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Database: PDB
Entry: 6ALZ
LinkDB: 6ALZ
Original site: 6ALZ 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           08-AUG-17   6ALZ              
TITLE     CRYSTAL STRUCTURE OF PROTEIN PHOSPHATASE 1 BOUND TO THE NATURAL       
TITLE    2 INHIBITOR TAUTOMYCETIN                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-ALPHA CATALYTIC   
COMPND   3 SUBUNIT;                                                             
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: RESIDUES 7-300;                                            
COMPND   6 SYNONYM: PP-1A;                                                      
COMPND   7 EC: 3.1.3.16;                                                        
COMPND   8 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    INHIBITOR, COMPLEX, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.S.CHOY,W.PETI,R.PAGE                                                
REVDAT   4   11-DEC-19 6ALZ    1       REMARK                                   
REVDAT   3   27-DEC-17 6ALZ    1       JRNL                                     
REVDAT   2   13-DEC-17 6ALZ    1       JRNL                                     
REVDAT   1   29-NOV-17 6ALZ    0                                                
JRNL        AUTH   M.S.CHOY,M.SWINGLE,B.D'ARCY,K.ABNEY,S.F.RUSIN,               
JRNL        AUTH 2 A.N.KETTENBACH,R.PAGE,R.E.HONKANEN,W.PETI                    
JRNL        TITL   PP1:TAUTOMYCETIN COMPLEX REVEALS A PATH TOWARD THE           
JRNL        TITL 2 DEVELOPMENT OF PP1-SPECIFIC INHIBITORS.                      
JRNL        REF    J. AM. CHEM. SOC.             V. 139 17703 2017              
JRNL        REFN                   ESSN 1520-5126                               
JRNL        PMID   29156132                                                     
JRNL        DOI    10.1021/JACS.7B09368                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.21 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575)                                 
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) : 2.21                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.82                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 35156                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.110                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1795                            
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 38.8222 -  5.1868    1.00     2795   150  0.1782 0.1845        
REMARK   3     2  5.1868 -  4.1184    1.00     2672   139  0.1363 0.1321        
REMARK   3     3  4.1184 -  3.5982    1.00     2685   118  0.1588 0.2181        
REMARK   3     4  3.5982 -  3.2694    1.00     2608   154  0.1751 0.2101        
REMARK   3     5  3.2694 -  3.0352    1.00     2589   140  0.1979 0.2396        
REMARK   3     6  3.0352 -  2.8563    1.00     2602   146  0.2011 0.2375        
REMARK   3     7  2.8563 -  2.7133    1.00     2603   141  0.2109 0.2577        
REMARK   3     8  2.7133 -  2.5952    1.00     2616   136  0.2206 0.2799        
REMARK   3     9  2.5952 -  2.4953    1.00     2600   122  0.2300 0.2453        
REMARK   3    10  2.4953 -  2.4092    1.00     2547   155  0.2217 0.2989        
REMARK   3    11  2.4092 -  2.3339    1.00     2594   146  0.2259 0.3009        
REMARK   3    12  2.3339 -  2.2672    1.00     2559   147  0.2354 0.2864        
REMARK   3    13  2.2672 -  2.2075    0.74     1891   101  0.2987 0.2876        
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)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.610           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.82                          
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      :  0.002           4922                                  
REMARK   3   ANGLE     :  0.562           6669                                  
REMARK   3   CHIRALITY :  0.038            725                                  
REMARK   3   PLANARITY :  0.003            871                                  
REMARK   3   DIHEDRAL  :  7.518           4015                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 6ALZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229336.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-FEB-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.17                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35351                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.822                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.11800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 72.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.81400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 1.11.1                                         
REMARK 200 STARTING MODEL: 4MOV                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 6000, 1 M LITHIUM CHLORIDE,      
REMARK 280  0.1 M TRIS PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
REMARK 280  298K                                                                
