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Database: PDB
Entry: 3E7A
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Original site: 3E7A 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           18-AUG-08   3E7A              
TITLE     CRYSTAL STRUCTURE OF PROTEIN PHOSPHATASE-1 BOUND TO THE NATURAL TOXIN 
TITLE    2 NODULARIN-R                                                          
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;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: NODULARIN R;                                               
COMPND  11 CHAIN: C, D;                                                         
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PPP1CA, PPP1A;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: IN HOUSE DERIVED;                         
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: NODULARIA SPUMIGENA;                            
SOURCE  14 ORGANISM_TAXID: 70799                                                
KEYWDS    CARBOHYDRATE METABOLISM, CELL CYCLE, CELL DIVISION, GLYCOGEN          
KEYWDS   2 METABOLISM, HYDROLASE, IRON, MANGANESE, METAL-BINDING,               
KEYWDS   3 PHOSPHOPROTEIN, PROTEIN PHOSPHATASE, HYDROLASE-HYDROLASE INHIBITOR   
KEYWDS   4 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.S.KELKER,R.PAGE,W.PETI                                              
REVDAT   5   25-OCT-17 3E7A    1       REMARK                                   
REVDAT   4   10-APR-13 3E7A    1       REMARK                                   
REVDAT   3   13-JUL-11 3E7A    1       VERSN                                    
REVDAT   2   13-JAN-09 3E7A    1       JRNL   VERSN                             
REVDAT   1   04-NOV-08 3E7A    0                                                
JRNL        AUTH   M.S.KELKER,R.PAGE,W.PETI                                     
JRNL        TITL   CRYSTAL STRUCTURES OF PROTEIN PHOSPHATASE-1 BOUND TO         
JRNL        TITL 2 NODULARIN-R AND TAUTOMYCIN: A NOVEL SCAFFOLD FOR             
JRNL        TITL 3 STRUCTURE-BASED DRUG DESIGN OF SERINE/THREONINE PHOSPHATASE  
JRNL        TITL 4 INHIBITORS                                                   
JRNL        REF    J.MOL.BIOL.                   V. 385    11 2009              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   18992256                                                     
JRNL        DOI    10.1016/J.JMB.2008.10.053                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.63 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 1.63                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 79699                          
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) : 0.144                           
REMARK   3   R VALUE            (WORKING SET) : 0.143                           
REMARK   3   FREE R VALUE                     : 0.169                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4185                            
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) : 1.63                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5611                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.74                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2120                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 286                          
REMARK   3   BIN FREE R VALUE                    : 0.2590                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4753                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 682                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.38000                                             
REMARK   3    B22 (A**2) : 0.15000                                              
REMARK   3    B33 (A**2) : 0.23000                                              
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): 0.075         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.075         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.046         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.373         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.971                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.961                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5080 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3486 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6926 ; 1.374 ; 1.997       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8498 ; 0.930 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   647 ; 6.607 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   240 ;32.809 ;23.833       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   850 ;10.805 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    34 ;16.732 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   757 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5756 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1105 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1067 ; 0.219 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3896 ; 0.203 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2526 ; 0.181 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2603 ; 0.083 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   494 ; 0.163 ; 0.200       
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):    13 ; 0.183 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    41 ; 0.228 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    45 ; 0.195 ; 0.200       
