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Database: PDB
Entry: 3PUV
LinkDB: 3PUV
Original site: 3PUV 
HEADER    HYDROLASE/TRANSPORT PROTEIN             06-DEC-10   3PUV              
TITLE     CRYSTAL STRUCTURE OF AN OUTWARD-FACING MBP-MALTOSE TRANSPORTER COMPLEX
TITLE    2 BOUND TO ADP-VO4                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MALTOSE-BINDING PERIPLASMIC PROTEIN;                       
COMPND   3 CHAIN: E;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 27-396;                                       
COMPND   5 SYNONYM: MMBP, MALTODEXTRIN-BINDING PROTEIN;                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: MALTOSE TRANSPORT SYSTEM PERMEASE PROTEIN MALF;            
COMPND   9 CHAIN: F;                                                            
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: MALTOSE TRANSPORT SYSTEM PERMEASE PROTEIN MALG;            
COMPND  13 CHAIN: G;                                                            
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 4;                                                           
COMPND  16 MOLECULE: MALTOSE/MALTODEXTRIN IMPORT ATP-BINDING PROTEIN MALK;      
COMPND  17 CHAIN: A, B;                                                         
COMPND  18 EC: 3.6.3.19;                                                        
COMPND  19 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: B4034, ECDH10B_4223, JW3994, MALE;                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PJF2;                                     
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  12 ORGANISM_TAXID: 83333;                                               
SOURCE  13 STRAIN: K12;                                                         
SOURCE  14 GENE: B4033, ECDH10B_4222, JW3993, MALF;                             
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PFG23;                                    
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  21 ORGANISM_TAXID: 83333;                                               
SOURCE  22 STRAIN: K12;                                                         
SOURCE  23 GENE: B4032, ECDH10B_4221, JW3992, MALG;                             
SOURCE  24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  27 EXPRESSION_SYSTEM_PLASMID: PFG23;                                    
SOURCE  28 MOL_ID: 4;                                                           
SOURCE  29 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  30 ORGANISM_TAXID: 83333;                                               
SOURCE  31 STRAIN: K12;                                                         
SOURCE  32 GENE: B4035, ECDH10B_4224, JW3995, MALK;                             
SOURCE  33 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  34 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  35 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  36 EXPRESSION_SYSTEM_PLASMID: PKJ                                       
KEYWDS    ATP BINDING CASSETTE, NUCLEOTIDE BINDING DOMAIN, SUBSTRATE BINDING    
KEYWDS   2 PROTEIN, ABC TRANSPORTER, IMPORTER, ATPASE, ATP BINDING,             
KEYWDS   3 MALTODEXTRIN BINDING, TRANSMEMBRANE INTEGRAL MEMBRANE, HYDROLASE-    
KEYWDS   4 TRANSPORT PROTEIN COMPLEX                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.L.OLDHAM,J.CHEN                                                     
REVDAT   2   28-SEP-11 3PUV    1       JRNL                                     
REVDAT   1   10-AUG-11 3PUV    0                                                
JRNL        AUTH   M.L.OLDHAM,J.CHEN                                            
JRNL        TITL   SNAPSHOTS OF THE MALTOSE TRANSPORTER DURING ATP HYDROLYSIS.  
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 108 15152 2011              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   21825153                                                     
JRNL        DOI    10.1073/PNAS.1108858108                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 63.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 76178                          
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) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4002                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1217                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 13.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2840                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 68                           
REMARK   3   BIN FREE R VALUE                    : 0.3150                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14602                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 262                                     
REMARK   3   SOLVENT ATOMS            : 180                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.71                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.52000                                             
REMARK   3    B22 (A**2) : 1.13000                                              
REMARK   3    B33 (A**2) : 1.52000                                              
REMARK   3    B12 (A**2) : -1.80000                                             
REMARK   3    B13 (A**2) : -0.67000                                             
REMARK   3    B23 (A**2) : 1.29000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.619         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.321         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.236         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.152        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.918                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.893                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 15234 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 20678 ; 0.936 ; 4.884       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1885 ; 4.237 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   627 ;37.824 ;24.226       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2513 ;15.226 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    79 ;15.348 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2362 ; 0.059 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11282 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  9380 ; 0.182 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15120 ; 0.345 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5854 ; 0.421 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5557 ; 0.723 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 16                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A    29                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.4510 -10.4010  17.1640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7254 T22:   0.2640                                     
REMARK   3      T33:   0.1550 T12:  -0.1607                                     
REMARK   3      T13:   0.1789 T23:   0.0017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.8942 L22:   7.2230                                     
REMARK   3      L33:   6.5953 L12:  -1.8804                                     
REMARK   3      L13:  -0.0492 L23:   1.6517                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0656 S12:   0.4969 S13:  -0.3610                       
REMARK   3      S21:   0.4503 S22:  -0.2183 S23:   0.8650                       
REMARK   3      S31:   1.1021 S32:  -0.4664 S33:   0.1527                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 5                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    30        A    94                          
REMARK   3    RESIDUE RANGE :   A  1501        A  1501                          
REMARK   3    RESIDUE RANGE :   A  2501        A  2501                          
REMARK   3    RESIDUE RANGE :   A  3001        A  3001                          
REMARK   3    RESIDUE RANGE :   A   382        A   383                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.1960  -1.7090  21.7390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4788 T22:   0.1931                                     
REMARK   3      T33:   0.0649 T12:   0.0645                                     
REMARK   3      T13:   0.0838 T23:   0.0314                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2862 L22:   4.7058                                     
REMARK   3      L33:   4.2789 L12:   0.0248                                     
REMARK   3      L13:   0.8295 L23:   1.8846                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0729 S12:  -0.2458 S13:  -0.0819                       
REMARK   3      S21:   0.7364 S22:   0.0617 S23:   0.3142                       
