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Database: PDB
Entry: 2OJW
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HEADER    LIGASE                                  15-JAN-07   2OJW              
TITLE     CRYSTAL STRUCTURE OF HUMAN GLUTAMINE SYNTHETASE IN COMPLEX WITH ADP   
TITLE    2 AND PHOSPHATE                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMINE SYNTHETASE;                                      
COMPND   3 CHAIN: A, B, C, D, E;                                                
COMPND   4 FRAGMENT: RESIDUES 4-364;                                            
COMPND   5 SYNONYM: GLUTAMATE-AMMONIA LIGASE, GS;                               
COMPND   6 EC: 6.3.1.2;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GLUL, GLNS;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC-BSA4                                 
KEYWDS    AMINO-ACID BIOSYNTHESIS, LIGASE, SYNTHETASE, STRUCTURAL GENOMICS,     
KEYWDS   2 STRUCTURAL GENOMICS CONSORTIUM, SGC                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.KARLBERG,J.UPPENBERG,C.ARROWSMITH,H.BERGLUND,R.D.BUSAM,R.COLLINS,   
AUTHOR   2 A.EDWARDS,S.FLODIN,A.FLORES,S.GRASLUND,B.M.HALLBERG,M.HAMMARSTROM,   
AUTHOR   3 M.HOGBOM,I.JOHANSSON,T.KOTENYOVA,M.MOCHE,M.E.NILSSON,P.NORDLUND,     
AUTHOR   4 T.NYMAN,D.OGG,C.PERSSON,J.SAGEMARK,P.STENMARK,M.SUNDSTROM,           
AUTHOR   5 A.G.THORSELL,S.VAN DEN BERG,K.WALLDEN,J.WEIGELT,L.HOLMBERG-          
AUTHOR   6 SCHIAVONE,STRUCTURAL GENOMICS CONSORTIUM (SGC)                       
REVDAT   5   13-JUL-11 2OJW    1       VERSN                                    
REVDAT   4   24-FEB-09 2OJW    1       VERSN                                    
REVDAT   3   18-DEC-07 2OJW    1       JRNL                                     
REVDAT   2   27-NOV-07 2OJW    1       JRNL                                     
REVDAT   1   13-MAR-07 2OJW    0                                                
JRNL        AUTH   W.W.KRAJEWSKI,R.COLLINS,L.HOLMBERG-SCHIAVONE,T.A.JONES,      
JRNL        AUTH 2 T.KARLBERG,S.L.MOWBRAY                                       
JRNL        TITL   CRYSTAL STRUCTURES OF MAMMALIAN GLUTAMINE SYNTHETASES        
JRNL        TITL 2 ILLUSTRATE SUBSTRATE-INDUCED CONFORMATIONAL CHANGES AND      
JRNL        TITL 3 PROVIDE OPPORTUNITIES FOR DRUG AND HERBICIDE DESIGN.         