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       33.09950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.88950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.42750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.88950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.09950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.42750            
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, 3                                                 
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 300 REMARK: MONOMER AS DETERMINED BY GEL FILTRATION                      
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     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     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 211    CD   CE   NZ                                        
REMARK 470     GLU A 218    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 260    CE   NZ                                             
REMARK 470     GLU A 275    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  41    CG   CD   CE   NZ                                   
REMARK 470     LYS B  98    CD   CE   NZ                                        
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     LYS B 234    CD   CE   NZ                                        
REMARK 470     LYS B 260    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   O    HOH A   559     O    HOH B   596              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  95      160.33     73.68                                   
REMARK 500    ARG A  96      -48.31     69.86                                   
REMARK 500    TYR A 144     -112.78   -137.80                                   
REMARK 500    TRP A 206      -31.91   -132.88                                   
REMARK 500    SER A 224     -153.74     65.81                                   
REMARK 500    ALA A 247     -118.82   -132.57                                   
REMARK 500    HIS A 248      -33.84     75.99                                   
REMARK 500    ASP B  95      150.20     79.72                                   
REMARK 500    ARG B  96      -32.17     66.50                                   
REMARK 500    GLU B 126       34.97    -86.98                                   
REMARK 500    TYR B 144     -112.91   -139.25                                   
REMARK 500    TRP B 206      -33.99   -133.60                                   
REMARK 500    SER B 224     -148.07     59.95                                   
REMARK 500    ALA B 247     -122.42   -132.27                                   
REMARK 500    HIS B 248      -31.92     77.12                                   
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 ASP A  64   OD2                                                    
REMARK 620 2 HIS A  66   NE2 104.1                                              
REMARK 620 3 ASP A  92   OD2  91.5  98.1                                        
REMARK 620 4 HOH A 543   O   105.5 150.2  78.0                                  
REMARK 620 5 HOH A 504   O   103.1  90.8 160.6  85.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  92   OD2                                                    
REMARK 620 2 ASN A 124   OD1  91.1                                              
REMARK 620 3 HIS A 173   NE2  88.9  91.5                                        
REMARK 620 4 HIS A 248   ND1 161.1 107.6  93.0                                  
REMARK 620 5 HOH A 543   O    76.7 122.9 142.3  90.6                            
REMARK 620 N                    1     2     3     4                             
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 ASP B  64   OD2                                                    
REMARK 620 2 HIS B  66   NE2 105.0                                              
REMARK 620 3 ASP B  92   OD2  88.7  95.7                                        
REMARK 620 4 HOH B 510   O   101.8 151.0  73.9                                  
REMARK 620 5 HOH B 546   O   106.8  82.9 164.2  99.8                            
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 ASP B  92   OD2                                                    
REMARK 620 2 ASN B 124   OD1  95.1                                              
REMARK 620 3 HIS B 173   NE2  93.2  93.1                                        
REMARK 620 4 HIS B 248   ND1 157.6 105.4  94.7                                  
REMARK 620 5 HOH B 510   O    73.9 121.3 143.7  87.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 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 BKM A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS 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 CL A 406                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 407                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 404                  
DBREF  6ALZ A    7   300  UNP    P62136   PP1A_HUMAN       7    300             
DBREF  6ALZ B    7   300  UNP    P62136   PP1A_HUMAN       7    300             
SEQADV 6ALZ GLY A    2  UNP  P62136              EXPRESSION TAG                 
SEQADV 6ALZ HIS A    3  UNP  P62136              EXPRESSION TAG                 
SEQADV 6ALZ MET A    4  UNP  P62136              EXPRESSION TAG                 