REMARK   3      S31:   0.9244 S32:  -0.3180 S33:   0.0112                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    95        A   188                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.0520   3.5400  21.0000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4688 T22:   0.4325                                     
REMARK   3      T33:   0.3911 T12:   0.2268                                     
REMARK   3      T13:  -0.0935 T23:  -0.1547                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9134 L22:   3.5000                                     
REMARK   3      L33:   4.0879 L12:   0.7823                                     
REMARK   3      L13:  -1.4451 L23:   0.7189                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1100 S12:  -0.3854 S13:  -0.0857                       
REMARK   3      S21:   0.5421 S22:   0.3409 S23:  -0.9004                       
REMARK   3      S31:   0.7063 S32:   0.9482 S33:  -0.2309                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   189        A   289                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.2300 -17.0670  -6.9460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6819 T22:   0.0811                                     
REMARK   3      T33:   0.0796 T12:   0.0988                                     
REMARK   3      T13:   0.0147 T23:  -0.0292                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4554 L22:   6.5237                                     
REMARK   3      L33:   5.0224 L12:   0.0004                                     
REMARK   3      L13:   0.0765 L23:   4.1593                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1864 S12:   0.1847 S13:  -0.2209                       
REMARK   3      S21:  -0.4810 S22:  -0.2069 S23:   0.2199                       
REMARK   3      S31:   0.2674 S32:  -0.2736 S33:   0.0205                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   290        A   372                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.1190 -11.5720 -16.5270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4284 T22:   0.2813                                     
REMARK   3      T33:   0.1786 T12:   0.2160                                     
REMARK   3      T13:   0.2313 T23:  -0.1365                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0465 L22:   7.7244                                     
REMARK   3      L33:   5.5917 L12:   2.9939                                     
REMARK   3      L13:  -0.3429 L23:  -1.0723                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0725 S12:   0.5629 S13:  -0.1614                       
REMARK   3      S21:  -1.5175 S22:   0.1172 S23:  -0.4664                       
REMARK   3      S31:   0.4888 S32:   0.4537 S33:  -0.1897                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     2        B    29                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.9590  27.6530  -0.8960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8635 T22:   0.2321                                     
REMARK   3      T33:   0.6598 T12:  -0.0171                                     
REMARK   3      T13:   0.4627 T23:  -0.0492                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.3728 L22:   6.8527                                     
REMARK   3      L33:   6.2464 L12:   0.3202                                     
REMARK   3      L13:  -0.7861 L23:  -1.8012                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2099 S12:  -0.5336 S13:   1.1330                       
REMARK   3      S21:   0.0823 S22:  -0.0195 S23:  -0.7638                       
REMARK   3      S31:  -0.1937 S32:   1.1064 S33:  -0.1904                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 5                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    30        B   228                          
REMARK   3    RESIDUE RANGE :   B  3002        B  3002                          
REMARK   3    RESIDUE RANGE :   B  2502        B  2502                          
REMARK   3    RESIDUE RANGE :   B  1502        B  1502                          
REMARK   3    RESIDUE RANGE :   B   382        B   383                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.8950  17.1590  -2.3670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6245 T22:   0.1421                                     
REMARK   3      T33:   0.0789 T12:   0.0657                                     
REMARK   3      T13:   0.1439 T23:   0.0262                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6959 L22:   4.1663                                     
REMARK   3      L33:   3.0034 L12:  -0.6578                                     
REMARK   3      L13:  -1.1259 L23:   0.6779                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2146 S12:   0.3476 S13:   0.4020                       
REMARK   3      S21:  -0.9855 S22:  -0.0520 S23:  -0.3204                       
REMARK   3      S31:  -0.3982 S32:  -0.1065 S33:  -0.1625                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   229        B   369                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.2550  -4.6900  -4.4090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9247 T22:   1.0111                                     
REMARK   3      T33:   1.3314 T12:   0.3708                                     
REMARK   3      T13:   0.4368 T23:  -0.3020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8939 L22:   5.9900                                     
REMARK   3      L33:   1.5852 L12:   3.1699                                     
REMARK   3      L13:  -0.9549 L23:  -1.7892                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1550 S12:   0.2459 S13:  -0.5932                       
REMARK   3      S21:  -0.7197 S22:  -0.1445 S23:  -1.9396                       
REMARK   3      S31:   0.4639 S32:   1.0121 S33:  -0.0105                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     1        E   118                          
REMARK   3    ORIGIN FOR THE GROUP (A): -43.9130  53.6180  68.5250              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4990 T22:   0.3094                                     
REMARK   3      T33:   0.2151 T12:   0.1366                                     
REMARK   3      T13:  -0.0460 T23:  -0.2258                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3235 L22:   3.7149                                     
REMARK   3      L33:   4.1470 L12:   0.0901                                     
REMARK   3      L13:  -0.6754 L23:  -0.2922                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0454 S12:  -0.0667 S13:  -0.0993                       
REMARK   3      S21:   0.3467 S22:  -0.1849 S23:   0.2583                       
REMARK   3      S31:  -0.2938 S32:  -0.5667 S33:   0.2303                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   119        E   218                          
REMARK   3    ORIGIN FOR THE GROUP (A): -51.3860  72.7840  44.6100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1641 T22:   0.4794                                     
REMARK   3      T33:   0.3338 T12:   0.6624                                     
REMARK   3      T13:  -0.2241 T23:  -0.1525                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6989 L22:   3.3651                                     
REMARK   3      L33:   4.0048 L12:   0.1059                                     
REMARK   3      L13:  -0.7571 L23:   0.3218                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1162 S12:   0.3352 S13:   0.3372                       
REMARK   3      S21:  -0.2542 S22:  -0.1017 S23:   0.5779                       
REMARK   3      S31:  -1.3114 S32:  -1.0121 S33:   0.2179                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   219        E   374                          
REMARK   3    RESIDUE RANGE :   F  5004        F  5004                          
REMARK   3    ORIGIN FOR THE GROUP (A): -47.2070  65.1640  57.3580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8022 T22:   0.3314                                     
REMARK   3      T33:   0.2202 T12:   0.3531                                     
REMARK   3      T13:  -0.0776 T23:  -0.2040                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9481 L22:   2.1633                                     
REMARK   3      L33:   3.1521 L12:  -0.2566                                     
REMARK   3      L13:  -0.1833 L23:   0.2462                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1506 S12:   0.0717 S13:   0.0867                       
REMARK   3      S21:   0.0573 S22:  -0.2583 S23:   0.2522                       
