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Database: PDB
Entry: 2VGG
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HEADER    TRANSFERASE                             13-NOV-07   2VGG              
TITLE     HUMAN ERYTHROCYTE PYRUVATE KINASE: R479H MUTANT                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PYRUVATE KINASE ISOZYMES R/L;                              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: RESIDUES 47-574;                                           
COMPND   5 SYNONYM: R-TYPE/L-TYPE PYRUVATE KINASE, RED CELL/LIVER PYRUVATE      
COMPND   6 KINASE, PYRUVATE KINASE 1PYRUVATE KINASE;                            
COMPND   7 EC: 2.7.1.40;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21                                       
KEYWDS    METAL-BINDING, PHOSPHORYLATION, PYRUVATE KINASE IN THE ACTIVE R-      
KEYWDS   2 STATE, KINASE, PYRUVATE, MAGNESIUM, GLYCOLYSIS, TRANSFERASE, DISEASE 
KEYWDS   3 MUTATION                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.VALENTINI,L.R.CHIARELLI,R.FORTIN,M.DOLZAN,A.GALIZZI,D.J.ABRAHAM,    
AUTHOR   2 C.WANG,P.BIANCHI,A.ZANELLA,A.MATTEVI                                 
REVDAT   5   24-JUL-19 2VGG    1       REMARK LINK                              
REVDAT   4   07-DEC-11 2VGG    1       AUTHOR JRNL                              
REVDAT   3   13-JUL-11 2VGG    1       VERSN                                    
REVDAT   2   24-FEB-09 2VGG    1       VERSN                                    
REVDAT   1   20-NOV-07 2VGG    0                                                
SPRSDE     20-NOV-07 2VGG      1LIY                                             
JRNL        AUTH   G.VALENTINI,L.R.CHIARELLI,R.FORTIN,M.DOLZAN,A.GALIZZI,       
JRNL        AUTH 2 D.J.ABRAHAM,C.WANG,P.BIANCHI,A.ZANELLA,A.MATTEVI             
JRNL        TITL   STRUCTURE AND FUNCTION OF HUMAN ERYTHROCYTE PYRUVATE KINASE. 
JRNL        TITL 2 MOLECULAR BASIS OF NONSPHEROCYTIC HEMOLYTIC ANEMIA.          
JRNL        REF    J.BIOL.CHEM.                  V. 277 23807 2002              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   11960989                                                     
JRNL        DOI    10.1074/JBC.M202107200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.74 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.74                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 50700                          
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) : 0.254                           
REMARK   3   R VALUE            (WORKING SET) : 0.253                           
REMARK   3   FREE R VALUE                     : 0.294                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 759                             
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) : 2.74                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.81                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3553                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3870                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 49                           
REMARK   3   BIN FREE R VALUE                    : 0.4680                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 15181                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 124                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
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) : 58.18                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.73000                                              
REMARK   3    B22 (A**2) : -0.46000                                             
REMARK   3    B33 (A**2) : -0.31000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.04000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.456         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.461         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 50.583        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.918                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.882                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 15532 ; 0.025 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 21057 ; 1.952 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1986 ; 5.463 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   645 ;36.325 ;22.946       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2617 ;21.428 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   154 ;22.870 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2455 ; 0.115 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11543 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  7978 ; 0.293 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 10706 ; 0.342 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   816 ; 0.193 ; 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):   133 ; 0.477 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.373 ; 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):  9931 ; 0.593 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15985 ; 1.153 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5633 ; 1.966 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5072 ; 3.275 ; 4.500       
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 : 3                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     57       A     160      1                      
REMARK   3           1     B     57       B     160      1                      
REMARK   3           1     C     57       C     160      1                      
REMARK   3           1     D     57       D     160      1                      
REMARK   3           2     A    262       A     430      1                      
REMARK   3           2     B    262       B     430      1                      
REMARK   3           2     C    262       C     430      1                      
REMARK   3           2     D    262       D     430      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1959 ;  0.12 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):   1959 ;  0.08 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    C    (A):   1959 ;  0.10 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    D    (A):   1959 ;  0.09 ;  0.05           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1959 ;  0.20 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):   1959 ;  0.20 ;  0.50           
REMARK   3   TIGHT THERMAL      1    C (A**2):   1959 ;  0.18 ;  0.50           
REMARK   3   TIGHT THERMAL      1    D (A**2):   1959 ;  0.19 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    163       A     259      4                      
REMARK   3           1     B    163       B     259      4                      
REMARK   3           1     C    163       C     259      4                      
REMARK   3           1     D    163       D     259      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):    484 ;  0.24 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    B    (A):    484 ;  0.24 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    C    (A):    484 ;  0.24 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    D    (A):    484 ;  0.24 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    A (A**2):    484 ;  0.43 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    B (A**2):    484 ;  0.41 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    C (A**2):    484 ;  0.62 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    D (A**2):    484 ;  0.55 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    431       A     573      1                      
REMARK   3           1     B    431       B     573      1                      
REMARK   3           1     C    431       C     573      1                      
REMARK   3           1     D    431       D     573      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    A    (A):   1111 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    B    (A):   1111 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    C    (A):   1111 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    D    (A):   1111 ;  0.05 ;  0.05           
REMARK   3   TIGHT THERMAL      3    A (A**2):   1111 ;  0.08 ;  0.50           
REMARK   3   TIGHT THERMAL      3    B (A**2):   1111 ;  0.08 ;  0.50           
REMARK   3   TIGHT THERMAL      3    C (A**2):   1111 ;  0.08 ;  0.50           
REMARK   3   TIGHT THERMAL      3    D (A**2):   1111 ;  0.10 ;  0.50           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    57        A   160                          
REMARK   3    RESIDUE RANGE :   A   261        A   573                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.0448  -6.5808  37.5238              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1705 T22:  -0.2040                                     
REMARK   3      T33:  -0.1520 T12:   0.1448                                     
REMARK   3      T13:  -0.2430 T23:  -0.0774                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1236 L22:   2.3982                                     
REMARK   3      L33:   2.0558 L12:   0.3062                                     
REMARK   3      L13:   0.6065 L23:   0.6647                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2729 S12:   0.1544 S13:  -0.2716                       
REMARK   3      S21:  -0.0172 S22:  -0.0612 S23:   0.0449                       
REMARK   3      S31:   0.5666 S32:   0.0701 S33:  -0.2117                       
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   161        A   260                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.7559  24.0127  35.1570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0232 T22:   0.4014                                     
REMARK   3      T33:   0.5164 T12:  -0.1021                                     
REMARK   3      T13:   0.0138 T23:   0.0283                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.8016 L22:  12.7051                                     
REMARK   3      L33:   7.9372 L12:  -1.5759                                     
REMARK   3      L13:  -0.1045 L23:   1.0955                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2148 S12:   0.9201 S13:   1.4561                       
REMARK   3      S21:  -0.2764 S22:   0.0599 S23:  -1.7627                       
REMARK   3      S31:  -0.4010 S32:   0.8157 S33:  -0.2747                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    57        B   160                          
REMARK   3    RESIDUE RANGE :   B   261        B   573                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.1801 -28.3834  12.3039              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4207 T22:  -0.4810                                     
REMARK   3      T33:  -0.1092 T12:  -0.0822                                     
REMARK   3      T13:  -0.1693 T23:  -0.0618                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6082 L22:   1.7228                                     
REMARK   3      L33:   3.4685 L12:  -0.2763                                     
REMARK   3      L13:   0.8689 L23:  -0.5666                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0135 S12:  -0.1895 S13:  -0.0898                       
REMARK   3      S21:   0.4744 S22:   0.0273 S23:  -0.1238                       
REMARK   3      S31:   0.3487 S32:  -0.0345 S33:  -0.0139                       
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 :   B   161        B   260                          
REMARK   3    ORIGIN FOR THE GROUP (A): -39.5542 -21.0481   1.5240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1881 T22:   0.6249                                     
REMARK   3      T33:   0.5580 T12:  -0.1998                                     
REMARK   3      T13:   0.0404 T23:   0.2073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0112 L22:  17.0475                                     
REMARK   3      L33:  16.8906 L12:  -1.0320                                     
REMARK   3      L13:   1.7106 L23:  -4.5712                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5059 S12:  -0.1045 S13:   0.3727                       
REMARK   3      S21:   0.0737 S22:   1.1567 S23:   1.9141                       
REMARK   3      S31:  -0.4153 S32:  -1.7546 S33:  -0.6508                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    57        C   160                          
REMARK   3    RESIDUE RANGE :   C   261        C   573                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.0661  27.4348  31.8379              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0244 T22:  -0.3336                                     
REMARK   3      T33:  -0.0735 T12:   0.0328                                     
REMARK   3      T13:  -0.1540 T23:  -0.1260                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7131 L22:   1.5630                                     
REMARK   3      L33:   3.7718 L12:  -0.5921                                     
REMARK   3      L13:   1.9834 L23:  -0.6279                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1374 S12:  -0.2109 S13:   0.3233                       
REMARK   3      S21:  -0.1752 S22:  -0.0990 S23:   0.1560                       
REMARK   3      S31:  -0.1477 S32:  -0.2241 S33:   0.2364                       
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 :   C   161        C   260                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.7292  21.4319  67.7102              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4586 T22:  -0.2984                                     
REMARK   3      T33:  -0.0166 T12:  -0.0104                                     
REMARK   3      T13:  -0.1964 T23:  -0.1108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.5473 L22:   8.7578                                     
REMARK   3      L33:   9.7220 L12:  -2.2631                                     
REMARK   3      L13:   0.4965 L23:   0.6524                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2558 S12:   0.0071 S13:  -0.8036                       
REMARK   3      S21:   1.3216 S22:   0.0787 S23:  -0.1587                       
REMARK   3      S31:   0.5366 S32:  -0.1431 S33:  -0.3345                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    57        D   160                          
REMARK   3    RESIDUE RANGE :   D   261        D   573                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.5102   6.5089  -6.5473              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0412 T22:  -0.3915                                     
REMARK   3      T33:  -0.1490 T12:  -0.0268                                     
REMARK   3      T13:  -0.2012 T23:  -0.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4823 L22:   3.4287                                     
REMARK   3      L33:   1.9962 L12:   0.4870                                     
REMARK   3      L13:   0.3425 L23:   1.0577                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0716 S12:  -0.0122 S13:   0.2452                       
REMARK   3      S21:   0.1917 S22:  -0.0518 S23:   0.1222                       
REMARK   3      S31:  -0.1164 S32:  -0.1153 S33:   0.1233                       
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 :   D   161        D   260                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.5589 -21.7393 -29.5818              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8154 T22:  -0.3762                                     
REMARK   3      T33:  -0.0265 T12:  -0.0452                                     
REMARK   3      T13:  -0.2189 T23:  -0.1340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2985 L22:  15.2111                                     
REMARK   3      L33:  16.6223 L12:  -0.5677                                     
REMARK   3      L13:  -1.9813 L23:  -5.8172                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2938 S12:  -0.1774 S13:  -0.3608                       
REMARK   3      S21:  -2.3356 S22:  -0.0792 S23:   0.0148                       
REMARK   3      S31:   2.4924 S32:  -0.3281 S33:  -0.2146                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 2VGG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-NOV-07.                  