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):  3033 ; 1.230 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1221 ; 0.318 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4883 ; 1.954 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2229 ; 3.066 ; 8.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2010 ; 4.418 ;11.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 10                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     7        A    21                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.7446 -25.5462  -6.6025              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0698 T22:   0.0167                                     
REMARK   3      T33:   0.0016 T12:   0.0009                                     
REMARK   3      T13:  -0.0051 T23:  -0.0078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1623 L22:   3.7081                                     
REMARK   3      L33:   1.4901 L12:  -0.3390                                     
REMARK   3      L13:   1.1157 L23:  -0.4632                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0070 S12:   0.0562 S13:  -0.0241                       
REMARK   3      S21:  -0.0529 S22:  -0.0047 S23:   0.0667                       
REMARK   3      S31:   0.0296 S32:  -0.2119 S33:   0.0116                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    22        A    40                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.7655 -25.7022  -7.5893              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0537 T22:  -0.0032                                     
REMARK   3      T33:  -0.0089 T12:   0.0035                                     
REMARK   3      T13:  -0.0146 T23:  -0.0075                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2778 L22:   0.1159                                     
REMARK   3      L33:   1.0877 L12:  -0.1707                                     
REMARK   3      L13:  -0.3737 L23:   0.3099                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0218 S12:   0.0929 S13:  -0.0556                       
REMARK   3      S21:  -0.0969 S22:   0.0030 S23:   0.0310                       
REMARK   3      S31:  -0.0198 S32:  -0.0272 S33:   0.0188                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    41        A   186                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.4146 -24.0622   8.0421              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0552 T22:  -0.0167                                     
REMARK   3      T33:  -0.0254 T12:  -0.0033                                     
REMARK   3      T13:  -0.0065 T23:   0.0102                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4826 L22:   0.6520                                     
REMARK   3      L33:   0.6332 L12:  -0.0319                                     
REMARK   3      L13:  -0.2837 L23:  -0.0158                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0117 S12:  -0.0494 S13:  -0.0183                       
REMARK   3      S21:   0.0816 S22:  -0.0123 S23:  -0.0082                       
REMARK   3      S31:  -0.0119 S32:   0.0346 S33:   0.0006                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   187        A   200                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.9798 -14.4878  16.5892              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0054 T22:   0.0368                                     
REMARK   3      T33:   0.0131 T12:  -0.0451                                     
REMARK   3      T13:  -0.0468 T23:  -0.0178                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3786 L22:   2.9493                                     
REMARK   3      L33:   1.5031 L12:  -0.6727                                     
REMARK   3      L13:  -0.0511 L23:  -0.4850                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0079 S12:  -0.0702 S13:   0.2171                       
REMARK   3      S21:   0.3724 S22:  -0.0544 S23:  -0.3200                       
REMARK   3      S31:  -0.2034 S32:   0.2191 S33:   0.0465                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   201        A   299                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.3289 -32.8039  22.3471              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0444 T22:   0.0330                                     
REMARK   3      T33:  -0.0192 T12:   0.0106                                     
REMARK   3      T13:  -0.0079 T23:   0.0426                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6965 L22:   0.9075                                     
REMARK   3      L33:   0.5948 L12:   0.0802                                     
REMARK   3      L13:  -0.3130 L23:   0.0638                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0581 S12:  -0.1894 S13:  -0.1170                       
REMARK   3      S21:   0.2623 S22:  -0.0060 S23:  -0.0142                       
REMARK   3      S31:   0.0602 S32:   0.1147 S33:   0.0641                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     7        B    21                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.0072 -38.9372  46.0518              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0270 T22:  -0.0427                                     
REMARK   3      T33:  -0.0081 T12:  -0.0090                                     
REMARK   3      T13:  -0.0005 T23:  -0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0008 L22:   2.1452                                     
REMARK   3      L33:   2.8855 L12:   0.2865                                     
REMARK   3      L13:   1.7380 L23:   0.1441                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0447 S12:  -0.0709 S13:   0.0776                       