REMARK   3      S31:  -1.1283 S32:  -0.7155 S33:   0.1077                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F    10        F    53                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.2930  11.2500  60.3450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4359 T22:   0.3537                                     
REMARK   3      T33:   0.1335 T12:   0.1425                                     
REMARK   3      T13:   0.4115 T23:   0.0052                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  17.5817 L22:  10.1501                                     
REMARK   3      L33:  10.9532 L12:  -6.2721                                     
REMARK   3      L13:  -3.1381 L23:   3.6906                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.1475 S12:  -1.7088 S13:  -0.1116                       
REMARK   3      S21:   2.3081 S22:   0.8849 S23:   0.6991                       
REMARK   3      S31:   1.9630 S32:   0.4730 S33:   0.2626                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F    54        F   274                          
REMARK   3    ORIGIN FOR THE GROUP (A): -52.2760  37.9180  74.9320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6081 T22:   0.3224                                     
REMARK   3      T33:   0.3425 T12:  -0.1856                                     
REMARK   3      T13:   0.2096 T23:  -0.2521                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6241 L22:   1.7298                                     
REMARK   3      L33:   4.2563 L12:  -0.6922                                     
REMARK   3      L13:  -1.3308 L23:   1.6113                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2242 S12:   0.2445 S13:  -0.2840                       
REMARK   3      S21:   0.7243 S22:  -0.4372 S23:   0.6152                       
REMARK   3      S31:   0.6419 S32:  -0.9825 S33:   0.6613                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   275        F   503                          
REMARK   3    RESIDUE RANGE :   F  2000        F  2000                          
REMARK   3    RESIDUE RANGE :   F  4001        F  4001                          
REMARK   3    RESIDUE RANGE :   F  4010        F  4010                          
REMARK   3    ORIGIN FOR THE GROUP (A): -36.6940  43.0270  27.9040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4178 T22:   0.2756                                     
REMARK   3      T33:   0.1198 T12:   0.1667                                     
REMARK   3      T13:  -0.1206 T23:  -0.1187                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2410 L22:   2.6257                                     
REMARK   3      L33:   3.2025 L12:  -1.1622                                     
REMARK   3      L13:  -1.1301 L23:   1.4909                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0667 S12:   0.2909 S13:  -0.0338                       
REMARK   3      S21:  -0.4634 S22:  -0.3990 S23:   0.1110                       
REMARK   3      S31:  -0.4324 S32:  -0.6142 S33:   0.3323                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G     9        G   145                          
REMARK   3    ORIGIN FOR THE GROUP (A): -25.2310  44.1430  41.1280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1756 T22:   0.1450                                     
REMARK   3      T33:   0.2059 T12:   0.0486                                     
REMARK   3      T13:  -0.0042 T23:  -0.0762                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0179 L22:   3.4579                                     
REMARK   3      L33:   3.6826 L12:  -0.6700                                     
REMARK   3      L13:  -0.3585 L23:   1.0376                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1416 S12:   0.0275 S13:   0.1225                       
REMARK   3      S21:  -0.1083 S22:  -0.2436 S23:  -0.0960                       
REMARK   3      S31:  -0.4630 S32:  -0.0319 S33:   0.1020                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G   146        G   296                          
REMARK   3    RESIDUE RANGE :   G  4003        G  4009                          
REMARK   3    RESIDUE RANGE :   F  4002        F  4008                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.0250  31.8340  41.8250              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1980 T22:   0.1528                                     
REMARK   3      T33:   0.1637 T12:   0.0082                                     
REMARK   3      T13:  -0.0461 T23:  -0.0208                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1790 L22:   4.0028                                     
REMARK   3      L33:   3.7417 L12:  -1.4758                                     
REMARK   3      L13:  -1.0287 L23:   2.7417                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0328 S12:  -0.0441 S13:   0.0510                       
REMARK   3      S21:   0.1033 S22:  -0.0388 S23:  -0.0676                       
REMARK   3      S31:   0.1792 S32:   0.0221 S33:   0.0716                       
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 3PUV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-DEC-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062840.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAY-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97965                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR AND   
REMARK 200                                   VERTICALLY FOCUSING MIRROR         
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 77414                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
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     (%) : 58.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 14.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.48300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2R6G                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 27% PEG 400, 0.1M HEPES, 10 MM           
REMARK 280  MAGNESIUM CHLORIDE, 50 MM SODIUM CHLORIDE, VAPOR DIFFUSION,         
REMARK 280  SITTING DROP, TEMPERATURE 293K, PH 7.5                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 34960 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 76190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -299.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, A, B                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS E   375                                                      
REMARK 465     HIS E   376                                                      
REMARK 465     HIS E   377                                                      
REMARK 465     HIS E   378                                                      
REMARK 465     MET F     1                                                      
REMARK 465     ASP F     2                                                      
REMARK 465     VAL F     3                                                      
REMARK 465     ILE F     4                                                      
REMARK 465     LYS F     5                                                      
REMARK 465     LYS F     6                                                      
REMARK 465     LYS F     7                                                      
REMARK 465     HIS F     8                                                      
REMARK 465     TRP F     9                                                      
REMARK 465     THR F   241                                                      
REMARK 465     ALA F   242                                                      
REMARK 465     ASP F   243                                                      
REMARK 465     GLY F   244                                                      
REMARK 465     VAL F   504                                                      
REMARK 465     ASN F   505                                                      
REMARK 465     LEU F   506                                                      
REMARK 465     LYS F   507                                                      
REMARK 465     ALA F   508                                                      
REMARK 465     THR F   509                                                      
REMARK 465     ARG F   510                                                      
REMARK 465     MET F   511                                                      
REMARK 465     LYS F   512                                                      
REMARK 465     PHE F   513                                                      
REMARK 465     ASP F   514                                                      
REMARK 465     MET G     1                                                      
REMARK 465     ALA G     2                                                      
REMARK 465     MET G     3                                                      
REMARK 465     VAL G     4                                                      