REMARK 100 THE DEPOSITION ID IS D_1290034412.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUL-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50701                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.6                               
REMARK 200  DATA REDUNDANCY                : 2.100                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CCP4                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 2VGB                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.4                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       85.89750            
REMARK 290   SMTRY3   2  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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 19100 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 89420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -118.5 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ARG 479 TO HIS                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ARG 479 TO HIS                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, ARG 479 TO HIS                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, ARG 479 TO HIS                        
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     LEU A    47                                                      
REMARK 465     THR A    48                                                      
REMARK 465     GLN A    49                                                      
REMARK 465     GLU A    50                                                      
REMARK 465     LEU A    51                                                      
REMARK 465     GLY A    52                                                      
REMARK 465     THR A    53                                                      
REMARK 465     ALA A    54                                                      
REMARK 465     PHE A    55                                                      
REMARK 465     PHE A    56                                                      
REMARK 465     GLN A    57                                                      
REMARK 465     GLN A    58                                                      
REMARK 465     GLN A    59                                                      
REMARK 465     GLN A    60                                                      
REMARK 465     LEU A    61                                                      
REMARK 465     PRO A    62                                                      
REMARK 465     ALA A    63                                                      
REMARK 465     LYS A   230                                                      
REMARK 465     ILE A   231                                                      
REMARK 465     GLY A   232                                                      
REMARK 465     PRO A   233                                                      
REMARK 465     SER A   574                                                      
REMARK 465     LEU B    47                                                      
REMARK 465     THR B    48                                                      
REMARK 465     GLN B    49                                                      
REMARK 465     GLU B    50                                                      
REMARK 465     LEU B    51                                                      
REMARK 465     GLY B    52                                                      
REMARK 465     THR B    53                                                      
REMARK 465     ALA B    54                                                      
REMARK 465     PHE B    55                                                      
REMARK 465     PHE B    56                                                      
REMARK 465     ALA B    63                                                      
REMARK 465     ALA B    64                                                      
REMARK 465     MET B    65                                                      
REMARK 465     GLY B   165                                                      
REMARK 465     LEU B   167                                                      
REMARK 465     GLN B   168                                                      
REMARK 465     GLY B   169                                                      
REMARK 465     GLY B   170                                                      
REMARK 465     PRO B   171                                                      
REMARK 465     GLU B   172                                                      
REMARK 465     SER B   173                                                      
REMARK 465     GLU B   174                                                      
REMARK 465     VAL B   187                                                      
REMARK 465     ASP B   188                                                      
REMARK 465     PRO B   189                                                      
REMARK 465     ALA B   190                                                      
REMARK 465     PHE B   191                                                      
REMARK 465     ARG B   192                                                      
REMARK 465     THR B   193                                                      
REMARK 465     ARG B   194                                                      
REMARK 465     GLY B   195                                                      
REMARK 465     ASN B   196                                                      
REMARK 465     GLN B   229                                                      
REMARK 465     LYS B   230                                                      
REMARK 465     ILE B   231                                                      
REMARK 465     GLY B   232                                                      
REMARK 465     PRO B   233                                                      
REMARK 465     GLU B   234                                                      
REMARK 465     GLY B   235                                                      
REMARK 465     LEU B   236                                                      
REMARK 465     VAL B   237                                                      
REMARK 465     THR B   238                                                      
REMARK 465     GLN B   239                                                      
REMARK 465     VAL B   259                                                      
REMARK 465     SER B   574                                                      
REMARK 465     LEU C    47                                                      
REMARK 465     THR C    48                                                      
REMARK 465     GLN C    49                                                      
REMARK 465     GLU C    50                                                      
REMARK 465     LEU C    51                                                      
REMARK 465     GLY C    52                                                      
REMARK 465     THR C    53                                                      
REMARK 465     ALA C    54                                                      
REMARK 465     PHE C    55                                                      
REMARK 465     PHE C    56                                                      
REMARK 465     GLN C    57                                                      
REMARK 465     ALA C    64                                                      
REMARK 465     MET C    65                                                      
REMARK 465     SER C   574                                                      
REMARK 465     LEU D    47                                                      
REMARK 465     THR D    48                                                      
REMARK 465     GLN D    49                                                      
REMARK 465     GLU D    50                                                      
REMARK 465     LEU D    51                                                      
REMARK 465     GLY D    52                                                      
REMARK 465     THR D    53                                                      
REMARK 465     ALA D    54                                                      
REMARK 465     PHE D    55                                                      
REMARK 465     PHE D    56                                                      
REMARK 465     GLN D    57                                                      
REMARK 465     GLN D    58                                                      
REMARK 465     GLN D    59                                                      
REMARK 465     GLN D    60                                                      
REMARK 465     LEU D    61                                                      
REMARK 465     MET D    65                                                      
REMARK 465     ALA D    66                                                      
REMARK 465     ASP D    67                                                      
REMARK 465     ASP D    77                                                      
REMARK 465     GLN D   168                                                      
REMARK 465     GLY D   169                                                      
REMARK 465     GLY D   170                                                      
REMARK 465     PRO D   171                                                      
REMARK 465     VAL D   183                                                      
REMARK 465     GLY D   232                                                      
REMARK 465     GLY D   235                                                      
REMARK 465     SER D   574                                                      
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   OD2  ASP D   339     O2P  PGA D   581              1.90            
REMARK 500   OD2  ASP C   339     O4P  PGA C   581              1.95            
REMARK 500   OG1  THR A   371     O2   PGA A   581              2.00            
REMARK 500   OD2  ASP B   339     O4P  PGA B   581              2.02            
REMARK 500   NH2  ARG A    99     OE1  GLU A   129              2.11            
REMARK 500   OG1  THR D   371     O1   PGA D   581              2.11            
REMARK 500   N    SER D    87     OE1  GLU D   429              2.15            
REMARK 500   NH2  ARG D   532     O1P  FBP D   580              2.16            
REMARK 500   OE2  GLU C   315     OD2  ASP C   339              2.19            
REMARK 500   O    TRP A   525     N    ASP A   528              2.19            
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   NH2  ARG A   209     NH2  ARG C   449     1655     1.91            
REMARK 500   CD   GLU B   102     NE2  GLN C   534     2545     2.07            
REMARK 500   OE2  GLU B   102     NE2  GLN C   534     2545     2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  71   CD    GLU A  71   OE1     0.114                       
REMARK 500    LEU A  73   CG    LEU A  73   CD2     0.269                       
REMARK 500    GLU A  81   CD    GLU A  81   OE2     0.071                       
REMARK 500    VAL A  83   CB    VAL A  83   CG2     0.168                       
REMARK 500    GLU A 102   CG    GLU A 102   CD      0.318                       
REMARK 500    GLU A 102   CD    GLU A 102   OE1    -0.111                       
REMARK 500    ARG A 103   CD    ARG A 103   NE      0.116                       
REMARK 500    ARG A 103   NE    ARG A 103   CZ      0.126                       
REMARK 500    ARG A 103   CZ    ARG A 103   NH2    -0.245                       
REMARK 500    GLU A 106   CG    GLU A 106   CD      0.123                       
REMARK 500    LYS A 109   CD    LYS A 109   CE      0.260                       
REMARK 500    SER A 123   CB    SER A 123   OG      0.079                       
REMARK 500    GLU A 125   CD    GLU A 125   OE1     0.087                       
REMARK 500    SER A 130   CB    SER A 130   OG      0.135                       
REMARK 500    GLU A 136   CD    GLU A 136   OE1     0.072                       
REMARK 500    SER A 147   CB    SER A 147   OG      0.122                       
REMARK 500    LYS A 158   CE    LYS A 158   NZ     -0.253                       
REMARK 500    GLY A 169   C     GLY A 170   N       0.162                       
REMARK 500    GLU A 176   CD    GLU A 176   OE2     0.082                       
REMARK 500    LYS A 179   CE    LYS A 179   NZ      0.171                       
REMARK 500    ARG A 192   CZ    ARG A 192   NH1     0.152                       
REMARK 500    ARG A 209   CZ    ARG A 209   NH1    -0.125                       
REMARK 500    ARG A 209   CZ    ARG A 209   NH2     0.120                       
REMARK 500    GLN A 229   CD    GLN A 229   NE2     0.235                       
REMARK 500    GLN A 258   CD    GLN A 258   OE1     0.186                       
REMARK 500    GLN A 258   CD    GLN A 258   NE2     0.217                       
REMARK 500    ARG A 382   CD    ARG A 382   NE      0.158                       
REMARK 500    ARG A 382   NE    ARG A 382   CZ     -0.175                       
REMARK 500    ARG A 382   CZ    ARG A 382   NH2     0.252                       
REMARK 500    CYS A 401   CB    CYS A 401   SG     -0.103                       
REMARK 500    LYS A 410   CE    LYS A 410   NZ      0.192                       
REMARK 500    ARG A 426   CZ    ARG A 426   NH1     0.142                       
REMARK 500    PRO B  62   CG    PRO B  62   CD      0.206                       
REMARK 500    ASP B  67   CG    ASP B  67   OD2     0.159                       
REMARK 500    GLU B  71   CB    GLU B  71   CG      0.171                       
REMARK 500    LYS B 105   CE    LYS B 105   NZ      0.212                       
REMARK 500    GLU B 106   CD    GLU B 106   OE2     0.097                       
REMARK 500    HIS B 124   CE1   HIS B 124   NE2    -0.077                       
REMARK 500    GLU B 129   CD    GLU B 129   OE2    -0.144                       
REMARK 500    SER B 130   CB    SER B 130   OG      0.083                       
REMARK 500    GLU B 136   CD    GLU B 136   OE2    -0.100                       
REMARK 500    GLU B 139   CD    GLU B 139   OE2     0.131                       
REMARK 500    SER B 144   CB    SER B 144   OG      0.359                       
REMARK 500    SER B 147   CB    SER B 147   OG      0.182                       
REMARK 500    GLU B 161   CB    GLU B 161   CG      0.133                       
REMARK 500    GLU B 176   CB    GLU B 176   CG      0.133                       
REMARK 500    GLU B 176   CG    GLU B 176   CD      0.156                       
REMARK 500    GLU B 176   CD    GLU B 176   OE1     0.204                       
REMARK 500    ASN B 198   CG    ASN B 198   OD1    -0.385                       
REMARK 500    ASN B 198   CG    ASN B 198   ND2     0.291                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     111 BOND DEVIATIONS.                              
