GenomeNet

Database: PDB
Entry: 4MOV
LinkDB: 4MOV
Original site: 4MOV 
HEADER    HYDROLASE                               12-SEP-13   4MOV              
TITLE     1.45 A RESOLUTION CRYSTAL STRUCTURE OF PROTEIN PHOSPHATASE 1          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-ALPHA CATALYTIC   
COMPND   3 SUBUNIT;                                                             
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 SYNONYM: PP-1A;                                                      
COMPND   6 EC: 3.1.3.16;                                                        
COMPND   7 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                                         
KEYWDS    CATALYTIC SUBUNIT, SERINE/THREONINE PHOSPHATASE, NUCLEUS, HYDROLASE   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.S.CHOY,W.PETI,R.PAGE                                                
REVDAT   3   15-NOV-17 4MOV    1       REMARK                                   
REVDAT   2   23-APR-14 4MOV    1       JRNL                                     
REVDAT   1   26-MAR-14 4MOV    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.    1.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.2_1309                                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.93                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 120168                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.151                           
REMARK   3   R VALUE            (WORKING SET) : 0.150                           
REMARK   3   FREE R VALUE                     : 0.167                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6022                            
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 46.9534 -  4.5053    1.00     4108   220  0.1664 0.1714        
REMARK   3     2  4.5053 -  3.5764    1.00     3974   183  0.1376 0.1354        
REMARK   3     3  3.5764 -  3.1244    1.00     3881   216  0.1489 0.1762        
REMARK   3     4  3.1244 -  2.8388    1.00     3858   223  0.1596 0.1616        
REMARK   3     5  2.8388 -  2.6353    1.00     3867   201  0.1605 0.1917        
REMARK   3     6  2.6353 -  2.4800    1.00     3875   192  0.1557 0.1694        
REMARK   3     7  2.4800 -  2.3558    1.00     3802   215  0.1513 0.1693        
REMARK   3     8  2.3558 -  2.2532    1.00     3831   224  0.1507 0.1644        
REMARK   3     9  2.2532 -  2.1665    1.00     3849   200  0.1442 0.1581        
REMARK   3    10  2.1665 -  2.0917    1.00     3806   215  0.1414 0.1559        
REMARK   3    11  2.0917 -  2.0263    1.00     3821   209  0.1469 0.1680        
REMARK   3    12  2.0263 -  1.9684    1.00     3818   203  0.1426 0.1531        
REMARK   3    13  1.9684 -  1.9166    1.00     3798   203  0.1456 0.1721        
REMARK   3    14  1.9166 -  1.8698    1.00     3815   205  0.1483 0.1846        
REMARK   3    15  1.8698 -  1.8273    1.00     3796   193  0.1448 0.1613        
REMARK   3    16  1.8273 -  1.7884    1.00     3811   211  0.1451 0.1709        
REMARK   3    17  1.7884 -  1.7526    1.00     3824   170  0.1459 0.1567        
REMARK   3    18  1.7526 -  1.7196    1.00     3823   185  0.1446 0.1767        
REMARK   3    19  1.7196 -  1.6889    1.00     3797   181  0.1411 0.1628        
REMARK   3    20  1.6889 -  1.6602    1.00     3850   181  0.1369 0.1573        
REMARK   3    21  1.6602 -  1.6334    1.00     3785   206  0.1381 0.1677        
REMARK   3    22  1.6334 -  1.6083    1.00     3782   195  0.1387 0.1465        
REMARK   3    23  1.6083 -  1.5847    1.00     3794   193  0.1405 0.1653        
REMARK   3    24  1.5847 -  1.5623    1.00     3794   197  0.1459 0.1722        
REMARK   3    25  1.5623 -  1.5412    1.00     3754   233  0.1481 0.1566        
REMARK   3    26  1.5412 -  1.5212    1.00     3775   196  0.1553 0.1934        
REMARK   3    27  1.5212 -  1.5022    0.99     3766   189  0.1635 0.1927        
REMARK   3    28  1.5022 -  1.4841    0.97     3649   204  0.1659 0.1991        
REMARK   3    29  1.4841 -  1.4668    0.95     3545   200  0.1670 0.1781        
REMARK   3    30  1.4668 -  1.4503    0.92     3498   179  0.1792 0.2204        
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)     : 0.110            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.830           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 11.81                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.77                          
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      :  0.013           4906                                  
REMARK   3   ANGLE     :  1.536           6681                                  
REMARK   3   CHIRALITY :  0.107            731                                  
REMARK   3   PLANARITY :  0.008            872                                  
REMARK   3   DIHEDRAL  : 12.449           1838                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 7:32                                 