REMARK   3      S21:   0.0700 S22:   0.0138 S23:  -0.0734                       
REMARK   3      S31:  -0.2190 S32:   0.1166 S33:   0.0309                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    22        B    49                          
REMARK   3    ORIGIN FOR THE GROUP (A): -36.3817 -46.0101  41.9984              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0492 T22:  -0.0418                                     
REMARK   3      T33:  -0.0060 T12:  -0.0015                                     
REMARK   3      T13:   0.0010 T23:   0.0141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6595 L22:   0.7948                                     
REMARK   3      L33:   1.3836 L12:  -0.0310                                     
REMARK   3      L13:   0.3089 L23:  -0.0949                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0099 S12:  -0.0708 S13:   0.0449                       
REMARK   3      S21:   0.0307 S22:  -0.0024 S23:   0.0716                       
REMARK   3      S31:  -0.0334 S32:  -0.0613 S33:   0.0122                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    50        B   181                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.0100 -47.7932  31.3207              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0357 T22:  -0.0504                                     
REMARK   3      T33:  -0.0210 T12:  -0.0056                                     
REMARK   3      T13:  -0.0050 T23:   0.0151                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5058 L22:   0.6830                                     
REMARK   3      L33:   0.6491 L12:   0.1183                                     
REMARK   3      L13:  -0.0683 L23:   0.0287                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0247 S12:   0.0257 S13:   0.0124                       
REMARK   3      S21:  -0.0905 S22:   0.0209 S23:   0.0347                       
REMARK   3      S31:  -0.0078 S32:  -0.0126 S33:   0.0038                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   182        B   198                          
REMARK   3    ORIGIN FOR THE GROUP (A): -45.7654 -52.0833  20.0553              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0027 T22:   0.0410                                     
REMARK   3      T33:   0.0369 T12:  -0.0297                                     
REMARK   3      T13:  -0.0643 T23:  -0.0024                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4438 L22:   1.0190                                     
REMARK   3      L33:   1.9216 L12:  -0.5127                                     
REMARK   3      L13:  -0.5708 L23:  -0.0523                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0564 S12:   0.1929 S13:  -0.0774                       
REMARK   3      S21:  -0.2131 S22:  -0.0094 S23:   0.2202                       
REMARK   3      S31:   0.0234 S32:  -0.3722 S33:   0.0657                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   199        B   299                          
REMARK   3    ORIGIN FOR THE GROUP (A): -25.7101 -50.6155  16.1721              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0466 T22:   0.0041                                     
REMARK   3      T33:  -0.0230 T12:  -0.0231                                     
REMARK   3      T13:   0.0199 T23:   0.0081                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7956 L22:   0.7897                                     
REMARK   3      L33:   0.5866 L12:   0.1230                                     
REMARK   3      L13:  -0.1001 L23:  -0.0226                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0811 S12:   0.1721 S13:  -0.0427                       
REMARK   3      S21:  -0.2599 S22:   0.0468 S23:  -0.0641                       
REMARK   3      S31:   0.0221 S32:   0.0264 S33:   0.0343                       
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 3E7A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-AUG-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000048964.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-FEB-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X6A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : MONOCHROMATOR: SI(111) CHANNEL     
REMARK 200                                   CUT MONOCHROMATOR.                 
REMARK 200  OPTICS                         : OXFORD DANFYSIK TOROIDAL           
REMARK 200                                   FOCUSING MIRROR.                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 83444                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.630                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.63                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.51000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1FJM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350 AND 0.2 M NAI, PH 7.0,      
REMARK 280  UNDER PARAFIN OIL, TEMPERATURE 298K, MICROBATCH                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       32.67700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.22200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.63700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.22200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.67700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.63700            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3190 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2930 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400                                                                      
REMARK 400 THE NODULARIN-R IS OLIGOPEPTIDE, A MEMBER OF TOXIN CLASS.            