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    LEU A  73   CB  -  CG  -  CD1 ANGL. DEV. = -11.6 DEGREES          
REMARK 500    GLU A 102   OE1 -  CD  -  OE2 ANGL. DEV. = -16.5 DEGREES          
REMARK 500    GLU A 102   CG  -  CD  -  OE2 ANGL. DEV. =  19.4 DEGREES          
REMARK 500    ARG A 103   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG A 103   NE  -  CZ  -  NH2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    GLU A 125   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    LYS A 158   CD  -  CE  -  NZ  ANGL. DEV. =  19.8 DEGREES          
REMARK 500    GLY A 169   CA  -  C   -  O   ANGL. DEV. =  11.6 DEGREES          
REMARK 500    GLY A 170   C   -  N   -  CA  ANGL. DEV. = -13.1 DEGREES          
REMARK 500    ARG A 382   CD  -  NE  -  CZ  ANGL. DEV. = -10.0 DEGREES          
REMARK 500    ARG A 382   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG A 426   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    ARG A 426   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    GLU B  71   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.8 DEGREES          
REMARK 500    GLU B 129   OE1 -  CD  -  OE2 ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    GLU B 139   OE1 -  CD  -  OE2 ANGL. DEV. =   8.9 DEGREES          
REMARK 500    VAL B 175   N   -  CA  -  CB  ANGL. DEV. = -18.8 DEGREES          
REMARK 500    ASN B 198   OD1 -  CG  -  ND2 ANGL. DEV. =  15.8 DEGREES          
REMARK 500    ASN B 198   CB  -  CG  -  ND2 ANGL. DEV. = -16.8 DEGREES          
REMARK 500    LEU B 396   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    VAL B 473   CB  -  CA  -  C   ANGL. DEV. = -12.7 DEGREES          
REMARK 500    GLU C  71   OE1 -  CD  -  OE2 ANGL. DEV. = -16.8 DEGREES          
REMARK 500    ARG C  86   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    GLU C 102   OE1 -  CD  -  OE2 ANGL. DEV. =   9.1 DEGREES          
REMARK 500    ARG C 103   CD  -  NE  -  CZ  ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    ARG C 103   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    ARG C 103   NE  -  CZ  -  NH1 ANGL. DEV. =  11.6 DEGREES          
REMARK 500    ARG C 103   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    GLU C 106   OE1 -  CD  -  OE2 ANGL. DEV. = -12.0 DEGREES          
REMARK 500    LYS C 109   CD  -  CE  -  NZ  ANGL. DEV. = -17.8 DEGREES          
REMARK 500    GLU C 125   OE1 -  CD  -  OE2 ANGL. DEV. =  11.1 DEGREES          
REMARK 500    ARG C 149   NE  -  CZ  -  NH2 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG C 192   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG C 192   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ARG C 216   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    PHE C 413   CG  -  CD2 -  CE2 ANGL. DEV. =  -8.5 DEGREES          
REMARK 500    PHE C 413   CD1 -  CE1 -  CZ  ANGL. DEV. =   8.9 DEGREES          
REMARK 500    PHE C 413   CZ  -  CE2 -  CD2 ANGL. DEV. =   9.1 DEGREES          
REMARK 500    VAL C 473   CB  -  CA  -  C   ANGL. DEV. = -12.3 DEGREES          
REMARK 500    GLU D  81   OE1 -  CD  -  OE2 ANGL. DEV. = -15.0 DEGREES          
REMARK 500    GLU D  81   CG  -  CD  -  OE2 ANGL. DEV. =  14.8 DEGREES          
REMARK 500    GLU D 139   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.8 DEGREES          
REMARK 500    ARG D 149   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG D 149   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    PHE D 191   CB  -  CG  -  CD2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    ARG D 194   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG D 194   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ARG D 216   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    GLU D 234   OE1 -  CD  -  OE2 ANGL. DEV. =  12.0 DEGREES          
REMARK 500    GLU D 234   CG  -  CD  -  OE1 ANGL. DEV. = -12.0 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      56 ANGLE DEVIATIONS.                             
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    ALA A  84      141.51    149.53                                   
REMARK 500    SER A  98       36.62   -163.42                                   
REMARK 500    PHE A 119        5.13    -62.59                                   
REMARK 500    GLN A 168      105.19    -52.77                                   
REMARK 500    ARG A 192      -10.59    -49.35                                   
REMARK 500    ARG A 194       42.85    -99.74                                   
REMARK 500    ASP A 220       84.00     58.91                                   
REMARK 500    GLU A 241      -74.30    -68.56                                   
REMARK 500    ARG A 249       76.92     50.03                                   
REMARK 500    PHE A 287       35.34     34.08                                   
REMARK 500    LYS A 290      149.31   -171.03                                   
REMARK 500    GLU A 304       -8.49    -57.26                                   
REMARK 500    THR A 371      122.96     86.90                                   
REMARK 500    SER A 405      -99.31   -132.33                                   
REMARK 500    PHE A 413       43.61   -142.64                                   
REMARK 500    ARG A 435      -82.42    -26.40                                   
REMARK 500    ALA A 468      136.04    -38.55                                   
REMARK 500    ARG A 486      -46.71    -28.91                                   
REMARK 500    TRP A 525      -96.45    -55.01                                   
REMARK 500    ALA A 526      -70.28      4.82                                   
REMARK 500    ASN A 566       26.91   -163.04                                   
REMARK 500    LEU B  70      -70.18    -53.40                                   
REMARK 500    CYS B  74       -9.63    -50.93                                   
REMARK 500    ALA B  84      138.10    150.87                                   
REMARK 500    SER B  98       34.50   -170.19                                   
REMARK 500    PHE B 119        5.23    -66.41                                   
REMARK 500    SER B 144       83.72   -160.36                                   
REMARK 500    ASN B 206       -7.62    -57.45                                   
REMARK 500    ASP B 220       94.89     48.45                                   
REMARK 500    ARG B 249       77.26     55.08                                   
REMARK 500    PHE B 287       33.42     34.41                                   
REMARK 500    GLU B 304       -9.85    -54.90                                   
REMARK 500    THR B 371      121.90     80.87                                   
REMARK 500    LEU B 374       40.93   -141.30                                   
REMARK 500    SER B 405      -94.15   -130.49                                   
REMARK 500    ARG B 435      -84.45    -28.17                                   
REMARK 500    ALA B 468      136.17    -36.42                                   
REMARK 500    ARG B 486      -49.54    -21.96                                   
REMARK 500    GLU B 519      150.78    -48.70                                   
REMARK 500    TRP B 525      -96.12    -55.34                                   
REMARK 500    ALA B 526      -64.26     -0.34                                   
REMARK 500    ASN B 566       24.66   -166.15                                   
REMARK 500    GLN C  59       15.86     51.40                                   
REMARK 500    HIS C  72      -70.17    -40.83                                   
REMARK 500    CYS C  74       -9.82    -52.97                                   
REMARK 500    ALA C  84      139.03    148.87                                   
REMARK 500    SER C  98       36.61   -165.30                                   
REMARK 500    PHE C 119        6.66    -64.90                                   
REMARK 500    GLN C 168       93.39    -40.91                                   
REMARK 500    ASP C 220       76.43     58.00                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      85 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    GLU A 125         0.09    SIDE CHAIN                              
REMARK 500    ARG A 382         0.12    SIDE CHAIN                              
REMARK 500    GLU B 136         0.07    SIDE CHAIN                              
REMARK 500    GLU C  71         0.09    SIDE CHAIN                              
REMARK 500    GLU C 102         0.08    SIDE CHAIN                              
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 583  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PGA A 581   P                                                      