REMARK   3    ORIGIN FOR THE GROUP (A):  42.8254  28.5577  58.9214              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0456 T22:   0.0791                                     
REMARK   3      T33:   0.0826 T12:  -0.0128                                     
REMARK   3      T13:   0.0058 T23:   0.0081                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0014 L22:   0.0003                                     
REMARK   3      L33:   0.0010 L12:  -0.0001                                     
REMARK   3      L13:   0.0002 L23:  -0.0005                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0025 S12:   0.0034 S13:   0.0073                       
REMARK   3      S21:  -0.0019 S22:   0.0014 S23:  -0.0018                       
REMARK   3      S31:  -0.0091 S32:   0.0091 S33:  -0.0005                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 33:216                               
REMARK   3    ORIGIN FOR THE GROUP (A):  34.0052  23.3853  75.9364              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0480 T22:   0.0243                                     
REMARK   3      T33:   0.0089 T12:  -0.0306                                     
REMARK   3      T13:  -0.0005 T23:   0.0007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0724 L22:   0.0344                                     
REMARK   3      L33:   0.0287 L12:   0.0196                                     
REMARK   3      L13:   0.0452 L23:   0.0129                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0233 S12:  -0.0672 S13:  -0.0023                       
REMARK   3      S21:   0.0386 S22:   0.0064 S23:   0.0096                       
REMARK   3      S31:   0.0193 S32:  -0.0467 S33:   0.0836                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 217:299                              
REMARK   3    ORIGIN FOR THE GROUP (A):  36.8140  33.4252  88.6364              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1033 T22:   0.1100                                     
REMARK   3      T33:   0.0715 T12:   0.0120                                     
REMARK   3      T13:  -0.0037 T23:  -0.0232                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0110 L22:   0.0132                                     
REMARK   3      L33:   0.0063 L12:   0.0045                                     
REMARK   3      L13:   0.0025 L23:   0.0087                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0170 S12:  -0.0714 S13:   0.0330                       
REMARK   3      S21:   0.0351 S22:  -0.0268 S23:  -0.0063                       
REMARK   3      S31:  -0.0259 S32:  -0.0581 S33:  -0.0098                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 7:32                                 
REMARK   3    ORIGIN FOR THE GROUP (A):  61.0725  42.5818 113.4912              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1005 T22:   0.0603                                     
REMARK   3      T33:   0.0797 T12:  -0.0287                                     
REMARK   3      T13:  -0.0023 T23:  -0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0011 L22:   0.0012                                     
REMARK   3      L33:   0.0011 L12:   0.0001                                     
REMARK   3      L13:  -0.0005 L23:   0.0002                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0015 S12:  -0.0044 S13:   0.0031                       
REMARK   3      S21:   0.0022 S22:   0.0003 S23:   0.0060                       
REMARK   3      S31:   0.0162 S32:  -0.0095 S33:   0.0004                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 33:198                               
REMARK   3    ORIGIN FOR THE GROUP (A):  67.5813  48.4906  97.6596              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1129 T22:   0.0266                                     
REMARK   3      T33:   0.0638 T12:  -0.0402                                     
REMARK   3      T13:   0.0313 T23:  -0.0392                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0230 L22:   0.0454                                     
REMARK   3      L33:   0.0282 L12:   0.0069                                     
REMARK   3      L13:   0.0191 L23:   0.0262                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0010 S12:   0.0338 S13:  -0.0101                       
REMARK   3      S21:  -0.0415 S22:   0.0294 S23:  -0.0460                       
REMARK   3      S31:  -0.0345 S32:   0.0395 S33:   0.0314                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 199:299                              
REMARK   3    ORIGIN FOR THE GROUP (A):  58.7053  50.5540  82.7702              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1742 T22:   0.0901                                     
REMARK   3      T33:   0.0691 T12:  -0.0178                                     
