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Database: PDB
Entry: 3PUW
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HEADER    HYDROLASE/TRANSPORT PROTEIN             06-DEC-10   3PUW              
TITLE     CRYSTAL STRUCTURE OF AN OUTWARD-FACING MBP-MALTOSE TRANSPORTER COMPLEX
TITLE    2 BOUND TO ADP-ALF4                                                    
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 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  10 ORGANISM_TAXID: 83333;                                               
SOURCE  11 STRAIN: K12;                                                         
SOURCE  12 GENE: B4033, ECDH10B_4222, JW3993, MALF;                             
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  17 ORGANISM_TAXID: 83333;                                               
SOURCE  18 STRAIN: K12;                                                         
SOURCE  19 GENE: B4032, ECDH10B_4221, JW3992, MALG;                             
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  24 ORGANISM_TAXID: 83333;                                               
SOURCE  25 STRAIN: K12;                                                         
SOURCE  26 GENE: B4035, ECDH10B_4224, JW3995, MALK;                             
SOURCE  27 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ATP BINDING CASSETTE NUCLEOTIDE BINDING DOMAIN SUBSTRATE BINDING      
KEYWDS   2 PROTEIN TRANSMEMBRANE DOMAIN, ABC TRANSPORTER IMPORTER ATPASE, ATP   
KEYWDS   3 BINDING MALTODEXTRIN BINDING, TRANSMEMBRANE INTEGRAL MEMBRANE,       
KEYWDS   4 HYDROLASE-TRANSPORT PROTEIN COMPLEX                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.L.OLDHAM,J.CHEN                                                     
REVDAT   2   28-SEP-11 3PUW    1       JRNL                                     
REVDAT   1   10-AUG-11 3PUW    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.    2.30 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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.99                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 66.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 91058                          
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) : 0.222                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4819                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1813                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 18.28                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2790                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 110                          
REMARK   3   BIN FREE R VALUE                    : 0.3400                       
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          : 287                                     
REMARK   3   SOLVENT ATOMS            : 273                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.64000                                              
REMARK   3    B22 (A**2) : 0.51000                                              
REMARK   3    B33 (A**2) : -0.31000                                             
REMARK   3    B12 (A**2) : -0.93000                                             
REMARK   3    B13 (A**2) : -1.03000                                             
REMARK   3    B23 (A**2) : 0.68000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.420         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.279         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.188         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.644        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.931                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.906                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 15287 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 20752 ; 1.003 ; 1.984       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1895 ; 4.627 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   633 ;38.584 ;24.313       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2517 ;15.650 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    78 ;17.231 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2368 ; 0.064 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11321 ; 0.004 ; 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):  9392 ; 0.222 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15146 ; 0.419 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5895 ; 0.577 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5599 ; 0.970 ; 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  : 15                                         
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):   8.0800  82.4700  17.3800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7646 T22:   0.3727                                     
REMARK   3      T33:   0.2975 T12:  -0.1662                                     
REMARK   3      T13:   0.1907 T23:   0.1044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3175 L22:   7.8083                                     
REMARK   3      L33:   5.2680 L12:   0.1105                                     
REMARK   3      L13:   0.4505 L23:   2.6173                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0357 S12:   0.0897 S13:  -0.0850                       
REMARK   3      S21:   0.1734 S22:  -0.0108 S23:   0.8072                       
REMARK   3      S31:   1.4732 S32:  -0.8544 S33:   0.0465                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    30        A   319                          
REMARK   3    RESIDUE RANGE :   A  2501        A  2501                          
REMARK   3    RESIDUE RANGE :   A  3001        A  3001                          
REMARK   3    RESIDUE RANGE :   A  1501        A  1501                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.0960  86.6010   7.5220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1878 T22:   0.0755                                     
REMARK   3      T33:   0.1191 T12:   0.0848                                     
REMARK   3      T13:   0.0706 T23:   0.0425                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9171 L22:   3.6404                                     
REMARK   3      L33:   2.3224 L12:  -0.1211                                     
