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Database: PDB
Entry: 2VGB
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Original site: 2VGB 
HEADER    TRANSFERASE                             12-NOV-07   2VGB              
TITLE     HUMAN ERYTHROCYTE PYRUVATE KINASE                                     
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 1, PYRUVATE KINASE;                          
COMPND   7 EC: 2.7.1.40;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 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.CHIARELLI,R.FORTIN,M.DOLZAN,A.GALIZZI,D.J.ABRAHAM,      
AUTHOR   2 C.WANG,P.BIANCHI,A.ZANELLA,A.MATTEVI                                 
REVDAT   5   08-MAY-19 2VGB    1       REMARK                                   
REVDAT   4   16-MAY-18 2VGB    1       REMARK                                   
REVDAT   3   13-JUL-11 2VGB    1       VERSN                                    
REVDAT   2   24-FEB-09 2VGB    1       VERSN                                    
REVDAT   1   20-NOV-07 2VGB    0                                                
SPRSDE     20-NOV-07 2VGB      1LIU                                             
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.    2.73 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) : 2.73                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 52174                          
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) : 0.229                           
REMARK   3   R VALUE            (WORKING SET) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2780                            
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) : 2.73                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.79                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3194                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3340                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 151                          
REMARK   3   BIN FREE R VALUE                    : 0.3840                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 15423                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 124                                     
REMARK   3   SOLVENT ATOMS            : 65                                      
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) : 40.86                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.14000                                             
REMARK   3    B22 (A**2) : 0.20000                                              
REMARK   3    B33 (A**2) : -0.05000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.12000                                              
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): 0.416         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.332         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 35.492        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.915                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.881                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 15782 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 21409 ; 1.513 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2029 ; 5.423 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   657 ;36.011 ;23.014       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2668 ;20.809 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   158 ;23.116 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2490 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11775 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  7652 ; 0.257 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 10829 ; 0.322 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   658 ; 0.163 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   116 ; 0.540 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.315 ; 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): 10104 ; 0.399 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16275 ; 0.785 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5710 ; 1.546 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5134 ; 2.564 ; 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 : 3                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     57       A     161      1                      
REMARK   3           1     B     57       B     161      1                      
REMARK   3           1     C     57       C     161      1                      
REMARK   3           1     D     57       D     161      1                      
REMARK   3           2     A    261       A     430      1                      
REMARK   3           2     B    261       B     430      1                      
REMARK   3           2     C    261       C     430      1                      
REMARK   3           2     D    261       D     430      1                      
REMARK   3           3     A    580       A     580      4                      
REMARK   3           3     B    580       B     580      4                      
REMARK   3           3     C    580       C     580      4                      
REMARK   3           3     D    580       D     580      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   2066 ;  0.07 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):   2066 ;  0.06 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    C    (A):   2066 ;  0.06 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    D    (A):   2066 ;  0.05 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):     20 ;  0.28 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):     20 ;  0.62 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):     20 ;  0.43 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):     20 ;  0.35 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):   2066 ;  0.09 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):   2066 ;  0.09 ;  0.50           
REMARK   3   TIGHT THERMAL      1    C (A**2):   2066 ;  0.10 ;  0.50           
REMARK   3   TIGHT THERMAL      1    D (A**2):   2066 ;  0.10 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):     20 ;  0.83 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):     20 ;  1.25 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):     20 ;  1.17 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    D (A**2):     20 ;  0.81 ;  2.00           
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    162       A     260      4                      
REMARK   3           1     B    162       B     260      4                      
REMARK   3           1     C    162       C     260      4                      
REMARK   3           1     D    162       D     260      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):    541 ;  0.40 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    B    (A):    541 ;  0.30 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    C    (A):    541 ;  0.23 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    D    (A):    541 ;  0.25 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    A (A**2):    541 ;  0.41 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    B (A**2):    541 ;  0.36 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    C (A**2):    541 ;  0.44 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    D (A**2):    541 ;  0.46 ;  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 : 2                               
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           2     A    581       A     581      4                      
REMARK   3           2     B    581       B     581      4                      
REMARK   3           2     C    581       C     581      4                      