JRNL        REF    J.MOL.BIOL.                   V. 375   217 2008              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   18005987                                                     
JRNL        DOI    10.1016/J.JMB.2007.10.029                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0021                                      
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) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.25                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 121373                         
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) : 0.162                           
REMARK   3   R VALUE            (WORKING SET) : 0.159                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6388                            
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) : 2.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8909                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1980                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 468                          
REMARK   3   BIN FREE R VALUE                    : 0.2890                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14250                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 221                                     
REMARK   3   SOLVENT ATOMS            : 1390                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 11.84                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.15000                                              
REMARK   3    B22 (A**2) : 0.13000                                              
REMARK   3    B33 (A**2) : 1.03000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.01000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.174         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.160         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.110         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.039         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 14840 ; 0.019 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A): 10359 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 20083 ; 1.776 ; 1.958       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 24991 ; 1.094 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1796 ;12.756 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   729 ;36.810 ;23.388       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2414 ;14.792 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   122 ;17.345 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2023 ; 0.118 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 16607 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  3167 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2676 ; 0.203 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A): 10497 ; 0.204 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6671 ; 0.176 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  7178 ; 0.084 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1047 ; 0.187 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    24 ; 0.182 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    77 ; 0.195 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.234 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 11515 ; 1.096 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3658 ; 0.244 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14361 ; 1.301 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7035 ; 2.203 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5719 ; 3.051 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D E                       
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 10                              
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     18       A     310      5                      
REMARK   3           2     B     18       B     310      5                      
REMARK   3           3     C     18       C     310      5                      
REMARK   3           4     D     18       D     310      5                      
REMARK   3           5     E     18       E     310      5                      
REMARK   3           6     A    317       A     365      5                      
REMARK   3           7     B    317       B     365      5                      
REMARK   3           8     C    317       C     365      5                      
REMARK   3           9     D    317       D     365      5                      
REMARK   3          10     E    317       E     364      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1940 ;  0.15 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1940 ;  0.13 ;  0.00           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   1940 ;  0.13 ;  0.00           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   1940 ;  0.14 ;  0.00           
REMARK   3   MEDIUM POSITIONAL  1    E    (A):   1940 ;  0.15 ;  0.00           
REMARK   3   LOOSE POSITIONAL   1    A    (A):   2571 ;  0.46 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    B    (A):   2571 ;  0.45 ;  0.00           
REMARK   3   LOOSE POSITIONAL   1    C    (A):   2571 ;  0.45 ;  0.00           
REMARK   3   LOOSE POSITIONAL   1    D    (A):   2571 ;  0.44 ;  0.00           
REMARK   3   LOOSE POSITIONAL   1    E    (A):   2571 ;  0.44 ;  0.00           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1940 ;  0.87 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1940 ;  0.68 ;  0.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   1940 ;  0.61 ;  0.00           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   1940 ;  0.58 ;  0.00           
REMARK   3   MEDIUM THERMAL     1    E (A**2):   1940 ;  0.79 ;  0.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):   2571 ;  0.89 ; 10.00           
REMARK   3   LOOSE THERMAL      1    B (A**2):   2571 ;  0.78 ;  0.00           
REMARK   3   LOOSE THERMAL      1    C (A**2):   2571 ;  0.82 ;  0.00           
REMARK   3   LOOSE THERMAL      1    D (A**2):   2571 ;  0.78 ;  0.00           
REMARK   3   LOOSE THERMAL      1    E (A**2):   2571 ;  0.83 ;  0.00           