REMARK 620 2 PGA A 581   O4P  78.7                                              
REMARK 620 3 ASP A 339   OD2 164.4 100.2                                        
REMARK 620 4 PGA A 581   O3P  53.6 114.3 114.7                                  
REMARK 620 5 PGA A 581   O2P  52.6 109.3 139.9  77.3                            
REMARK 620 6 GLU A 315   OE2  98.1 161.2  77.9  52.3  82.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 582   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 156   OD1                                                    
REMARK 620 2 THR A 157   O    68.5                                              
REMARK 620 3 SER A 286   OG   65.7  46.4                                        
REMARK 620 4 SER A 120   OG  151.0 109.5 135.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 587  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PGA B 581   P                                                      
REMARK 620 2 PGA B 581   O4P  63.1                                              
REMARK 620 3 GLU B 315   OE2 112.5 175.5                                        
REMARK 620 4 ASP B 339   OD2 158.3  95.4  89.0                                  
REMARK 620 5 PGA B 581   O1P  52.6 103.4  73.6 138.0                            
REMARK 620 6 PGA B 581   O2P  43.5  86.8  89.1 145.0  74.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B 586   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 120   OG                                                     
REMARK 620 2 THR B 157   O    97.9                                              
REMARK 620 3 ASN B 118   OD1  67.1 111.5                                        
REMARK 620 4 ASP B 156   OD1 146.6  61.4  94.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 591  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PGA C 581   O4P                                                    
REMARK 620 2 PGA C 581   P    69.9                                              
REMARK 620 3 PGA C 581   O1P 107.4  61.3                                        
REMARK 620 4 ASP C 339   OD2  77.4 146.7 126.2                                  
REMARK 620 5 GLU C 315   OE2 152.2 134.3  81.3  76.4                            
REMARK 620 6 PGA C 581   O2P 100.9  54.6  91.3 141.6 105.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C 590   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C 157   O                                                      
REMARK 620 2 ASN C 118   OD1 117.2                                              
REMARK 620 3 SER C 120   OG  107.0  67.2                                        
REMARK 620 4 ASP C 156   OD1  63.9  96.3 156.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 595  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PGA D 581   P                                                      
REMARK 620 2 PGA D 581   O4P  79.5                                              
REMARK 620 3 PGA D 581   O2P  78.9 141.0                                        
REMARK 620 4 GLU D 315   OE2 123.6  60.1 155.6                                  
REMARK 620 5 ASP D 339   OD2 156.9 118.5  78.0  79.4                            
REMARK 620 6 PGA D 581   O3P  49.0  94.9  95.0  94.5 135.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K D 594   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR D 157   O                                                      
REMARK 620 2 ASP D 156   OD1  67.0                                              
REMARK 620 3 SER D 120   OG  101.6 150.1                                        
REMARK 620 4 ASN D 118   OD1 115.7  90.4  69.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  9-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700 THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700 THE SHEETS PRESENTED AS "CA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700 THE SHEETS PRESENTED AS "DA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  7-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FBP A 580                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGA A 581                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 582                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 583                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FBP B 580                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGA B 581                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 586                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 587                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FBP C 580                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGA C 581                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 590                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 591                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FBP D 580                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGA D 581                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D 594                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 595                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VGB   RELATED DB: PDB                                   
REMARK 900 HUMAN ERYTHROCYTE PYRUVATE KINASE                                    
REMARK 900 RELATED ID: 2VGF   RELATED DB: PDB                                   
REMARK 900 HUMAN ERYTHROCYTE PYRUVATE KINASE: T384M MUTANT                      
DBREF  2VGG A   47   574  UNP    P30613   KPYR_HUMAN      47    574             
DBREF  2VGG B   47   574  UNP    P30613   KPYR_HUMAN      47    574             
DBREF  2VGG C   47   574  UNP    P30613   KPYR_HUMAN      47    574             
DBREF  2VGG D   47   574  UNP    P30613   KPYR_HUMAN      47    574             
SEQADV 2VGG HIS A  479  UNP  P30613    ARG   479 ENGINEERED MUTATION            
SEQADV 2VGG HIS B  479  UNP  P30613    ARG   479 ENGINEERED MUTATION            
SEQADV 2VGG HIS C  479  UNP  P30613    ARG   479 ENGINEERED MUTATION            
SEQADV 2VGG HIS D  479  UNP  P30613    ARG   479 ENGINEERED MUTATION            
SEQRES   1 A  528  LEU THR GLN GLU LEU GLY THR ALA PHE PHE GLN GLN GLN          
SEQRES   2 A  528  GLN LEU PRO ALA ALA MET ALA ASP THR PHE LEU GLU HIS          
SEQRES   3 A  528  LEU CYS LEU LEU ASP ILE ASP SER GLU PRO VAL ALA ALA          
SEQRES   4 A  528  ARG SER THR SER ILE ILE ALA THR ILE GLY PRO ALA SER          
SEQRES   5 A  528  ARG SER VAL GLU ARG LEU LYS GLU MET ILE LYS ALA GLY          
SEQRES   6 A  528  MET ASN ILE ALA ARG LEU ASN PHE SER HIS GLY SER HIS          
SEQRES   7 A  528  GLU TYR HIS ALA GLU SER ILE ALA ASN VAL ARG GLU ALA          
SEQRES   8 A  528  VAL GLU SER PHE ALA GLY SER PRO LEU SER TYR ARG PRO          
SEQRES   9 A  528  VAL ALA ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG          
SEQRES  10 A  528  THR GLY ILE LEU GLN GLY GLY PRO GLU SER GLU VAL GLU          
SEQRES  11 A  528  LEU VAL LYS GLY SER GLN VAL LEU VAL THR VAL ASP PRO          
SEQRES  12 A  528  ALA PHE ARG THR ARG GLY ASN ALA ASN THR VAL TRP VAL          
SEQRES  13 A  528  ASP TYR PRO ASN ILE VAL ARG VAL VAL PRO VAL GLY GLY          
SEQRES  14 A  528  ARG ILE TYR ILE ASP ASP GLY LEU ILE SER LEU VAL VAL          
SEQRES  15 A  528  GLN LYS ILE GLY PRO GLU GLY LEU VAL THR GLN VAL GLU          
SEQRES  16 A  528  ASN GLY GLY VAL LEU GLY SER ARG LYS GLY VAL ASN LEU          
SEQRES  17 A  528  PRO GLY ALA GLN VAL ASP LEU PRO GLY LEU SER GLU GLN          
SEQRES  18 A  528  ASP VAL ARG ASP LEU ARG PHE GLY VAL GLU HIS GLY VAL          
SEQRES  19 A  528  ASP ILE VAL PHE ALA SER PHE VAL ARG LYS ALA SER ASP          
SEQRES  20 A  528  VAL ALA ALA VAL ARG ALA ALA LEU GLY PRO GLU GLY HIS          
SEQRES  21 A  528  GLY ILE LYS ILE ILE SER LYS ILE GLU ASN HIS GLU GLY          
SEQRES  22 A  528  VAL LYS ARG PHE ASP GLU ILE LEU GLU VAL SER ASP GLY          
SEQRES  23 A  528  ILE MET VAL ALA ARG GLY ASP LEU GLY ILE GLU ILE PRO          
SEQRES  24 A  528  ALA GLU LYS VAL PHE LEU ALA GLN LYS MET MET ILE GLY          
SEQRES  25 A  528  ARG CYS ASN LEU ALA GLY LYS PRO VAL VAL CYS ALA THR          
SEQRES  26 A  528  GLN MET LEU GLU SER MET ILE THR LYS PRO ARG PRO THR          
SEQRES  27 A  528  ARG ALA GLU THR SER ASP VAL ALA ASN ALA VAL LEU ASP          
SEQRES  28 A  528  GLY ALA ASP CYS ILE MET LEU SER GLY GLU THR ALA LYS          
SEQRES  29 A  528  GLY ASN PHE PRO VAL GLU ALA VAL LYS MET GLN HIS ALA          
SEQRES  30 A  528  ILE ALA ARG GLU ALA GLU ALA ALA VAL TYR HIS ARG GLN          
SEQRES  31 A  528  LEU PHE GLU GLU LEU ARG ARG ALA ALA PRO LEU SER ARG          
SEQRES  32 A  528  ASP PRO THR GLU VAL THR ALA ILE GLY ALA VAL GLU ALA          