REMARK 400                                                                      
REMARK 400  GROUP: 1                                                            
REMARK 400   NAME: NODULARIN-R                                                  
REMARK 400   CHAIN: C, D                                                        
REMARK 400   COMPONENT_1: PEPTIDE LIKE POLYMER                                  
REMARK 400   DESCRIPTION: NULL                                                  
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     MET A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     ASP A   300                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     MET B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     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  26    NZ                                                  
REMARK 470     LYS A  41    CD   CE   NZ                                        
REMARK 470     LYS A  98    NZ                                                  
REMARK 470     LYS A 211    CG   CD   CE   NZ                                   
REMARK 470     GLN A 214    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 218    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 230    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 234    CG   CD   CE   NZ                                   
REMARK 470     LYS A 260    CD   CE   NZ                                        
REMARK 470     GLU A 275    OE1  OE2                                            
REMARK 470     ARG B  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  26    NZ                                                  
REMARK 470     GLU B  77    CD   OE1  OE2                                       
REMARK 470     LYS B 211    CE   NZ                                             
REMARK 470     GLN B 214    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 218    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 230    CD   OE1  OE2                                       
REMARK 470     LYS B 234    CG   CD   CE   NZ                                   
REMARK 470     LYS B 260    CD   CE   NZ                                        
REMARK 470     GLU B 275    OE1  OE2                                            
REMARK 470     GLU B 287    CG   CD   OE1  OE2                                  
REMARK 470     ARG D   2    CD   NE   CZ   NH1  NH2                             
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    GLN A   214     O    HOH A   652              1.90            
REMARK 500   O    HOH A   689     O    HOH A   690              1.96            
REMARK 500   O    HOH B   464     O    HOH B   555              2.03            
REMARK 500   ND2  ASN B   271     O    PHE B   276              2.15            
REMARK 500   OE2  GLU B    32     O    HOH B   447              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   473     O    HOH B   690     2444     2.06            
REMARK 500   OG   SER A   129     O    HOH A   499     4545     2.17            
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    ARG A  43   CB  -  CA  -  C   ANGL. DEV. =  13.2 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    ARG A  23       60.49     69.39                                   
REMARK 500    ASP A  95      153.18     77.32                                   
REMARK 500    ARG A  96      -49.75     76.58                                   
REMARK 500    TYR A 144     -114.56   -136.61                                   
REMARK 500    GLN A 214      -71.68    -77.38                                   
REMARK 500    SER A 224     -152.30     59.72                                   
REMARK 500    ALA A 247     -132.18   -132.25                                   
REMARK 500    HIS A 248      -27.11     82.94                                   
REMARK 500    ARG B  23       62.91     67.70                                   
REMARK 500    ASP B  95      151.72     79.16                                   
REMARK 500    ARG B  96      -48.70     77.26                                   
REMARK 500    TYR B 144     -111.89   -137.21                                   
REMARK 500    SER B 224     -153.86     65.74                                   
REMARK 500    ALA B 247     -126.32   -133.69                                   
REMARK 500    HIS B 248      -25.19     78.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 SER A   22     ARG A   23                   41.80                    
REMARK 500 SER B   22     ARG B   23                   35.62                    
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 B 403  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 698   O                                                      