REMARK   3           2     D    581       D     581      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    A    (A):   1112 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    B    (A):   1112 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    C    (A):   1112 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    D    (A):   1112 ;  0.05 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  3    A    (A):      9 ;  0.26 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  3    B    (A):      9 ;  0.24 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  3    C    (A):      9 ;  0.19 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  3    D    (A):      9 ;  0.35 ;  0.50           
REMARK   3   TIGHT THERMAL      3    A (A**2):   1112 ;  0.08 ;  0.50           
REMARK   3   TIGHT THERMAL      3    B (A**2):   1112 ;  0.07 ;  0.50           
REMARK   3   TIGHT THERMAL      3    C (A**2):   1112 ;  0.09 ;  0.50           
REMARK   3   TIGHT THERMAL      3    D (A**2):   1112 ;  0.08 ;  0.50           
REMARK   3   MEDIUM THERMAL     3    A (A**2):      9 ;  0.28 ;  2.00           
REMARK   3   MEDIUM THERMAL     3    B (A**2):      9 ;  0.46 ;  2.00           
REMARK   3   MEDIUM THERMAL     3    C (A**2):      9 ;  0.31 ;  2.00           
REMARK   3   MEDIUM THERMAL     3    D (A**2):      9 ;  0.38 ;  2.00           
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):  27.9022  -6.5686  37.3360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1639 T22:   0.0030                                     
REMARK   3      T33:  -0.1044 T12:   0.0735                                     
REMARK   3      T13:   0.0277 T23:  -0.0118                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8780 L22:   1.8684                                     
REMARK   3      L33:   1.5789 L12:   0.1428                                     
REMARK   3      L13:   1.0719 L23:   0.4468                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2209 S12:   0.1550 S13:  -0.3718                       
REMARK   3      S21:  -0.0067 S22:  -0.0333 S23:  -0.0336                       
REMARK   3      S31:   0.3819 S32:   0.1085 S33:  -0.1876                       
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):  49.9273  24.1544  33.9283              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0942 T22:   0.2678                                     
REMARK   3      T33:   0.5202 T12:  -0.0302                                     
REMARK   3      T13:   0.0805 T23:   0.1469                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.1872 L22:  11.6732                                     
REMARK   3      L33:  10.7703 L12:  -0.0612                                     
REMARK   3      L13:  -0.3443 L23:   1.7381                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2367 S12:   0.7691 S13:   1.2113                       
REMARK   3      S21:  -0.0518 S22:   0.1215 S23:  -1.7249                       
REMARK   3      S31:  -0.1413 S32:   0.2198 S33:  -0.3582                       
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):  -6.8293 -27.9279  12.4788              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0210 T22:  -0.1004                                     
REMARK   3      T33:  -0.0433 T12:  -0.0130                                     
REMARK   3      T13:   0.0600 T23:   0.0735                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2121 L22:   1.8136                                     
REMARK   3      L33:   2.1907 L12:   0.3638                                     
REMARK   3      L13:   1.1439 L23:  -0.3382                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1057 S12:  -0.3222 S13:  -0.3799                       
REMARK   3      S21:   0.4001 S22:   0.0935 S23:  -0.1703                       
REMARK   3      S31:   0.1305 S32:  -0.0997 S33:  -0.1991                       
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): -40.3889 -19.5393   2.0063              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0613 T22:   0.7433                                     
REMARK   3      T33:   0.6573 T12:  -0.0942                                     
REMARK   3      T13:   0.1766 T23:   0.3164                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.7967 L22:   9.8383                                     
REMARK   3      L33:  17.6017 L12:  -0.4967                                     
REMARK   3      L13:  -0.4898 L23:  -1.9484                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.0607 S12:  -0.0025 S13:   0.3386                       
REMARK   3      S21:  -0.0812 S22:   1.2946 S23:   1.9249                       
REMARK   3      S31:  -0.3117 S32:  -2.5602 S33:  -0.2339                       
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):   9.0178  27.2882  30.8966              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1885 T22:  -0.1358                                     
REMARK   3      T33:  -0.1258 T12:   0.0013                                     
REMARK   3      T13:   0.0353 T23:  -0.0331                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1948 L22:   1.3700                                     
REMARK   3      L33:   2.1764 L12:  -0.2406                                     
REMARK   3      L13:   0.6342 L23:  -0.2900                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0375 S12:   0.0208 S13:   0.1438                       
REMARK   3      S21:  -0.0874 S22:  -0.0253 S23:   0.0986                       
REMARK   3      S31:  -0.1245 S32:  -0.0410 S33:   0.0628                       
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):  15.5615  21.1803  67.4129              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1113 T22:   0.0140                                     
REMARK   3      T33:  -0.1175 T12:  -0.0393                                     
REMARK   3      T13:   0.0336 T23:  -0.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3704 L22:   6.4412                                     
REMARK   3      L33:   5.9273 L12:   0.0833                                     
REMARK   3      L13:  -0.0582 L23:   0.7559                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0701 S12:  -0.4608 S13:  -0.4480                       
REMARK   3      S21:   0.6801 S22:   0.1267 S23:  -0.0665                       
REMARK   3      S31:   0.3466 S32:  -0.0560 S33:  -0.1968                       
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): -11.0003   6.2724  -6.7195              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1963 T22:  -0.1063                                     
REMARK   3      T33:  -0.1328 T12:  -0.0021                                     
REMARK   3      T13:   0.0132 T23:   0.0236                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1383 L22:   2.7547                                     
REMARK   3      L33:   0.8158 L12:   0.3273                                     
REMARK   3      L13:   0.2816 L23:   0.5332                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0934 S12:  -0.0438 S13:   0.2294                       
REMARK   3      S21:   0.1680 S22:  -0.0084 S23:   0.1378                       
REMARK   3      S31:  -0.1126 S32:  -0.0377 S33:   0.1018                       
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):  -4.3537 -22.6928 -29.6628              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1643 T22:  -0.0110                                     
REMARK   3      T33:  -0.0480 T12:  -0.0416                                     
REMARK   3      T13:   0.0659 T23:  -0.0207                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6513 L22:   8.0690                                     
REMARK   3      L33:   6.4676 L12:   1.9334                                     
REMARK   3      L13:  -0.6495 L23:  -1.3336                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0244 S12:   0.3304 S13:  -0.2735                       
REMARK   3      S21:  -1.1082 S22:   0.0727 S23:  -0.2886                       
REMARK   3      S31:   0.5538 S32:   0.2116 S33:  -0.0971                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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 2VGB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-NOV-07.                  