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    11        A   127                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.0970  17.9210 -36.1190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0218 T22:   0.0321                                     
REMARK   3      T33:  -0.0564 T12:   0.0028                                     
REMARK   3      T13:   0.0129 T23:   0.0084                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3781 L22:   0.4079                                     
REMARK   3      L33:   0.1311 L12:  -0.2948                                     
REMARK   3      L13:  -0.1802 L23:   0.1315                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0136 S12:  -0.0020 S13:   0.0590                       
REMARK   3      S21:  -0.0562 S22:   0.0122 S23:  -0.0337                       
REMARK   3      S31:  -0.0269 S32:   0.0263 S33:   0.0015                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   128        A   177                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.2540  -3.8390 -26.5830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0166 T22:   0.0396                                     
REMARK   3      T33:  -0.0592 T12:   0.0043                                     
REMARK   3      T13:  -0.0003 T23:  -0.0102                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0185 L22:   0.2633                                     
REMARK   3      L33:   0.1844 L12:   0.0439                                     
REMARK   3      L13:  -0.0569 L23:  -0.1731                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0243 S12:   0.0202 S13:  -0.0404                       
REMARK   3      S21:   0.0460 S22:  -0.0154 S23:   0.0091                       
REMARK   3      S31:   0.0276 S32:   0.0237 S33:  -0.0089                       
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   178        A   365                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.4500  -6.8830 -31.9490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0249 T22:   0.0115                                     
REMARK   3      T33:  -0.0566 T12:   0.0076                                     
REMARK   3      T13:   0.0097 T23:  -0.0045                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2571 L22:   0.3035                                     
REMARK   3      L33:   0.3167 L12:  -0.1111                                     
REMARK   3      L13:  -0.1498 L23:   0.0639                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0091 S12:  -0.0030 S13:  -0.0199                       
REMARK   3      S21:  -0.0140 S22:  -0.0018 S23:  -0.0028                       
REMARK   3      S31:   0.0143 S32:  -0.0275 S33:  -0.0073                       
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    13        B   127                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.5190  43.3780 -28.6060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0169 T22:  -0.0052                                     
REMARK   3      T33:  -0.0272 T12:  -0.0082                                     
REMARK   3      T13:  -0.0210 T23:   0.0402                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5337 L22:   0.2425                                     
REMARK   3      L33:   0.1155 L12:   0.0154                                     
REMARK   3      L13:  -0.1830 L23:   0.0912                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0127 S12:   0.0419 S13:   0.0658                       
REMARK   3      S21:  -0.0615 S22:  -0.0262 S23:   0.0090                       
REMARK   3      S31:  -0.0088 S32:  -0.0255 S33:   0.0135                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   128        B   177                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.8920  33.1850 -25.9550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0250 T22:   0.0242                                     
REMARK   3      T33:  -0.0311 T12:   0.0014                                     
REMARK   3      T13:  -0.0012 T23:   0.0010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2717 L22:   0.4343                                     
REMARK   3      L33:   0.1710 L12:  -0.0925                                     
REMARK   3      L13:   0.0680 L23:  -0.1235                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0394 S12:  -0.0051 S13:   0.0453                       
REMARK   3      S21:   0.0065 S22:   0.0442 S23:  -0.0310                       
REMARK   3      S31:   0.0064 S32:   0.0252 S33:  -0.0048                       
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   178        B   365                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.4790  38.3930 -30.9450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0369 T22:   0.0169                                     
REMARK   3      T33:  -0.0086 T12:  -0.0115                                     
REMARK   3      T13:   0.0085 T23:  -0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3883 L22:   0.3221                                     
REMARK   3      L33:   0.4896 L12:   0.0112                                     
REMARK   3      L13:  -0.1807 L23:  -0.0560                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0064 S12:   0.0056 S13:   0.0791                       
REMARK   3      S21:  -0.0269 S22:   0.0459 S23:  -0.0535                       
REMARK   3      S31:   0.0161 S32:   0.0805 S33:  -0.0523                       
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 :   C    10        C   127                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.7960  26.7420 -18.1960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0450 T22:   0.0124                                     
REMARK   3      T33:  -0.0093 T12:   0.0037                                     
REMARK   3      T13:  -0.0360 T23:   0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1934 L22:   0.5267                                     
REMARK   3      L33:   0.0710 L12:   0.0153                                     
