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Database: PDB
Entry: 4MP0
LinkDB: 4MP0
Original site: 4MP0 
HEADER    HYDROLASE                               12-SEP-13   4MP0              
TITLE     STRUCTURE OF A SECOND NUCLEAR PP1 HOLOENZYME, CRYSTAL FORM 2          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-ALPHA CATALYTIC   
COMPND   3 SUBUNIT;                                                             
COMPND   4 CHAIN: A, C;                                                         
COMPND   5 FRAGMENT: PP1 ALPHA CATALYTIC SUBUNIT;                               
COMPND   6 SYNONYM: PP-1A;                                                      
COMPND   7 EC: 3.1.3.16;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT  
COMPND  11 10;                                                                  
COMPND  12 CHAIN: B, D;                                                         
COMPND  13 FRAGMENT: PP1 NUCLEAR TARGETING SUBUNIT;                             
COMPND  14 SYNONYM: MHC CLASS I REGION PROLINE-RICH PROTEIN CAT53, PHOSPHATASE 1
COMPND  15 NUCLEAR TARGETING SUBUNIT, PROTEIN PNUTS;                            
COMPND  16 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: PPP1CA, PPP1A;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  10 ORGANISM_COMMON: BROWN RAT,RAT,RATS;                                 
SOURCE  11 ORGANISM_TAXID: 10116;                                               
SOURCE  12 GENE: PPP1R10, CAT53, PNUTS;                                         
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SERINE/THREONINE PHOSPHATASE, NUCLEUS, HYDROLASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.S.CHOY,M.HIEKE,W.PETI,R.PAGE                                        
REVDAT   2   23-APR-14 4MP0    1       JRNL                                     
REVDAT   1   26-MAR-14 4MP0    0                                                
JRNL        AUTH   M.S.CHOY,M.HIEKE,G.S.KUMAR,G.R.LEWIS,K.R.GONZALEZ-DEWHITT,   
JRNL        AUTH 2 R.P.KESSLER,B.J.STEIN,M.HESSENBERGER,A.C.NAIRN,W.PETI,R.PAGE 
JRNL        TITL   UNDERSTANDING THE ANTAGONISM OF RETINOBLASTOMA PROTEIN       
JRNL        TITL 2 DEPHOSPHORYLATION BY PNUTS PROVIDES INSIGHTS INTO THE PP1    
JRNL        TITL 3 REGULATORY CODE.                                             
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 111  4097 2014              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   24591642                                                     
JRNL        DOI    10.1073/PNAS.1317395111                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.84                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.370                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 51197                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.202                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2578                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.8495 -  5.5019    1.00     2963   150  0.1883 0.2291        
REMARK   3     2  5.5019 -  4.3678    1.00     2790   150  0.1539 0.1800        
REMARK   3     3  4.3678 -  3.8160    1.00     2755   153  0.1471 0.1573        
REMARK   3     4  3.8160 -  3.4672    1.00     2716   148  0.1736 0.2028        
REMARK   3     5  3.4672 -  3.2187    1.00     2720   145  0.1732 0.2198        
REMARK   3     6  3.2187 -  3.0289    1.00     2698   142  0.1883 0.1859        
REMARK   3     7  3.0289 -  2.8773    1.00     2682   145  0.1695 0.2237        
REMARK   3     8  2.8773 -  2.7520    1.00     2701   135  0.1783 0.2072        
REMARK   3     9  2.7520 -  2.6461    1.00     2685   128  0.1696 0.1923        
REMARK   3    10  2.6461 -  2.5548    1.00     2667   159  0.1721 0.2017        
REMARK   3    11  2.5548 -  2.4749    1.00     2663   140  0.1705 0.2013        
REMARK   3    12  2.4749 -  2.4042    1.00     2660   157  0.1672 0.2097        
REMARK   3    13  2.4042 -  2.3409    1.00     2648   144  0.1733 0.1921        
REMARK   3    14  2.3409 -  2.2838    1.00     2666   137  0.1772 0.2196        
REMARK   3    15  2.2838 -  2.2318    1.00     2676   136  0.1859 0.2356        
REMARK   3    16  2.2318 -  2.1844    1.00     2652   138  0.1904 0.2338        
REMARK   3    17  2.1844 -  2.1407    1.00     2635   132  0.1962 0.2336        
REMARK   3    18  2.1407 -  2.1003    0.99     2642   139  0.2173 0.2648        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.490           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           5233                                  
REMARK   3   ANGLE     :  0.807           7133                                  
REMARK   3   CHIRALITY :  0.030            775                                  
REMARK   3   PLANARITY :  0.002            919                                  
REMARK   3   DIHEDRAL  : 12.065           1874                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 6 through 300 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  85.6666  28.3993  83.0188              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1125 T22:   0.2417                                     