REMARK 465     GLN G     5                                                      
REMARK 465     PRO G     6                                                      
REMARK 465     LYS G     7                                                      
REMARK 465     SER G     8                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A   373                                                      
REMARK 465     ALA A   374                                                      
REMARK 465     SER A   375                                                      
REMARK 465     HIS A   376                                                      
REMARK 465     HIS A   377                                                      
REMARK 465     HIS A   378                                                      
REMARK 465     HIS A   379                                                      
REMARK 465     HIS A   380                                                      
REMARK 465     HIS A   381                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LYS B   245                                                      
REMARK 465     VAL B   246                                                      
REMARK 465     SER B   272                                                      
REMARK 465     ARG B   273                                                      
REMARK 465     ASP B   274                                                      
REMARK 465     VAL B   275                                                      
REMARK 465     GLN B   276                                                      
REMARK 465     VAL B   277                                                      
REMARK 465     GLY B   278                                                      
REMARK 465     ALA B   279                                                      
REMARK 465     GLY B   370                                                      
REMARK 465     VAL B   371                                                      
REMARK 465     ALA B   372                                                      
REMARK 465     SER B   373                                                      
REMARK 465     ALA B   374                                                      
REMARK 465     SER B   375                                                      
REMARK 465     HIS B   376                                                      
REMARK 465     HIS B   377                                                      
REMARK 465     HIS B   378                                                      
REMARK 465     HIS B   379                                                      
REMARK 465     HIS B   380                                                      
REMARK 465     HIS B   381                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER E 372    OG                                                  
REMARK 470     SER E 374    OG                                                  
REMARK 470     TRP F  10    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP F  10    CZ3  CH2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP E  55     -159.04   -119.19                                   
REMARK 500    ILE E 108      -59.88   -123.04                                   
REMARK 500    ALA E 146      -71.72    -75.59                                   
REMARK 500    GLU E 172      -78.92    -68.61                                   
REMARK 500    ASN E 173       64.13   -150.56                                   
REMARK 500    ASP E 207       44.87   -109.43                                   
REMARK 500    ASN E 241       95.41    -67.94                                   
REMARK 500    ASN E 332       30.96    -92.28                                   
REMARK 500    GLU F  39      -67.56   -126.78                                   
REMARK 500    TYR F  40      -69.90     55.17                                   
REMARK 500    ALA F  58      -74.67    -74.77                                   
REMARK 500    ALA F  62       34.60    -99.25                                   
REMARK 500    GLU F 130     -164.82   -101.91                                   
REMARK 500    ILE F 417      -60.93   -127.45                                   
REMARK 500    ASN F 440       62.14    -69.73                                   
REMARK 500    PRO F 460      112.12    -31.87                                   
REMARK 500    GLU F 477     -144.61    -89.01                                   
REMARK 500    ALA F 502       84.38    -69.55                                   
REMARK 500    LEU G 167       -7.39    -59.76                                   
REMARK 500    ASP A  21       51.69     38.98                                   
REMARK 500    TYR A  84      -48.63     67.54                                   
REMARK 500    ALA A 133       33.88    -91.59                                   
REMARK 500    ASP A 333      171.00     69.03                                   
REMARK 500    GLU B  15      -34.65   -139.51                                   
REMARK 500    TYR B  84      -45.21     70.73                                   
REMARK 500    ALA B 103       49.99    -96.27                                   
REMARK 500    ALA B 133       31.58    -98.38                                   
REMARK 500    ALA B 250     -169.30   -110.55                                   
REMARK 500    ARG B 263       78.92     57.82                                   
REMARK 500    ASP B 333      178.51     73.13                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PGV F 4002                                                       
REMARK 610     PGV F 4008                                                       
REMARK 610     PGV F 4010                                                       
REMARK 610     PGV G 4003                                                       
REMARK 610     PGV G 4004                                                       
REMARK 610     PGV G 4005                                                       
REMARK 610     PGV G 4006                                                       
REMARK 610     PGV G 4007                                                       
REMARK 610     PGV G 4009                                                       
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                              MG B1502  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VO4 B3002   O3                                                     
REMARK 620 2 HOH B 382   O    97.3                                              
REMARK 620 3 SER B  43   OG  175.2  87.3                                        
REMARK 620 4 ADP B2502   O2B 101.1 100.3  79.3                                  
REMARK 620 5 HOH B 383   O    93.9 161.9  81.3  91.5                            
REMARK 620 6 GLN B  82   OE1 101.5  88.1  77.2 154.7  75.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 382   O                                                      
REMARK 620 2 VO4 A3001   O3   88.9                                              
REMARK 620 3 SER A  43   OG   80.2 168.3                                        
REMARK 620 4 HOH A 383   O   163.8  86.7 102.6                                  
REMARK 620 5 ADP A2501   O2B  98.5 100.5  85.4  97.7                            
REMARK 620 6 GLN A  82   OE1  78.3  87.5  86.1  85.9 171.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             VO4 A3001   V                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A2501   O3B                                                    
REMARK 620 2 VO4 A3001   O1   86.8                                              
REMARK 620 3 VO4 A3001   O2   94.4 104.3                                        
REMARK 620 4 VO4 A3001   O3   89.7 129.2 126.5                                  
REMARK 620 5 VO4 A3001   O4  175.3  90.6  90.0  89.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             VO4 B3002   V                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP B2502   O3B                                                    
REMARK 620 2 VO4 B3002   O1   89.4                                              
REMARK 620 3 VO4 B3002   O2   95.8 116.9                                        
REMARK 620 4 VO4 B3002   O3   86.4 119.5 123.6                                  