REMARK 620 2 ASN B 124   OD1 128.2                                              
REMARK 620 3 HIS B 173   NE2 134.9  95.8                                        
REMARK 620 4 ASP B  92   OD2  79.6  95.6  87.7                                  
REMARK 620 5 HIS B 248   ND1  91.7  97.4  91.7 167.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 403  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 669   O                                                      
REMARK 620 2 ASN A 124   OD1 126.3                                              
REMARK 620 3 HIS A 173   NE2 136.0  95.8                                        
REMARK 620 4 HIS A 248   ND1  90.7 100.9  93.3                                  
REMARK 620 5 ASP A  92   OD2  79.2  93.6  86.9 165.4                            
REMARK 620 N                    1     2     3     4                             
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 HOH A 669   O   105.5                                              
REMARK 620 3 HIS A  66   NE2 106.3 147.4                                        
REMARK 620 4 HOH C 769   O   103.0  93.9  85.8                                  
REMARK 620 5 ASP A  92   OD2  93.5  77.9  93.3 163.1                            
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  64   OD2                                                    
REMARK 620 2 HOH B 698   O   102.4                                              
REMARK 620 3 HOH D 724   O   101.6  94.4                                        
REMARK 620 4 HIS B  66   NE2 105.8 151.1  85.8                                  
REMARK 620 5 ASP B  92   OD2  93.8  76.8 163.8  95.4                            
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 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 408                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI B 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF nodularin R            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF nodularin R            
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JK7   RELATED DB: PDB                                   
REMARK 900 PP1:OKADAIC ACID CO-CRYSTAL STRUCTURE                                
REMARK 900 RELATED ID: 1IT6   RELATED DB: PDB                                   
REMARK 900 PP1:CALYCULIN A CO-CRYSTAL STRUCTURE                                 
REMARK 900 RELATED ID: 1FJM   RELATED DB: PDB                                   
REMARK 900 PP1 COMPLEXED WITH MICROCYSTIN-LR                                    
REMARK 900 RELATED ID: 2BCD   RELATED DB: PDB                                   
REMARK 900 PP1 COMPLEXED WITH NODULARIN-V (MOTUPORIN)                           
REMARK 900 RELATED ID: 3E7B   RELATED DB: PDB                                   
DBREF  3E7A A    7   300  UNP    P62136   PP1A_HUMAN       7    300             
DBREF  3E7A B    7   300  UNP    P62136   PP1A_HUMAN       7    300             
DBREF  3E7A C    1     5  NOR    NOR00279 NOR00279         1      5             
DBREF  3E7A D    1     5  NOR    NOR00279 NOR00279         1      5             
SEQADV 3E7A GLY A    2  UNP  P62136              EXPRESSION TAG                 
SEQADV 3E7A HIS A    3  UNP  P62136              EXPRESSION TAG                 
SEQADV 3E7A MET A    4  UNP  P62136              EXPRESSION TAG                 
SEQADV 3E7A GLY A    5  UNP  P62136              EXPRESSION TAG                 
SEQADV 3E7A SER A    6  UNP  P62136              EXPRESSION TAG                 
SEQADV 3E7A GLY B    2  UNP  P62136              EXPRESSION TAG                 
SEQADV 3E7A HIS B    3  UNP  P62136              EXPRESSION TAG                 
SEQADV 3E7A MET B    4  UNP  P62136              EXPRESSION TAG                 
SEQADV 3E7A GLY B    5  UNP  P62136              EXPRESSION TAG                 
SEQADV 3E7A 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          
SEQRES   1 C    5  ACB ARG 1ZN FGA MDH                                          
SEQRES   1 D    5  ACB ARG 1ZN FGA MDH                                          
HET    ACB  C   1       9                                                       
HET    1ZN  C   3      23                                                       
HET    FGA  C   4       9                                                       
HET    MDH  C   5       7                                                       
HET    ACB  D   1       9                                                       
HET    1ZN  D   3      23                                                       
HET    FGA  D   4       9                                                       
HET    MDH  D   5       7                                                       
