                                  13    
HELIX   14  14 ASP B   52  GLY B   63  1                                  12    
HELIX   15  15 THR B   75  ASP B   83  1                                   9    
HELIX   16  16 ASN B   85  ASN B   95  1                                  11    
HELIX   17  17 ILE B  108  GLY B  117  1                                  10    
HELIX   18  18 TYR B  118  GLN B  128  1                                  11    
HELIX   19  19 THR B  141  ALA B  146  1                                   6    
HELIX   20  20 GLU B  148  GLY B  163  1                                  16    
HELIX   21  21 ASP B  165  GLY B  188  1                                  24    
HELIX   22  22 THR B  201  GLY B  210  1                                  10    
HELIX   23  23 TYR B  211  GLN B  220  1                                  10    
HELIX   24  24 THR B  234  TRP B  242  1                                   9    
HELIX   25  25 LYS B  244  ASN B  254  1                                  11    
HELIX   26  26 GLU B  274  ILE B  276  5                                   3    
HELIX   27  27 LEU B  277  GLN B  287  1                                  11    
SHEET    1   A 6 LEU A  52  LEU A  55  0                                        
SHEET    2   A 6 ALA A 162  VAL A 165  1  O  ALA A 162   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  LEU A 243   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  PHE A 258   O  LEU A 263           
SHEET    1   B 6 PHE A 118  LEU A 120  0                                        
SHEET    2   B 6 TYR A  87  PHE A  89  1  N  PHE A  89   O  PHE A 119           
SHEET    3   B 6 LEU A  59  CYS A  62  1  N  CYS A  62   O  LEU A  88           
SHEET    4   B 6 MET A 283  VAL A 285 -1  O  VAL A 285   N  LEU A  59           
SHEET    5   B 6 MET A 290  PHE A 293 -1  O  SER A 292   N  SER A 284           
SHEET    6   B 6 LYS B  37  PHE B  38  1  O  LYS B  37   N  CYS A 291           
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         OD1 ASP A  64                MN    MN A 401     1555   1555  2.46  
LINK         NE2 HIS A  66                MN    MN A 401     1555   1555  2.54  
LINK         OD2 ASP A  92                MN    MN A 400     1555   1555  2.37  
LINK         OD2 ASP A  92                MN    MN A 401     1555   1555  2.34  
LINK         OD1 ASN A 124                MN    MN A 400     1555   1555  2.15  
LINK         NE2 HIS A 173                MN    MN A 400     1555   1555  2.28  
LINK         ND1 HIS A 248                MN    MN A 400     1555   1555  2.24  
CISPEP   1 ALA A   57    PRO A   58          0        -0.25                     
CISPEP   2 PRO A   82    PRO A   83          0         0.05                     
CISPEP   3 ARG A  191    PRO A  192          0         0.17                     
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 415                                          
SITE     1 AC2  5 ASP A  64  HIS A  66  ASP A  92   MN A 400                    
SITE     2 AC2  5 HOH A 415                                                     
SITE     1 AC3 10 VAL A  19  GLY A  21  CYS A  22  PRO A  24                    
SITE     2 AC3 10 GLY A  25  LYS A  26  THR A  70  GLU A  77                    
SITE     3 AC3 10 GLN A  99  VAL B 264                                          
CRYST1   75.188   75.188  241.753  90.00  90.00  90.00 P 43 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      0.013300  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013300  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004136        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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