REMARK 620 5 VO4 B3002   O4  174.6  90.6  89.0  88.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAL F 2000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 2501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 2502                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO4 A 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO4 B 3002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV F 4001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV F 4002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV G 4004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV G 4005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV G 4006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV F 4008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV F 4010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UMQ F 5004                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3PUW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3PUX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3PUY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3PUZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3PU0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3RLF   RELATED DB: PDB                                   
DBREF  3PUV E    1   370  UNP    P0AEX9   MALE_ECOLI      27    396             
DBREF  3PUV F    1   514  UNP    P02916   MALF_ECOLI       1    514             
DBREF  3PUV G    1   296  UNP    P68183   MALG_ECOLI       1    296             
DBREF  3PUV A    1   371  UNP    P68187   MALK_ECOLI       1    371             
DBREF  3PUV B    1   371  UNP    P68187   MALK_ECOLI       1    371             
SEQADV 3PUV ALA E  371  UNP  P0AEX9              EXPRESSION TAG                 
SEQADV 3PUV SER E  372  UNP  P0AEX9              EXPRESSION TAG                 
SEQADV 3PUV ALA E  373  UNP  P0AEX9              EXPRESSION TAG                 
SEQADV 3PUV SER E  374  UNP  P0AEX9              EXPRESSION TAG                 
SEQADV 3PUV HIS E  375  UNP  P0AEX9              EXPRESSION TAG                 
SEQADV 3PUV HIS E  376  UNP  P0AEX9              EXPRESSION TAG                 
SEQADV 3PUV HIS E  377  UNP  P0AEX9              EXPRESSION TAG                 
SEQADV 3PUV HIS E  378  UNP  P0AEX9              EXPRESSION TAG                 
SEQADV 3PUV ALA A  372  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUV SER A  373  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUV ALA A  374  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUV SER A  375  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUV HIS A  376  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUV HIS A  377  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUV HIS A  378  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUV HIS A  379  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUV HIS A  380  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUV HIS A  381  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUV ALA B  372  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUV SER B  373  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUV ALA B  374  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUV SER B  375  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUV HIS B  376  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUV HIS B  377  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUV HIS B  378  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUV HIS B  379  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUV HIS B  380  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUV HIS B  381  UNP  P68187              EXPRESSION TAG                 
SEQRES   1 E  378  LYS ILE GLU GLU GLY LYS LEU VAL ILE TRP ILE ASN GLY          
SEQRES   2 E  378  ASP LYS GLY TYR ASN GLY LEU ALA GLU VAL GLY LYS LYS          
SEQRES   3 E  378  PHE GLU LYS ASP THR GLY ILE LYS VAL THR VAL GLU HIS          
SEQRES   4 E  378  PRO ASP LYS LEU GLU GLU LYS PHE PRO GLN VAL ALA ALA          
SEQRES   5 E  378  THR GLY ASP GLY PRO ASP ILE ILE PHE TRP ALA HIS ASP          
SEQRES   6 E  378  ARG PHE GLY GLY TYR ALA GLN SER GLY LEU LEU ALA GLU          
SEQRES   7 E  378  ILE THR PRO ASP LYS ALA PHE GLN ASP LYS LEU TYR PRO          
SEQRES   8 E  378  PHE THR TRP ASP ALA VAL ARG TYR ASN GLY LYS LEU ILE          
SEQRES   9 E  378  ALA TYR PRO ILE ALA VAL GLU ALA LEU SER LEU ILE TYR          
SEQRES  10 E  378  ASN LYS ASP LEU LEU PRO ASN PRO PRO LYS THR TRP GLU          
SEQRES  11 E  378  GLU ILE PRO ALA LEU ASP LYS GLU LEU LYS ALA LYS GLY          
SEQRES  12 E  378  LYS SER ALA LEU MET PHE ASN LEU GLN GLU PRO TYR PHE          
SEQRES  13 E  378  THR TRP PRO LEU ILE ALA ALA ASP GLY GLY TYR ALA PHE          
SEQRES  14 E  378  LYS TYR GLU ASN GLY LYS TYR ASP ILE LYS ASP VAL GLY          
SEQRES  15 E  378  VAL ASP ASN ALA GLY ALA LYS ALA GLY LEU THR PHE LEU          
SEQRES  16 E  378  VAL ASP LEU ILE LYS ASN LYS HIS MET ASN ALA ASP THR          
SEQRES  17 E  378  ASP TYR SER ILE ALA GLU ALA ALA PHE ASN LYS GLY GLU          
SEQRES  18 E  378  THR ALA MET THR ILE ASN GLY PRO TRP ALA TRP SER ASN          
SEQRES  19 E  378  ILE ASP THR SER LYS VAL ASN TYR GLY VAL THR VAL LEU          
SEQRES  20 E  378  PRO THR PHE LYS GLY GLN PRO SER LYS PRO PHE VAL GLY          
SEQRES  21 E  378  VAL LEU SER ALA GLY ILE ASN ALA ALA SER PRO ASN LYS          
SEQRES  22 E  378  GLU LEU ALA LYS GLU PHE LEU GLU ASN TYR LEU LEU THR          
SEQRES  23 E  378  ASP GLU GLY LEU GLU ALA VAL ASN LYS ASP LYS PRO LEU          
SEQRES  24 E  378  GLY ALA VAL ALA LEU LYS SER TYR GLU GLU GLU LEU ALA          
SEQRES  25 E  378  LYS ASP PRO ARG ILE ALA ALA THR MET GLU ASN ALA GLN          
SEQRES  26 E  378  LYS GLY GLU ILE MET PRO ASN ILE PRO GLN MET SER ALA          
SEQRES  27 E  378  PHE TRP TYR ALA VAL ARG THR ALA VAL ILE ASN ALA ALA          
SEQRES  28 E  378  SER GLY ARG GLN THR VAL ASP GLU ALA LEU LYS ASP ALA          
SEQRES  29 E  378  GLN THR ARG ILE THR LYS ALA SER ALA SER HIS HIS HIS          
SEQRES  30 E  378  HIS                                                          
SEQRES   1 F  514  MET ASP VAL ILE LYS LYS LYS HIS TRP TRP GLN SER ASP          
SEQRES   2 F  514  ALA LEU LYS TRP SER VAL LEU GLY LEU LEU GLY LEU LEU          
SEQRES   3 F  514  VAL GLY TYR LEU VAL VAL LEU MET TYR ALA GLN GLY GLU          
SEQRES   4 F  514  TYR LEU PHE ALA ILE THR THR LEU ILE LEU SER SER ALA          
SEQRES   5 F  514  GLY LEU TYR ILE PHE ALA ASN ARG LYS ALA TYR ALA TRP          
SEQRES   6 F  514  ARG TYR VAL TYR PRO GLY MET ALA GLY MET GLY LEU PHE          
SEQRES   7 F  514  VAL LEU PHE PRO LEU VAL CYS THR ILE ALA ILE ALA PHE          
SEQRES   8 F  514  THR ASN TYR SER SER THR ASN GLN LEU THR PHE GLU ARG          
SEQRES   9 F  514  ALA GLN GLU VAL LEU LEU ASP ARG SER TRP GLN ALA GLY          
SEQRES  10 F  514  LYS THR TYR ASN PHE GLY LEU TYR PRO ALA GLY ASP GLU          
SEQRES  11 F  514  TRP GLN LEU ALA LEU SER ASP GLY GLU THR GLY LYS ASN          
SEQRES  12 F  514  TYR LEU SER ASP ALA PHE LYS PHE GLY GLY GLU GLN LYS          
SEQRES  13 F  514  LEU GLN LEU LYS GLU THR THR ALA GLN PRO GLU GLY GLU          
SEQRES  14 F  514  ARG ALA ASN LEU ARG VAL ILE THR GLN ASN ARG GLN ALA          
SEQRES  15 F  514  LEU SER ASP ILE THR ALA ILE LEU PRO ASP GLY ASN LYS          
SEQRES  16 F  514  VAL MET MET SER SER LEU ARG GLN PHE SER GLY THR GLN          
SEQRES  17 F  514  PRO LEU TYR THR LEU ASP GLY ASP GLY THR LEU THR ASN          
SEQRES  18 F  514  ASN GLN SER GLY VAL LYS TYR ARG PRO ASN ASN GLN ILE          
SEQRES  19 F  514  GLY PHE TYR GLN SER ILE THR ALA ASP GLY ASN TRP GLY          
SEQRES  20 F  514  ASP GLU LYS LEU SER PRO GLY TYR THR VAL THR THR GLY          
SEQRES  21 F  514  TRP LYS ASN PHE THR ARG VAL PHE THR ASP GLU GLY ILE          
SEQRES  22 F  514  GLN LYS PRO PHE LEU ALA ILE PHE VAL TRP THR VAL VAL          
SEQRES  23 F  514  PHE SER LEU ILE THR VAL PHE LEU THR VAL ALA VAL GLY          
SEQRES  24 F  514  MET VAL LEU ALA CYS LEU VAL GLN TRP GLU ALA LEU ARG          
SEQRES  25 F  514  GLY LYS ALA VAL TYR ARG VAL LEU LEU ILE LEU PRO TYR          
SEQRES  26 F  514  ALA VAL PRO SER PHE ILE SER ILE LEU ILE PHE LYS GLY          
SEQRES  27 F  514  LEU PHE ASN GLN SER PHE GLY GLU ILE ASN MET MET LEU          
SEQRES  28 F  514  SER ALA LEU PHE GLY VAL LYS PRO ALA TRP PHE SER ASP          
SEQRES  29 F  514  PRO THR THR ALA ARG THR MET LEU ILE ILE VAL ASN THR          
SEQRES  30 F  514  TRP LEU GLY TYR PRO TYR MET MET ILE LEU CYS MET GLY          
SEQRES  31 F  514  LEU LEU LYS ALA ILE PRO ASP ASP LEU TYR GLU ALA SER          
SEQRES  32 F  514  ALA MET ASP GLY ALA GLY PRO PHE GLN ASN PHE PHE LYS          
SEQRES  33 F  514  ILE THR LEU PRO LEU LEU ILE LYS PRO LEU THR PRO LEU          
SEQRES  34 F  514  MET ILE ALA SER PHE ALA PHE ASN PHE ASN ASN PHE VAL          
SEQRES  35 F  514  LEU ILE GLN LEU LEU THR ASN GLY GLY PRO ASP ARG LEU          
SEQRES  36 F  514  GLY THR THR THR PRO ALA GLY TYR THR ASP LEU LEU VAL          
SEQRES  37 F  514  ASN TYR THR TYR ARG ILE ALA PHE GLU GLY GLY GLY GLY          
SEQRES  38 F  514  GLN ASP PHE GLY LEU ALA ALA ALA ILE ALA THR LEU ILE          
SEQRES  39 F  514  PHE LEU LEU VAL GLY ALA LEU ALA ILE VAL ASN LEU LYS          
SEQRES  40 F  514  ALA THR ARG MET LYS PHE ASP                                  
SEQRES   1 G  296  MET ALA MET VAL GLN PRO LYS SER GLN LYS ALA ARG LEU          