HET     MN  A 402       1                                                       
HET     MN  A 403       1                                                       
HET    IOD  A 301       2                                                       
HET    IOD  A 302       2                                                       
HET    IOD  A 303       1                                                       
HET    IOD  A 404       2                                                       
HET    IOD  A 405       2                                                       
HET    IOD  A 406       2                                                       
HET    IOD  A 407       2                                                       
HET     CL  A 408       1                                                       
HET     CL  A 304       1                                                       
HET     CL  A 305       1                                                       
HET    GOL  A 409       6                                                       
HET     MN  B 402       1                                                       
HET     MN  B 403       1                                                       
HET    IOD  B 301       2                                                       
HET    IOD  B 302       2                                                       
HET    IOD  B 404       1                                                       
HET    IOD  B 405       1                                                       
HET    IOD  B 407       2                                                       
HET    IOD  B 406       2                                                       
HET    IOD  B 408       2                                                       
HET     CL  B 409       1                                                       
HET    AZI  B 303       3                                                       
HET    AZI  B 410       3                                                       
HET    GOL  B 411       6                                                       
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      MN MANGANESE (II) ION                                               
HETNAM     IOD IODIDE ION                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETNAM     AZI AZIDE ION                                                        
HETSYN     ACB (3S)-3-METHYL-D-ASPARTIC ACID; D-METHYL ASPARTIC ACID            
HETSYN     FGA D-GLUTAMIC ACID                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  ACB    2(C5 H9 N O4)                                                
FORMUL   3  1ZN    2(C20 H29 N O3)                                              
FORMUL   3  FGA    2(C5 H9 N O4)                                                
FORMUL   3  MDH    2(C5 H9 N O2)                                                
FORMUL   5   MN    4(MN 2+)                                                     
FORMUL   7  IOD    14(I 1-)                                                     
FORMUL  14   CL    4(CL 1-)                                                     
FORMUL  17  GOL    2(C3 H8 O3)                                                  
FORMUL  28  AZI    2(N3 1-)                                                     
FORMUL  31  HOH   *682(H2 O)                                                    
HELIX    1   1 ASN A    8  GLU A   18  1                                  11    
HELIX    2   2 THR A   31  GLN A   49  1                                  19    
HELIX    3   3 GLN A   68  GLY A   80  1                                  13    
HELIX    4   4 GLN A   99  TYR A  114  1                                  16    
HELIX    5   5 CYS A  127  GLY A  135  1                                   9    
HELIX    6   6 GLY A  135  TYR A  144  1                                  10    
HELIX    7   7 ASN A  145  ASN A  157  1                                  13    
HELIX    8   8 MET A  183  ARG A  188  1                                   6    
HELIX    9   9 GLY A  199  SER A  207  1                                   9    
HELIX   10  10 GLY A  228  ASP A  240  1                                  13    
HELIX   11  11 ASN A  271  GLU A  275  5                                   5    
HELIX   12  12 ASN B    8  GLU B   18  1                                  11    
HELIX   13  13 THR B   31  GLN B   49  1                                  19    
HELIX   14  14 GLN B   68  GLY B   80  1                                  13    
HELIX   15  15 GLN B   99  TYR B  114  1                                  16    
HELIX   16  16 CYS B  127  GLY B  135  1                                   9    