REMARK   3      T13:  -0.0028 T23:  -0.0160                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0128 L22:   0.0036                                     
REMARK   3      L33:   0.0071 L12:  -0.0031                                     
REMARK   3      L13:   0.0080 L23:  -0.0049                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0231 S12:   0.0569 S13:  -0.0226                       
REMARK   3      S21:  -0.0684 S22:  -0.0012 S23:   0.0346                       
REMARK   3      S31:  -0.0610 S32:  -0.0038 S33:  -0.0042                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4MOV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-SEP-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000082180.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
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 : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALA, SCALEPACK                   
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 120264                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.929                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
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) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.1                               
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: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3E7A                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 1.0 M LITHIUM CHLORIDE,     
REMARK 280  20% PEG 6000, PH 7, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE      
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       32.86200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.51750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.80000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.51750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.86200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.80000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER A     6                                                      
REMARK 465     ASP A   300                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     MET B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     ARG B    23                                                      
REMARK 465     PRO B    24                                                      
REMARK 465     ASP B   300                                                      
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  98    CD   CE   NZ                                        
REMARK 470     GLU A 116    CD   OE1  OE2                                       
REMARK 470     LYS A 211    CG   CD   CE   NZ                                   
REMARK 470     GLN A 214    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 218    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 234    CG   CD   CE   NZ                                   
REMARK 470     LYS A 260    CD   CE   NZ                                        
REMARK 470     GLU A 275    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  54    CD   OE1  OE2                                       
REMARK 470     GLU B  77    CD   OE1  OE2                                       
REMARK 470     LYS B  98    CD   CE   NZ                                        
REMARK 470     LYS B 150    CD   CE   NZ                                        
REMARK 470     ARG B 188    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 194    CG   OD1  OD2                                       
REMARK 470     ASP B 197    CG   OD1  OD2                                       
REMARK 470     LYS B 211    CG   CD   CE   NZ                                   
REMARK 470     GLN B 214    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 218    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 230    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 234    CG   CD   CE   NZ                                   
REMARK 470     LYS B 260    CG   CD   CE   NZ                                   
REMARK 470     GLU B 275    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500  MN     MN A   402     O    HOH A   737              1.70            
REMARK 500   O    LEU B     7     O    HOH B   733              2.11            
REMARK 500   OE1  GLU B    18     O    HOH B   801              2.16            
REMARK 500   OE1  GLU B    84     O    HOH B   584              2.17            
REMARK 500   O    HOH A   622     O    HOH A   760              2.19            
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    PRO A  24      107.90    -47.83                                   
REMARK 500    ASP A  92       62.08     60.17                                   
REMARK 500    ASP A  95      153.12     77.77                                   
REMARK 500    ARG A  96      -47.15     74.85                                   
REMARK 500    TYR A 144     -114.84   -135.32                                   