SEQRES  33 A  528  ALA PHE LYS CYS CYS ALA ALA ALA ILE ILE VAL LEU THR          
SEQRES  34 A  528  THR THR GLY HIS SER ALA GLN LEU LEU SER ARG TYR ARG          
SEQRES  35 A  528  PRO ARG ALA ALA VAL ILE ALA VAL THR ARG SER ALA GLN          
SEQRES  36 A  528  ALA ALA ARG GLN VAL HIS LEU CYS ARG GLY VAL PHE PRO          
SEQRES  37 A  528  LEU LEU TYR ARG GLU PRO PRO GLU ALA ILE TRP ALA ASP          
SEQRES  38 A  528  ASP VAL ASP ARG ARG VAL GLN PHE GLY ILE GLU SER GLY          
SEQRES  39 A  528  LYS LEU ARG GLY PHE LEU ARG VAL GLY ASP LEU VAL ILE          
SEQRES  40 A  528  VAL VAL THR GLY TRP ARG PRO GLY SER GLY TYR THR ASN          
SEQRES  41 A  528  ILE MET ARG VAL LEU SER ILE SER                              
SEQRES   1 B  528  LEU THR GLN GLU LEU GLY THR ALA PHE PHE GLN GLN GLN          
SEQRES   2 B  528  GLN LEU PRO ALA ALA MET ALA ASP THR PHE LEU GLU HIS          
SEQRES   3 B  528  LEU CYS LEU LEU ASP ILE ASP SER GLU PRO VAL ALA ALA          
SEQRES   4 B  528  ARG SER THR SER ILE ILE ALA THR ILE GLY PRO ALA SER          
SEQRES   5 B  528  ARG SER VAL GLU ARG LEU LYS GLU MET ILE LYS ALA GLY          
SEQRES   6 B  528  MET ASN ILE ALA ARG LEU ASN PHE SER HIS GLY SER HIS          
SEQRES   7 B  528  GLU TYR HIS ALA GLU SER ILE ALA ASN VAL ARG GLU ALA          
SEQRES   8 B  528  VAL GLU SER PHE ALA GLY SER PRO LEU SER TYR ARG PRO          
SEQRES   9 B  528  VAL ALA ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG          
SEQRES  10 B  528  THR GLY ILE LEU GLN GLY GLY PRO GLU SER GLU VAL GLU          
SEQRES  11 B  528  LEU VAL LYS GLY SER GLN VAL LEU VAL THR VAL ASP PRO          
SEQRES  12 B  528  ALA PHE ARG THR ARG GLY ASN ALA ASN THR VAL TRP VAL          
SEQRES  13 B  528  ASP TYR PRO ASN ILE VAL ARG VAL VAL PRO VAL GLY GLY          
SEQRES  14 B  528  ARG ILE TYR ILE ASP ASP GLY LEU ILE SER LEU VAL VAL          
SEQRES  15 B  528  GLN LYS ILE GLY PRO GLU GLY LEU VAL THR GLN VAL GLU          
SEQRES  16 B  528  ASN GLY GLY VAL LEU GLY SER ARG LYS GLY VAL ASN LEU          
SEQRES  17 B  528  PRO GLY ALA GLN VAL ASP LEU PRO GLY LEU SER GLU GLN          
SEQRES  18 B  528  ASP VAL ARG ASP LEU ARG PHE GLY VAL GLU HIS GLY VAL          
SEQRES  19 B  528  ASP ILE VAL PHE ALA SER PHE VAL ARG LYS ALA SER ASP          
SEQRES  20 B  528  VAL ALA ALA VAL ARG ALA ALA LEU GLY PRO GLU GLY HIS          
SEQRES  21 B  528  GLY ILE LYS ILE ILE SER LYS ILE GLU ASN HIS GLU GLY          
SEQRES  22 B  528  VAL LYS ARG PHE ASP GLU ILE LEU GLU VAL SER ASP GLY          
SEQRES  23 B  528  ILE MET VAL ALA ARG GLY ASP LEU GLY ILE GLU ILE PRO          
SEQRES  24 B  528  ALA GLU LYS VAL PHE LEU ALA GLN LYS MET MET ILE GLY          
SEQRES  25 B  528  ARG CYS ASN LEU ALA GLY LYS PRO VAL VAL CYS ALA THR          
SEQRES  26 B  528  GLN MET LEU GLU SER MET ILE THR LYS PRO ARG PRO THR          
SEQRES  27 B  528  ARG ALA GLU THR SER ASP VAL ALA ASN ALA VAL LEU ASP          
SEQRES  28 B  528  GLY ALA ASP CYS ILE MET LEU SER GLY GLU THR ALA LYS          
SEQRES  29 B  528  GLY ASN PHE PRO VAL GLU ALA VAL LYS MET GLN HIS ALA          
SEQRES  30 B  528  ILE ALA ARG GLU ALA GLU ALA ALA VAL TYR HIS ARG GLN          
SEQRES  31 B  528  LEU PHE GLU GLU LEU ARG ARG ALA ALA PRO LEU SER ARG          
SEQRES  32 B  528  ASP PRO THR GLU VAL THR ALA ILE GLY ALA VAL GLU ALA          
SEQRES  33 B  528  ALA PHE LYS CYS CYS ALA ALA ALA ILE ILE VAL LEU THR          
SEQRES  34 B  528  THR THR GLY HIS SER ALA GLN LEU LEU SER ARG TYR ARG          
SEQRES  35 B  528  PRO ARG ALA ALA VAL ILE ALA VAL THR ARG SER ALA GLN          
SEQRES  36 B  528  ALA ALA ARG GLN VAL HIS LEU CYS ARG GLY VAL PHE PRO          
SEQRES  37 B  528  LEU LEU TYR ARG GLU PRO PRO GLU ALA ILE TRP ALA ASP          
SEQRES  38 B  528  ASP VAL ASP ARG ARG VAL GLN PHE GLY ILE GLU SER GLY          
SEQRES  39 B  528  LYS LEU ARG GLY PHE LEU ARG VAL GLY ASP LEU VAL ILE          
SEQRES  40 B  528  VAL VAL THR GLY TRP ARG PRO GLY SER GLY TYR THR ASN          
SEQRES  41 B  528  ILE MET ARG VAL LEU SER ILE SER                              
SEQRES   1 C  528  LEU THR GLN GLU LEU GLY THR ALA PHE PHE GLN GLN GLN          
SEQRES   2 C  528  GLN LEU PRO ALA ALA MET ALA ASP THR PHE LEU GLU HIS          
SEQRES   3 C  528  LEU CYS LEU LEU ASP ILE ASP SER GLU PRO VAL ALA ALA          
SEQRES   4 C  528  ARG SER THR SER ILE ILE ALA THR ILE GLY PRO ALA SER          
SEQRES   5 C  528  ARG SER VAL GLU ARG LEU LYS GLU MET ILE LYS ALA GLY          
SEQRES   6 C  528  MET ASN ILE ALA ARG LEU ASN PHE SER HIS GLY SER HIS          
SEQRES   7 C  528  GLU TYR HIS ALA GLU SER ILE ALA ASN VAL ARG GLU ALA          
SEQRES   8 C  528  VAL GLU SER PHE ALA GLY SER PRO LEU SER TYR ARG PRO          
SEQRES   9 C  528  VAL ALA ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG          
SEQRES  10 C  528  THR GLY ILE LEU GLN GLY GLY PRO GLU SER GLU VAL GLU          
SEQRES  11 C  528  LEU VAL LYS GLY SER GLN VAL LEU VAL THR VAL ASP PRO          
SEQRES  12 C  528  ALA PHE ARG THR ARG GLY ASN ALA ASN THR VAL TRP VAL          
SEQRES  13 C  528  ASP TYR PRO ASN ILE VAL ARG VAL VAL PRO VAL GLY GLY          
SEQRES  14 C  528  ARG ILE TYR ILE ASP ASP GLY LEU ILE SER LEU VAL VAL          
SEQRES  15 C  528  GLN LYS ILE GLY PRO GLU GLY LEU VAL THR GLN VAL GLU          
SEQRES  16 C  528  ASN GLY GLY VAL LEU GLY SER ARG LYS GLY VAL ASN LEU          
SEQRES  17 C  528  PRO GLY ALA GLN VAL ASP LEU PRO GLY LEU SER GLU GLN          
SEQRES  18 C  528  ASP VAL ARG ASP LEU ARG PHE GLY VAL GLU HIS GLY VAL          
SEQRES  19 C  528  ASP ILE VAL PHE ALA SER PHE VAL ARG LYS ALA SER ASP          
SEQRES  20 C  528  VAL ALA ALA VAL ARG ALA ALA LEU GLY PRO GLU GLY HIS          
SEQRES  21 C  528  GLY ILE LYS ILE ILE SER LYS ILE GLU ASN HIS GLU GLY          
SEQRES  22 C  528  VAL LYS ARG PHE ASP GLU ILE LEU GLU VAL SER ASP GLY          
SEQRES  23 C  528  ILE MET VAL ALA ARG GLY ASP LEU GLY ILE GLU ILE PRO          
SEQRES  24 C  528  ALA GLU LYS VAL PHE LEU ALA GLN LYS MET MET ILE GLY          
SEQRES  25 C  528  ARG CYS ASN LEU ALA GLY LYS PRO VAL VAL CYS ALA THR          
SEQRES  26 C  528  GLN MET LEU GLU SER MET ILE THR LYS PRO ARG PRO THR          
SEQRES  27 C  528  ARG ALA GLU THR SER ASP VAL ALA ASN ALA VAL LEU ASP          
SEQRES  28 C  528  GLY ALA ASP CYS ILE MET LEU SER GLY GLU THR ALA LYS          
SEQRES  29 C  528  GLY ASN PHE PRO VAL GLU ALA VAL LYS MET GLN HIS ALA          
SEQRES  30 C  528  ILE ALA ARG GLU ALA GLU ALA ALA VAL TYR HIS ARG GLN          
SEQRES  31 C  528  LEU PHE GLU GLU LEU ARG ARG ALA ALA PRO LEU SER ARG          
SEQRES  32 C  528  ASP PRO THR GLU VAL THR ALA ILE GLY ALA VAL GLU ALA          
SEQRES  33 C  528  ALA PHE LYS CYS CYS ALA ALA ALA ILE ILE VAL LEU THR          
SEQRES  34 C  528  THR THR GLY HIS SER ALA GLN LEU LEU SER ARG TYR ARG          
SEQRES  35 C  528  PRO ARG ALA ALA VAL ILE ALA VAL THR ARG SER ALA GLN          
SEQRES  36 C  528  ALA ALA ARG GLN VAL HIS LEU CYS ARG GLY VAL PHE PRO          
SEQRES  37 C  528  LEU LEU TYR ARG GLU PRO PRO GLU ALA ILE TRP ALA ASP          
SEQRES  38 C  528  ASP VAL ASP ARG ARG VAL GLN PHE GLY ILE GLU SER GLY          
SEQRES  39 C  528  LYS LEU ARG GLY PHE LEU ARG VAL GLY ASP LEU VAL ILE          
SEQRES  40 C  528  VAL VAL THR GLY TRP ARG PRO GLY SER GLY TYR THR ASN          
SEQRES  41 C  528  ILE MET ARG VAL LEU SER ILE SER                              
SEQRES   1 D  528  LEU THR GLN GLU LEU GLY THR ALA PHE PHE GLN GLN GLN          
SEQRES   2 D  528  GLN LEU PRO ALA ALA MET ALA ASP THR PHE LEU GLU HIS          
SEQRES   3 D  528  LEU CYS LEU LEU ASP ILE ASP SER GLU PRO VAL ALA ALA          
SEQRES   4 D  528  ARG SER THR SER ILE ILE ALA THR ILE GLY PRO ALA SER          
SEQRES   5 D  528  ARG SER VAL GLU ARG LEU LYS GLU MET ILE LYS ALA GLY          
SEQRES   6 D  528  MET ASN ILE ALA ARG LEU ASN PHE SER HIS GLY SER HIS          
SEQRES   7 D  528  GLU TYR HIS ALA GLU SER ILE ALA ASN VAL ARG GLU ALA          
SEQRES   8 D  528  VAL GLU SER PHE ALA GLY SER PRO LEU SER TYR ARG PRO          
SEQRES   9 D  528  VAL ALA ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG          
SEQRES  10 D  528  THR GLY ILE LEU GLN GLY GLY PRO GLU SER GLU VAL GLU          
SEQRES  11 D  528  LEU VAL LYS GLY SER GLN VAL LEU VAL THR VAL ASP PRO          
SEQRES  12 D  528  ALA PHE ARG THR ARG GLY ASN ALA ASN THR VAL TRP VAL          
SEQRES  13 D  528  ASP TYR PRO ASN ILE VAL ARG VAL VAL PRO VAL GLY GLY          
SEQRES  14 D  528  ARG ILE TYR ILE ASP ASP GLY LEU ILE SER LEU VAL VAL          
SEQRES  15 D  528  GLN LYS ILE GLY PRO GLU GLY LEU VAL THR GLN VAL GLU          
SEQRES  16 D  528  ASN GLY GLY VAL LEU GLY SER ARG LYS GLY VAL ASN LEU          
SEQRES  17 D  528  PRO GLY ALA GLN VAL ASP LEU PRO GLY LEU SER GLU GLN          