REMARK   3      T33:   0.2513 T12:  -0.0007                                     
REMARK   3      T13:  -0.0150 T23:  -0.0158                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9795 L22:   1.3991                                     
REMARK   3      L33:   2.4075 L12:   0.0830                                     
REMARK   3      L13:  -0.0534 L23:   0.4662                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0047 S12:  -0.0094 S13:  -0.0764                       
REMARK   3      S21:   0.0264 S22:  -0.0370 S23:  -0.0117                       
REMARK   3      S31:   0.0622 S32:  -0.1356 S33:   0.0242                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'C' and (resid 7 through 297 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  94.9350  65.3926  78.3415              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7849 T22:   0.4118                                     
REMARK   3      T33:   0.3183 T12:  -0.2907                                     
REMARK   3      T13:  -0.0866 T23:  -0.0310                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1327 L22:   0.8089                                     
REMARK   3      L33:   2.5536 L12:  -0.0605                                     
REMARK   3      L13:   0.1097 L23:  -0.0085                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0944 S12:  -0.1189 S13:   0.2295                       
REMARK   3      S21:   0.1659 S22:  -0.0773 S23:  -0.0678                       
REMARK   3      S31:  -1.3104 S32:   0.8582 S33:  -0.0163                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'B' and (resid 396 through 425 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  72.2387  23.0830  77.8746              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1910 T22:   0.4909                                     
REMARK   3      T33:   0.5351 T12:  -0.0581                                     
REMARK   3      T13:  -0.0545 T23:  -0.1180                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3721 L22:   1.9529                                     
REMARK   3      L33:   1.4960 L12:  -0.3411                                     
REMARK   3      L13:  -0.1447 L23:   0.0500                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0258 S12:   0.0407 S13:   0.4910                       
REMARK   3      S21:   0.0169 S22:  -0.0562 S23:   0.0571                       
REMARK   3      S31:  -0.1280 S32:  -0.5125 S33:   0.0170                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'D' and (resid 397 through 424 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  84.1738  76.1618  82.8135              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6016 T22:   0.6166                                     
REMARK   3      T33:   0.9249 T12:   0.1051                                     
REMARK   3      T13:  -0.1840 T23:  -0.2131                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5503 L22:   0.1195                                     
REMARK   3      L33:   0.6593 L12:  -0.0082                                     
REMARK   3      L13:  -0.6301 L23:   0.0279                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0382 S12:  -0.1014 S13:   0.0706                       
REMARK   3      S21:   0.2470 S22:  -0.1287 S23:   0.3335                       
REMARK   3      S31:  -0.9150 S32:  -0.0177 S33:   0.0326                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 2                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: NULL                                        
REMARK   3     SELECTION          : NULL                                        
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4MP0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB082185.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51308                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: MIR                          
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.47                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2% V/V TACSIMATE, 0.1 M TRIS, 16% W/V    
REMARK 280  POLYETHYLENE GLYCOL 3,350, PH 8.5, VAPOR DIFFUSION, SITTING DROP,   
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
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       99.67100            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       46.20350            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       46.20350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       49.83550            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       46.20350            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       46.20350            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      149.50650            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       46.20350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       46.20350            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       49.83550            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       46.20350            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       46.20350            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      149.50650            