REMARK   3      L13:  -0.0360 L23:   1.5767                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0025 S12:  -0.0878 S13:  -0.0429                       
REMARK   3      S21:  -0.0301 S22:   0.0848 S23:  -0.1685                       
REMARK   3      S31:   0.4426 S32:   0.1683 S33:  -0.0823                       
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   320        A   372                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.4800  78.5840 -13.9620              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9569 T22:   0.1224                                     
REMARK   3      T33:   0.1696 T12:   0.1218                                     
REMARK   3      T13:   0.1093 T23:  -0.0991                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2767 L22:   7.2684                                     
REMARK   3      L33:   6.0615 L12:   2.5841                                     
REMARK   3      L13:  -1.3272 L23:  -1.9395                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0068 S12:   0.2203 S13:   0.0338                       
REMARK   3      S21:  -1.2460 S22:   0.1910 S23:  -0.1199                       
REMARK   3      S31:   0.5233 S32:   0.1460 S33:  -0.1978                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     2        B    29                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.6810 120.1650  -0.6830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4621 T22:   0.2721                                     
REMARK   3      T33:   0.5948 T12:  -0.0956                                     
REMARK   3      T13:   0.3308 T23:   0.0242                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.5747 L22:   7.4045                                     
REMARK   3      L33:   2.2027 L12:  -2.0087                                     
REMARK   3      L13:  -0.2000 L23:   0.0741                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1995 S12:  -0.7231 S13:   0.9168                       
REMARK   3      S21:   0.0909 S22:   0.0211 S23:  -0.9041                       
REMARK   3      S31:  -0.4387 S32:   0.6120 S33:   0.1784                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    30        B   228                          
REMARK   3    RESIDUE RANGE :   B  1502        B  1502                          
REMARK   3    RESIDUE RANGE :   B  2502        B  2502                          
REMARK   3    RESIDUE RANGE :   B  3002        B  3002                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.8460 109.8110  -2.1020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3672 T22:   0.0906                                     
REMARK   3      T33:   0.1000 T12:   0.0238                                     
REMARK   3      T13:   0.1290 T23:   0.0289                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3923 L22:   3.4030                                     
REMARK   3      L33:   2.5599 L12:  -0.2278                                     
REMARK   3      L13:  -0.9101 L23:   0.2676                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0459 S12:   0.2383 S13:   0.1761                       
REMARK   3      S21:  -0.8320 S22:   0.0340 S23:  -0.1508                       
REMARK   3      S31:  -0.3628 S32:  -0.1006 S33:  -0.0799                       
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   229        B   369                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.9250  87.9300  -3.7950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5872 T22:   0.8199                                     
REMARK   3      T33:   1.1319 T12:   0.3704                                     
REMARK   3      T13:   0.3937 T23:  -0.2106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1106 L22:   6.4292                                     
REMARK   3      L33:   2.6286 L12:   1.7474                                     
REMARK   3      L13:  -0.8710 L23:  -2.3358                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1923 S12:   0.0228 S13:  -0.3585                       
REMARK   3      S21:  -0.7280 S22:  -0.2014 S23:  -1.9455                       
REMARK   3      S31:   0.6297 S32:   1.1307 S33:   0.0091                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     1        E   123                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.3380 147.4910  67.7410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1415 T22:   0.1723                                     
REMARK   3      T33:   0.1747 T12:   0.0191                                     
REMARK   3      T13:   0.0485 T23:  -0.1416                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0504 L22:   2.3840                                     
REMARK   3      L33:   3.5691 L12:  -0.2760                                     
REMARK   3      L13:  -0.4264 L23:  -0.2352                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0303 S12:  -0.0257 S13:  -0.0550                       
REMARK   3      S21:   0.2704 S22:  -0.1189 S23:   0.1750                       
REMARK   3      S31:  -0.3184 S32:  -0.4183 S33:   0.0886                       
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 :   E   124        E   198                          
REMARK   3    ORIGIN FOR THE GROUP (A): -24.1140 164.7450  46.2400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7473 T22:   0.5069                                     
REMARK   3      T33:   0.3529 T12:   0.5984                                     
REMARK   3      T13:  -0.0729 T23:  -0.0602                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7709 L22:   3.8814                                     
REMARK   3      L33:   4.4748 L12:  -0.4684                                     
REMARK   3      L13:  -0.2825 L23:   0.9874                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0003 S12:   0.2631 S13:   0.2095                       
REMARK   3      S21:  -0.1593 S22:  -0.1710 S23:   0.5619                       
REMARK   3      S31:  -1.1767 S32:  -1.0107 S33:   0.1706                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   199        E   374                          
REMARK   3    RESIDUE RANGE :   F  5004        F  5004                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.1800 158.7130  55.2790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4504 T22:   0.2283                                     