REMARK 100 THE DEPOSITION ID IS D_1290034402.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
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                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55091                              
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     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : 2.100                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.4000                            
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) : 2.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.24000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1PKN                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: RECOMBINANT WILD-TYPE RPK WAS            
REMARK 280  CRYSTALLIZED USING THE VAPOR DIFFUSION METHOD AT 22 C. WELL         
REMARK 280  SOLUTIONS CONSISTED OF 50 MM MES/KOH, PH 6.4, 10 MM MNSO4, AND      
REMARK 280  10-14% W/V PEG8000. HANGING DROPS WERE FORMED BY MIXING EQUAL       
REMARK 280  VOLUMES OF 12 MG/ML PROTEIN IN 50 MM KCL, 5 MM FBP, 5 MM            
REMARK 280  PHOSPHOGLYCOLATE, 20 MM POTASSIUM PHOSPHATE, PH 7.0, AND WELL       
REMARK 280  SOLUTIONS., PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  295K                                                                
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       86.02900            
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: 21560 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 89210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.1 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 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     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     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     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     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     LEU D   167                                                      
REMARK 465     GLN D   168                                                      
REMARK 465     GLY D   169                                                      
REMARK 465     GLY D   170                                                      
REMARK 465     PRO D   171                                                      
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   OG   SER B    89     O    HOH B  2001              2.06            
REMARK 500   O    SER B   144     O    HOH B  2004              2.14            
REMARK 500   OE2  GLU D   315     OD2  ASP D   339              2.17            
REMARK 500   OG   SER C    89     O    HOH C  2001              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   CE1  HIS A   306     NH1  ARG B   322     1655     1.57            
REMARK 500   CE1  HIS A   306     NH2  ARG B   322     1655     1.63            
REMARK 500   NE2  HIS A   306     NH1  ARG B   322     1655     1.65            
REMARK 500   CE1  HIS A   306     CZ   ARG B   322     1655     1.67            
REMARK 500   NE2  HIS A   306     CZ   ARG B   322     1655     2.09            
REMARK 500   NE2  GLN C   258     O    ARG D   298     1556     2.17            
REMARK 500   ND1  HIS A   306     NH2  ARG B   322     1655     2.19            
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    LYS A 410   CD    LYS A 410   CE     -0.161                       
REMARK 500    LYS A 410   CE    LYS A 410   NZ      0.338                       
REMARK 500    SER B 144   CB    SER B 144   OG      0.360                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    VAL A 473   CB  -  CA  -  C   ANGL. DEV. = -12.7 DEGREES          
REMARK 500    VAL B 473   CB  -  CA  -  C   ANGL. DEV. = -11.9 DEGREES          
REMARK 500    VAL C 473   CB  -  CA  -  C   ANGL. DEV. = -14.0 DEGREES          
REMARK 500    LEU D 374   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    VAL D 473   CB  -  CA  -  C   ANGL. DEV. = -12.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A  83       79.17   -158.49                                   
REMARK 500    ALA A  84      148.77    174.10                                   
REMARK 500    SER A  98       42.19   -142.40                                   
REMARK 500    GLN A 168       99.87    -66.27                                   
REMARK 500    ARG A 192      -14.66    -47.94                                   
REMARK 500    ARG A 194       48.58    -99.23                                   
REMARK 500    ASP A 220       78.29     53.54                                   
REMARK 500    GLU A 234       -3.85   -152.42                                   
REMARK 500    THR A 371      120.33     88.40                                   
REMARK 500    LEU A 374       38.78   -146.41                                   
REMARK 500    SER A 405      -97.90   -126.90                                   
REMARK 500    LEU A 447      164.40    -49.94                                   
REMARK 500    ARG A 486      -38.04    -33.69                                   
REMARK 500    ASN A 566       16.29   -169.82                                   