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       99.67100            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 4190 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 3110 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 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     GLY A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     MET A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     HIS C     3                                                      
REMARK 465     MET C     4                                                      
REMARK 465     GLY C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     PRO C   298                                                      
REMARK 465     ALA C   299                                                      
REMARK 465     ASP C   300                                                      
REMARK 465     GLY B   390                                                      
REMARK 465     ALA B   391                                                      
REMARK 465     MET B   392                                                      
REMARK 465     GLY B   393                                                      
REMARK 465     ARG B   394                                                      
REMARK 465     LYS B   395                                                      
REMARK 465     ILE B   426                                                      
REMARK 465     LYS B   427                                                      
REMARK 465     ASP B   428                                                      
REMARK 465     PHE B   429                                                      
REMARK 465     GLY B   430                                                      
REMARK 465     GLU B   431                                                      
REMARK 465     ALA B   432                                                      
REMARK 465     ALA B   433                                                      
REMARK 465     GLY D   390                                                      
REMARK 465     ALA D   391                                                      
REMARK 465     MET D   392                                                      
REMARK 465     GLY D   393                                                      
REMARK 465     ARG D   394                                                      
REMARK 465     LYS D   395                                                      
REMARK 465     ARG D   396                                                      
REMARK 465     LYS D   425                                                      
REMARK 465     ILE D   426                                                      
REMARK 465     LYS D   427                                                      
REMARK 465     ASP D   428                                                      
REMARK 465     PHE D   429                                                      
REMARK 465     GLY D   430                                                      
REMARK 465     GLU D   431                                                      
REMARK 465     ALA D   432                                                      
REMARK 465     ALA D   433                                                      
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  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  26    CE   NZ                                             
REMARK 470     LYS A  41    CG   CD   CE   NZ                                   
REMARK 470     GLU A  54    CD   OE1  OE2                                       
REMARK 470     GLU A  84    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 147    CD   CE   NZ                                        
REMARK 470     LYS A 211    CG   CD   CE   NZ                                   
REMARK 470     GLN A 214    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 230    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 260    CD   CE   NZ                                        
REMARK 470     ASP A 277    CG   OD1  OD2                                       
REMARK 470     GLU A 287    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  18    CD   OE1  OE2                                       
REMARK 470     ARG C  23    NE   CZ   NH1  NH2                                  
REMARK 470     LYS C  26    CD   CE   NZ                                        
REMARK 470     LYS C  41    CG   CD   CE   NZ                                   
REMARK 470     GLU C  54    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  56    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  77    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  98    CG   CD   CE   NZ                                   
REMARK 470     LYS C 147    CG   CD   CE   NZ                                   
REMARK 470     GLU C 167    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 168    CG   CD   CE   NZ                                   
REMARK 470     ARG C 188    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 198    CD   OE1  NE2                                       