REMARK   3      T33:   0.1901 T12:   0.2487                                     
REMARK   3      T13:   0.0411 T23:  -0.1001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6694 L22:   1.9482                                     
REMARK   3      L33:   3.1774 L12:  -0.2668                                     
REMARK   3      L13:  -0.1366 L23:   0.0945                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1768 S12:   0.0514 S13:   0.1291                       
REMARK   3      S21:   0.0469 S22:  -0.2025 S23:   0.1635                       
REMARK   3      S31:  -0.9951 S32:  -0.6677 S33:   0.0257                       
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 :   F    10        F    53                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.2310 103.9740  60.5160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3722 T22:   0.3898                                     
REMARK   3      T33:   0.1232 T12:   0.1190                                     
REMARK   3      T13:   0.3845 T23:   0.0926                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  15.9705 L22:   9.0670                                     
REMARK   3      L33:   9.7767 L12:  -3.0606                                     
REMARK   3      L13:  -4.4307 L23:   4.1511                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.4651 S12:  -1.7537 S13:  -0.5343                       
REMARK   3      S21:   2.6014 S22:   0.8890 S23:   0.8541                       
REMARK   3      S31:   2.2516 S32:   0.6610 S33:   0.5761                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F    54        F   273                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.1020 130.6410  75.2330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3170 T22:   0.2736                                     
REMARK   3      T33:   0.3443 T12:  -0.1985                                     
REMARK   3      T13:   0.2103 T23:  -0.1383                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5824 L22:   1.5671                                     
REMARK   3      L33:   3.7809 L12:  -0.5711                                     
REMARK   3      L13:  -1.0618 L23:   1.3344                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1987 S12:   0.2292 S13:  -0.2238                       
REMARK   3      S21:   0.5767 S22:  -0.2993 S23:   0.4753                       
REMARK   3      S31:   0.5338 S32:  -0.8619 S33:   0.4979                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   274        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):  -6.0760 135.7610  28.0690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1850 T22:   0.2227                                     
REMARK   3      T33:   0.1517 T12:   0.1179                                     
REMARK   3      T13:  -0.0311 T23:  -0.0680                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2183 L22:   1.9392                                     
REMARK   3      L33:   2.4478 L12:  -1.0117                                     
REMARK   3      L13:  -1.0731 L23:   1.2343                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1143 S12:   0.2487 S13:  -0.0284                       
REMARK   3      S21:  -0.4329 S22:  -0.3181 S23:   0.1100                       
REMARK   3      S31:  -0.3406 S32:  -0.5268 S33:   0.2038                       
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 :   G     9        G   112                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.1480 142.4790  39.5580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1702 T22:   0.1925                                     
REMARK   3      T33:   0.3598 T12:  -0.0323                                     
REMARK   3      T13:   0.0819 T23:  -0.0224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7548 L22:   3.5637                                     
REMARK   3      L33:   2.8280 L12:  -0.6360                                     
REMARK   3      L13:  -0.5293 L23:   0.4958                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2048 S12:  -0.0740 S13:   0.2287                       
REMARK   3      S21:  -0.2485 S22:  -0.0932 S23:  -0.5139                       
REMARK   3      S31:  -0.6546 S32:   0.2527 S33:  -0.1116                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G   113        G   155                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.3710 116.9640  47.8130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3844 T22:   0.2545                                     
REMARK   3      T33:   0.4631 T12:  -0.2283                                     
REMARK   3      T13:   0.2561 T23:  -0.0634                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8671 L22:   4.8918                                     
REMARK   3      L33:   9.7641 L12:  -2.4790                                     
REMARK   3      L13:  -1.0892 L23:   4.3555                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0534 S12:   0.1959 S13:  -0.4378                       
REMARK   3      S21:   0.3448 S22:  -0.5446 S23:   0.3332                       
REMARK   3      S31:   0.7787 S32:  -1.1498 S33:   0.5980                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G   156        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):   8.0580 125.0270  40.4840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1223 T22:   0.1732                                     
REMARK   3      T33:   0.2200 T12:   0.0332                                     
REMARK   3      T13:   0.0133 T23:  -0.0166                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4383 L22:   2.3240                                     
REMARK   3      L33:   2.4340 L12:  -0.5233                                     
REMARK   3      L13:  -0.7801 L23:   2.1893                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0153 S12:  -0.0777 S13:   0.0917                       
REMARK   3      S21:   0.0743 S22:   0.0314 S23:  -0.1367                       
REMARK   3      S31:   0.0971 S32:   0.0835 S33:  -0.0468                       
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 3PUW 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 RCSB062841.                                      