REMARK   3      L13:   0.0210 L23:  -0.1884                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0346 S12:   0.0240 S13:   0.0434                       
REMARK   3      S21:  -0.0211 S22:   0.0264 S23:   0.0493                       
REMARK   3      S31:   0.0193 S32:  -0.0299 S33:   0.0083                       
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 :   C   128        C   177                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.1910  42.1910 -14.8590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0408 T22:   0.0121                                     
REMARK   3      T33:  -0.0159 T12:  -0.0008                                     
REMARK   3      T13:  -0.0146 T23:  -0.0003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6280 L22:   0.1937                                     
REMARK   3      L33:   0.2841 L12:   0.0851                                     
REMARK   3      L13:   0.3344 L23:   0.0947                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0017 S12:  -0.0959 S13:   0.0876                       
REMARK   3      S21:  -0.0225 S22:  -0.0124 S23:   0.0117                       
REMARK   3      S31:   0.0106 S32:  -0.0331 S33:   0.0107                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   178        C   365                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.5050  48.4630 -17.2480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0567 T22:  -0.0069                                     
REMARK   3      T33:   0.0189 T12:   0.0103                                     
REMARK   3      T13:  -0.0189 T23:   0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3925 L22:   0.3162                                     
REMARK   3      L33:   0.2000 L12:  -0.0134                                     
REMARK   3      L13:   0.1862 L23:   0.0024                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0313 S12:  -0.0285 S13:   0.0994                       
REMARK   3      S21:  -0.0373 S22:   0.0035 S23:   0.0475                       
REMARK   3      S31:   0.0084 S32:  -0.0028 S33:   0.0278                       
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 :   D    11        D   127                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.3430  -8.9050 -20.3740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0336 T22:   0.0194                                     
REMARK   3      T33:  -0.0087 T12:  -0.0380                                     
REMARK   3      T13:  -0.0079 T23:  -0.0312                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7508 L22:   0.3053                                     
REMARK   3      L33:   0.0230 L12:  -0.1857                                     
REMARK   3      L13:  -0.0946 L23:   0.0771                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0019 S12:   0.0547 S13:  -0.0986                       
REMARK   3      S21:  -0.0369 S22:  -0.0217 S23:   0.0688                       
REMARK   3      S31:   0.0197 S32:  -0.0121 S33:   0.0236                       
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 :   D   128        D   177                          
REMARK   3    ORIGIN FOR THE GROUP (A): -36.0080  10.9340  -8.8470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0271 T22:   0.0104                                     
REMARK   3      T33:  -0.0176 T12:  -0.0189                                     
REMARK   3      T13:  -0.0078 T23:  -0.0090                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4292 L22:   0.5658                                     
REMARK   3      L33:   0.0609 L12:   0.1677                                     
REMARK   3      L13:  -0.0045 L23:   0.1727                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0164 S12:   0.0060 S13:  -0.0202                       
REMARK   3      S21:   0.0396 S22:  -0.0194 S23:   0.0275                       
REMARK   3      S31:  -0.0133 S32:  -0.0069 S33:   0.0358                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   178        D   365                          
REMARK   3    ORIGIN FOR THE GROUP (A): -43.7620   9.5070 -10.1480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0538 T22:   0.0056                                     
REMARK   3      T33:   0.0087 T12:  -0.0325                                     
REMARK   3      T13:   0.0005 T23:  -0.0152                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4714 L22:   0.3507                                     
REMARK   3      L33:   0.1699 L12:  -0.0955                                     
REMARK   3      L13:   0.0407 L23:   0.2001                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0005 S12:   0.0250 S13:  -0.0389                       
REMARK   3      S21:   0.0250 S22:  -0.0508 S23:   0.0868                       
REMARK   3      S31:  -0.0039 S32:  -0.0021 S33:   0.0514                       
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 :   E    15        E   127                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.6720 -14.5710 -31.8560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0013 T22:   0.0189                                     
REMARK   3      T33:  -0.0485 T12:   0.0039                                     
REMARK   3      T13:   0.0046 T23:  -0.0404                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4080 L22:   0.4261                                     
REMARK   3      L33:   0.1562 L12:   0.0491                                     
REMARK   3      L13:  -0.1319 L23:   0.0603                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0124 S12:   0.1128 S13:  -0.0514                       
REMARK   3      S21:  -0.0137 S22:  -0.0233 S23:   0.0257                       
REMARK   3      S31:   0.0439 S32:   0.0324 S33:   0.0356                       
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 :   E   128        E   177                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.4050 -17.6310 -16.3390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0132 T22:   0.0129                                     
REMARK   3      T33:  -0.0306 T12:  -0.0178                                     