SEQRES  18 D  528  ASP VAL ARG ASP LEU ARG PHE GLY VAL GLU HIS GLY VAL          
SEQRES  19 D  528  ASP ILE VAL PHE ALA SER PHE VAL ARG LYS ALA SER ASP          
SEQRES  20 D  528  VAL ALA ALA VAL ARG ALA ALA LEU GLY PRO GLU GLY HIS          
SEQRES  21 D  528  GLY ILE LYS ILE ILE SER LYS ILE GLU ASN HIS GLU GLY          
SEQRES  22 D  528  VAL LYS ARG PHE ASP GLU ILE LEU GLU VAL SER ASP GLY          
SEQRES  23 D  528  ILE MET VAL ALA ARG GLY ASP LEU GLY ILE GLU ILE PRO          
SEQRES  24 D  528  ALA GLU LYS VAL PHE LEU ALA GLN LYS MET MET ILE GLY          
SEQRES  25 D  528  ARG CYS ASN LEU ALA GLY LYS PRO VAL VAL CYS ALA THR          
SEQRES  26 D  528  GLN MET LEU GLU SER MET ILE THR LYS PRO ARG PRO THR          
SEQRES  27 D  528  ARG ALA GLU THR SER ASP VAL ALA ASN ALA VAL LEU ASP          
SEQRES  28 D  528  GLY ALA ASP CYS ILE MET LEU SER GLY GLU THR ALA LYS          
SEQRES  29 D  528  GLY ASN PHE PRO VAL GLU ALA VAL LYS MET GLN HIS ALA          
SEQRES  30 D  528  ILE ALA ARG GLU ALA GLU ALA ALA VAL TYR HIS ARG GLN          
SEQRES  31 D  528  LEU PHE GLU GLU LEU ARG ARG ALA ALA PRO LEU SER ARG          
SEQRES  32 D  528  ASP PRO THR GLU VAL THR ALA ILE GLY ALA VAL GLU ALA          
SEQRES  33 D  528  ALA PHE LYS CYS CYS ALA ALA ALA ILE ILE VAL LEU THR          
SEQRES  34 D  528  THR THR GLY HIS SER ALA GLN LEU LEU SER ARG TYR ARG          
SEQRES  35 D  528  PRO ARG ALA ALA VAL ILE ALA VAL THR ARG SER ALA GLN          
SEQRES  36 D  528  ALA ALA ARG GLN VAL HIS LEU CYS ARG GLY VAL PHE PRO          
SEQRES  37 D  528  LEU LEU TYR ARG GLU PRO PRO GLU ALA ILE TRP ALA ASP          
SEQRES  38 D  528  ASP VAL ASP ARG ARG VAL GLN PHE GLY ILE GLU SER GLY          
SEQRES  39 D  528  LYS LEU ARG GLY PHE LEU ARG VAL GLY ASP LEU VAL ILE          
SEQRES  40 D  528  VAL VAL THR GLY TRP ARG PRO GLY SER GLY TYR THR ASN          
SEQRES  41 D  528  ILE MET ARG VAL LEU SER ILE SER                              
HET    FBP  A 580      20                                                       
HET    PGA  A 581       9                                                       
HET      K  A 582       1                                                       
HET     MN  A 583       1                                                       
HET    FBP  B 580      20                                                       
HET    PGA  B 581       9                                                       
HET      K  B 586       1                                                       
HET     MN  B 587       1                                                       
HET    FBP  C 580      20                                                       
HET    PGA  C 581       9                                                       
HET      K  C 590       1                                                       
HET     MN  C 591       1                                                       
HET    FBP  D 580      20                                                       
HET    PGA  D 581       9                                                       
HET      K  D 594       1                                                       
HET     MN  D 595       1                                                       
HETNAM     FBP BETA-FRUCTOSE-1,6-DIPHOSPHATE                                    
HETNAM     PGA 2-PHOSPHOGLYCOLIC ACID                                           
HETNAM       K POTASSIUM ION                                                    
HETNAM      MN MANGANESE (II) ION                                               
HETSYN     FBP FRUCTOSE-1,6-BISPHOSPHATE                                        
FORMUL   5  FBP    4(C6 H14 O12 P2)                                             
FORMUL   6  PGA    4(C2 H5 O6 P)                                                
FORMUL   7    K    4(K 1+)                                                      
FORMUL   8   MN    4(MN 2+)                                                     
HELIX    1   1 THR A   68  LEU A   75  1                                   8    
HELIX    2   2 GLY A   95  ARG A   99  5                                   5    
HELIX    3   3 SER A  100  GLY A  111  1                                  12    
HELIX    4   4 SER A  123  SER A  140  1                                  18    
HELIX    5   5 ASP A  188  ARG A  194  5                                   7    
HELIX    6   6 ASN A  206  VAL A  211  1                                   6    
HELIX    7   7 SER A  265  GLY A  279  1                                  15    
HELIX    8   8 LYS A  290  GLY A  302  1                                  13    
HELIX    9   9 PRO A  303  HIS A  306  5                                   4    
HELIX   10  10 ASN A  316  ARG A  322  1                                   7    
HELIX   11  11 ARG A  322  SER A  330  1                                   9    
HELIX   12  12 ARG A  337  ILE A  344  1                                   8    
HELIX   13  13 PRO A  345  GLU A  347  5                                   3    
HELIX   14  14 LYS A  348  GLY A  364  1                                  17    
HELIX   15  15 LEU A  374  THR A  379  5                                   6    
HELIX   16  16 THR A  384  GLY A  398  1                                  15    
HELIX   17  17 SER A  405  LYS A  410  1                                   6    
HELIX   18  18 PHE A  413  VAL A  432  1                                  20    
HELIX   19  19 TYR A  433  ALA A  445  1                                  13    
HELIX   20  20 ASP A  450  CYS A  466  1                                  17    
HELIX   21  21 GLY A  478  TYR A  487  1                                  10    
HELIX   22  22 SER A  499  VAL A  506  1                                   8    
HELIX   23  23 HIS A  507  CYS A  509  5                                   3    
HELIX   24  24 ALA A  526  ARG A  543  1                                  18    
HELIX   25  25 THR B   68  LEU B   75  1                                   8    
HELIX   26  26 GLY B   95  ARG B   99  5                                   5    
HELIX   27  27 SER B  100  GLY B  111  1                                  12    
HELIX   28  28 SER B  123  SER B  140  1                                  18    
HELIX   29  29 ASN B  206  VAL B  211  1                                   6    
HELIX   30  30 SER B  265  GLY B  279  1                                  15    
HELIX   31  31 LYS B  290  GLY B  302  1                                  13    
HELIX   32  32 PRO B  303  HIS B  306  5                                   4    
HELIX   33  33 ASN B  316  ARG B  322  1                                   7    
HELIX   34  34 ARG B  322  SER B  330  1                                   9    
HELIX   35  35 ARG B  337  ILE B  344  1                                   8    
HELIX   36  36 PRO B  345  GLU B  347  5                                   3    
HELIX   37  37 LYS B  348  GLY B  364  1                                  17    
HELIX   38  38 LEU B  374  THR B  379  5                                   6    
HELIX   39  39 THR B  384  GLY B  398  1                                  15    
HELIX   40  40 SER B  405  LYS B  410  1                                   6    
HELIX   41  41 PHE B  413  ALA B  430  1                                  18    
HELIX   42  42 TYR B  433  ALA B  445  1                                  13    
HELIX   43  43 ASP B  450  CYS B  467  1                                  18    
HELIX   44  44 GLY B  478  TYR B  487  1                                  10    
HELIX   45  45 SER B  499  VAL B  506  1                                   8    
HELIX   46  46 HIS B  507  CYS B  509  5                                   3    
HELIX   47  47 ILE B  524  ARG B  543  1                                  20    
HELIX   48  48 THR C   68  LEU C   75  1                                   8    
HELIX   49  49 GLY C   95  ARG C   99  5                                   5    
HELIX   50  50 SER C  100  GLY C  111  1                                  12    
HELIX   51  51 SER C  123  SER C  140  1                                  18    
HELIX   52  52 ASP C  188  ARG C  192  5                                   5    
HELIX   53  53 ASN C  206  VAL C  211  1                                   6    
HELIX   54  54 SER C  265  GLY C  279  1                                  15    
HELIX   55  55 LYS C  290  GLY C  302  1                                  13    
HELIX   56  56 PRO C  303  HIS C  306  5                                   4    
HELIX   57  57 ASN C  316  ARG C  322  1                                   7    
HELIX   58  58 ARG C  322  SER C  330  1                                   9    
HELIX   59  59 ARG C  337  ILE C  344  1                                   8    