REMARK 500    GLN B  59       16.07     59.31                                   
REMARK 500    VAL B  83       81.88   -160.49                                   
REMARK 500    ALA B  84      150.75    170.94                                   
REMARK 500    VAL B 213      119.39    -36.74                                   
REMARK 500    ASP B 220       93.75     67.17                                   
REMARK 500    ARG B 249       72.50     47.12                                   
REMARK 500    GLU B 304        1.08    -61.30                                   
REMARK 500    THR B 371      118.79     86.34                                   
REMARK 500    LEU B 374       37.30   -152.58                                   
REMARK 500    SER B 405      -96.30   -125.20                                   
REMARK 500    PHE B 413       51.84   -141.65                                   
REMARK 500    LEU B 447      169.02    -49.21                                   
REMARK 500    ARG B 486      -37.44    -39.11                                   
REMARK 500    THR B 556     -158.87   -134.88                                   
REMARK 500    ASN B 566       14.34   -167.37                                   
REMARK 500    VAL C  83       73.60   -159.17                                   
REMARK 500    PHE C 119        1.00    -69.91                                   
REMARK 500    ASP C 220       82.14     68.39                                   
REMARK 500    THR C 371      119.97     86.19                                   
REMARK 500    LEU C 374       40.89   -147.05                                   
REMARK 500    SER C 405      -92.67   -126.84                                   
REMARK 500    LEU C 447      167.50    -47.43                                   
REMARK 500    ASN C 566       14.48   -169.51                                   
REMARK 500    VAL D  83       79.76   -162.43                                   
REMARK 500    ALA D  84      149.77    172.56                                   
REMARK 500    PRO D 160       59.17    -69.56                                   
REMARK 500    ASP D 220       82.42     61.76                                   
REMARK 500    LYS D 230      133.97   -172.71                                   
REMARK 500    THR D 371      123.28     90.82                                   
REMARK 500    LEU D 374       36.00   -148.35                                   
REMARK 500    SER D 405      -95.46   -127.35                                   
REMARK 500    PHE D 413       55.67   -143.01                                   
REMARK 500    THR D 556     -158.32   -134.04                                   
REMARK 500    ASN D 566       11.48   -166.81                                   
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                               K A 582   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 156   OD1                                                    
REMARK 620 2 THR A 157   O    57.2                                              
REMARK 620 3 SER A 120   OG  147.7 104.2                                        
REMARK 620 4 PGA A 581   O2P  93.4 138.0 114.4                                  
REMARK 620 5 ASN A 118   OD1  88.5 112.1  73.9  94.5                            
REMARK 620 N                    1     2     3     4                             
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 GLU A 315   OE2                                                    
REMARK 620 2 PGA A 581   O1P 100.1                                              
REMARK 620 3 PGA A 581   O1   94.0  72.9                                        
REMARK 620 4 PGA A 581   O4P 165.9  69.5  92.0                                  
REMARK 620 5 ASP A 339   OD2  88.3 165.2  94.5 104.1                            
REMARK 620 N                    1     2     3     4                             
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 ASP B 156   OD1                                                    
REMARK 620 2 PGA B 581   O2P  95.7                                              
REMARK 620 3 ASN B 118   OD1  94.1  93.2                                        
REMARK 620 4 THR B 157   O    61.5 144.2 114.3                                  
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   O1                                                     
REMARK 620 2 PGA B 581   O4P 103.1                                              
REMARK 620 3 PGA B 581   O1P  75.8  64.5                                        
REMARK 620 4 GLU B 315   OE2  94.5 153.0 101.1                                  
REMARK 620 5 ASP B 339   OD2  94.2 117.4 169.8  80.9                            
REMARK 620 N                    1     2     3     4                             
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 ASP C 156   OD1                                                    
REMARK 620 2 THR C 157   O    61.7                                              
REMARK 620 3 PGA C 581   O2P 100.1 137.7                                        