REMARK   3      T13:   0.0149 T23:  -0.0066                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5126 L22:   0.0362                                     
REMARK   3      L33:   0.4101 L12:  -0.1326                                     
REMARK   3      L13:  -0.2773 L23:   0.0498                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0443 S12:  -0.0258 S13:  -0.0555                       
REMARK   3      S21:   0.0303 S22:  -0.0122 S23:   0.0523                       
REMARK   3      S31:   0.0822 S32:  -0.0046 S33:   0.0566                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   178        E   364                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.4560 -24.6800 -19.6390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0011 T22:  -0.0047                                     
REMARK   3      T33:   0.0083 T12:  -0.0180                                     
REMARK   3      T13:   0.0185 T23:  -0.0343                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4787 L22:   0.3626                                     
REMARK   3      L33:   0.3435 L12:   0.0835                                     
REMARK   3      L13:  -0.0976 L23:   0.0768                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0465 S12:   0.0161 S13:  -0.1393                       
REMARK   3      S21:   0.0107 S22:   0.0093 S23:   0.0300                       
REMARK   3      S31:   0.0577 S32:  -0.0307 S33:   0.0372                       
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 2OJW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JAN-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB041227.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-SEP-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.93300                            
REMARK 200  MONOCHROMATOR                  : DIAMOND (111), GE(220)             
REMARK 200  OPTICS                         : FOCUSING: TOROIDAL MIRROR          
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 125431                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.12050                            
REMARK 200  R SYM                      (I) : 0.14000                            
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) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.48500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2D3A                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% ISOPROPANOL, 200 MM NACL, 100 MM     
REMARK 280  HEPES, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K,     
REMARK 280  PH 7.50                                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       88.80000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.30000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       88.80000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       61.30000            
REMARK 290   SMTRY3   4  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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DECAMER GENERATED FROM THE      
REMARK 300 PENTAMER IN THE ASYMMETRIC UNIT BY THE OPERATION: -X, Y, -Z          
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: DECAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC                  
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 73600 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 117210 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -758.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     MET A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     SER A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     VAL A    -8                                                      
REMARK 465     ASP A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     GLY A    -5                                                      
REMARK 465     THR A    -4                                                      
REMARK 465     GLU A    -3                                                      
REMARK 465     ASN A    -2                                                      
REMARK 465     LEU A    -1                                                      
REMARK 465     THR A   142                                                      
REMARK 465     GLY A   302                                                      
REMARK 465     PHE A   303                                                      
REMARK 465     HIS A   304                                                      
REMARK 465     GLU A   305                                                      
REMARK 465     THR A   306                                                      
REMARK 465     MET B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     SER B   -11                                                      
REMARK 465     SER B   -10                                                      
REMARK 465     GLY B    -9                                                      
REMARK 465     VAL B    -8                                                      
REMARK 465     ASP B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     GLY B    -5                                                      
REMARK 465     THR B    -4                                                      
REMARK 465     GLU B    -3                                                      
REMARK 465     ASN B    -2                                                      
REMARK 465     LEU B    -1                                                      
REMARK 465     THR B   142                                                      
REMARK 465     PHE B   303                                                      
REMARK 465     HIS B   304                                                      
REMARK 465     GLU B   305                                                      
REMARK 465     MET C   -18                                                      
REMARK 465     HIS C   -17                                                      
REMARK 465     HIS C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     SER C   -11                                                      
