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Database: PDB
Entry: 2BCD
LinkDB: 2BCD
Original site: 2BCD 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           19-OCT-05   2BCD              
TITLE     X-RAY CRYSTAL STRUCTURE OF PROTEIN PHOSPHATASE-1 WITH THE MARINE TOXIN
TITLE    2 MOTUPORIN BOUND                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC   
COMPND   3 SUBUNIT;                                                             
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: PP-1G, PROTEIN PHOSPHATASE 1C CATALYTIC SUBUNIT;            
COMPND   6 EC: 3.1.3.16;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: MOTUPORIN;                                                 
COMPND  10 CHAIN: B;                                                            
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PPP1CC;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET;                                  
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES                                                       
KEYWDS    PROTEIN PHOSPHTASE, NATURAL PRODUCT INHIBITORS, MOTUPORIN, NODULARIN, 
KEYWDS   2 HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.T.MAYNES,H.A.LUU,M.M.CHERNEY,R.J.ANDERSEN,D.WILLIAMS,C.F.HOLMES,    
AUTHOR   2 M.N.JAMES                                                            
REVDAT   5   27-JUL-11 2BCD    1       DBREF                                    
REVDAT   4   13-JUL-11 2BCD    1       VERSN                                    
REVDAT   3   24-FEB-09 2BCD    1       VERSN                                    
REVDAT   2   31-JAN-06 2BCD    1       JRNL                                     
REVDAT   1   17-JAN-06 2BCD    0                                                
JRNL        AUTH   J.T.MAYNES,H.A.LUU,M.M.CHERNEY,R.J.ANDERSEN,D.WILLIAMS,      
JRNL        AUTH 2 C.F.HOLMES,M.N.JAMES                                         
JRNL        TITL   CRYSTAL STRUCTURES OF PROTEIN PHOSPHATASE-1 BOUND TO         
JRNL        TITL 2 MOTUPORIN AND DIHYDROMICROCYSTIN-LA: ELUCIDATION OF THE      
JRNL        TITL 3 MECHANISM OF ENZYME INHIBITION BY CYANOBACTERIAL TOXINS.     
JRNL        REF    J.MOL.BIOL.                   V. 356   111 2006              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   16343532                                                     
JRNL        DOI    10.1016/J.JMB.2005.11.019                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.75                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 19682                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1008                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1331                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2460                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 83                           
REMARK   3   BIN FREE R VALUE                    : 0.2970                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2405                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 16                                      
REMARK   3   SOLVENT ATOMS            : 73                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.253         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.206         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.147         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.421         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.902                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2477 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3331 ; 1.838 ; 1.992       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   292 ; 6.782 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   119 ;36.609 ;24.034       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   416 ;15.034 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;15.697 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   359 ; 0.117 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1892 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1002 ; 0.155 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1631 ; 0.300 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   188 ; 0.169 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    33 ; 0.169 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.101 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1519 ; 0.926 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2342 ; 1.486 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1110 ; 2.116 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   989 ; 2.943 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2BCD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-NOV-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB034929.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19722                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.130                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : 0.06500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.29300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ID 1JK7                                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.3 M LITHIUM SULFATE, TRIS-HCL (100     
REMARK 280  MM, PH 8.0), POLYETHYLENE GLYCOL 400 (2%), BETA-MERCAPTOETHANOL     
REMARK 280  (10 MM), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 273K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       50.47750            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       50.47750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       31.74250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       50.47750            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       50.47750            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       31.74250            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       50.47750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.47750            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       31.74250            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       50.47750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.47750            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       31.74250            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
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     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     ASP A     5                                                      
REMARK 465     ALA A   299                                                      
REMARK 465     GLU A   300                                                      
REMARK 465     LYS A   301                                                      