REMARK 470     LYS C 211    CD   CE   NZ                                        
REMARK 470     GLN C 214    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 230    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 234    CD   CE   NZ                                        
REMARK 470     GLU C 252    CD   OE1  OE2                                       
REMARK 470     LYS C 260    CG   CD   CE   NZ                                   
REMARK 470     ASP C 277    CG   OD1  OD2                                       
REMARK 470     GLU C 287    CG   CD   OE1  OE2                                  
REMARK 470     MET C 290    CG   SD   CE                                        
REMARK 470     LEU C 296    CG   CD1  CD2                                       
REMARK 470     LYS C 297    CG   CD   CE   NZ                                   
REMARK 470     GLU B 403    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 406    CE   NZ                                             
REMARK 470     GLU B 414    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 417    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 425    CG   CD   CE   NZ                                   
REMARK 470     LYS D 397    CG   CD   CE   NZ                                   
REMARK 470     GLU D 403    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 404    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 406    CG   CD   CE   NZ                                   
REMARK 470     ARG D 408    NE   CZ   NH1  NH2                                  
REMARK 470     TYR D 412    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU D 414    CG   CD   OE1  OE2                                  
REMARK 470     ASP D 416    CG   OD1  OD2                                       
REMARK 470     GLU D 417    CG   CD   OE1  OE2                                  
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      152.31     81.52                                   
REMARK 500    ARG A  96      -49.53     69.77                                   
REMARK 500    TYR A 144     -109.54   -138.22                                   
REMARK 500    SER A 224     -151.27     62.62                                   
REMARK 500    ALA A 247     -125.29   -133.02                                   
REMARK 500    HIS A 248      -17.46     74.84                                   
REMARK 500    ASP C  95      152.48     80.75                                   
REMARK 500    ARG C  96      -49.69     69.75                                   
REMARK 500    TYR C 144     -109.61   -138.68                                   
REMARK 500    LYS C 168      -32.27   -130.03                                   
REMARK 500    SER C 224     -150.99     62.51                                   
REMARK 500    ALA C 247     -124.98   -133.09                                   
REMARK 500    HIS C 248      -18.15     74.03                                   
REMARK 500    CYS C 273       34.80     39.84                                   
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 C 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PO4 C 403   O2                                                     
REMARK 620 2 ASP C  64   OD2 155.3                                              
REMARK 620 3 ASP C  92   OD2  94.5  91.6                                        
REMARK 620 4 HIS C  66   NE2  92.8 109.8  99.5                                  
REMARK 620 5 HOH C 566   O    72.4  84.7  82.5 165.2                            
REMARK 620 6 HOH C 567   O    77.6  95.0 172.0  82.6  93.5                      
REMARK 620 N                    1     2     3     4     5                       
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 PO4 A 405   O4                                                     
REMARK 620 2 ASP A  64   OD2 161.2                                              
REMARK 620 3 ASP A  92   OD2  93.7  89.7                                        
REMARK 620 4 HIS A  66   NE2  93.3 104.5  98.1                                  
REMARK 620 5 HOH A 642   O    72.8  89.4  82.5 166.1                            
REMARK 620 6 HOH A 538   O    82.6  92.6 174.7  85.9  92.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 173   NE2                                                    
REMARK 620 2 ASN A 124   OD1  83.4                                              
REMARK 620 3 ASP A  92   OD2  86.9  97.5                                        
REMARK 620 4 PO4 A 405   O3  167.8  85.5  99.6                                  
REMARK 620 5 HIS A 248   ND1  85.3 102.0 158.0  92.1                            
REMARK 620 6 HOH A 642   O   116.1 160.3  81.7  75.3  83.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C 124   OD1                                                    
REMARK 620 2 HIS C 173   NE2  81.0                                              
REMARK 620 3 ASP C  92   OD2  93.0  86.3                                        
REMARK 620 4 PO4 C 403   O1   85.1 166.0  96.0                                  
REMARK 620 5 HIS C 248   ND1  99.6  89.3 165.9  91.5                            
REMARK 620 6 HOH C 566   O   160.4 117.3  81.8  76.8  88.3                      