HELIX   17  17 GLY B  135  TYR B  144  1                                  10    
HELIX   18  18 ASN B  145  ASN B  157  1                                  13    
HELIX   19  19 MET B  183  ARG B  188  1                                   6    
HELIX   20  20 GLY B  199  SER B  207  1                                   9    
HELIX   21  21 GLY B  228  ASP B  240  1                                  13    
HELIX   22  22 ASN B  271  GLU B  275  5                                   5    
SHEET    1   A 6 LEU A  52  LEU A  55  0                                        
SHEET    2   A 6 ALA A 162  VAL A 165  1  O  ALA A 162   N  LEU A  53           
SHEET    3   A 6 ILE A 169  CYS A 172 -1  O  CYS A 171   N  ALA A 163           
SHEET    4   A 6 LEU A 243  ARG A 246  1  O  CYS A 245   N  PHE A 170           
SHEET    5   A 6 LEU A 263  LEU A 266  1  O  LEU A 266   N  ARG A 246           
SHEET    6   A 6 TYR A 255  PHE A 258 -1  N  GLU A 256   O  THR A 265           
SHEET    1   B 5 PHE A 118  LEU A 120  0                                        
SHEET    2   B 5 TYR A  87  PHE A  89  1  N  PHE A  89   O  PHE A 119           
SHEET    3   B 5 LEU A  59  CYS A  62  1  N  CYS A  62   O  LEU A  88           
SHEET    4   B 5 GLY A 280  VAL A 285 -1  O  MET A 283   N  ILE A  61           
SHEET    5   B 5 CYS A 291  LEU A 296 -1  O  LEU A 296   N  GLY A 280           
SHEET    1   C 3 ASP A 208  PRO A 209  0                                        
SHEET    2   C 3 PHE A 225  PHE A 227  1  O  PHE A 227   N  ASP A 208           
SHEET    3   C 3 TRP A 216  GLU A 218 -1  N  GLY A 217   O  THR A 226           
SHEET    1   D 6 LEU B  52  LEU B  55  0                                        
SHEET    2   D 6 ALA B 162  VAL B 165  1  O  ILE B 164   N  LEU B  53           
SHEET    3   D 6 ILE B 169  CYS B 172 -1  O  CYS B 171   N  ALA B 163           
SHEET    4   D 6 LEU B 243  ARG B 246  1  O  CYS B 245   N  PHE B 170           
SHEET    5   D 6 LEU B 263  LEU B 266  1  O  VAL B 264   N  ARG B 246           
SHEET    6   D 6 TYR B 255  PHE B 258 -1  N  PHE B 258   O  LEU B 263           
SHEET    1   E 5 PHE B 118  LEU B 120  0                                        
SHEET    2   E 5 TYR B  87  PHE B  89  1  N  PHE B  89   O  PHE B 119           
SHEET    3   E 5 LEU B  59  CYS B  62  1  N  LYS B  60   O  LEU B  88           
SHEET    4   E 5 GLY B 280  VAL B 285 -1  O  VAL B 285   N  LEU B  59           
SHEET    5   E 5 CYS B 291  LEU B 296 -1  O  LEU B 296   N  GLY B 280           
SHEET    1   F 3 ASP B 208  PRO B 209  0                                        
SHEET    2   F 3 PHE B 225  PHE B 227  1  O  PHE B 227   N  ASP B 208           
SHEET    3   F 3 TRP B 216  GLU B 218 -1  N  GLY B 217   O  THR B 226           
LINK         CG  ACB C   1                 N   ARG C   2     1555   1555  1.33  
LINK         C   ARG C   2                 N1  1ZN C   3     1555   1555  1.34  
LINK         C20 1ZN C   3                 N   FGA C   4     1555   1555  1.33  
LINK         CG  ACB D   1                 N   ARG D   2     1555   1555  1.33  
LINK         C   ARG D   2                 N1  1ZN D   3     1555   1555  1.35  
LINK         C20 1ZN D   3                 N   FGA D   4     1555   1555  1.34  
LINK        MN    MN B 403                 O   HOH B 698     1555   1555  1.99  
LINK        MN    MN A 403                 O   HOH A 669     1555   1555  2.00  
LINK         OD1 ASN B 124                MN    MN B 403     1555   1555  2.06  
LINK         OD2 ASP A  64                MN    MN A 402     1555   1555  2.06  
LINK        MN    MN A 402                 O   HOH A 669     1555   1555  2.07  
LINK         OD1 ASN A 124                MN    MN A 403     1555   1555  2.08  
LINK         OD2 ASP B  64                MN    MN B 402     1555   1555  2.08  
LINK        MN    MN B 402                 O   HOH B 698     1555   1555  2.09  
LINK        MN    MN B 402                 O   HOH D 724     1555   1555  2.14  
LINK         NE2 HIS B 173                MN    MN B 403     1555   1555  2.17  
LINK         NE2 HIS A 173                MN    MN A 403     1555   1555  2.19  
LINK         NE2 HIS A  66                MN    MN A 402     1555   1555  2.20  
LINK         NE2 HIS B  66                MN    MN B 402     1555   1555  2.20  
LINK         OD2 ASP B  92                MN    MN B 403     1555   1555  2.20  
LINK        MN    MN A 402                 O   HOH C 769     1555   1555  2.21  
LINK         ND1 HIS A 248                MN    MN A 403     1555   1555  2.23  
LINK         ND1 HIS B 248                MN    MN B 403     1555   1555  2.23  
LINK         OD2 ASP B  92                MN    MN B 402     1555   1555  2.24  
LINK         OD2 ASP A  92                MN    MN A 402     1555   1555  2.24  