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   : 93125                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
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     (%) : 60.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 16.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.45900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 27 % PEG 400, 0.1 M 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: 31170 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 76210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -168.0 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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O3B  ADP A  2501    AL    ALF A  3001              2.02            
REMARK 500   O3B  ADP B  2502    AL    ALF B  3002              2.07            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP E  55     -157.21   -111.79                                   
REMARK 500    ALA E 168      -79.32    -74.18                                   
REMARK 500    GLU E 172      -85.43    -69.73                                   
REMARK 500    ASN E 241       95.32    -65.00                                   
REMARK 500    LYS E 256       75.96   -119.31                                   
REMARK 500    ALA E 373      -63.02    -93.55                                   
REMARK 500    GLN F  37      -54.09     48.24                                   
REMARK 500    PHE F 344     -165.35   -108.75                                   
REMARK 500    PHE F 355      -44.56     69.46                                   
REMARK 500    ILE F 417      -60.32   -129.51                                   
REMARK 500    GLU F 477     -136.93   -111.85                                   
REMARK 500    ALA F 502       84.24    -69.94                                   
REMARK 500    PRO G 132      102.89    -56.67                                   
REMARK 500    ASP A  21       53.36     37.40                                   
REMARK 500    TYR A  84      -45.94     71.82                                   
REMARK 500    ALA A 133       38.91    -94.67                                   
REMARK 500    ASP A 333      176.14     70.15                                   
REMARK 500    TYR B  84      -51.96     79.09                                   
REMARK 500    ALA B 133       34.10    -98.57                                   
REMARK 500    PRO B 269       75.62    -69.92                                   
REMARK 500    ASP B 333      178.22     72.61                                   
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 A1501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A2501   O2B                                                    
REMARK 620 2 SER A  43   OG   85.3                                              
REMARK 620 3 GLN A  82   OE1 172.6  88.3                                        
REMARK 620 4 HOH A 382   O    92.3  78.2  90.0                                  
REMARK 620 5 HOH A 383   O    95.5  89.9  80.8 165.2                            
REMARK 620 N                    1     2     3     4                             
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 GLN B  82   OE1                                                    
REMARK 620 2 ADP B2502   O2B 151.3                                              
REMARK 620 3 SER B  43   OG   78.3  77.0                                        
REMARK 620 4 HOH B 383   O    99.3  84.8  68.5                                  
REMARK 620 5 HOH B 382   O    81.7  79.8  79.5 146.8                            
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 MAL F 2000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV F 4001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV F 4002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV F 4008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UMQ F 5004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV G 4003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV G 4004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV G 4005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV G 4006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 2501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF A 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 2502                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF B 3002                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3PUV   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: 3PV0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3RLF   RELATED DB: PDB                                   