REMARK 620 N                    1     2     3     4     5                       
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 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 403                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3V4Y   RELATED DB: PDB                                   
REMARK 900 NIPP1:PP1 HOLOENZYME                                                 
REMARK 900 RELATED ID: 4MOY   RELATED DB: PDB                                   
REMARK 900 PNUTS:PP1 HOLOENZYME, CRYSTAL FORM 1                                 
DBREF  4MP0 A    7   300  UNP    P62136   PP1A_HUMAN       7    300             
DBREF  4MP0 C    7   300  UNP    P62136   PP1A_HUMAN       7    300             
DBREF  4MP0 B  394   433  UNP    O55000   PP1RA_RAT      394    433             
DBREF  4MP0 D  394   433  UNP    O55000   PP1RA_RAT      394    433             
SEQADV 4MP0 GLY A    2  UNP  P62136              EXPRESSION TAG                 
SEQADV 4MP0 HIS A    3  UNP  P62136              EXPRESSION TAG                 
SEQADV 4MP0 MET A    4  UNP  P62136              EXPRESSION TAG                 
SEQADV 4MP0 GLY A    5  UNP  P62136              EXPRESSION TAG                 
SEQADV 4MP0 SER A    6  UNP  P62136              EXPRESSION TAG                 
SEQADV 4MP0 GLY C    2  UNP  P62136              EXPRESSION TAG                 
SEQADV 4MP0 HIS C    3  UNP  P62136              EXPRESSION TAG                 
SEQADV 4MP0 MET C    4  UNP  P62136              EXPRESSION TAG                 
SEQADV 4MP0 GLY C    5  UNP  P62136              EXPRESSION TAG                 
SEQADV 4MP0 SER C    6  UNP  P62136              EXPRESSION TAG                 
SEQADV 4MP0 GLY B  390  UNP  O55000              EXPRESSION TAG                 
SEQADV 4MP0 ALA B  391  UNP  O55000              EXPRESSION TAG                 
SEQADV 4MP0 MET B  392  UNP  O55000              EXPRESSION TAG                 
SEQADV 4MP0 GLY B  393  UNP  O55000              EXPRESSION TAG                 
SEQADV 4MP0 GLY D  390  UNP  O55000              EXPRESSION TAG                 
SEQADV 4MP0 ALA D  391  UNP  O55000              EXPRESSION TAG                 
SEQADV 4MP0 MET D  392  UNP  O55000              EXPRESSION TAG                 
SEQADV 4MP0 GLY D  393  UNP  O55000              EXPRESSION TAG                 
SEQRES   1 A  299  GLY HIS MET GLY SER LEU ASN LEU ASP SER ILE ILE GLY          
SEQRES   2 A  299  ARG LEU LEU GLU VAL GLN GLY SER ARG PRO GLY LYS ASN          
SEQRES   3 A  299  VAL GLN LEU THR GLU ASN GLU ILE ARG GLY LEU CYS LEU          
SEQRES   4 A  299  LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU LEU          
SEQRES   5 A  299  GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE HIS          
SEQRES   6 A  299  GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR GLY          
SEQRES   7 A  299  GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY ASP          
SEQRES   8 A  299  TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE CYS          
SEQRES   9 A  299  LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN PHE          
SEQRES  10 A  299  PHE LEU LEU ARG GLY ASN HIS GLU CYS ALA SER ILE ASN          
SEQRES  11 A  299  ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG TYR          
SEQRES  12 A  299  ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE ASN          
SEQRES  13 A  299  CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE PHE          
SEQRES  14 A  299  CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER MET          
SEQRES  15 A  299  GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL PRO          
SEQRES  16 A  299  ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP PRO          
SEQRES  17 A  299  ASP LYS ASP VAL GLN GLY TRP GLY GLU ASN ASP ARG GLY          
SEQRES  18 A  299  VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS PHE          
SEQRES  19 A  299  LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA HIS          
SEQRES  20 A  299  GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS ARG          
SEQRES  21 A  299  GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CYS GLY          
SEQRES  22 A  299  GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP GLU          
SEQRES  23 A  299  THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA ASP          
SEQRES   1 C  299  GLY HIS MET GLY SER LEU ASN LEU ASP SER ILE ILE GLY          
SEQRES   2 C  299  ARG LEU LEU GLU VAL GLN GLY SER ARG PRO GLY LYS ASN          
SEQRES   3 C  299  VAL GLN LEU THR GLU ASN GLU ILE ARG GLY LEU CYS LEU          
SEQRES   4 C  299  LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU LEU          
SEQRES   5 C  299  GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE HIS          
SEQRES   6 C  299  GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR GLY          
SEQRES   7 C  299  GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY ASP          
SEQRES   8 C  299  TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE CYS          
SEQRES   9 C  299  LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN PHE          
SEQRES  10 C  299  PHE LEU LEU ARG GLY ASN HIS GLU CYS ALA SER ILE ASN          