HELIX   60  60 PRO C  345  GLU C  347  5                                   3    
HELIX   61  61 LYS C  348  GLY C  364  1                                  17    
HELIX   62  62 LEU C  374  THR C  379  5                                   6    
HELIX   63  63 THR C  384  GLY C  398  1                                  15    
HELIX   64  64 SER C  405  LYS C  410  1                                   6    
HELIX   65  65 PHE C  413  ALA C  430  1                                  18    
HELIX   66  66 TYR C  433  ALA C  445  1                                  13    
HELIX   67  67 ASP C  450  CYS C  467  1                                  18    
HELIX   68  68 GLY C  478  TYR C  487  1                                  10    
HELIX   69  69 SER C  499  VAL C  506  1                                   8    
HELIX   70  70 HIS C  507  CYS C  509  5                                   3    
HELIX   71  71 ILE C  524  ARG C  543  1                                  20    
HELIX   72  72 THR D   68  LEU D   75  1                                   8    
HELIX   73  73 GLY D   95  ARG D   99  5                                   5    
HELIX   74  74 SER D  100  GLY D  111  1                                  12    
HELIX   75  75 SER D  123  SER D  140  1                                  18    
HELIX   76  76 ASN D  206  VAL D  211  1                                   6    
HELIX   77  77 SER D  265  GLY D  279  1                                  15    
HELIX   78  78 LYS D  290  GLY D  302  1                                  13    
HELIX   79  79 PRO D  303  HIS D  306  5                                   4    
HELIX   80  80 ASN D  316  ARG D  322  1                                   7    
HELIX   81  81 ARG D  322  SER D  330  1                                   9    
HELIX   82  82 ARG D  337  ILE D  344  1                                   8    
HELIX   83  83 PRO D  345  GLU D  347  5                                   3    
HELIX   84  84 LYS D  348  GLY D  364  1                                  17    
HELIX   85  85 LEU D  374  THR D  379  5                                   6    
HELIX   86  86 THR D  384  GLY D  398  1                                  15    
HELIX   87  87 SER D  405  LYS D  410  1                                   6    
HELIX   88  88 PHE D  413  VAL D  432  1                                  20    
HELIX   89  89 TYR D  433  ALA D  445  1                                  13    
HELIX   90  90 ASP D  450  CYS D  466  1                                  17    
HELIX   91  91 GLY D  478  TYR D  487  1                                  10    
HELIX   92  92 SER D  499  VAL D  506  1                                   8    
HELIX   93  93 HIS D  507  CYS D  509  5                                   3    
HELIX   94  94 ILE D  524  ARG D  543  1                                  20    
SHEET    1  AA10 SER A  89  ILE A  94  0                                        
SHEET    2  AA10 CYS A 401  LEU A 404  1  O  ILE A 402   N  ILE A  91           
SHEET    3  AA10 VAL A 367  ALA A 370  1  O  CYS A 369   N  MET A 403           
SHEET    4  AA10 ILE A 333  ALA A 336  1  O  ILE A 333   N  VAL A 368           
SHEET    5  AA10 LYS A 309  ILE A 314  1  O  SER A 312   N  MET A 334           
SHEET    6  AA10 ILE A 282  ALA A 285  1  O  VAL A 283   N  ILE A 311           
SHEET    7  AA10 ALA A 152  ASP A 156  1  O  LEU A 155   N  PHE A 284           
SHEET    8  AA10 MET A 112  ASN A 118  1  O  ASN A 113   N  ALA A 152           
SHEET    9  AA10 SER A  89  ILE A  94  1  O  ILE A  90   N  ASN A 113           
SHEET   10  AA10 SER A  89  ILE A  94  0                                        
SHEET    1  AB 2 VAL A 175  LEU A 177  0                                        
SHEET    2  AB 2 GLY A 244  LEU A 246 -1  O  GLY A 244   N  LEU A 177           
SHEET    1  AC 6 THR A 199  TRP A 201  0                                        
SHEET    2  AC 6 GLN A 182  THR A 186  1  O  LEU A 184   N  VAL A 200           
SHEET    3  AC 6 LEU A 236  ASN A 242 -1  O  LEU A 236   N  VAL A 185           
SHEET    4  AC 6 ILE A 224  VAL A 228 -1  O  SER A 225   N  GLU A 241           
SHEET    5  AC 6 ARG A 216  ILE A 219 -1  O  ILE A 217   N  LEU A 226           
SHEET    6  AC 6 VAL A 252  ASN A 253 -1  O  ASN A 253   N  TYR A 218           
SHEET    1  AD10 VAL A 512  LEU A 516  0                                        
SHEET    2  AD10 ALA A 492  THR A 497  1  O  VAL A 493   N  PHE A 513           
SHEET    3  AD10 ALA A 470  LEU A 474  1  O  ILE A 471   N  ILE A 494           
SHEET    4  AD10 LEU A 551  GLY A 557  1  O  ILE A 553   N  ILE A 472           
SHEET    5  AD10 THR A 565  SER A 572 -1  N  ASN A 566   O  THR A 556           
SHEET    6  AD10 THR B 565  SER B 572 -1  O  ASN B 566   N  VAL A 570           
SHEET    7  AD10 LEU B 551  GLY B 557 -1  O  VAL B 552   N  LEU B 571           
SHEET    8  AD10 ALA B 470  LEU B 474  1  O  ALA B 470   N  ILE B 553           
SHEET    9  AD10 ALA B 492  THR B 497  1  O  ALA B 492   N  ILE B 471           
SHEET   10  AD10 VAL B 512  LEU B 516  1  O  PHE B 513   N  ALA B 495           
SHEET    1  BA 9 SER B  89  ILE B  94  0                                        
SHEET    2  BA 9 CYS B 401  LEU B 404  1  O  ILE B 402   N  ILE B  91           
SHEET    3  BA 9 VAL B 367  ALA B 370  1  O  CYS B 369   N  MET B 403           
SHEET    4  BA 9 ILE B 333  ALA B 336  1  O  ILE B 333   N  VAL B 368           
SHEET    5  BA 9 LYS B 309  ILE B 314  1  O  SER B 312   N  MET B 334           
SHEET    6  BA 9 ILE B 282  ALA B 285  1  O  VAL B 283   N  ILE B 311           
SHEET    7  BA 9 ALA B 152  ASP B 156  1  O  LEU B 155   N  PHE B 284           
SHEET    8  BA 9 MET B 112  ASN B 118  1  O  ASN B 113   N  ALA B 152           
SHEET    9  BA 9 SER B  89  ILE B  94  1  O  ILE B  90   N  ASN B 113           
SHEET    1  BB 2 GLU B 176  LEU B 177  0                                        
SHEET    2  BB 2 GLY B 244  VAL B 245 -1  O  GLY B 244   N  LEU B 177           
SHEET    1  BC 2 LEU B 184  THR B 186  0                                        
SHEET    2  BC 2 THR B 199  TRP B 201  1  O  VAL B 200   N  THR B 186           
SHEET    1  BD 3 ILE B 224  VAL B 227  0                                        
SHEET    2  BD 3 ARG B 216  ILE B 219 -1  O  ILE B 217   N  LEU B 226           
SHEET    3  BD 3 VAL B 252  ASN B 253 -1  O  ASN B 253   N  TYR B 218           
SHEET    1  CA 9 SER C  89  ILE C  94  0                                        
SHEET    2  CA 9 CYS C 401  LEU C 404  1  O  ILE C 402   N  ILE C  91           
SHEET    3  CA 9 VAL C 367  ALA C 370  1  O  CYS C 369   N  MET C 403           
SHEET    4  CA 9 ILE C 333  ALA C 336  1  O  ILE C 333   N  VAL C 368           
SHEET    5  CA 9 LYS C 309  ILE C 314  1  O  SER C 312   N  MET C 334           
SHEET    6  CA 9 ILE C 282  ALA C 285  1  O  VAL C 283   N  ILE C 311           
SHEET    7  CA 9 ALA C 152  ASP C 156  1  O  LEU C 155   N  PHE C 284           
SHEET    8  CA 9 ILE C 114  ASN C 118  1  O  ALA C 115   N  ALA C 154           
SHEET    9  CA 9 SER C  89  ILE C  94  1  O  ALA C  92   N  ARG C 116           
SHEET    1  CB 7 ILE C 162  ARG C 163  0                                        
SHEET    2  CB 7 GLY C 251  ASN C 253 -1  O  VAL C 252   N  ILE C 162           
SHEET    3  CB 7 GLY C 215  ILE C 219 -1  O  TYR C 218   N  ASN C 253           
SHEET    4  CB 7 ILE C 224  LYS C 230 -1  O  ILE C 224   N  ILE C 219           
SHEET    5  CB 7 LEU C 236  ASN C 242 -1  O  VAL C 237   N  LYS C 230           
SHEET    6  CB 7 GLN C 182  THR C 186 -1  O  VAL C 183   N  THR C 238           
SHEET    7  CB 7 THR C 199  TRP C 201  1  O  VAL C 200   N  THR C 186           
SHEET    1  CC 2 VAL C 175  LEU C 177  0                                        
SHEET    2  CC 2 GLY C 244  LEU C 246 -1  O  GLY C 244   N  LEU C 177           
SHEET    1  CD10 VAL C 512  LEU C 516  0                                        
SHEET    2  CD10 ALA C 492  THR C 497  1  O  VAL C 493   N  PHE C 513           
SHEET    3  CD10 ALA C 470  LEU C 474  1  O  ILE C 471   N  ILE C 494           
SHEET    4  CD10 LEU C 551  GLY C 557  1  O  ILE C 553   N  ILE C 472           
SHEET    5  CD10 THR C 565  SER C 572 -1  N  ASN C 566   O  THR C 556           
SHEET    6  CD10 THR D 565  SER D 572 -1  O  ASN D 566   N  VAL C 570           
SHEET    7  CD10 LEU D 551  GLY D 557 -1  O  VAL D 552   N  LEU D 571           
SHEET    8  CD10 ALA D 470  LEU D 474  1  O  ALA D 470   N  ILE D 553           
SHEET    9  CD10 ALA D 492  THR D 497  1  O  ALA D 492   N  ILE D 471           
SHEET   10  CD10 VAL D 512  LEU D 516  1  O  PHE D 513   N  ALA D 495           
SHEET    1  DA17 SER D  89  ILE D  94  0                                        