DBREF  3PUW E    1   370  UNP    P0AEX9   MALE_ECOLI      27    396             
DBREF  3PUW F    1   514  UNP    P02916   MALF_ECOLI       1    514             
DBREF  3PUW G    1   296  UNP    P68183   MALG_ECOLI       1    296             
DBREF  3PUW A    1   371  UNP    P68187   MALK_ECOLI       1    371             
DBREF  3PUW B    1   371  UNP    P68187   MALK_ECOLI       1    371             
SEQADV 3PUW ALA E  371  UNP  P0AEX9              EXPRESSION TAG                 
SEQADV 3PUW SER E  372  UNP  P0AEX9              EXPRESSION TAG                 
SEQADV 3PUW ALA E  373  UNP  P0AEX9              EXPRESSION TAG                 
SEQADV 3PUW SER E  374  UNP  P0AEX9              EXPRESSION TAG                 
SEQADV 3PUW HIS E  375  UNP  P0AEX9              EXPRESSION TAG                 
SEQADV 3PUW HIS E  376  UNP  P0AEX9              EXPRESSION TAG                 
SEQADV 3PUW HIS E  377  UNP  P0AEX9              EXPRESSION TAG                 
SEQADV 3PUW HIS E  378  UNP  P0AEX9              EXPRESSION TAG                 
SEQADV 3PUW ALA A  372  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUW SER A  373  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUW ALA A  374  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUW SER A  375  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUW HIS A  376  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUW HIS A  377  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUW HIS A  378  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUW HIS A  379  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUW HIS A  380  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUW HIS A  381  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUW ALA B  372  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUW SER B  373  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUW ALA B  374  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUW SER B  375  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUW HIS B  376  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUW HIS B  377  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUW HIS B  378  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUW HIS B  379  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUW HIS B  380  UNP  P68187              EXPRESSION TAG                 
SEQADV 3PUW 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      17                                                       
HET    UMQ  F5004      34                                                       
HET    PGV  G4003      14                                                       
HET    PGV  G4004      12                                                       
HET    PGV  G4005      12                                                       
HET    PGV  G4006      15                                                       
HET    PGV  G4007      12                                                       
HET    PGV  G4009      14                                                       
HET     MG  A1501       1                                                       
HET     MG  B1502       1                                                       
HET    ADP  A2501      27                                                       
HET    ALF  A3001       5                                                       
HET    ADP  B2502      27                                                       
HET    ALF  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     ALF TETRAFLUOROALUMINATE 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  ALF    2(AL F4 1-)                                                  
FORMUL  24  HOH   *273(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  ALA E  141  1                                  11    
HELIX    7   7 GLU E  153  ALA E  163  1                                  11    
HELIX    8   8 ASN E  185  ASN E  201  1                                  17    
HELIX    9   9 ASP E  209  LYS E  219  1                                  11    
HELIX   10  10 GLY E  228  TRP E  230  5                                   3    
HELIX   11  11 ALA E  231  LYS E  239  1                                   9    
HELIX   12  12 ASN E  272  TYR E  283  1                                  12    