SEQRES  11 C  299  ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG TYR          
SEQRES  12 C  299  ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE ASN          
SEQRES  13 C  299  CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE PHE          
SEQRES  14 C  299  CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER MET          
SEQRES  15 C  299  GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL PRO          
SEQRES  16 C  299  ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP PRO          
SEQRES  17 C  299  ASP LYS ASP VAL GLN GLY TRP GLY GLU ASN ASP ARG GLY          
SEQRES  18 C  299  VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS PHE          
SEQRES  19 C  299  LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA HIS          
SEQRES  20 C  299  GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS ARG          
SEQRES  21 C  299  GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CYS GLY          
SEQRES  22 C  299  GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP GLU          
SEQRES  23 C  299  THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA ASP          
SEQRES   1 B   44  GLY ALA MET GLY ARG LYS ARG LYS THR VAL THR TRP PRO          
SEQRES   2 B   44  GLU GLU GLY LYS LEU ARG GLU TYR PHE TYR PHE GLU LEU          
SEQRES   3 B   44  ASP GLU THR GLU ARG VAL ASN VAL ASN LYS ILE LYS ASP          
SEQRES   4 B   44  PHE GLY GLU ALA ALA                                          
SEQRES   1 D   44  GLY ALA MET GLY ARG LYS ARG LYS THR VAL THR TRP PRO          
SEQRES   2 D   44  GLU GLU GLY LYS LEU ARG GLU TYR PHE TYR PHE GLU LEU          
SEQRES   3 D   44  ASP GLU THR GLU ARG VAL ASN VAL ASN LYS ILE LYS ASP          
SEQRES   4 D   44  PHE GLY GLU ALA ALA                                          
HET     MN  A 401       1                                                       
HET     MN  A 402       1                                                       
HET    GOL  A 403       6                                                       
HET    GOL  A 404       6                                                       
HET    PO4  A 405       5                                                       
HET     MN  C 401       1                                                       
HET     MN  C 402       1                                                       
HET    PO4  C 403       5                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     GOL GLYCEROL                                                         
HETNAM     PO4 PHOSPHATE ION                                                    
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5   MN    4(MN 2+)                                                     
FORMUL   7  GOL    2(C3 H8 O3)                                                  
FORMUL   9  PO4    2(O4 P 3-)                                                   
FORMUL  13  HOH   *315(H2 O)                                                    
HELIX    1   1 ASN A    8  VAL A   19  1                                  12    
HELIX    2   2 THR 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 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  HIS A  239  1                                  12    
HELIX   11  11 ASN A  271  GLU A  275  5                                   5    
HELIX   12  12 ASN C    8  GLU C   18  1                                  11    
HELIX   13  13 THR C   31  GLN C   49  1                                  19    
HELIX   14  14 GLN C   68  GLY C   80  1                                  13    
HELIX   15  15 GLN C   99  TYR C  114  1                                  16    
HELIX   16  16 CYS C  127  ARG C  132  1                                   6    
HELIX   17  17 GLY C  135  TYR C  144  1                                  10    
HELIX   18  18 ASN C  145  ASN C  157  1                                  13    
HELIX   19  19 MET C  183  ARG C  188  1                                   6    
HELIX   20  20 GLY C  199  SER C  207  1                                   9    
HELIX   21  21 GLY C  228  HIS C  239  1                                  12    
HELIX   22  22 ASN C  271  GLU C  275  5                                   5    
HELIX   23  23 GLU B  403  LYS B  406  5                                   4    
HELIX   24  24 GLU D  403  LYS D  406  5                                   4    
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 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 GLY A 280  VAL A 285 -1  O  VAL A 285   N  LEU A  59           
SHEET    5   B 6 CYS A 291  PRO A 298 -1  O  LEU A 296   N  GLY A 280           
SHEET    6   B 6 ARG B 408  PHE B 413  1  O  GLU B 409   N  ILE A 295           
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           
SHEET    1   D 6 LEU C  52  LEU C  55  0                                        
SHEET    2   D 6 ALA C 162  VAL C 165  1  O  ILE C 164   N  LEU C  53           
SHEET    3   D 6 ILE C 169  CYS C 172 -1  O  CYS C 171   N  ALA C 163           
SHEET    4   D 6 LEU C 243  ARG C 246  1  O  CYS C 245   N  PHE C 170           
SHEET    5   D 6 LEU C 263  LEU C 266  1  O  LEU C 266   N  ARG C 246           