SHEET    2  DA17 CYS D 401  LEU D 404  1  O  ILE D 402   N  ILE D  91           
SHEET    3  DA17 VAL D 367  ALA D 370  1  O  CYS D 369   N  MET D 403           
SHEET    4  DA17 ILE D 114  ASN D 118  0                                        
SHEET    5  DA17 SER D  89  ILE D  94  1  O  ALA D  92   N  ARG D 116           
SHEET    6  DA17 ALA D 152  ASP D 156  0                                        
SHEET    7  DA17 ILE D 114  ASN D 118  1  O  ALA D 115   N  ALA D 154           
SHEET    8  DA17 ILE D 282  ALA D 285  0                                        
SHEET    9  DA17 ALA D 152  ASP D 156  1  O  LEU D 155   N  PHE D 284           
SHEET   10  DA17 LYS D 309  ILE D 314  0                                        
SHEET   11  DA17 ILE D 282  ALA D 285  1  O  VAL D 283   N  ILE D 311           
SHEET   12  DA17 ILE D 333  ALA D 336  0                                        
SHEET   13  DA17 LYS D 309  ILE D 314  1  O  SER D 312   N  MET D 334           
SHEET   14  DA17 VAL D 367  ALA D 370  0                                        
SHEET   15  DA17 ILE D 333  ALA D 336  1  O  ILE D 333   N  VAL D 368           
SHEET   16  DA17 CYS D 401  LEU D 404  0                                        
SHEET   17  DA17 SER D  89  ILE D  94  1  O  SER D  89   N  ILE D 402           
SHEET    1  DB 2 VAL D 175  LEU D 177  0                                        
SHEET    2  DB 2 GLY D 244  LEU D 246 -1  O  GLY D 244   N  LEU D 177           
SHEET    1  DC 2 VAL D 185  THR D 186  0                                        
SHEET    2  DC 2 VAL D 200  TRP D 201  1  O  VAL D 200   N  THR D 186           
SHEET    1  DD 4 VAL D 237  ASN D 242  0                                        
SHEET    2  DD 4 ILE D 224  LYS D 230 -1  O  SER D 225   N  GLU D 241           
SHEET    3  DD 4 ARG D 216  ILE D 219 -1  O  ILE D 217   N  LEU D 226           
SHEET    4  DD 4 VAL D 252  ASN D 253 -1  O  ASN D 253   N  TYR D 218           
LINK         OE2 GLU A 315                 O3P PGA A 581     1555   1555  1.73  
LINK         P   PGA A 581                MN    MN A 583     1555   1555  1.31  
LINK         O4P PGA A 581                MN    MN A 583     1555   1555  1.22  
LINK         K     K A 582                 OD1 ASP A 156     1555   1555  2.66  
LINK         K     K A 582                 O   THR A 157     1555   1555  2.74  
LINK         K     K A 582                 OG  SER A 286     1555   1555  3.45  
LINK         K     K A 582                 OG  SER A 120     1555   1555  3.02  
LINK        MN    MN A 583                 OD2 ASP A 339     1555   1555  1.65  
LINK        MN    MN A 583                 O3P PGA A 581     1555   1555  1.89  
LINK        MN    MN A 583                 O2P PGA A 581     1555   1555  1.99  
LINK        MN    MN A 583                 OE2 GLU A 315     1555   1555  2.02  
LINK         P   PGA B 581                MN    MN B 587     1555   1555  1.59  
LINK         O4P PGA B 581                MN    MN B 587     1555   1555  1.26  
LINK         K     K B 586                 OG  SER B 120     1555   1555  3.19  
LINK         K     K B 586                 O   THR B 157     1555   1555  2.98  
LINK         K     K B 586                 OD1 ASN B 118     1555   1555  3.13  
LINK         K     K B 586                 OD1 ASP B 156     1555   1555  2.61  
LINK        MN    MN B 587                 OE2 GLU B 315     1555   1555  1.71  
LINK        MN    MN B 587                 OD2 ASP B 339     1555   1555  1.46  
LINK        MN    MN B 587                 O1P PGA B 581     1555   1555  1.96  
LINK        MN    MN B 587                 O2P PGA B 581     1555   1555  2.27  
LINK         O4P PGA C 581                MN    MN C 591     1555   1555  1.37  
LINK         P   PGA C 581                MN    MN C 591     1555   1555  1.33  
LINK         K     K C 590                 O   THR C 157     1555   1555  2.91  
LINK         K     K C 590                 OD1 ASN C 118     1555   1555  3.04  
LINK         K     K C 590                 OG  SER C 120     1555   1555  2.98  
LINK         K     K C 590                 OD1 ASP C 156     1555   1555  2.71  
LINK        MN    MN C 591                 O1P PGA C 581     1555   1555  1.81  
LINK        MN    MN C 591                 OD2 ASP C 339     1555   1555  1.72  
LINK        MN    MN C 591                 OE2 GLU C 315     1555   1555  1.82  
LINK        MN    MN C 591                 O2P PGA C 581     1555   1555  1.94  
LINK         OE2 GLU D 315                 O4P PGA D 581     1555   1555  1.65  
LINK         P   PGA D 581                MN    MN D 595     1555   1555  1.03  
LINK         O4P PGA D 581                MN    MN D 595     1555   1555  1.31  
LINK         O2P PGA D 581                MN    MN D 595     1555   1555  1.35  
LINK         K     K D 594                 O   THR D 157     1555   1555  2.97  
LINK         K     K D 594                 OD1 ASP D 156     1555   1555  2.62  
LINK         K     K D 594                 OG  SER D 120     1555   1555  2.89  
LINK         K     K D 594                 OD1 ASN D 118     1555   1555  3.14  
LINK        MN    MN D 595                 OE2 GLU D 315     1555   1555  1.85  
LINK        MN    MN D 595                 OD2 ASP D 339     1555   1555  1.65  
LINK        MN    MN D 595                 O3P PGA D 581     1555   1555  1.98  
SITE     1 AC1 14 LEU A 474  THR A 475  THR A 476  THR A 477                    
SITE     2 AC1 14 SER A 480  TRP A 525  ARG A 532  GLY A 557                    
SITE     3 AC1 14 ARG A 559  GLY A 561  SER A 562  GLY A 563                    
SITE     4 AC1 14 TYR A 564  THR A 565                                          
SITE     1 AC2  8 SER A 286  LYS A 313  GLU A 315  ALA A 336                    
SITE     2 AC2  8 GLY A 338  ASP A 339  THR A 371   MN A 583                    
SITE     1 AC3  5 ASN A 118  SER A 120  ASP A 156  THR A 157                    
SITE     2 AC3  5 SER A 286                                                     
SITE     1 AC4  3 GLU A 315  ASP A 339  PGA A 581                               
SITE     1 AC5 14 LEU B 474  THR B 475  THR B 476  THR B 477                    
SITE     2 AC5 14 GLY B 478  HIS B 479  SER B 480  ARG B 532                    
SITE     3 AC5 14 GLY B 557  ARG B 559  GLY B 561  SER B 562                    
SITE     4 AC5 14 GLY B 563  TYR B 564                                          
SITE     1 AC6  9 SER B 286  LYS B 313  GLU B 315  ALA B 336                    
SITE     2 AC6  9 ARG B 337  GLY B 338  ASP B 339  THR B 371                    
SITE     3 AC6  9  MN B 587                                                     
SITE     1 AC7  6 ASN B 118  SER B 120  ASP B 156  THR B 157                    
SITE     2 AC7  6 SER B 286  LYS B 313                                          
SITE     1 AC8  3 GLU B 315  ASP B 339  PGA B 581                               
SITE     1 AC9 16 LEU C 474  THR C 475  THR C 476  THR C 477                    
SITE     2 AC9 16 HIS C 479  SER C 480  TRP C 525  ARG C 532                    
SITE     3 AC9 16 GLY C 557  ARG C 559  PRO C 560  GLY C 561                    
SITE     4 AC9 16 SER C 562  GLY C 563  TYR C 564  THR C 565                    
SITE     1 BC1  8 SER C 286  LYS C 313  GLU C 315  ALA C 336                    
SITE     2 BC1  8 GLY C 338  ASP C 339  THR C 371   MN C 591                    
SITE     1 BC2  5 ASN C 118  SER C 120  ASP C 156  THR C 157                    
SITE     2 BC2  5 SER C 286                                                     
SITE     1 BC3  3 GLU C 315  ASP C 339  PGA C 581                               
SITE     1 BC4 14 LEU D 474  THR D 475  THR D 476  THR D 477                    
SITE     2 BC4 14 SER D 480  TRP D 525  ARG D 532  GLY D 557                    
SITE     3 BC4 14 ARG D 559  GLY D 561  SER D 562  GLY D 563                    
SITE     4 BC4 14 TYR D 564  THR D 565                                          
SITE     1 BC5  8 SER D 286  LYS D 313  GLU D 315  ALA D 336                    
SITE     2 BC5  8 GLY D 338  ASP D 339  THR D 371   MN D 595                    
SITE     1 BC6  5 ASN D 118  SER D 120  ASP D 156  THR D 157                    
SITE     2 BC6  5 SER D 286                                                     
SITE     1 BC7  3 GLU D 315  ASP D 339  PGA D 581                               
CRYST1   74.036  171.795   85.086  90.00  91.17  90.00 P 1 21 1      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      0.013507  0.000000  0.000276        0.00000                         
SCALE2      0.000000  0.005821  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011755        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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