HELIX   13  13 THR E  286  LYS E  297  1                                  12    
HELIX   14  14 LEU E  304  ALA E  312  1                                   9    
HELIX   15  15 ASP E  314  GLY E  327  1                                  14    
HELIX   16  16 GLN E  335  GLY E  353  1                                  19    
HELIX   17  17 THR E  356  SER E  374  1                                  19    
HELIX   18  18 ASP F   13  LEU F   30  1                                  18    
HELIX   19  19 LEU F   30  ALA F   36  1                                   7    
HELIX   20  20 GLU F   39  ASN F   59  1                                  21    
HELIX   21  21 ARG F   60  TYR F   63  5                                   4    
HELIX   22  22 ALA F   64  VAL F   79  1                                  16    
HELIX   23  23 VAL F   79  ALA F   90  1                                  12    
HELIX   24  24 THR F  101  ARG F  112  1                                  12    
HELIX   25  25 ASN F  172  ASN F  179  1                                   8    
HELIX   26  26 ASN F  179  SER F  184  1                                   6    
HELIX   27  27 TRP F  261  ASP F  270  1                                  10    
HELIX   28  28 PRO F  276  VAL F  306  1                                  31    
HELIX   29  29 GLY F  313  ILE F  322  1                                  10    
HELIX   30  30 ILE F  322  VAL F  327  1                                   6    
HELIX   31  31 PRO F  328  PHE F  340  1                                  13    
HELIX   32  32 GLY F  345  LEU F  354  1                                  10    
HELIX   33  33 ASP F  364  LEU F  392  1                                  29    
HELIX   34  34 LYS F  393  PRO F  396  5                                   4    
HELIX   35  35 ASP F  397  ASP F  406  1                                  10    
HELIX   36  36 GLY F  409  ILE F  417  1                                   9    
HELIX   37  37 ILE F  417  ASN F  439  1                                  23    
HELIX   38  38 ASN F  440  THR F  448  1                                   9    
HELIX   39  39 LEU F  466  GLU F  477  1                                  12    
HELIX   40  40 ASP F  483  ALA F  502  1                                  20    
HELIX   41  41 LYS G   10  LEU G   39  1                                  30    
HELIX   42  42 TRP G   56  GLY G   64  1                                   9    
HELIX   43  43 PRO G   80  MET G  113  1                                  34    
HELIX   44  44 GLY G  117  GLN G  129  1                                  13    
HELIX   45  45 LEU G  135  GLU G  149  1                                  15    
HELIX   46  46 ILE G  151  GLY G  155  5                                   5    
HELIX   47  47 THR G  158  LEU G  167  1                                  10    
HELIX   48  48 ILE G  170  ILE G  184  1                                  15    
HELIX   49  49 SER G  186  ASP G  195  1                                  10    
HELIX   50  50 THR G  198  VAL G  206  1                                   9    
HELIX   51  51 VAL G  206  GLU G  229  1                                  24    
HELIX   52  52 VAL G  230  LEU G  237  1                                   8    
HELIX   53  53 ASP G  239  TYR G  243  5                                   5    
HELIX   54  54 THR G  244  MET G  249  1                                   6    
HELIX   55  55 GLN G  250  LEU G  253  5                                   4    
HELIX   56  56 LEU G  259  GLN G  282  1                                  24    
HELIX   57  57 ARG G  283  LEU G  285  5                                   3    
HELIX   58  58 GLY A   41  GLY A   51  1                                  11    
HELIX   59  59 PRO A   71  ARG A   75  5                                   5    
HELIX   60  60 SER A   91  ALA A  103  1                                  13    
HELIX   61  61 LYS A  106  LEU A  121  1                                  16    
HELIX   62  62 LYS A  130  LEU A  134  5                                   5    
HELIX   63  63 SER A  135  GLU A  151  1                                  17    
HELIX   64  64 ASP A  165  GLY A  184  1                                  20    
HELIX   65  65 ASP A  193  ALA A  201  1                                   9    
HELIX   66  66 LYS A  217  TYR A  224  1                                   8    
HELIX   67  67 ASP A  227  ILE A  234  1                                   8    