REMARK 500    SER A 224     -150.49     61.36                                   
REMARK 500    ALA A 247     -130.45   -135.35                                   
REMARK 500    HIS A 248      -39.92     79.82                                   
REMARK 500    ASP B  95      152.37     77.14                                   
REMARK 500    ARG B  96      -47.77     74.52                                   
REMARK 500    TYR B 144     -110.73   -136.88                                   
REMARK 500    SER B 224     -150.02     63.54                                   
REMARK 500    ALA B 247     -130.02   -134.77                                   
REMARK 500    HIS B 248      -42.07     81.86                                   
REMARK 500    CYS B 273       33.30     35.42                                   
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 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  66   NE2                                                    
REMARK 620 2 ASP A  92   OD2  96.5                                              
REMARK 620 3 PO4 A 403   O1   92.5 102.5                                        
REMARK 620 4 ASP A  64   OD2  99.6  85.8 164.5                                  
REMARK 620 5 HOH A 746   O    87.6 174.7  73.9  96.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  66   NE2                                                    
REMARK 620 2 PO4 B 403   O3   93.9                                              
REMARK 620 3 ASP B  92   OD2  94.9 100.4                                        
REMARK 620 4 ASP B  64   OD2 100.6 164.3  84.4                                  
REMARK 620 5 HOH B 508   O   176.5  82.8  84.7  82.8                            
REMARK 620 6 HOH B 685   O    87.7  80.2 177.3  94.3  92.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B 124   OD1                                                    
REMARK 620 2 PO4 B 403   O1   83.8                                              
REMARK 620 3 ASP B  92   OD2  98.3  94.4                                        
REMARK 620 4 HIS B 173   NE2  87.4 171.1  86.1                                  
REMARK 620 5 HIS B 248   ND1  97.3  93.1 163.4  88.9                            
REMARK 620 6 HOH B 508   O   156.8  74.2  76.8 114.5  91.0                      
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 ASN A 124   OD1                                                    
REMARK 620 2 PO4 A 403   O3   84.0                                              
REMARK 620 3 HIS A 173   NE2  87.6 171.6                                        
REMARK 620 4 ASP A  92   OD2  98.2  96.4  85.0                                  
REMARK 620 5 HIS A 248   ND1  99.3  90.6  90.6 161.8                            
REMARK 620 6 HOH A 737   O   155.4  73.1 115.2  76.0  90.1                      
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 PO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 405                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 403                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3E7A   RELATED DB: PDB                                   
REMARK 900 PP1 COMPLEXED WITH NODULARIN R                                       
REMARK 900 RELATED ID: 3EGG   RELATED DB: PDB                                   
REMARK 900 PP1:SPINOPHILIN CRYSTAL STRUCTURE                                    
REMARK 900 RELATED ID: 3V4Y   RELATED DB: PDB                                   
REMARK 900 PP1:NIPP1 CRYSTAL STRUCTURE                                          
DBREF  4MOV A    7   300  UNP    P62136   PP1A_HUMAN       7    300             
DBREF  4MOV B    7   300  UNP    P62136   PP1A_HUMAN       7    300             
SEQADV 4MOV GLY A    2  UNP  P62136              EXPRESSION TAG                 
SEQADV 4MOV HIS A    3  UNP  P62136              EXPRESSION TAG                 
SEQADV 4MOV MET A    4  UNP  P62136              EXPRESSION TAG                 
SEQADV 4MOV GLY A    5  UNP  P62136              EXPRESSION TAG                 
SEQADV 4MOV SER A    6  UNP  P62136              EXPRESSION TAG                 
SEQADV 4MOV GLY B    2  UNP  P62136              EXPRESSION TAG                 
SEQADV 4MOV HIS B    3  UNP  P62136              EXPRESSION TAG                 
SEQADV 4MOV MET B    4  UNP  P62136              EXPRESSION TAG                 
SEQADV 4MOV GLY B    5  UNP  P62136              EXPRESSION TAG                 
SEQADV 4MOV SER B    6  UNP  P62136              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 B  299  GLY HIS MET GLY SER LEU ASN LEU ASP SER ILE ILE GLY          
SEQRES   2 B  299  ARG LEU LEU GLU VAL GLN GLY SER ARG PRO GLY LYS ASN          
SEQRES   3 B  299  VAL GLN LEU THR GLU ASN GLU ILE ARG GLY LEU CYS LEU          
SEQRES   4 B  299  LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU LEU          
SEQRES   5 B  299  GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE HIS          