SEQRES   2 G  296  PHE ILE THR HIS LEU LEU LEU LEU LEU PHE ILE ALA ALA          
SEQRES   3 G  296  ILE MET PHE PRO LEU LEU MET VAL VAL ALA ILE SER LEU          
SEQRES   4 G  296  ARG GLN GLY ASN PHE ALA THR GLY SER LEU ILE PRO GLU          
SEQRES   5 G  296  GLN ILE SER TRP ASP HIS TRP LYS LEU ALA LEU GLY PHE          
SEQRES   6 G  296  SER VAL GLU GLN ALA ASP GLY ARG ILE THR PRO PRO PRO          
SEQRES   7 G  296  PHE PRO VAL LEU LEU TRP LEU TRP ASN SER VAL LYS VAL          
SEQRES   8 G  296  ALA GLY ILE SER ALA ILE GLY ILE VAL ALA LEU SER THR          
SEQRES   9 G  296  THR CYS ALA TYR ALA PHE ALA ARG MET ARG PHE PRO GLY          
SEQRES  10 G  296  LYS ALA THR LEU LEU LYS GLY MET LEU ILE PHE GLN MET          
SEQRES  11 G  296  PHE PRO ALA VAL LEU SER LEU VAL ALA LEU TYR ALA LEU          
SEQRES  12 G  296  PHE ASP ARG LEU GLY GLU TYR ILE PRO PHE ILE GLY LEU          
SEQRES  13 G  296  ASN THR HIS GLY GLY VAL ILE PHE ALA TYR LEU GLY GLY          
SEQRES  14 G  296  ILE ALA LEU HIS VAL TRP THR ILE LYS GLY TYR PHE GLU          
SEQRES  15 G  296  THR ILE ASP SER SER LEU GLU GLU ALA ALA ALA LEU ASP          
SEQRES  16 G  296  GLY ALA THR PRO TRP GLN ALA PHE ARG LEU VAL LEU LEU          
SEQRES  17 G  296  PRO LEU SER VAL PRO ILE LEU ALA VAL VAL PHE ILE LEU          
SEQRES  18 G  296  SER PHE ILE ALA ALA ILE THR GLU VAL PRO VAL ALA SER          
SEQRES  19 G  296  LEU LEU LEU ARG ASP VAL ASN SER TYR THR LEU ALA VAL          
SEQRES  20 G  296  GLY MET GLN GLN TYR LEU ASN PRO GLN ASN TYR LEU TRP          
SEQRES  21 G  296  GLY ASP PHE ALA ALA ALA ALA VAL MET SER ALA LEU PRO          
SEQRES  22 G  296  ILE THR ILE VAL PHE LEU LEU ALA GLN ARG TRP LEU VAL          
SEQRES  23 G  296  ASN GLY LEU THR ALA GLY GLY VAL LYS GLY                      
SEQRES   1 A  381  MET ALA SER VAL GLN LEU GLN ASN VAL THR LYS ALA TRP          
SEQRES   2 A  381  GLY GLU VAL VAL VAL SER LYS ASP ILE ASN LEU ASP ILE          
SEQRES   3 A  381  HIS GLU GLY GLU PHE VAL VAL PHE VAL GLY PRO SER GLY          
SEQRES   4 A  381  CYS GLY LYS SER THR LEU LEU ARG MET ILE ALA GLY LEU          
SEQRES   5 A  381  GLU THR ILE THR SER GLY ASP LEU PHE ILE GLY GLU LYS          
SEQRES   6 A  381  ARG MET ASN ASP THR PRO PRO ALA GLU ARG GLY VAL GLY          
SEQRES   7 A  381  MET VAL PHE GLN SER TYR ALA LEU TYR PRO HIS LEU SER          
SEQRES   8 A  381  VAL ALA GLU ASN MET SER PHE GLY LEU LYS LEU ALA GLY          
SEQRES   9 A  381  ALA LYS LYS GLU VAL ILE ASN GLN ARG VAL ASN GLN VAL          
SEQRES  10 A  381  ALA GLU VAL LEU GLN LEU ALA HIS LEU LEU ASP ARG LYS          
SEQRES  11 A  381  PRO LYS ALA LEU SER GLY GLY GLN ARG GLN ARG VAL ALA          
SEQRES  12 A  381  ILE GLY ARG THR LEU VAL ALA GLU PRO SER VAL PHE LEU          
SEQRES  13 A  381  LEU ASP GLU PRO LEU SER ASN LEU ASP ALA ALA LEU ARG          
SEQRES  14 A  381  VAL GLN MET ARG ILE GLU ILE SER ARG LEU HIS LYS ARG          
SEQRES  15 A  381  LEU GLY ARG THR MET ILE TYR VAL THR HIS ASP GLN VAL          
SEQRES  16 A  381  GLU ALA MET THR LEU ALA ASP LYS ILE VAL VAL LEU ASP          
SEQRES  17 A  381  ALA GLY ARG VAL ALA GLN VAL GLY LYS PRO LEU GLU LEU          
SEQRES  18 A  381  TYR HIS TYR PRO ALA ASP ARG PHE VAL ALA GLY PHE ILE          
SEQRES  19 A  381  GLY SER PRO LYS MET ASN PHE LEU PRO VAL LYS VAL THR          
SEQRES  20 A  381  ALA THR ALA ILE ASP GLN VAL GLN VAL GLU LEU PRO MET          
SEQRES  21 A  381  PRO ASN ARG GLN GLN VAL TRP LEU PRO VAL GLU SER ARG          
SEQRES  22 A  381  ASP VAL GLN VAL GLY ALA ASN MET SER LEU GLY ILE ARG          
SEQRES  23 A  381  PRO GLU HIS LEU LEU PRO SER ASP ILE ALA ASP VAL ILE          
SEQRES  24 A  381  LEU GLU GLY GLU VAL GLN VAL VAL GLU GLN LEU GLY ASN          
SEQRES  25 A  381  GLU THR GLN ILE HIS ILE GLN ILE PRO SER ILE ARG GLN          
SEQRES  26 A  381  ASN LEU VAL TYR ARG GLN ASN ASP VAL VAL LEU VAL GLU          
SEQRES  27 A  381  GLU GLY ALA THR PHE ALA ILE GLY LEU PRO PRO GLU ARG          
SEQRES  28 A  381  CYS HIS LEU PHE ARG GLU ASP GLY THR ALA CYS ARG ARG          
SEQRES  29 A  381  LEU HIS LYS GLU PRO GLY VAL ALA SER ALA SER HIS HIS          
SEQRES  30 A  381  HIS HIS HIS HIS                                              
SEQRES   1 B  381  MET ALA SER VAL GLN LEU GLN ASN VAL THR LYS ALA TRP          
SEQRES   2 B  381  GLY GLU VAL VAL VAL SER LYS ASP ILE ASN LEU ASP ILE          
SEQRES   3 B  381  HIS GLU GLY GLU PHE VAL VAL PHE VAL GLY PRO SER GLY          
SEQRES   4 B  381  CYS GLY LYS SER THR LEU LEU ARG MET ILE ALA GLY LEU          
SEQRES   5 B  381  GLU THR ILE THR SER GLY ASP LEU PHE ILE GLY GLU LYS          
SEQRES   6 B  381  ARG MET ASN ASP THR PRO PRO ALA GLU ARG GLY VAL GLY          
SEQRES   7 B  381  MET VAL PHE GLN SER TYR ALA LEU TYR PRO HIS LEU SER          
SEQRES   8 B  381  VAL ALA GLU ASN MET SER PHE GLY LEU LYS LEU ALA GLY          
SEQRES   9 B  381  ALA LYS LYS GLU VAL ILE ASN GLN ARG VAL ASN GLN VAL          
SEQRES  10 B  381  ALA GLU VAL LEU GLN LEU ALA HIS LEU LEU ASP ARG LYS          
SEQRES  11 B  381  PRO LYS ALA LEU SER GLY GLY GLN ARG GLN ARG VAL ALA          
SEQRES  12 B  381  ILE GLY ARG THR LEU VAL ALA GLU PRO SER VAL PHE LEU          
SEQRES  13 B  381  LEU ASP GLU PRO LEU SER ASN LEU ASP ALA ALA LEU ARG          
SEQRES  14 B  381  VAL GLN MET ARG ILE GLU ILE SER ARG LEU HIS LYS ARG          
SEQRES  15 B  381  LEU GLY ARG THR MET ILE TYR VAL THR HIS ASP GLN VAL          
SEQRES  16 B  381  GLU ALA MET THR LEU ALA ASP LYS ILE VAL VAL LEU ASP          
SEQRES  17 B  381  ALA GLY ARG VAL ALA GLN VAL GLY LYS PRO LEU GLU LEU          
SEQRES  18 B  381  TYR HIS TYR PRO ALA ASP ARG PHE VAL ALA GLY PHE ILE          
SEQRES  19 B  381  GLY SER PRO LYS MET ASN PHE LEU PRO VAL LYS VAL THR          
SEQRES  20 B  381  ALA THR ALA ILE ASP GLN VAL GLN VAL GLU LEU PRO MET          
SEQRES  21 B  381  PRO ASN ARG GLN GLN VAL TRP LEU PRO VAL GLU SER ARG          
SEQRES  22 B  381  ASP VAL GLN VAL GLY ALA ASN MET SER LEU GLY ILE ARG          
SEQRES  23 B  381  PRO GLU HIS LEU LEU PRO SER ASP ILE ALA ASP VAL ILE          
SEQRES  24 B  381  LEU GLU GLY GLU VAL GLN VAL VAL GLU GLN LEU GLY ASN          
SEQRES  25 B  381  GLU THR GLN ILE HIS ILE GLN ILE PRO SER ILE ARG GLN          
SEQRES  26 B  381  ASN LEU VAL TYR ARG GLN ASN ASP VAL VAL LEU VAL GLU          
SEQRES  27 B  381  GLU GLY ALA THR PHE ALA ILE GLY LEU PRO PRO GLU ARG          
SEQRES  28 B  381  CYS HIS LEU PHE ARG GLU ASP GLY THR ALA CYS ARG ARG          
SEQRES  29 B  381  LEU HIS LYS GLU PRO GLY VAL ALA SER ALA SER HIS HIS          
SEQRES  30 B  381  HIS HIS HIS HIS                                              
HET    MAL  F2000      23                                                       
HET    PGV  F4001      51                                                       
HET    PGV  F4002       9                                                       
HET    PGV  F4008       8                                                       
HET    PGV  F4010      13                                                       
HET    UMQ  F5004      34                                                       
HET    PGV  G4003       8                                                       
HET    PGV  G4004      12                                                       
HET    PGV  G4005      10                                                       
HET    PGV  G4006       7                                                       
HET    PGV  G4007       9                                                       
HET    PGV  G4009      12                                                       
HET     MG  A1501       1                                                       
HET     MG  B1502       1                                                       
HET    ADP  A2501      27                                                       
HET    VO4  A3001       5                                                       
HET    ADP  B2502      27                                                       
HET    VO4  B3002       5                                                       
HETNAM     MAL MALTOSE                                                          
HETNAM     PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)                
HETNAM   2 PGV  PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-            
HETNAM   3 PGV  OCTADEC-11-ENOATE                                               
HETNAM     UMQ UNDECYL-MALTOSIDE                                                
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     VO4 VANADATE ION                                                     
HETSYN     PGV PHOSPHATIDYLGLYCEROL, 2-VACCENOYL-1-PALMITOYL-SN-                
HETSYN   2 PGV  GLYCEROL-3-PHOSPHOGLYCEROL                                      
HETSYN     UMQ UNDECYL-BETA-D-MALTOPYRANOSIDE                                   
FORMUL   6  MAL    C12 H22 O11                                                  