HELIX   68  68 ASP A  294  ALA A  296  5                                   3    
HELIX   69  69 PRO A  348  CYS A  352  5                                   5    
HELIX   70  70 GLY B   41  GLY B   51  1                                  11    
HELIX   71  71 PRO B   71  ARG B   75  5                                   5    
HELIX   72  72 SER B   91  SER B   97  1                                   7    
HELIX   73  73 SER B   97  ALA B  103  1                                   7    
HELIX   74  74 LYS B  106  LEU B  121  1                                  16    
HELIX   75  75 LEU B  123  LEU B  127  5                                   5    
HELIX   76  76 LYS B  130  LEU B  134  5                                   5    
HELIX   77  77 SER B  135  GLU B  151  1                                  17    
HELIX   78  78 ASP B  165  GLY B  184  1                                  20    
HELIX   79  79 ASP B  193  ALA B  201  1                                   9    
HELIX   80  80 LYS B  217  TYR B  224  1                                   8    
HELIX   81  81 ASP B  227  ILE B  234  1                                   8    
HELIX   82  82 PRO B  348  CYS B  352  5                                   5    
SHEET    1   A 6 VAL E  35  GLU E  38  0                                        
SHEET    2   A 6 LEU E   7  TRP E  10  1  N  ILE E   9   O  THR E  36           
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 VAL E  35  GLU E  38  0                                        
SHEET    2   B 5 LEU E   7  TRP E  10  1  N  ILE E   9   O  THR E  36           
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 8 SER F 113  ALA F 127  0                                        
SHEET    2   F 8 GLU F 130  SER F 136 -1  O  GLU F 130   N  ALA F 127           
SHEET    3   F 8 ASN F 143  SER F 146 -1  O  TYR F 144   N  LEU F 135           
SHEET    4   F 8 GLN F 155  THR F 162 -1  O  THR F 162   N  ASN F 143           
SHEET    5   F 8 ILE F 186  ILE F 189  1  O  ILE F 189   N  LEU F 159           
SHEET    6   F 8 LYS F 195  MET F 198 -1  O  VAL F 196   N  ALA F 188           
SHEET    7   F 8 GLN F 203  PRO F 209 -1  O  SER F 205   N  MET F 197           
SHEET    8   F 8 SER F 113  ALA F 127 -1  N  TYR F 120   O  PHE F 204           
SHEET    1   G 5 TYR F 211  LEU F 213  0                                        
SHEET    2   G 5 LEU F 219  ASN F 221 -1  O  THR F 220   N  THR F 212           
SHEET    3   G 5 LYS F 227  ASN F 231 -1  O  TYR F 228   N  LEU F 219           
SHEET    4   G 5 PHE F 236  SER F 239 -1  O  GLN F 238   N  ARG F 229           
SHEET    5   G 5 LYS F 250  LEU F 251 -1  O  LEU F 251   N  TYR F 237           
SHEET    1   H 2 ASP F 453  ARG F 454  0                                        
SHEET    2   H 2 ALA F 461  GLY F 462 -1  O  ALA F 461   N  ARG F 454           
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 4 VAL A  16  ILE A  26  0                                        
SHEET    2   J 4 VAL A   4  TRP A  13 -1  N  TRP A  13   O  VAL A  16           
SHEET    3   J 4 SER A  57  ILE A  62 -1  O  SER A  57   N  THR A  10           
SHEET    4   J 4 LYS A  65  ARG A  66 -1  O  LYS A  65   N  ILE A  62           
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  VAL A 190   N  LEU A 157           
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  35           
SHEET    6   K 6 ARG A 211  GLY A 216 -1  O  GLY A 216   N  ILE A 204           
SHEET    1   L 5 GLN A 265  LEU A 268  0                                        
SHEET    2   L 5 GLN A 253  GLU A 257 -1  N  VAL A 254   O  LEU A 268           
SHEET    3   L 5 ASN A 240  ALA A 250 -1  N  THR A 247   O  GLN A 255           
SHEET    4   L 5 ASN A 280  ILE A 285 -1  O  LEU A 283   N  LEU A 242           
SHEET    5   L 5 HIS A 353  PHE A 355 -1  O  HIS A 353   N  GLY A 284           
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  GLY A 302   O  PHE A 343           
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  GLN A 331   N  THR A 314           
SHEET    1   N 3 VAL B  16  ILE B  26  0                                        
SHEET    2   N 3 VAL B   4  TRP B  13 -1  N  VAL B   9   O  ILE B  22           
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  MET B 187           
SHEET    5   O 6 LYS B 203  ASP B 208  1  O  VAL B 205   N  VAL B  33           
SHEET    6   O 6 ARG B 211  GLY B 216 -1  O  ARG B 211   N  ASP B 208           
SHEET    1   P 3 ASN B 240  VAL B 244  0                                        