REMARK 620 4 ASN C 118   OD1 101.0 121.6  98.4                                  
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   O1                                                     
REMARK 620 2 PGA C 581   O4P  84.3                                              
REMARK 620 3 PGA C 581   O1P  68.5  66.4                                        
REMARK 620 4 ASP C 339   OD2  91.1 108.3 159.0                                  
REMARK 620 5 GLU C 315   OE2  88.4 166.0  99.8  83.8                            
REMARK 620 N                    1     2     3     4                             
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 ASN D 118   OD1                                                    
REMARK 620 2 ASP D 156   OD1 100.8                                              
REMARK 620 3 PGA D 581   O2P  95.3  99.5                                        
REMARK 620 4 THR D 157   O   119.7  63.3 142.5                                  
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 GLU D 315   OE2                                                    
REMARK 620 2 PGA D 581   O1   90.5                                              
REMARK 620 3 ASP D 339   OD2  80.2  86.5                                        
REMARK 620 4 PGA D 581   O1P 111.9  73.0 155.8                                  
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: 1LIY   RELATED DB: PDB                                   
REMARK 900 HUMAN ERYTHROCYTE PYRUVATE KINASE: ARG479HIS MUTANT                  
REMARK 900 RELATED ID: 1LIU   RELATED DB: PDB                                   
REMARK 900 HUMAN ERYTHROCYTE PYRUVATE KINASE                                    
REMARK 900 RELATED ID: 1LIW   RELATED DB: PDB                                   
REMARK 900 HUMAN ERYTHROCYTE PYRUVATE KINASE: THR384MET MUTANT                  
REMARK 900 RELATED ID: 1LIX   RELATED DB: PDB                                   
REMARK 900 HUMAN ERYTHROCYTE PYRUVATE KINASE: ARG486TRP MUTANT                  
DBREF  2VGB A   47   574  UNP    P30613   KPYR_HUMAN      47    574             
DBREF  2VGB B   47   574  UNP    P30613   KPYR_HUMAN      47    574             
DBREF  2VGB C   47   574  UNP    P30613   KPYR_HUMAN      47    574             
DBREF  2VGB D   47   574  UNP    P30613   KPYR_HUMAN      47    574             
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 ARG 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 ARG 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 ARG 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 ARG 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+)                                                     
FORMUL  21  HOH   *65(H2 O)                                                     
HELIX    1   1 GLN A   60  MET A   65  1                                   6    
HELIX    2   2 THR A   68  CYS A   74  1                                   7    
HELIX    3   3 GLY A   95  ARG A   99  5                                   5    
HELIX    4   4 SER A  100  GLY A  111  1                                  12    
HELIX    5   5 SER A  123  SER A  140  1                                  18    
HELIX    6   6 ASP A  188  THR A  193  5                                   6    
HELIX    7   7 ASN A  206  VAL A  211  1                                   6    
HELIX    8   8 SER A  265  HIS A  278  1                                  14    
HELIX    9   9 LYS A  290  GLY A  302  1                                  13    
HELIX   10  10 PRO A  303  HIS A  306  5                                   4    
HELIX   11  11 ASN A  316  ARG A  322  1                                   7    
HELIX   12  12 ARG A  322  SER A  330  1                                   9    
HELIX   13  13 ARG A  337  ILE A  344  1                                   8    
HELIX   14  14 PRO A  345  GLU A  347  5                                   3    
HELIX   15  15 LYS A  348  GLY A  364  1                                  17    
HELIX   16  16 LEU A  374  THR A  379  5                                   6    
HELIX   17  17 THR A  384  GLY A  398  1                                  15    
HELIX   18  18 SER A  405  LYS A  410  1                                   6    
HELIX   19  19 PHE A  413  VAL A  432  1                                  20    
HELIX   20  20 TYR A  433  ALA A  445  1                                  13    
HELIX   21  21 ASP A  450  CYS A  466  1                                  17    
HELIX   22  22 GLY A  478  ARG A  486  1                                   9    
HELIX   23  23 SER A  499  VAL A  506  1                                   8    
HELIX   24  24 HIS A  507  CYS A  509  5                                   3    
HELIX   25  25 ILE A  524  ARG A  543  1                                  20    
HELIX   26  26 GLN B   60  MET B   65  1                                   6    
HELIX   27  27 THR B   68  CYS B   74  1                                   7    
HELIX   28  28 GLY B   95  ARG B   99  5                                   5    
HELIX   29  29 SER B  100  GLY B  111  1                                  12    