SEQRES   6 B  299  GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR GLY          
SEQRES   7 B  299  GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY ASP          
SEQRES   8 B  299  TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE CYS          
SEQRES   9 B  299  LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN PHE          
SEQRES  10 B  299  PHE LEU LEU ARG GLY ASN HIS GLU CYS ALA SER ILE ASN          
SEQRES  11 B  299  ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG TYR          
SEQRES  12 B  299  ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE ASN          
SEQRES  13 B  299  CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE PHE          
SEQRES  14 B  299  CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER MET          
SEQRES  15 B  299  GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL PRO          
SEQRES  16 B  299  ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP PRO          
SEQRES  17 B  299  ASP LYS ASP VAL GLN GLY TRP GLY GLU ASN ASP ARG GLY          
SEQRES  18 B  299  VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS PHE          
SEQRES  19 B  299  LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA HIS          
SEQRES  20 B  299  GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS ARG          
SEQRES  21 B  299  GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CYS GLY          
SEQRES  22 B  299  GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP GLU          
SEQRES  23 B  299  THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA ASP          
HET     MN  A 401       1                                                       
HET     MN  A 402       1                                                       
HET    PO4  A 403       5                                                       
HET     CL  A 404       1                                                       
HET     CL  A 405       1                                                       
HET     MN  B 401       1                                                       
HET     MN  B 402       1                                                       
HET    PO4  B 403       5                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3   MN    4(MN 2+)                                                     
FORMUL   5  PO4    2(O4 P 3-)                                                   
FORMUL   6   CL    2(CL 1-)                                                     
FORMUL  11  HOH   *621(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  GLY A  135  1                                   9    
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  ASP A  240  1                                  13    
HELIX   11  11 ASN A  271  GLU A  275  5                                   5    
HELIX   12  12 ASN B    8  VAL B   19  1                                  12    
HELIX   13  13 THR B   31  GLN B   49  1                                  19    
HELIX   14  14 GLN B   68  GLY B   80  1                                  13    
HELIX   15  15 GLN B   99  TYR B  114  1                                  16    
HELIX   16  16 CYS B  127  TYR B  134  1                                   8    
HELIX   17  17 GLY B  135  TYR B  144  1                                  10    
HELIX   18  18 ASN B  145  ASN B  157  1                                  13    
HELIX   19  19 MET B  183  ARG B  188  1                                   6    
HELIX   20  20 GLY B  199  SER B  207  1                                   9    
HELIX   21  21 GLY B  228  ASP B  240  1                                  13    
HELIX   22  22 ASN B  271  GLU B  275  5                                   5    
SHEET    1   A 6 LEU A  52  LEU A  55  0                                        
SHEET    2   A 6 ALA A 162  VAL A 165  1  O  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  CYS A 245   N  PHE A 170           
SHEET    5   A 6 LEU A 263  LEU A 266  1  O  VAL A 264   N  ILE A 244           
SHEET    6   A 6 TYR A 255  PHE A 258 -1  N  PHE A 258   O  LEU A 263           
SHEET    1   B 5 PHE A 118  LEU A 120  0                                        
SHEET    2   B 5 TYR A  87  PHE A  89  1  N  PHE A  89   O  PHE A 119           
SHEET    3   B 5 LEU A  59  CYS A  62  1  N  CYS A  62   O  LEU A  88           
SHEET    4   B 5 GLY A 280  VAL A 285 -1  O  MET A 283   N  ILE A  61           
SHEET    5   B 5 CYS A 291  LEU A 296 -1  O  LEU A 296   N  GLY A 280           
SHEET    1   C 3 ASP A 208  PRO A 209  0                                        
SHEET    2   C 3 PHE A 225  PHE A 227  1  O  PHE A 225   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 B  52  LEU B  55  0                                        
SHEET    2   D 6 ALA B 162  VAL B 165  1  O  ILE B 164   N  LEU B  55           
SHEET    3   D 6 ILE B 169  CYS B 171 -1  O  CYS B 171   N  ALA B 163           
SHEET    4   D 6 LEU B 243  ARG B 246  1  O  CYS B 245   N  PHE B 170           