LINK         OD2 ASP A  92                MN    MN A 403     1555   1555  2.24  
LINK         N   ACB D   1                 C   MDH D   5     1555   1555  1.33  
LINK         N   ACB C   1                 C   MDH C   5     1555   1555  1.33  
LINK         CD  FGA C   4                 N   MDH C   5     1555   1555  1.34  
LINK         CD  FGA D   4                 N   MDH D   5     1555   1555  1.35  
CISPEP   1 ALA A   57    PRO A   58          0         3.71                     
CISPEP   2 PRO A   82    PRO A   83          0         3.18                     
CISPEP   3 ARG A  191    PRO A  192          0         1.90                     
CISPEP   4 ALA B   57    PRO B   58          0         1.82                     
CISPEP   5 PRO B   82    PRO B   83          0         7.02                     
CISPEP   6 ARG B  191    PRO B  192          0         0.22                     
SITE     1 AC1  6 ASP A  64  HIS A  66  ASP A  92   MN A 403                    
SITE     2 AC1  6 HOH A 669  HOH C 769                                          
SITE     1 AC2  6 ASP A  92  ASN A 124  HIS A 173  HIS A 248                    
SITE     2 AC2  6  MN A 402  HOH A 669                                          
SITE     1 AC3  3 LYS A 260  GLN A 262  HOH A 681                               
SITE     1 AC4  3 LYS A 113  ARG A 132  HOH A 591                               
SITE     1 AC5  6 GLY A  97  SER A 100  GLY A 135  PHE A 136                    
SITE     2 AC5  6 GLU A 139  HOH A 483                                          
SITE     1 AC6  3 ARG A 261  ILE B 295  HOH B 548                               
SITE     1 AC7  2 LYS A 260  ARG A 261                                          
SITE     1 AC8  2 GLN A  99   CL A 304                                          
SITE     1 AC9  1 HOH A 636                                                     
SITE     1 BC1  3 ARG A 142  HOH A 530  HOH A 720                               
SITE     1 BC2  3 LYS A  98  IOD A 406  HOH A 740                               
SITE     1 BC3  6 GLN A 198  GLY A 199  ASP A 203  PHE A 225                    
SITE     2 BC3  6 HOH A 449  HOH A 761                                          
SITE     1 BC4  7 GLN A  49  PRO A  50  GLU A  54  PHE A 119                    
SITE     2 BC4  7 HOH A 533  HOH A 643  HOH A 655                               
SITE     1 BC5  6 ASP B  64  HIS B  66  ASP B  92   MN B 403                    
SITE     2 BC5  6 HOH B 698  HOH D 724                                          
SITE     1 BC6  6 ASP B  92  ASN B 124  HIS B 173  HIS B 248                    
SITE     2 BC6  6  MN B 402  HOH B 698                                          
SITE     1 BC7  2 ILE A 295  ARG B 261                                          
SITE     1 BC8  2 LYS B 260  ARG B 261                                          
SITE     1 BC9  6 GLY B  97  SER B 100  GLY B 135  PHE B 136                    
SITE     2 BC9  6 GLU B 139  HOH B 521                                          
SITE     1 CC1  2 GLN B 262  HOH B 703                                          
SITE     1 CC2  3 TYR B  69  TYR B  70  GLN B  99                               
SITE     1 CC3  3 GLY B 215  GLU B 230  VAL B 231                               
SITE     1 CC4  3 SER B 129  ARG B 132  HOH B 451                               
SITE     1 CC5  7 GLN B  49  PRO B  50  LEU B  53  GLU B  54                    
SITE     2 CC5  7 GLU B 116  PHE B 119  HOH B 667                               
SITE     1 CC6 22 ARG A  96  SER A 129  TYR A 134  VAL A 195                    
SITE     2 CC6 22 PRO A 196  TRP A 206  ASP A 220  ARG A 221                    
SITE     3 CC6 22 TYR A 272  GLU A 275  PHE A 276  GLU B 184                    
SITE     4 CC6 22 ARG B 187  HOH C 389  HOH C 766  HOH C 767                    
SITE     5 CC6 22 HOH C 768  HOH C 769  HOH C 770  HOH C 774                    
SITE     6 CC6 22 HOH C 775  HOH C 776                                          
SITE     1 CC7 20 ARG B  96  SER B 129  TYR B 134  VAL B 195                    
SITE     2 CC7 20 PRO B 196  ASP B 197  TRP B 206  ARG B 221                    
SITE     3 CC7 20 VAL B 223  TYR B 272  GLU B 275  PHE B 276                    
SITE     4 CC7 20 HOH B 607  HOH B 710  HOH D 719  HOH D 720                    
SITE     5 CC7 20 HOH D 721  HOH D 722  HOH D 723  HOH D 724                    
CRYST1   65.354   77.274  132.444  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      0.015301  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012941  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007550        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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