HELIX   30  30 SER B  123  SER B  140  1                                  18    
HELIX   31  31 ASN B  206  VAL B  211  1                                   6    
HELIX   32  32 SER B  265  HIS B  278  1                                  14    
HELIX   33  33 LYS B  290  GLY B  302  1                                  13    
HELIX   34  34 PRO B  303  HIS B  306  5                                   4    
HELIX   35  35 ASN B  316  ARG B  322  1                                   7    
HELIX   36  36 ARG B  322  SER B  330  1                                   9    
HELIX   37  37 ARG B  337  ILE B  344  1                                   8    
HELIX   38  38 PRO B  345  GLU B  347  5                                   3    
HELIX   39  39 LYS B  348  GLY B  364  1                                  17    
HELIX   40  40 LEU B  374  THR B  379  5                                   6    
HELIX   41  41 THR B  384  GLY B  398  1                                  15    
HELIX   42  42 SER B  405  LYS B  410  1                                   6    
HELIX   43  43 PHE B  413  ALA B  431  1                                  19    
HELIX   44  44 TYR B  433  ALA B  445  1                                  13    
HELIX   45  45 ASP B  450  CYS B  466  1                                  17    
HELIX   46  46 GLY B  478  TYR B  487  1                                  10    
HELIX   47  47 SER B  499  VAL B  506  1                                   8    
HELIX   48  48 HIS B  507  CYS B  509  5                                   3    
HELIX   49  49 ILE B  524  ARG B  543  1                                  20    
HELIX   50  50 GLN C   60  MET C   65  1                                   6    
HELIX   51  51 THR C   68  CYS C   74  1                                   7    
HELIX   52  52 GLY C   95  ARG C   99  5                                   5    
HELIX   53  53 SER C  100  GLY C  111  1                                  12    
HELIX   54  54 SER C  123  SER C  140  1                                  18    
HELIX   55  55 ASP C  188  ARG C  192  5                                   5    
HELIX   56  56 ASN C  206  VAL C  211  1                                   6    
HELIX   57  57 SER C  265  HIS C  278  1                                  14    
HELIX   58  58 LYS C  290  GLY C  302  1                                  13    
HELIX   59  59 PRO C  303  HIS C  306  5                                   4    
HELIX   60  60 ASN C  316  ARG C  322  1                                   7    
HELIX   61  61 ARG C  322  SER C  330  1                                   9    
HELIX   62  62 ARG C  337  ILE C  344  1                                   8    
HELIX   63  63 PRO C  345  GLU C  347  5                                   3    
HELIX   64  64 LYS C  348  GLY C  364  1                                  17    
HELIX   65  65 LEU C  374  THR C  379  5                                   6    
HELIX   66  66 THR C  384  GLY C  398  1                                  15    
HELIX   67  67 SER C  405  LYS C  410  1                                   6    
HELIX   68  68 PHE C  413  VAL C  432  1                                  20    
HELIX   69  69 TYR C  433  ALA C  445  1                                  13    
HELIX   70  70 ASP C  450  CYS C  467  1                                  18    
HELIX   71  71 GLY C  478  ARG C  486  1                                   9    
HELIX   72  72 SER C  499  VAL C  506  1                                   8    
HELIX   73  73 HIS C  507  CYS C  509  5                                   3    
HELIX   74  74 ILE C  524  ARG C  543  1                                  20    
HELIX   75  75 GLN D   60  MET D   65  1                                   6    
HELIX   76  76 THR D   68  CYS D   74  1                                   7    
HELIX   77  77 GLY D   95  ARG D   99  5                                   5    
HELIX   78  78 SER D  100  GLY D  111  1                                  12    
HELIX   79  79 SER D  123  SER D  140  1                                  18    
HELIX   80  80 ASP D  188  THR D  193  5                                   6    
HELIX   81  81 ASN D  206  VAL D  211  1                                   6    
HELIX   82  82 SER D  265  HIS D  278  1                                  14    
HELIX   83  83 LYS D  290  GLY D  302  1                                  13    
HELIX   84  84 PRO D  303  HIS D  306  5                                   4    
HELIX   85  85 ASN D  316  ARG D  322  1                                   7    
HELIX   86  86 ARG D  322  SER D  330  1                                   9    
HELIX   87  87 ARG D  337  ILE D  344  1                                   8    
HELIX   88  88 LYS D  348  GLY D  364  1                                  17    
HELIX   89  89 LEU D  374  THR D  379  5                                   6    
HELIX   90  90 THR D  384  GLY D  398  1                                  15    
HELIX   91  91 SER D  405  LYS D  410  1                                   6    
HELIX   92  92 PHE D  413  ALA D  431  1                                  19    