SHEET    5   D 6 LEU B 263  LEU B 266  1  O  VAL B 264   N  ILE B 244           
SHEET    6   D 6 TYR B 255  PHE B 258 -1  N  PHE B 258   O  LEU B 263           
SHEET    1   E 5 PHE B 118  LEU B 120  0                                        
SHEET    2   E 5 TYR B  87  PHE B  89  1  N  PHE B  89   O  PHE B 119           
SHEET    3   E 5 LEU B  59  CYS B  62  1  N  LYS B  60   O  LEU B  88           
SHEET    4   E 5 GLY B 280  VAL B 285 -1  O  VAL B 285   N  LEU B  59           
SHEET    5   E 5 CYS B 291  LEU B 296 -1  O  LEU B 296   N  GLY B 280           
SHEET    1   F 3 ASP B 208  PRO B 209  0                                        
SHEET    2   F 3 PHE B 225  PHE B 227  1  O  PHE B 225   N  ASP B 208           
SHEET    3   F 3 TRP B 216  GLU B 218 -1  N  GLY B 217   O  THR B 226           
LINK         NE2 HIS A  66                MN    MN A 402     1555   1555  2.07  
LINK         NE2 HIS B  66                MN    MN B 402     1555   1555  2.09  
LINK         OD1 ASN B 124                MN    MN B 401     1555   1555  2.11  
LINK         OD1 ASN A 124                MN    MN A 401     1555   1555  2.13  
LINK        MN    MN B 402                 O3  PO4 B 403     1555   1555  2.14  
LINK        MN    MN A 401                 O3  PO4 A 403     1555   1555  2.19  
LINK         NE2 HIS A 173                MN    MN A 401     1555   1555  2.21  
LINK         OD2 ASP A  92                MN    MN A 402     1555   1555  2.21  
LINK        MN    MN B 401                 O1  PO4 B 403     1555   1555  2.21  
LINK         OD2 ASP B  92                MN    MN B 401     1555   1555  2.21  
LINK         OD2 ASP A  92                MN    MN A 401     1555   1555  2.23  
LINK         NE2 HIS B 173                MN    MN B 401     1555   1555  2.24  
LINK         ND1 HIS B 248                MN    MN B 401     1555   1555  2.25  
LINK        MN    MN A 402                 O1  PO4 A 403     1555   1555  2.25  
LINK         ND1 HIS A 248                MN    MN A 401     1555   1555  2.25  
LINK         OD2 ASP B  92                MN    MN B 402     1555   1555  2.28  
LINK         OD2 ASP A  64                MN    MN A 402     1555   1555  2.29  
LINK         OD2 ASP B  64                MN    MN B 402     1555   1555  2.30  
LINK        MN    MN B 402                 O   HOH B 508     1555   1555  1.80  
LINK        MN    MN B 402                 O   HOH B 685     1555   1555  2.21  
LINK        MN    MN B 401                 O   HOH B 508     1555   1555  2.25  
LINK        MN    MN A 402                 O   HOH A 746     1555   1555  2.28  
LINK        MN    MN A 401                 O   HOH A 737     1555   1555  2.34  
CISPEP   1 ALA A   57    PRO A   58          0         3.36                     
CISPEP   2 PRO A   82    PRO A   83          0         4.48                     
CISPEP   3 ARG A  191    PRO A  192          0         3.70                     
CISPEP   4 ALA B   57    PRO B   58          0         3.82                     
CISPEP   5 PRO B   82    PRO B   83          0         6.44                     
CISPEP   6 ARG B  191    PRO B  192          0         0.26                     
SITE     1 AC1  7 ASP A  92  ASN A 124  HIS A 173  HIS A 248                    
SITE     2 AC1  7  MN A 402  PO4 A 403  HOH A 737                               
SITE     1 AC2  7 ASP A  64  HIS A  66  ASP A  92   MN A 401                    
SITE     2 AC2  7 PO4 A 403  HOH A 737  HOH A 746                               
SITE     1 AC3 13 HIS A  66  ASP A  92  ARG A  96  ASN A 124                    
SITE     2 AC3 13 HIS A 125  ARG A 221  HIS A 248   MN A 401                    
SITE     3 AC3 13  MN A 402  HOH A 737  HOH A 746  HOH A 754                    
SITE     4 AC3 13 HOH A 791                                                     
SITE     1 AC4  4 LYS A 113  ARG A 132  TRP A 149  HOH A 806                    
SITE     1 AC5  5 GLY A 215  GLY A 228  ALA A 229  GLU A 230                    
SITE     2 AC5  5 VAL A 231                                                     
SITE     1 AC6  7 ASP B  92  ASN B 124  HIS B 173  HIS B 248                    
SITE     2 AC6  7  MN B 402  PO4 B 403  HOH B 508                               
SITE     1 AC7  7 ASP B  64  HIS B  66  ASP B  92   MN B 401                    
SITE     2 AC7  7 PO4 B 403  HOH B 508  HOH B 685                               
SITE     1 AC8 12 HIS B  66  ASP B  92  ARG B  96  ASN B 124                    
SITE     2 AC8 12 HIS B 125  ARG B 221  HIS B 248   MN B 401                    
SITE     3 AC8 12  MN B 402  HOH B 508  HOH B 685  HOH B 688                    
CRYST1   65.724   77.600  133.035  90.00  90.00  90.00 P 21 21 21    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      0.015215  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012887  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007517        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system