SHEET    2   P 3 MET B 281  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  GLN B 331   N  THR B 314           
LINK        MG    MG A1501                 O2B ADP A2501     1555   1555  1.94  
LINK         OE1 GLN B  82                MG    MG B1502     1555   1555  2.13  
LINK         OG  SER A  43                MG    MG A1501     1555   1555  2.17  
LINK         OE1 GLN A  82                MG    MG A1501     1555   1555  2.21  
LINK        MG    MG B1502                 O2B ADP B2502     1555   1555  2.22  
LINK         OG  SER B  43                MG    MG B1502     1555   1555  2.35  
LINK        MG    MG B1502                 O   HOH B 383     1555   1555  1.98  
LINK        MG    MG A1501                 O   HOH A 382     1555   1555  1.99  
LINK        MG    MG B1502                 O   HOH B 382     1555   1555  2.05  
LINK        MG    MG A1501                 O   HOH A 383     1555   1555  2.09  
CISPEP   1 SER F  252    PRO F  253          0         4.96                     
CISPEP   2 GLY F  451    PRO F  452          0         3.84                     
CISPEP   3 SER A  236    PRO A  237          0        -0.65                     
CISPEP   4 SER B  236    PRO B  237          0        -4.41                     
SITE     1 AC1 10 THR F 291  TYR F 325  ASN F 376  GLY F 380                    
SITE     2 AC1 10 SER F 433  PHE F 436  ASN F 437  ASN F 440                    
SITE     3 AC1 10 HOH F 561  HOH F 569                                          
SITE     1 AC2 11 CYS F 304  GLN F 307  TRP F 308  TYR F 400                    
SITE     2 AC2 11 PRO F 410  PHE F 411  ASN F 413  HOH F 557                    
SITE     3 AC2 11 HOH F 567  ARG G  12  THR G  16                               
SITE     1 AC3  1 ARG F  66                                                     
SITE     1 AC4  1 PHE F  57                                                     
SITE     1 AC5  7 GLN A 253  TRP A 267  ASN E 282  TYR E 283                    
SITE     2 AC5  7 GLY E 289  ASN F 121  ARG F 202                               
SITE     1 AC6  1 TRP G  86                                                     
SITE     1 AC7  1 LEU G  83                                                     
SITE     1 AC8  1 LEU G  63                                                     
SITE     1 AC9  2 TRP G  59  LYS G  60                                          
SITE     1 BC1  6 SER A  43  GLN A  82  HOH A 382  HOH A 383                    
SITE     2 BC1  6 ADP A2501  ALF A3001                                          
SITE     1 BC2  7 SER B  43  GLN B  82  GLU B 159  HOH B 382                    
SITE     2 BC2  7 HOH B 383  ADP B2502  ALF B3002                               
SITE     1 BC3 16 TRP A  13  VAL A  18  GLY A  39  CYS A  40                    
SITE     2 BC3 16 GLY A  41  LYS A  42  SER A  43  THR A  44                    
SITE     3 BC3 16 HOH A 382  HOH A 383   MG A1501  ALF A3001                    
SITE     4 BC3 16 ARG B 129  ALA B 133  SER B 135  GLN B 138                    
SITE     1 BC4 14 SER A  38  GLY A  39  LYS A  42  GLN A  82                    
SITE     2 BC4 14 GLU A 159  HIS A 192  HOH A 382  HOH A 383                    
SITE     3 BC4 14 HOH A 384   MG A1501  ADP A2501  SER B 135                    
SITE     4 BC4 14 GLY B 136  GLY B 137                                          
SITE     1 BC5 15 ARG A 129  ALA A 133  SER A 135  GLN A 138                    
SITE     2 BC5 15 VAL B  18  GLY B  39  CYS B  40  GLY B  41                    
SITE     3 BC5 15 LYS B  42  SER B  43  THR B  44  HOH B 382                    
SITE     4 BC5 15 HOH B 383   MG B1502  ALF B3002                               
SITE     1 BC6 14 SER A 135  GLY A 136  GLY A 137  SER B  38                    
SITE     2 BC6 14 GLY B  39  LYS B  42  GLN B  82  GLU B 159                    
SITE     3 BC6 14 HIS B 192  HOH B 382  HOH B 383  HOH B 384                    
SITE     4 BC6 14  MG B1502  ADP B2502                                          
CRYST1   81.881   97.344  112.336  85.76  79.42  72.45 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      0.012213 -0.003862 -0.002205        0.00000                         
SCALE2      0.000000  0.010774 -0.000214        0.00000                         
SCALE3      0.000000  0.000000  0.009058        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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