SEQADV 6ALZ GLY A    5  UNP  P62136              EXPRESSION TAG                 
SEQADV 6ALZ SER A    6  UNP  P62136              EXPRESSION TAG                 
SEQADV 6ALZ GLY B    2  UNP  P62136              EXPRESSION TAG                 
SEQADV 6ALZ HIS B    3  UNP  P62136              EXPRESSION TAG                 
SEQADV 6ALZ MET B    4  UNP  P62136              EXPRESSION TAG                 
SEQADV 6ALZ GLY B    5  UNP  P62136              EXPRESSION TAG                 
SEQADV 6ALZ 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    BKM  A 403      44                                                       
HET    DMS  A 404       4                                                       
HET     CL  A 405       1                                                       
HET     CL  A 406       1                                                       
HET     CL  A 407       1                                                       
HET     MN  B 401       1                                                       
HET     MN  B 402       1                                                       
HET    BKM  B 403      44                                                       
HET     CL  B 404       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     BKM (2Z)-2-[(1R)-3-{[(2R,3S,4R,7S,8S,11S,13R,16E)-17-ETHYL-          
HETNAM   2 BKM  4,8-DIHYDROXY-3,7,11,13-TETRAMETHYL-6,15-                       
HETNAM   3 BKM  DIOXONONADECA-16,18-DIEN-2-YL]OXY}-1-HYDROXY-3-                 
HETNAM   4 BKM  OXOPROPYL]-3-METHYLBUT-2-ENEDIOIC ACID                          
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM      CL CHLORIDE ION                                                     
HETSYN     BKM TAUTOMYCETIN DIACID FORM                                         
FORMUL   3   MN    4(MN 2+)                                                     
FORMUL   5  BKM    2(C33 H52 O11)                                               
FORMUL   6  DMS    C2 H6 O S                                                    
FORMUL   7   CL    4(CL 1-)                                                     
FORMUL  14  HOH   *288(H2 O)                                                    
HELIX    1 AA1 ASN A    8  GLU A   18  1                                  11    
HELIX    2 AA2 THR A   31  GLN A   49  1                                  19    
HELIX    3 AA3 GLN A   68  GLY A   80  1                                  13    
HELIX    4 AA4 GLN A   99  TYR A  114  1                                  16    
HELIX    5 AA5 GLY A  123  GLU A  126  5                                   4    
HELIX    6 AA6 CYS A  127  ARG A  132  1                                   6    
HELIX    7 AA7 GLY A  135  TYR A  144  1                                  10    
HELIX    8 AA8 ASN A  145  ASN A  157  1                                  13    
HELIX    9 AA9 MET A  183  ARG A  188  1                                   6    
HELIX   10 AB1 GLY A  199  SER A  207  1                                   9    
HELIX   11 AB2 GLY A  228  ASP A  240  1                                  13    
HELIX   12 AB3 ASN A  271  GLU A  275  5                                   5    
HELIX   13 AB4 ASN B    8  VAL B   19  1                                  12    
HELIX   14 AB5 THR B   31  GLN B   49  1                                  19    
HELIX   15 AB6 GLN B   68  GLY B   80  1                                  13    
HELIX   16 AB7 GLN B   99  TYR B  114  1                                  16    
HELIX   17 AB8 CYS B  127  ARG B  132  1                                   6    
HELIX   18 AB9 GLY B  135  TYR B  144  1                                  10    
HELIX   19 AC1 ASN B  145  ASN B  157  1                                  13    
HELIX   20 AC2 MET B  183  ARG B  188  1                                   6    
HELIX   21 AC3 GLY B  199  LEU B  204  1                                   6    
HELIX   22 AC4 GLY B  228  HIS B  239  1                                  12    
HELIX   23 AC5 ASN B  271  GLU B  275  5                                   5    
SHEET    1 AA1 6 LEU A  52  LEU A  55  0                                        
SHEET    2 AA1 6 ALA A 162  VAL A 165  1  O  ILE A 164   N  LEU A  53           
SHEET    3 AA1 6 ILE A 169  CYS A 172 -1  O  CYS A 171   N  ALA A 163           
SHEET    4 AA1 6 LEU A 243  ARG A 246  1  O  CYS A 245   N  PHE A 170           
SHEET    5 AA1 6 LEU A 263  LEU A 266  1  O  LEU A 266   N  ARG A 246           
SHEET    6 AA1 6 TYR A 255  PHE A 258 -1  N  GLU A 256   O  THR A 265           
SHEET    1 AA2 5 PHE A 118  LEU A 120  0                                        
SHEET    2 AA2 5 TYR A  87  PHE A  89  1  N  PHE A  89   O  PHE A 119           
SHEET    3 AA2 5 LEU A  59  CYS A  62  1  N  LYS A  60   O  LEU A  88           
SHEET    4 AA2 5 GLY A 280  VAL A 285 -1  O  MET A 283   N  ILE A  61           
SHEET    5 AA2 5 CYS A 291  LEU A 296 -1  O  LEU A 296   N  GLY A 280           
SHEET    1 AA3 3 ASP A 208  PRO A 209  0                                        
SHEET    2 AA3 3 PHE A 225  PHE A 227  1  O  PHE A 227   N  ASP A 208           
SHEET    3 AA3 3 TRP A 216  GLU A 218 -1  N  GLY A 217   O  THR A 226           
SHEET    1 AA4 6 LEU B  52  LEU B  55  0                                        