SHEET    6   D 6 TYR C 255  PHE C 258 -1  N  GLU C 256   O  THR C 265           
SHEET    1   E 6 PHE C 118  LEU C 120  0                                        
SHEET    2   E 6 TYR C  87  PHE C  89  1  N  PHE C  89   O  PHE C 119           
SHEET    3   E 6 LEU C  59  CYS C  62  1  N  CYS C  62   O  LEU C  88           
SHEET    4   E 6 GLY C 280  VAL C 285 -1  O  VAL C 285   N  LEU C  59           
SHEET    5   E 6 CYS C 291  LYS C 297 -1  O  LEU C 296   N  GLY C 280           
SHEET    6   E 6 ARG D 408  TYR D 412  1  O  PHE D 411   N  ILE C 295           
SHEET    1   F 3 ASP C 208  PRO C 209  0                                        
SHEET    2   F 3 PHE C 225  PHE C 227  1  O  PHE C 227   N  ASP C 208           
SHEET    3   F 3 TRP C 216  GLU C 218 -1  N  GLY C 217   O  THR C 226           
LINK        MN    MN C 401                 O2  PO4 C 403     1555   1555  2.09  
LINK        MN    MN A 401                 O4  PO4 A 405     1555   1555  2.11  
LINK         OD2 ASP A  64                MN    MN A 401     1555   1555  2.15  
LINK         OD2 ASP C  64                MN    MN C 401     1555   1555  2.16  
LINK         OD2 ASP C  92                MN    MN C 401     1555   1555  2.16  
LINK         NE2 HIS A 173                MN    MN A 402     1555   1555  2.16  
LINK         OD1 ASN C 124                MN    MN C 402     1555   1555  2.17  
LINK         OD1 ASN A 124                MN    MN A 402     1555   1555  2.17  
LINK         OD2 ASP A  92                MN    MN A 401     1555   1555  2.18  
LINK         NE2 HIS C 173                MN    MN C 402     1555   1555  2.18  
LINK         NE2 HIS A  66                MN    MN A 401     1555   1555  2.19  
LINK         OD2 ASP A  92                MN    MN A 402     1555   1555  2.19  
LINK         OD2 ASP C  92                MN    MN C 402     1555   1555  2.20  
LINK        MN    MN A 402                 O3  PO4 A 405     1555   1555  2.21  
LINK        MN    MN C 402                 O1  PO4 C 403     1555   1555  2.21  
LINK         NE2 HIS C  66                MN    MN C 401     1555   1555  2.21  
LINK         ND1 HIS A 248                MN    MN A 402     1555   1555  2.23  
LINK         ND1 HIS C 248                MN    MN C 402     1555   1555  2.29  
LINK        MN    MN A 401                 O   HOH A 642     1555   1555  2.17  
LINK        MN    MN C 402                 O   HOH C 566     1555   1555  2.18  
LINK        MN    MN C 401                 O   HOH C 566     1555   1555  2.19  
LINK        MN    MN A 402                 O   HOH A 642     1555   1555  2.19  
LINK        MN    MN C 401                 O   HOH C 567     1555   1555  2.19  
LINK        MN    MN A 401                 O   HOH A 538     1555   1555  2.19  
CISPEP   1 ARG A   23    PRO A   24          0         0.22                     
CISPEP   2 ALA A   57    PRO A   58          0         4.02                     
CISPEP   3 PRO A   82    PRO A   83          0         1.88                     
CISPEP   4 ARG A  191    PRO A  192          0         2.29                     
CISPEP   5 ALA C   57    PRO C   58          0         2.88                     
CISPEP   6 PRO C   82    PRO C   83          0         2.59                     
CISPEP   7 ARG C  191    PRO C  192          0         1.63                     
SITE     1 AC1  7 ASP A  64  HIS A  66  ASP A  92   MN A 402                    
SITE     2 AC1  7 PO4 A 405  HOH A 538  HOH A 642                               
SITE     1 AC2  7 ASP A  92  ASN A 124  HIS A 173  HIS A 248                    
SITE     2 AC2  7  MN A 401  PO4 A 405  HOH A 642                               
SITE     1 AC3  5 PRO A  50  LEU A  53  GLU A  54  GLU A 116                    
SITE     2 AC3  5 PHE A 119                                                     
SITE     1 AC4  7 CYS A 127  SER A 129  VAL A 195  PRO A 196                    
SITE     2 AC4  7 ASP A 197  TRP A 206  HOH C 510                               
SITE     1 AC5 14 HIS A  66  ASP A  92  ARG A  96  ASN A 124                    
SITE     2 AC5 14 HIS A 125  ARG A 221  HIS A 248   MN A 401                    
SITE     3 AC5 14  MN A 402  HOH A 520  HOH A 538  HOH A 576                    
SITE     4 AC5 14 HOH A 594  HOH A 642                                          
SITE     1 AC6  7 ASP C  64  HIS C  66  ASP C  92   MN C 402                    
SITE     2 AC6  7 PO4 C 403  HOH C 566  HOH C 567                               
SITE     1 AC7  7 ASP C  92  ASN C 124  HIS C 173  HIS C 248                    
SITE     2 AC7  7  MN C 401  PO4 C 403  HOH C 566                               
SITE     1 AC8 12 HIS C  66  ASP C  92  ARG C  96  ASN C 124                    
SITE     2 AC8 12 HIS C 125  ARG C 221  HIS C 248   MN C 401                    
SITE     3 AC8 12  MN C 402  HOH C 557  HOH C 566  HOH C 567                    
CRYST1   92.407   92.407  199.342  90.00  90.00  90.00 P 41 21 2    16          
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      0.010822  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010822  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005017        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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