HELIX   93  93 TYR D  433  ALA D  445  1                                  13    
HELIX   94  94 ASP D  450  CYS D  466  1                                  17    
HELIX   95  95 GLY D  478  ARG D  486  1                                   9    
HELIX   96  96 SER D  499  VAL D  506  1                                   8    
HELIX   97  97 HIS D  507  CYS D  509  5                                   3    
HELIX   98  98 ILE D  524  ARG D  543  1                                  20    
SHEET    1  AA10 SER A  89  THR A  93  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 GLY A 332  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  THR A  93  1  O  ILE A  90   N  ASN A 113           
SHEET   10  AA10 SER A  89  THR A  93  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 GLY A 235  ASN A 242 -1  O  LEU A 236   N  VAL A 185           
SHEET    4  AC 6 ILE A 224  ILE A 231 -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  THR B  93  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 GLY B 332  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  THR B  93  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 6 THR B 199  TRP B 201  0                                        
SHEET    2  BC 6 GLN B 182  THR B 186  1  O  LEU B 184   N  VAL B 200           
SHEET    3  BC 6 THR B 238  ASN B 242 -1  O  THR B 238   N  VAL B 183           
SHEET    4  BC 6 ILE B 224  VAL B 227 -1  O  SER B 225   N  GLU B 241           
SHEET    5  BC 6 ARG B 216  ILE B 219 -1  O  ILE B 217   N  LEU B 226           
SHEET    6  BC 6 VAL B 252  ASN B 253 -1  O  ASN B 253   N  TYR B 218           
SHEET    1  CA 9 SER C  89  THR C  93  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 GLY C 332  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 MET C 112  ASN C 118  1  O  ASN C 113   N  ALA C 152           
SHEET    9  CA 9 SER C  89  THR C  93  1  O  ILE C  90   N  ASN C 113           
SHEET    1  CB 2 VAL C 175  LEU C 177  0                                        
SHEET    2  CB 2 GLY C 244  LEU C 246 -1  O  GLY C 244   N  LEU C 177           
SHEET    1  CC 6 THR C 199  TRP C 201  0                                        
SHEET    2  CC 6 GLN C 182  THR C 186  1  O  LEU C 184   N  VAL C 200           
SHEET    3  CC 6 GLY C 235  ASN C 242 -1  O  LEU C 236   N  VAL C 185           
SHEET    4  CC 6 ILE C 224  GLY C 232 -1  O  SER C 225   N  GLU C 241           
SHEET    5  CC 6 ARG C 216  ILE C 219 -1  O  ILE C 217   N  LEU C 226           
SHEET    6  CC 6 VAL C 252  ASN C 253 -1  O  ASN C 253   N  TYR C 218           
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  THR D  93  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 MET D 112  ASN D 118  0                                        
SHEET    5  DA17 SER D  89  THR D  93  1  O  ILE D  90   N  ASN D 113           
SHEET    6  DA17 ALA D 152  ASP D 156  0                                        
SHEET    7  DA17 MET D 112  ASN D 118  1  O  ASN D 113   N  ALA D 152           
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 GLY D 332  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 GLY D 332  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  THR D  93  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 6 THR D 199  TRP D 201  0                                        
SHEET    2  DC 6 GLN D 182  THR D 186  1  O  LEU D 184   N  VAL D 200           
SHEET    3  DC 6 GLY D 235  ASN D 242 -1  O  LEU D 236   N  VAL D 185           
SHEET    4  DC 6 ILE D 224  GLY D 232 -1  O  SER D 225   N  GLU D 241           
SHEET    5  DC 6 ARG D 216  ILE D 219 -1  O  ILE D 217   N  LEU D 226           
SHEET    6  DC 6 VAL D 252  ASN D 253 -1  O  ASN D 253   N  TYR D 218           
LINK         K     K A 582                 OD1 ASP A 156     1555   1555  2.95  
LINK         K     K A 582                 O   THR A 157     1555   1555  3.03  
LINK         K     K A 582                 OG  SER A 120     1555   1555  3.44  
LINK         K     K A 582                 O2P PGA A 581     1555   1555  3.14  
LINK         K     K A 582                 OD1 ASN A 118     1555   1555  3.15  
LINK        MN    MN A 583                 OE2 GLU A 315     1555   1555  1.61  
LINK        MN    MN A 583                 O1P PGA A 581     1555   1555  2.09  
LINK        MN    MN A 583                 O1  PGA A 581     1555   1555  2.27  
LINK        MN    MN A 583                 O4P PGA A 581     1555   1555  2.37  
LINK        MN    MN A 583                 OD2 ASP A 339     1555   1555  1.87  
LINK         K     K B 586                 OD1 ASP B 156     1555   1555  2.62  
LINK         K     K B 586                 O2P PGA B 581     1555   1555  2.92  
LINK         K     K B 586                 OD1 ASN B 118     1555   1555  3.21  
LINK         K     K B 586                 O   THR B 157     1555   1555  2.87  
LINK        MN    MN B 587                 O1  PGA B 581     1555   1555  2.07  
LINK        MN    MN B 587                 O4P PGA B 581     1555   1555  2.50  
LINK        MN    MN B 587                 O1P PGA B 581     1555   1555  2.19  
LINK        MN    MN B 587                 OE2 GLU B 315     1555   1555  1.75  