SHEET    2 AA4 6 ALA B 162  VAL B 165  1  O  ALA B 162   N  LEU B  53           
SHEET    3 AA4 6 ILE B 169  CYS B 172 -1  O  CYS B 171   N  ALA B 163           
SHEET    4 AA4 6 LEU B 243  ARG B 246  1  O  CYS B 245   N  PHE B 170           
SHEET    5 AA4 6 LEU B 263  LEU B 266  1  O  LEU B 266   N  ARG B 246           
SHEET    6 AA4 6 TYR B 255  PHE B 258 -1  N  PHE B 258   O  LEU B 263           
SHEET    1 AA5 5 PHE B 118  LEU B 120  0                                        
SHEET    2 AA5 5 TYR B  87  PHE B  89  1  N  PHE B  89   O  PHE B 119           
SHEET    3 AA5 5 LEU B  59  CYS B  62  1  N  CYS B  62   O  LEU B  88           
SHEET    4 AA5 5 GLY B 280  VAL B 285 -1  O  VAL B 285   N  LEU B  59           
SHEET    5 AA5 5 CYS B 291  LEU B 296 -1  O  LEU B 296   N  GLY B 280           
SHEET    1 AA6 3 ASP B 208  PRO B 209  0                                        
SHEET    2 AA6 3 PHE B 225  PHE B 227  1  O  PHE B 227   N  ASP B 208           
SHEET    3 AA6 3 TRP B 216  GLU B 218 -1  N  GLY B 217   O  THR B 226           
LINK         OD2 ASP A  64                MN    MN A 402     1555   1555  1.92  
LINK         NE2 HIS A  66                MN    MN A 402     1555   1555  2.12  
LINK         OD2 ASP A  92                MN    MN A 401     1555   1555  2.31  
LINK         OD2 ASP A  92                MN    MN A 402     1555   1555  2.10  
LINK         OD1 ASN A 124                MN    MN A 401     1555   1555  2.11  
LINK         SG  CYS A 127                 C01 BKM A 403     1555   1555  1.77  
LINK         NE2 HIS A 173                MN    MN A 401     1555   1555  2.18  
LINK         ND1 HIS A 248                MN    MN A 401     1555   1555  2.33  
LINK         OD2 ASP B  64                MN    MN B 401     1555   1555  2.13  
LINK         NE2 HIS B  66                MN    MN B 401     1555   1555  2.15  
LINK         OD2 ASP B  92                MN    MN B 402     1555   1555  2.26  
LINK         OD2 ASP B  92                MN    MN B 401     1555   1555  2.07  
LINK         OD1 ASN B 124                MN    MN B 402     1555   1555  2.12  
LINK         SG  CYS B 127                 C01 BKM B 403     1555   1555  1.77  
LINK         NE2 HIS B 173                MN    MN B 402     1555   1555  2.16  
LINK         ND1 HIS B 248                MN    MN B 402     1555   1555  2.28  
LINK        MN    MN A 401                 O   HOH A 543     1555   1555  1.99  
LINK        MN    MN A 402                 O   HOH A 543     1555   1555  2.16  
LINK        MN    MN A 402                 O   HOH A 504     1555   1555  2.25  
LINK        MN    MN B 401                 O   HOH B 510     1555   1555  2.10  
LINK        MN    MN B 401                 O   HOH B 546     1555   1555  2.16  
LINK        MN    MN B 402                 O   HOH B 510     1555   1555  1.88  
CISPEP   1 ALA A   57    PRO A   58          0         0.72                     
CISPEP   2 PRO A   82    PRO A   83          0         2.97                     
CISPEP   3 ARG A  191    PRO A  192          0         1.64                     
CISPEP   4 ALA B   57    PRO B   58          0         2.13                     
CISPEP   5 PRO B   82    PRO B   83          0         6.67                     
CISPEP   6 ARG B  191    PRO B  192          0         1.60                     
SITE     1 AC1  6 ASP A  92  ASN A 124  HIS A 173  HIS A 248                    
SITE     2 AC1  6  MN A 402  HOH A 543                                          
SITE     1 AC2  6 ASP A  64  HIS A  66  ASP A  92   MN A 401                    
SITE     2 AC2  6 HOH A 504  HOH A 543                                          
SITE     1 AC3 17 ARG A  96  CYS A 127  SER A 129  TYR A 134                    
SITE     2 AC3 17 VAL A 195  TRP A 206  ARG A 221  VAL A 223                    
SITE     3 AC3 17 HIS A 248  VAL A 250  TYR A 272  PHE A 276                    
SITE     4 AC3 17 HOH A 504  HOH A 530  HOH A 543  HOH A 547                    
SITE     5 AC3 17 HOH A 570                                                     
SITE     1 AC4  2 PRO A  50  GLU A  54                                          
SITE     1 AC5  4 GLY A 215  GLY A 228  GLU A 230  VAL A 231                    
SITE     1 AC6  3 LYS A 297  HOH A 664  PHE B 257                               
SITE     1 AC7  3 GLN A 294  ILE A 295  HOH B 512                               
SITE     1 AC8  6 ASP B  64  HIS B  66  ASP B  92   MN B 402                    
SITE     2 AC8  6 HOH B 510  HOH B 546                                          
SITE     1 AC9  6 ASP B  92  ASN B 124  HIS B 173  HIS B 248                    
SITE     2 AC9  6  MN B 401  HOH B 510                                          
SITE     1 AD1  5 GLY B 215  GLY B 228  ALA B 229  GLU B 230                    
SITE     2 AD1  5 VAL B 231                                                     
CRYST1   66.199   78.855  133.779  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      0.015106  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012682  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007475        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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