FORMUL   7  PGV    10(C40 H77 O10 P)                                            
FORMUL  11  UMQ    C23 H44 O11                                                  
FORMUL  18   MG    2(MG 2+)                                                     
FORMUL  20  ADP    2(C10 H15 N5 O10 P2)                                         
FORMUL  21  VO4    2(O4 V 3-)                                                   
FORMUL  24  HOH   *180(H2 O)                                                    
HELIX    1   1 GLY E   16  GLY E   32  1                                  17    
HELIX    2   2 LYS E   42  THR E   53  1                                  12    
HELIX    3   3 ARG E   66  GLY E   74  1                                   9    
HELIX    4   4 ASP E   82  ASP E   87  1                                   6    
HELIX    5   5 TYR E   90  VAL E   97  1                                   8    
HELIX    6   6 GLU E  131  LYS E  140  1                                  10    
HELIX    7   7 ALA E  141  GLY E  143  5                                   3    
HELIX    8   8 GLU E  153  ASP E  164  1                                  12    
HELIX    9   9 ASN E  185  ASN E  201  1                                  17    
HELIX   10  10 ASP E  209  LYS E  219  1                                  11    
HELIX   11  11 GLY E  228  TRP E  230  5                                   3    
HELIX   12  12 ALA E  231  LYS E  239  1                                   9    
HELIX   13  13 ASN E  272  TYR E  283  1                                  12    
HELIX   14  14 THR E  286  LYS E  297  1                                  12    
HELIX   15  15 LEU E  304  ALA E  312  1                                   9    
HELIX   16  16 ASP E  314  LYS E  326  1                                  13    
HELIX   17  17 GLN E  335  SER E  352  1                                  18    
HELIX   18  18 THR E  356  SER E  374  1                                  19    
HELIX   19  19 SER F   12  LEU F   30  1                                  19    
HELIX   20  20 LEU F   30  GLN F   37  1                                   8    
HELIX   21  21 TYR F   40  ASN F   59  1                                  20    
HELIX   22  22 ARG F   60  TYR F   63  5                                   4    
HELIX   23  23 ALA F   64  VAL F   79  1                                  16    
HELIX   24  24 VAL F   79  ALA F   90  1                                  12    
HELIX   25  25 THR F  101  LEU F  110  1                                  10    
HELIX   26  26 ASN F  172  ASN F  179  1                                   8    
HELIX   27  27 ASN F  179  SER F  184  1                                   6    
HELIX   28  28 TRP F  261  ASP F  270  1                                  10    
HELIX   29  29 PRO F  276  GLN F  307  1                                  32    
HELIX   30  30 GLY F  313  ILE F  322  1                                  10    
HELIX   31  31 ILE F  322  VAL F  327  1                                   6    
HELIX   32  32 PRO F  328  PHE F  340  1                                  13    
HELIX   33  33 GLY F  345  SER F  352  1                                   8    
HELIX   34  34 ASP F  364  LEU F  392  1                                  29    
HELIX   35  35 LYS F  393  PRO F  396  5                                   4    
HELIX   36  36 ASP F  397  ASP F  406  1                                  10    
HELIX   37  37 GLY F  409  ILE F  417  1                                   9    
HELIX   38  38 LEU F  419  ASN F  439  1                                  21    
HELIX   39  39 ASN F  440  THR F  448  1                                   9    
HELIX   40  40 LEU F  466  PHE F  476  1                                  11    
HELIX   41  41 ASP F  483  ALA F  502  1                                  20    
HELIX   42  42 LYS G   10  LEU G   39  1                                  30    
HELIX   43  43 TRP G   56  LEU G   63  1                                   8    
HELIX   44  44 PRO G   80  MET G  113  1                                  34    
HELIX   45  45 GLY G  117  MET G  130  1                                  14    
HELIX   46  46 LEU G  135  GLU G  149  1                                  15    
HELIX   47  47 TYR G  150  GLY G  155  5                                   6    
HELIX   48  48 THR G  158  LEU G  167  1                                  10    
HELIX   49  49 ILE G  170  GLU G  182  1                                  13    
HELIX   50  50 THR G  183  ASP G  185  5                                   3    
HELIX   51  51 SER G  186  ASP G  195  1                                  10    
HELIX   52  52 THR G  198  VAL G  206  1                                   9    
HELIX   53  53 VAL G  206  GLU G  229  1                                  24    
HELIX   54  54 VAL G  230  LEU G  237  1                                   8    
HELIX   55  55 ASP G  239  TYR G  243  5                                   5    
HELIX   56  56 THR G  244  MET G  249  1                                   6    
HELIX   57  57 GLN G  250  LEU G  253  5                                   4    
HELIX   58  58 LEU G  259  GLN G  282  1                                  24    
HELIX   59  59 ARG G  283  LEU G  285  5                                   3    
HELIX   60  60 GLY A   41  ALA A   50  1                                  10    
HELIX   61  61 PRO A   71  ARG A   75  5                                   5    
HELIX   62  62 SER A   91  ALA A  103  1                                  13    
HELIX   63  63 LYS A  106  LEU A  121  1                                  16    
HELIX   64  64 LYS A  130  LEU A  134  5                                   5    
HELIX   65  65 SER A  135  GLU A  151  1                                  17    
HELIX   66  66 ASP A  165  GLY A  184  1                                  20    
HELIX   67  67 ASP A  193  ALA A  201  1                                   9    
HELIX   68  68 LYS A  217  TYR A  224  1                                   8    
HELIX   69  69 ASP A  227  ILE A  234  1                                   8    
HELIX   70  70 PRO A  348  CYS A  352  5                                   5    
HELIX   71  71 GLY B   41  GLY B   51  1                                  11    
HELIX   72  72 PRO B   71  ARG B   75  5                                   5    
HELIX   73  73 SER B   91  SER B   97  1                                   7    
HELIX   74  74 SER B   97  ALA B  103  1                                   7    
HELIX   75  75 LYS B  106  LEU B  121  1                                  16    
HELIX   76  76 LEU B  123  LEU B  127  5                                   5    
HELIX   77  77 LYS B  130  LEU B  134  5                                   5    
HELIX   78  78 SER B  135  GLU B  151  1                                  17    
HELIX   79  79 ASP B  165  GLY B  184  1                                  20    
HELIX   80  80 ASP B  193  ALA B  201  1                                   9    
HELIX   81  81 LYS B  217  TYR B  224  1                                   8    
HELIX   82  82 ASP B  227  ILE B  234  1                                   8    
SHEET    1   A 6 LYS E  34  GLU E  38  0                                        
SHEET    2   A 6 LYS E   6  TRP E  10  1  N  ILE E   9   O  GLU E  38           
SHEET    3   A 6 ILE E  59  ALA E  63  1  O  PHE E  61   N  TRP E  10           
SHEET    4   A 6 PHE E 258  ILE E 266 -1  O  SER E 263   N  TRP E  62           
SHEET    5   A 6 TYR E 106  GLU E 111 -1  N  ILE E 108   O  LEU E 262           
SHEET    6   A 6 ALA E 301  VAL E 302 -1  O  ALA E 301   N  VAL E 110           
SHEET    1   B 5 LYS E  34  GLU E  38  0                                        
SHEET    2   B 5 LYS E   6  TRP E  10  1  N  ILE E   9   O  GLU E  38           
SHEET    3   B 5 ILE E  59  ALA E  63  1  O  PHE E  61   N  TRP E  10           
SHEET    4   B 5 PHE E 258  ILE E 266 -1  O  SER E 263   N  TRP E  62           
SHEET    5   B 5 GLU E 328  ILE E 329  1  O  GLU E 328   N  VAL E 259           
SHEET    1   C 2 ARG E  98  TYR E  99  0                                        
SHEET    2   C 2 LYS E 102  LEU E 103 -1  O  LYS E 102   N  TYR E  99           
SHEET    1   D 4 SER E 145  LEU E 147  0                                        
SHEET    2   D 4 THR E 222  ASN E 227  1  O  ALA E 223   N  SER E 145           
SHEET    3   D 4 SER E 114  ASN E 118 -1  N  ASN E 118   O  ALA E 223           
SHEET    4   D 4 TYR E 242  THR E 245 -1  O  THR E 245   N  LEU E 115           
SHEET    1   E 2 TYR E 167  TYR E 171  0                                        
SHEET    2   E 2 TYR E 176  GLY E 182 -1  O  ASP E 177   N  LYS E 170           
SHEET    1   F 2 ASN F  98  LEU F 100  0                                        
SHEET    2   F 2 GLY F 254  TYR F 255  1  O  GLY F 254   N  LEU F 100           
SHEET    1   G 8 SER F 113  ALA F 127  0                                        