REMARK 465     LYS A   302                                                      
REMARK 465     LYS A   303                                                      
REMARK 465     PRO A   304                                                      
REMARK 465     ASN A   305                                                      
REMARK 465     ALA A   306                                                      
REMARK 465     THR A   307                                                      
REMARK 465     ARG A   308                                                      
REMARK 465     PRO A   309                                                      
REMARK 465     VAL A   310                                                      
REMARK 465     THR A   311                                                      
REMARK 465     PRO A   312                                                      
REMARK 465     PRO A   313                                                      
REMARK 465     ARG A   314                                                      
REMARK 465     GLY A   315                                                      
REMARK 465     MET A   316                                                      
REMARK 465     ILE A   317                                                      
REMARK 465     THR A   318                                                      
REMARK 465     LYS A   319                                                      
REMARK 465     GLN A   320                                                      
REMARK 465     ALA A   321                                                      
REMARK 465     LYS A   322                                                      
REMARK 465     LYS A   323                                                      
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     LYS A   6    CG   CD   CE   NZ                                   
REMARK 470     GLU A  77    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  98    CE   NZ                                             
REMARK 470     LYS A 234    CE   NZ                                             
REMARK 470     LYS A 297    CG   CD   CE   NZ                                   
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   CB   CYS A   127     S2   BME A   604              1.66            
REMARK 500   SG   CYS A   127     C1   BME A   604              1.72            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    VAL B   2   N   -  CA  -  CB  ANGL. DEV. = -14.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  95      157.48     72.32                                   
REMARK 500    ARG A  96      -54.49     78.08                                   
REMARK 500    GLU A 126       55.48    -91.34                                   
REMARK 500    TYR A 144     -113.09   -136.18                                   
REMARK 500    GLU A 167        6.51     55.98                                   
REMARK 500    SER A 224     -152.43     63.37                                   
REMARK 500    ALA A 247     -129.38   -133.15                                   
REMARK 500    HIS A 248      -26.81     79.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN A 131        23.4      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  64   OD2                                                    
REMARK 620 2 ASP A  92   OD2  89.6                                              
REMARK 620 3 HIS A  66   NE2 106.9 105.8                                        
REMARK 620 4 HOH A 638   O   102.1 160.1  86.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 400  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 124   OD1                                                    
REMARK 620 2 ASP A  92   OD2 101.3                                              
REMARK 620 3 HIS A 173   NE2  94.5  92.5                                        
REMARK 620 4 HIS A 248   ND1 100.2 158.2  89.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF   MOTUPORIN            
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2BDX   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF DIHYDROMICROCYSTIN-LA BOUND TO            
REMARK 900 PROTEIN PHOSPHATASE-1                                                
DBREF  2BCD A    1   323  UNP    P36873   PP1G_HUMAN       1    323             
DBREF  2BCD B    1     5  NOR    NOR00825 NOR00825         1      5             
SEQRES   1 A  323  MET ALA ASP LEU ASP LYS LEU ASN ILE ASP SER ILE ILE          
SEQRES   2 A  323  GLN ARG LEU LEU GLU VAL ARG GLY SER LYS PRO GLY LYS          
SEQRES   3 A  323  ASN VAL GLN LEU GLN GLU ASN GLU ILE ARG GLY LEU CYS          
SEQRES   4 A  323  LEU LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU          
SEQRES   5 A  323  LEU GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE          
SEQRES   6 A  323  HIS GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR          
SEQRES   7 A  323  GLY GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY          
SEQRES   8 A  323  ASP TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE          
SEQRES   9 A  323  CYS LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN          
SEQRES  10 A  323  PHE PHE LEU LEU ARG GLY ASN HIS GLU CYS ALA SER ILE          
SEQRES  11 A  323  ASN ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG          
SEQRES  12 A  323  TYR ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE          
SEQRES  13 A  323  ASN CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE          
SEQRES  14 A  323  PHE CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER          
SEQRES  15 A  323  MET GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL          
SEQRES  16 A  323  PRO ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP          
SEQRES  17 A  323  PRO ASP LYS ASP VAL LEU GLY TRP GLY GLU ASN ASP ARG          
SEQRES  18 A  323  GLY VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS          
SEQRES  19 A  323  PHE LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA          
SEQRES  20 A  323  HIS GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS          
SEQRES  21 A  323  ARG GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CYS          
SEQRES  22 A  323  GLY GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP          
SEQRES  23 A  323  GLU THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA          
SEQRES  24 A  323  GLU LYS LYS LYS PRO ASN ALA THR ARG PRO VAL THR PRO          
SEQRES  25 A  323  PRO ARG GLY MET ILE THR LYS GLN ALA LYS LYS                  
SEQRES   1 B    5  ACB VAL 1ZN FGA MDH                                          
HET    ACB  B   1       9                                                       
HET    1ZN  B   3      23                                                       