LINK        MN    MN B 587                 OD2 ASP B 339     1555   1555  1.79  
LINK         K     K C 590                 OD1 ASP C 156     1555   1555  2.67  
LINK         K     K C 590                 O   THR C 157     1555   1555  2.90  
LINK         K     K C 590                 O2P PGA C 581     1555   1555  2.97  
LINK         K     K C 590                 OD1 ASN C 118     1555   1555  2.90  
LINK        MN    MN C 591                 O1  PGA C 581     1555   1555  2.15  
LINK        MN    MN C 591                 O4P PGA C 581     1555   1555  2.26  
LINK        MN    MN C 591                 O1P PGA C 581     1555   1555  2.32  
LINK        MN    MN C 591                 OD2 ASP C 339     1555   1555  1.72  
LINK        MN    MN C 591                 OE2 GLU C 315     1555   1555  1.57  
LINK         K     K D 594                 OD1 ASN D 118     1555   1555  2.97  
LINK         K     K D 594                 OD1 ASP D 156     1555   1555  2.63  
LINK         K     K D 594                 O2P PGA D 581     1555   1555  2.89  
LINK         K     K D 594                 O   THR D 157     1555   1555  3.04  
LINK        MN    MN D 595                 OE2 GLU D 315     1555   1555  1.52  
LINK        MN    MN D 595                 O1  PGA D 581     1555   1555  1.97  
LINK        MN    MN D 595                 OD2 ASP D 339     1555   1555  1.83  
LINK        MN    MN D 595                 O1P PGA D 581     1555   1555  2.38  
SITE     1 AC1 15 LEU A 474  THR A 475  THR A 476  THR A 477                    
SITE     2 AC1 15 SER A 480  TRP A 525  ARG A 532  GLY A 557                    
SITE     3 AC1 15 ARG A 559  PRO A 560  GLY A 561  SER A 562                    
SITE     4 AC1 15 GLY A 563  TYR A 564  THR A 565                               
SITE     1 AC2 10 ARG A 116  LYS A 313  GLU A 315  ALA A 336                    
SITE     2 AC2 10 ARG A 337  GLY A 338  ASP A 339  THR A 371                    
SITE     3 AC2 10   K A 582   MN A 583                                          
SITE     1 AC3  6 ASN A 118  SER A 120  ASP A 156  THR A 157                    
SITE     2 AC3  6 LYS A 313  PGA A 581                                          
SITE     1 AC4  3 GLU A 315  ASP A 339  PGA A 581                               
SITE     1 AC5 15 LEU B 474  THR B 475  THR B 476  THR B 477                    
SITE     2 AC5 15 SER B 480  TRP B 525  ARG B 532  GLY B 557                    
SITE     3 AC5 15 ARG B 559  PRO B 560  GLY B 561  SER B 562                    
SITE     4 AC5 15 GLY B 563  TYR B 564  THR B 565                               
SITE     1 AC6 11 ARG B 116  LYS B 313  GLU B 315  ALA B 336                    
SITE     2 AC6 11 ARG B 337  GLY B 338  ASP B 339  THR B 371                    
SITE     3 AC6 11   K B 586   MN B 587  HOH B2010                               
SITE     1 AC7  6 ASN B 118  ASP B 156  THR B 157  SER B 286                    
SITE     2 AC7  6 LYS B 313  PGA B 581                                          
SITE     1 AC8  3 GLU B 315  ASP B 339  PGA B 581                               
SITE     1 AC9 14 LEU C 474  THR C 475  THR C 476  THR C 477                    
SITE     2 AC9 14 SER C 480  TRP C 525  ARG C 532  GLY C 557                    
SITE     3 AC9 14 ARG C 559  GLY C 561  SER C 562  GLY C 563                    
SITE     4 AC9 14 TYR C 564  HOH C2019                                          
SITE     1 BC1 11 ARG C 116  LYS C 313  GLU C 315  ALA C 336                    
SITE     2 BC1 11 ARG C 337  GLY C 338  ASP C 339  THR C 371                    
SITE     3 BC1 11   K C 590   MN C 591  HOH C2014                               
SITE     1 BC2  5 ASN C 118  ASP C 156  THR C 157  LYS C 313                    
SITE     2 BC2  5 PGA C 581                                                     
SITE     1 BC3  3 GLU C 315  ASP C 339  PGA C 581                               
SITE     1 BC4 15 LEU D 474  THR D 475  THR D 476  THR D 477                    
SITE     2 BC4 15 SER D 480  TRP D 525  ARG D 532  GLY D 557                    
SITE     3 BC4 15 ARG D 559  PRO D 560  GLY D 561  SER D 562                    
SITE     4 BC4 15 GLY D 563  TYR D 564  THR D 565                               
SITE     1 BC5 10 ARG D 116  LYS D 313  GLU D 315  ALA D 336                    
SITE     2 BC5 10 ARG D 337  GLY D 338  ASP D 339  THR D 371                    
SITE     3 BC5 10   K D 594   MN D 595                                          
SITE     1 BC6  6 ASN D 118  SER D 120  ASP D 156  THR D 157                    
SITE     2 BC6  6 LYS D 313  PGA D 581                                          
SITE     1 BC7  3 GLU D 315  ASP D 339  PGA D 581                               
CRYST1   74.413  172.058   85.512  90.00  92.46  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      0.013439  0.000000  0.000577        0.00000                         
SCALE2      0.000000  0.005812  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011705        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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