REMARK 465     SER C   -10                                                      
REMARK 465     GLY C    -9                                                      
REMARK 465     VAL C    -8                                                      
REMARK 465     ASP C    -7                                                      
REMARK 465     LEU C    -6                                                      
REMARK 465     GLY C    -5                                                      
REMARK 465     THR C    -4                                                      
REMARK 465     GLU C    -3                                                      
REMARK 465     ASN C    -2                                                      
REMARK 465     PHE C   303                                                      
REMARK 465     HIS C   304                                                      
REMARK 465     GLU C   305                                                      
REMARK 465     MET D   -18                                                      
REMARK 465     HIS D   -17                                                      
REMARK 465     HIS D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     SER D   -11                                                      
REMARK 465     SER D   -10                                                      
REMARK 465     GLY D    -9                                                      
REMARK 465     VAL D    -8                                                      
REMARK 465     ASP D    -7                                                      
REMARK 465     LEU D    -6                                                      
REMARK 465     GLY D    -5                                                      
REMARK 465     THR D    -4                                                      
REMARK 465     GLU D    -3                                                      
REMARK 465     ASN D    -2                                                      
REMARK 465     LEU D    -1                                                      
REMARK 465     GLY D   302                                                      
REMARK 465     PHE D   303                                                      
REMARK 465     HIS D   304                                                      
REMARK 465     GLU D   305                                                      
REMARK 465     MET E   -18                                                      
REMARK 465     HIS E   -17                                                      
REMARK 465     HIS E   -16                                                      
REMARK 465     HIS E   -15                                                      
REMARK 465     HIS E   -14                                                      
REMARK 465     HIS E   -13                                                      
REMARK 465     HIS E   -12                                                      
REMARK 465     SER E   -11                                                      
REMARK 465     SER E   -10                                                      
REMARK 465     GLY E    -9                                                      
REMARK 465     VAL E    -8                                                      
REMARK 465     ASP E    -7                                                      
REMARK 465     LEU E    -6                                                      
REMARK 465     GLY E    -5                                                      
REMARK 465     THR E    -4                                                      
REMARK 465     GLU E    -3                                                      
REMARK 465     ASN E    -2                                                      
REMARK 465     LEU E    -1                                                      
REMARK 465     TYR E     0                                                      
REMARK 465     PHE E     1                                                      
REMARK 465     GLN E     2                                                      
REMARK 465     SER E     3                                                      
REMARK 465     MET E     4                                                      
REMARK 465     THR E   301                                                      
REMARK 465     GLY E   302                                                      
REMARK 465     PHE E   303                                                      
REMARK 465     HIS E   304                                                      
REMARK 465     GLU E   305                                                      
REMARK 465     THR E   306                                                      
REMARK 465     GLY E   365                                                      
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 A 307    OG                                                  
REMARK 470     LEU C  -1    CG   CD1  CD2                                       
REMARK 470     THR D 301    OG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1515     O    HOH A  1771              1.81            
REMARK 500   O    HOH A  1561     O    HOH A  1791              1.97            
REMARK 500   O    HOH A  1679     O    HOH A  1700              1.98            
REMARK 500   OE1  GLU C   110     O    HOH C  1729              1.99            
REMARK 500   O    GLY A    23     O    HOH A  1659              2.04            
REMARK 500   OE2  GLU D    59     O    HOH D  1732              2.06            
REMARK 500   O    HOH A  1671     O    HOH E  1752              2.08            
REMARK 500   ND2  ASN E   126     O    HOH E  1660              2.10            
REMARK 500   OD1  ASN B   126     O    HOH B  1771              2.10            
REMARK 500   O    HOH E  1522     O    HOH E  1667              2.10            
REMARK 500   OE1  GLN E   127     O    HOH E  1583              2.16            
REMARK 500   N    THR B   306     O    HOH B  1717              2.16            