SHEET    2   G 8 GLU F 130  ASP F 137 -1  O  GLN F 132   N  TYR F 125           
SHEET    3   G 8 LYS F 142  SER F 146 -1  O  LYS F 142   N  ASP F 137           
SHEET    4   G 8 GLN F 155  THR F 162 -1  O  THR F 162   N  ASN F 143           
SHEET    5   G 8 ILE F 186  ILE F 189  1  O  ILE F 189   N  LEU F 157           
SHEET    6   G 8 LYS F 195  MET F 198 -1  O  VAL F 196   N  ALA F 188           
SHEET    7   G 8 GLN F 203  PRO F 209 -1  O  SER F 205   N  MET F 197           
SHEET    8   G 8 SER F 113  ALA F 127 -1  N  TYR F 120   O  PHE F 204           
SHEET    1   H 5 TYR F 211  LEU F 213  0                                        
SHEET    2   H 5 LEU F 219  ASN F 221 -1  O  THR F 220   N  THR F 212           
SHEET    3   H 5 LYS F 227  ASN F 231 -1  O  TYR F 228   N  LEU F 219           
SHEET    4   H 5 PHE F 236  SER F 239 -1  O  GLN F 238   N  ARG F 229           
SHEET    5   H 5 LYS F 250  LEU F 251 -1  O  LEU F 251   N  TYR F 237           
SHEET    1   I 2 VAL G  67  GLU G  68  0                                        
SHEET    2   I 2 ILE G  74  THR G  75 -1  O  THR G  75   N  VAL G  67           
SHEET    1   J 3 VAL A  16  ILE A  26  0                                        
SHEET    2   J 3 VAL A   4  TRP A  13 -1  N  TRP A  13   O  VAL A  16           
SHEET    3   J 3 SER A  57  ILE A  62 -1  O  PHE A  61   N  GLN A   5           
SHEET    1   K 6 VAL A  77  VAL A  80  0                                        
SHEET    2   K 6 VAL A 154  ASP A 158  1  O  LEU A 156   N  VAL A  80           
SHEET    3   K 6 THR A 186  VAL A 190  1  O  ILE A 188   N  PHE A 155           
SHEET    4   K 6 PHE A  31  VAL A  35  1  N  VAL A  32   O  MET A 187           
SHEET    5   K 6 LYS A 203  ASP A 208  1  O  VAL A 205   N  VAL A  33           
SHEET    6   K 6 ARG A 211  GLY A 216 -1  O  ALA A 213   N  VAL A 206           
SHEET    1   L 6 GLN A 265  LEU A 268  0                                        
SHEET    2   L 6 GLN A 253  GLU A 257 -1  N  VAL A 256   O  VAL A 266           
SHEET    3   L 6 ASN A 240  ALA A 250 -1  N  ALA A 250   O  GLN A 253           
SHEET    4   L 6 ASN A 280  ILE A 285 -1  O  LEU A 283   N  LEU A 242           
SHEET    5   L 6 HIS A 353  PHE A 355 -1  O  HIS A 353   N  GLY A 284           
SHEET    6   L 6 ALA A 361  CYS A 362 -1  O  CYS A 362   N  LEU A 354           
SHEET    1   M 5 LEU A 291  PRO A 292  0                                        
SHEET    2   M 5 THR A 342  GLY A 346 -1  O  GLY A 346   N  LEU A 291           
SHEET    3   M 5 ILE A 299  GLN A 309 -1  N  LEU A 300   O  ILE A 345           
SHEET    4   M 5 GLU A 313  GLN A 319 -1  O  HIS A 317   N  GLN A 305           
SHEET    5   M 5 LEU A 327  ASN A 332 -1  O  LEU A 327   N  ILE A 318           
SHEET    1   N 3 VAL B  16  ILE B  26  0                                        
SHEET    2   N 3 VAL B   4  TRP B  13 -1  N  LYS B  11   O  VAL B  18           
SHEET    3   N 3 SER B  57  ILE B  62 -1  O  SER B  57   N  THR B  10           
SHEET    1   O 6 VAL B  77  VAL B  80  0                                        
SHEET    2   O 6 VAL B 154  ASP B 158  1  O  LEU B 156   N  VAL B  80           
SHEET    3   O 6 THR B 186  VAL B 190  1  O  VAL B 190   N  LEU B 157           
SHEET    4   O 6 PHE B  31  VAL B  35  1  N  VAL B  32   O  TYR B 189           
SHEET    5   O 6 LYS B 203  ASP B 208  1  O  LEU B 207   N  VAL B  35           
SHEET    6   O 6 ARG B 211  GLY B 216 -1  O  ALA B 213   N  VAL B 206           
SHEET    1   P 3 ASN B 240  LEU B 242  0                                        
SHEET    2   P 3 SER B 282  ILE B 285 -1  O  LEU B 283   N  LEU B 242           
SHEET    3   P 3 HIS B 353  PHE B 355 -1  O  HIS B 353   N  GLY B 284           
SHEET    1   Q 3 ALA B 248  THR B 249  0                                        
SHEET    2   Q 3 VAL B 254  GLU B 257 -1  O  GLN B 255   N  ALA B 248           
SHEET    3   Q 3 GLN B 265  LEU B 268 -1  O  LEU B 268   N  VAL B 254           
SHEET    1   R 5 LEU B 291  PRO B 292  0                                        
SHEET    2   R 5 THR B 342  GLY B 346 -1  O  GLY B 346   N  LEU B 291           
SHEET    3   R 5 ILE B 299  GLN B 309 -1  N  LEU B 300   O  ILE B 345           
SHEET    4   R 5 GLU B 313  GLN B 319 -1  O  GLN B 319   N  GLU B 303           
SHEET    5   R 5 LEU B 327  ASN B 332 -1  O  LEU B 327   N  ILE B 318           
LINK        MG    MG B1502                 O3  VO4 B3002     1555   1555  1.85  
LINK        MG    MG A1501                 O   HOH A 382     1555   1555  1.86  
LINK        MG    MG B1502                 O   HOH B 382     1555   1555  1.91  
LINK        MG    MG A1501                 O3  VO4 A3001     1555   1555  1.91  
LINK         OG  SER A  43                MG    MG A1501     1555   1555  1.97  
LINK         O3B ADP A2501                 V   VO4 A3001     1555   1555  1.98  
LINK        MG    MG A1501                 O   HOH A 383     1555   1555  2.01  
LINK         O3B ADP B2502                 V   VO4 B3002     1555   1555  2.07  
LINK        MG    MG A1501                 O2B ADP A2501     1555   1555  2.08  
LINK         OG  SER B  43                MG    MG B1502     1555   1555  2.10  
LINK        MG    MG B1502                 O2B ADP B2502     1555   1555  2.10  
LINK        MG    MG B1502                 O   HOH B 383     1555   1555  2.10  
LINK         OE1 GLN A  82                MG    MG A1501     1555   1555  2.31  
LINK         OE1 GLN B  82                MG    MG B1502     1555   1555  2.31  
CISPEP   1 SER F  252    PRO F  253          0         6.20                     
CISPEP   2 GLY F  451    PRO F  452          0         4.21                     
CISPEP   3 SER A  236    PRO A  237          0        -0.67                     
CISPEP   4 SER B  236    PRO B  237          0         8.01                     
SITE     1 AC1  6 SER A  43  GLN A  82  HOH A 382  HOH A 383                    
SITE     2 AC1  6 ADP A2501  VO4 A3001                                          
SITE     1 AC2  6 SER B  43  GLN B  82  HOH B 382  HOH B 383                    
SITE     2 AC2  6 ADP B2502  VO4 B3002                                          
SITE     1 AC3 12 THR F 291  TYR F 325  ASN F 376  LEU F 379                    
SITE     2 AC3 12 GLY F 380  TYR F 383  SER F 433  PHE F 436                    
SITE     3 AC3 12 ASN F 437  ASN F 440  HOH F 524  HOH F 547                    
SITE     1 AC4 16 TRP A  13  VAL A  18  GLY A  39  CYS A  40                    
SITE     2 AC4 16 GLY A  41  LYS A  42  SER A  43  THR A  44                    
SITE     3 AC4 16 HOH A 382  HOH A 383   MG A1501  VO4 A3001                    
SITE     4 AC4 16 ARG B 129  ALA B 133  SER B 135  GLN B 138                    
SITE     1 AC5 15 ARG A 129  ALA A 133  SER A 135  GLN A 138                    
SITE     2 AC5 15 VAL B  18  GLY B  39  CYS B  40  GLY B  41                    
SITE     3 AC5 15 LYS B  42  SER B  43  THR B  44  HOH B 382                    
SITE     4 AC5 15 HOH B 383   MG B1502  VO4 B3002                               
SITE     1 AC6 13 SER A  38  GLY A  39  LYS A  42  GLN A  82                    
SITE     2 AC6 13 GLU A 159  HIS A 192  HOH A 382  HOH A 383                    
SITE     3 AC6 13  MG A1501  ADP A2501  SER B 135  GLY B 137                    
SITE     4 AC6 13 ASN B 163                                                     
SITE     1 AC7 13 SER A 135  GLY A 137  ASN A 163  SER B  38                    
SITE     2 AC7 13 GLY B  39  LYS B  42  GLN B  82  GLU B 159                    
SITE     3 AC7 13 HIS B 192  HOH B 382  HOH B 383   MG B1502                    
SITE     4 AC7 13 ADP B2502                                                     
SITE     1 AC8  8 CYS F 304  TRP F 308  TYR F 400  PRO F 410                    
SITE     2 AC8  8 PHE F 411  ASN F 413  ARG G  12  THR G  16                    
SITE     1 AC9  1 ARG F  66                                                     
SITE     1 BC1  1 LEU G  82                                                     
SITE     1 BC2  1 LEU G  63                                                     
SITE     1 BC3  2 TRP G  56  TRP G  59                                          
SITE     1 BC4  1 PHE F  57                                                     
SITE     1 BC5  2 ARG F 369  THR F 370                                          
SITE     1 BC6  8 GLN A 253  TRP A 267  ASN E 282  TYR E 283                    
SITE     2 BC6  8 THR E 286  GLY E 289  ARG F 202  HOH F 529                    
CRYST1   81.786   97.125  112.791  85.58  78.71  72.69 P 1           2          
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      0.012227 -0.003811 -0.002365        0.00000                         
SCALE2      0.000000  0.010784 -0.000217        0.00000                         
SCALE3      0.000000  0.000000  0.009043        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system