HET    FGA  B   4       9                                                       
HET    MDH  B   5       7                                                       
HET    BME  A 604       4                                                       
HET    BME  A 605       4                                                       
HET     MN  A 400       1                                                       
HET     MN  A 401       1                                                       
HET     MN  A 402       1                                                       
HET     MN  A 403       1                                                       
HET     MN  A 404       1                                                       
HET     MN  A 405       1                                                       
HET     MN  A 406       1                                                       
HET     MN  A 407       1                                                       
HETNAM     ACB 3-METHYL-BETA-D-ASPARTIC ACID                                    
HETNAM     1ZN (2S,3S,4E,6E,8S,9S)-3-AMINO-9-METHOXY-2,6,8-TRIMETHYL-           
HETNAM   2 1ZN  10-PHENYLDECA-4,6-DIENOIC ACID                                  
HETNAM     FGA GAMMA-D-GLUTAMIC ACID                                            
HETNAM     MDH N-METHYLDEHYDROBUTYRINE                                          
HETNAM     BME BETA-MERCAPTOETHANOL                                             
HETNAM      MN MANGANESE (II) ION                                               
HETSYN     ACB (3S)-3-METHYL-D-ASPARTIC ACID; D-METHYL ASPARTIC ACID            
HETSYN     FGA D-GLUTAMIC ACID                                                  
FORMUL   2  ACB    C5 H9 N O4                                                   
FORMUL   2  1ZN    C20 H29 N O3                                                 
FORMUL   2  FGA    C5 H9 N O4                                                   
FORMUL   2  MDH    C5 H9 N O2                                                   
FORMUL   3  BME    2(C2 H6 O S)                                                 
FORMUL   5   MN    8(MN 2+)                                                     
FORMUL  13  HOH   *73(H2 O)                                                     
HELIX    1   1 ASN A    8  GLU A   18  1                                  11    
HELIX    2   2 GLN A   31  GLN A   49  1                                  19    
HELIX    3   3 GLN A   68  GLY A   80  1                                  13    
HELIX    4   4 GLN A   99  TYR A  114  1                                  16    
HELIX    5   5 CYS A  127  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  HIS A  239  1                                  12    
HELIX   11  11 ASN A  271  GLU A  275  5                                   5    
SHEET    1   A 6 LEU A  52  LEU A  55  0                                        
SHEET    2   A 6 ALA A 162  VAL A 165  1  O  ILE A 164   N  LEU A  55           
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  ARG A 246           
SHEET    6   A 6 TYR A 255  PHE A 258 -1  N  GLU A 256   O  THR A 265           
SHEET    1   B 5 PHE A 118  LEU A 120  0                                        
SHEET    2   B 5 TYR A  87  PHE A  89  1  N  TYR A  87   O  PHE A 119           
SHEET    3   B 5 LEU A  59  CYS A  62  1  N  CYS A  62   O  LEU A  88           
SHEET    4   B 5 GLY A 280  VAL A 285 -1  O  MET A 283   N  ILE A  61           
SHEET    5   B 5 CYS A 291  LEU A 296 -1  O  LEU A 296   N  GLY A 280           
SHEET    1   C 3 ASP A 208  PRO A 209  0                                        
SHEET    2   C 3 PHE A 225  PHE A 227  1  O  PHE A 227   N  ASP A 208           
SHEET    3   C 3 TRP A 216  GLU A 218 -1  N  GLY A 217   O  THR A 226           
LINK         CG  ACB B   1                 N   VAL B   2     1555   1555  1.32  
LINK         C   VAL B   2                 N1  1ZN B   3     1555   1555  1.33  
LINK         C20 1ZN B   3                 N   FGA B   4     1555   1555  1.33  
LINK         OD2 ASP A  64                MN    MN A 401     1555   1555  1.92  
LINK         OD1 ASN A 124                MN    MN A 400     1555   1555  1.94  
LINK         OD2 ASP A  92                MN    MN A 401     1555   1555  2.00  
LINK         OD2 ASP A  92                MN    MN A 400     1555   1555  2.02  
LINK         NE2 HIS A 173                MN    MN A 400     1555   1555  2.03  
LINK         NE2 HIS A  66                MN    MN A 401     1555   1555  2.06  
LINK         ND1 HIS A 248                MN    MN A 400     1555   1555  2.07  
LINK        MN    MN A 401                 O   HOH A 638     1555   1555  2.10  
LINK         N   ACB B   1                 C   MDH B   5     1555   1555  1.32  
LINK         CD  FGA B   4                 N   MDH B   5     1555   1555  1.37  
LINK         SG  CYS A 202                 S2  BME A 605     1555   1555  2.04  
LINK         SG  CYS A 127                 S2  BME A 604     1555   1555  2.09  
CISPEP   1 ALA A   57    PRO A   58          0         0.82                     
CISPEP   2 PRO A   82    PRO A   83          0         8.93                     
CISPEP   3 ARG A  191    PRO A  192          0        -2.17                     
SITE     1 AC1  6 ASN A 124  GLU A 126  CYS A 127  SER A 129                    
SITE     2 AC1  6 TRP A 206  1ZN B   3                                          
SITE     1 AC2  4 VAL A 195  GLN A 198  CYS A 202  TRP A 206                    
SITE     1 AC3  5 ASP A  92  ASN A 124  HIS A 173  HIS A 248                    
SITE     2 AC3  5  MN A 401                                                     
SITE     1 AC4  5 ASP A  64  HIS A  66  ASP A  92   MN A 400                    
SITE     2 AC4  5 HOH A 638                                                     
SITE     1 AC5  2 ILE A 146  LYS A 147                                          
SITE     1 AC6  1 SER A  22                                                     
SITE     1 AC7  1 MET A 183                                                     
SITE     1 AC8  2 ALA A 259  LYS A 260                                          
SITE     1 AC9 20 ARG A  96  SER A 129  TYR A 134  GLN A 185                    
SITE     2 AC9 20 ARG A 188  ASP A 220  ARG A 221  VAL A 223                    
SITE     3 AC9 20 HIS A 237  TYR A 272  CYS A 273  GLU A 275                    
SITE     4 AC9 20 PHE A 276  BME A 604  HOH A 608  HOH A 627                    
SITE     5 AC9 20 HOH A 650  HOH A 657  HOH A 662  HOH A 673                    
CRYST1  100.955  100.955   63.485  90.00  90.00  90.00 P 42 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009910  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009910  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015750        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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