REMARK 500   O    HOH A  1651     O    HOH A  1708              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   ND2  ASN A   362     ND2  ASN A   362     2554     1.92            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 299   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG A 299   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG B 280   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG B 299   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG B 299   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    THR C 142   OG1 -  CB  -  CG2 ANGL. DEV. =  13.8 DEGREES          
REMARK 500    ARG C 262   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG C 262   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ARG C 299   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG C 299   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ASP D 216   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG D 299   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG D 299   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG D 319   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG D 319   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    MET E  77   CG  -  SD  -  CE  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ARG E 299   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG E 299   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG E 327   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG E 327   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  74       65.44   -152.78                                   
REMARK 500    LYS A  91      166.32     77.98                                   
REMARK 500    ALA A 200       -4.65     88.47                                   
REMARK 500    ASN B  74       68.97   -153.62                                   
REMARK 500    LYS B  91      165.94     78.69                                   
REMARK 500    ASP B  92      137.78    -38.27                                   
REMARK 500    MET B 123       -9.99    -59.33                                   
REMARK 500    ARG B 169      -50.44   -132.34                                   
REMARK 500    LYS B 241       78.83   -150.02                                   
REMARK 500    ASN B 246       51.08    -94.76                                   
REMARK 500    ALA B 317       12.82     50.36                                   
REMARK 500    LEU C  68       35.75     71.12                                   
REMARK 500    ASN C  74       65.34   -152.95                                   
REMARK 500    LYS C  91      162.45     74.07                                   
REMARK 500    ARG C 169      -54.97   -121.31                                   
REMARK 500    ALA C 200        0.39     81.40                                   
REMARK 500    LYS C 241       74.01   -153.08                                   
REMARK 500    ASN C 246       48.89    -84.89                                   
REMARK 500    ASN D  74       66.74   -157.05                                   
REMARK 500    LYS D  91      171.64     74.62                                   
REMARK 500    ARG D 169      -56.46   -134.77                                   
REMARK 500    ALA D 200        2.47     80.72                                   
REMARK 500    LYS D 241       72.83   -150.57                                   
REMARK 500    ASN D 246       48.94    -83.41                                   
REMARK 500    ASN E  74       68.66   -152.74                                   
REMARK 500    LYS E  91      160.00     71.58                                   
REMARK 500    ARG E 169      -54.83   -131.25                                   
REMARK 500    ALA E 200       -1.70     80.92                                   
REMARK 500    LYS E 241       74.32   -154.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP A   92     PRO A   93                   31.81                    
REMARK 500 GLY A  207     PRO A  208                  -35.83                    
REMARK 500 SER A  307     ASN A  308                  144.05                    
REMARK 500 ASP B  143     GLY B  144                 -131.03                    
REMARK 500 GLY B  207     PRO B  208                  -39.51                    
REMARK 500 LEU B  300     THR B  301                  139.17                    
REMARK 500 ASP C   92     PRO C   93                   36.29                    
REMARK 500 GLY C  207     PRO C  208                  -37.82                    
REMARK 500 ASP D   92     PRO D   93                   34.14                    
REMARK 500 GLY D  207     PRO D  208                  -37.02                    
REMARK 500 THR D  306     SER D  307                  148.58                    
REMARK 500 ASP E   92     PRO E   93                   33.13                    
REMARK 500 GLY E  207     PRO E  208                  -43.03                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ASP A  92         14.01                                           
REMARK 500    GLY A 207        -13.75                                           
REMARK 500    GLY B 207        -12.83                                           
REMARK 500    ASP C  92         10.12                                           
REMARK 500    GLY C 207        -13.83                                           
REMARK 500    ASP D  92         11.31                                           
REMARK 500    GLY D 207        -13.39                                           
REMARK 500    GLY E 207        -12.85                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR A 358        22.9      L          L   OUTSIDE RANGE           
REMARK 500    LEU C 218        24.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1678        DISTANCE =  5.55 ANGSTROMS                       
REMARK 525    HOH B1668        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH D1620        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH D1670        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH E1585        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH E1653        DISTANCE =  5.75 ANGSTROMS                       
REMARK 525    HOH E1694        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH E1697        DISTANCE =  6.33 ANGSTROMS                       
REMARK 525    HOH E1769        DISTANCE =  6.81 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 134   OE1                                                    
REMARK 620 2 GLU A 338   OE2 142.7                                              
REMARK 620 3 ADP A 501   O3B  94.0  95.3                                        
REMARK 620 4 PO4 A 502   O1  102.8 112.7  92.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 403  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 134   OE1                                                    
REMARK 620 2 GLU A 203   OE2  90.9                                              
REMARK 620 3 ADP A 501   O2A  86.1  88.8                                        
REMARK 620 4 ADP A 501   O1B  97.2 169.0  84.5                                  
REMARK 620 5 HOH A1635   O   178.7  88.3  94.8  83.7                            
REMARK 620 6 PO4 A 502   O2   84.5  98.8 168.1  89.4  94.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 136   OE2                                                    
REMARK 620 2 GLU A 196   OE1  86.3                                              
REMARK 620 3 GLU A 203   OE1 105.8 100.0                                        
REMARK 620 4 PO4 A 502   O4   98.5  81.8 155.8                                  
REMARK 620 5 PO4 A 502   O2  155.0 105.8  93.8  62.8                            
REMARK 620 6 HOH A1686   O    82.2 168.3  84.9  98.2  84.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 404  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 196   OE1                                                    
REMARK 620 2 PO4 A 502   O4   82.5                                              
REMARK 620 3 HOH A1730   O   169.8  87.4                                        
REMARK 620 4 HOH A1729   O   106.6 164.6  83.5                                  
REMARK 620 5 HOH A1731   O    92.0  83.9  88.2  83.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 134   OE1                                                    
REMARK 620 2 GLU B 134   OE2  57.0                                              
REMARK 620 3 GLU B 338   OE2  94.5 150.5                                        
REMARK 620 4 ADP B 501   O2B  87.1  92.5  93.5                                  
REMARK 620 5 PO4 B 502   O2  156.1  99.3 109.4  91.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 403  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 134   OE2                                                    
REMARK 620 2 GLU B 203   OE2  84.3                                              
REMARK 620 3 ADP B 501   O2A  83.6  93.0                                        
REMARK 620 4 ADP B 501   O3B 103.7 169.7  81.6                                  
REMARK 620 5 HOH B1616   O   168.7  84.9  93.9  86.7                            
REMARK 620 6 PO4 B 502   O3   91.7  97.5 168.0  88.8  92.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 136   OE2                                                    
REMARK 620 2 GLU B 196   OE1  86.0                                              
REMARK 620 3 GLU B 203   OE1 110.2  94.7                                        
REMARK 620 4 PO4 B 502   O3  156.6 106.6  88.8                                  
REMARK 620 5 HOH B1747   O    83.3 169.0  86.2  84.4                            
REMARK 620 6 PO4 B 502   O4  100.7  87.8 149.1  61.1  97.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 403  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 134   OE1                                                    
REMARK 620 2 GLU C 203   OE1  97.3                                              
REMARK 620 3 ADP C 501   O2A  79.8  95.2                                        
REMARK 620 4 HOH C1604   O   171.3  83.1  91.5                                  
REMARK 620 5 ADP C 501   O3B  91.5 169.2  80.2  87.3                            
REMARK 620 6 PO4 C 502   O1   86.5  97.1 162.7 102.1  89.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 134   OE1                                                    
REMARK 620 2 GLU C 338   OE2 139.1                                              
REMARK 620 3 ADP C 501   O2B  87.6  97.6                                        
REMARK 620 4 PO4 C 502   O3  104.6 114.3  99.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 136   OE2                                                    
REMARK 620 2 GLU C 196   OE1  81.3                                              
REMARK 620 3 GLU C 203   OE2 108.7  95.7                                        
REMARK 620 4 PO4 C 502   O1  151.5 111.3  95.7                                  
REMARK 620 5 HOH C1745   O    81.8 163.0  91.1  83.4                            
REMARK 620 6 PO4 C 502   O4   98.4  79.4 151.4  61.1 101.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C 404  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 196   OE1                                                    
REMARK 620 2 PO4 C 502   O4   81.6                                              
REMARK 620 3 HOH B1741   O    97.1  95.2                                        
REMARK 620 4 HOH C1718   O    90.2  86.0 172.8                                  
REMARK 620 5 HOH C1719   O   173.8  97.0  89.0  83.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 134   OE1                                                    
REMARK 620 2 GLU D 338   OE2 144.2                                              
REMARK 620 3 ADP D 501   O2B  91.6  93.8                                        
REMARK 620 4 PO4 D 502   O3  102.7 110.7 101.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 403  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 134   OE1                                                    
REMARK 620 2 GLU D 203   OE1  91.9                                              
REMARK 620 3 ADP D 501   O2A  79.3  94.1                                        
REMARK 620 4 HOH D1615   O   173.8  85.1  95.5                                  
REMARK 620 5 ADP D 501   O3B  99.0 166.9  80.8  83.4                            
REMARK 620 6 PO4 D 502   O1   89.5  98.6 163.3  96.3  88.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 136   OE2                                                    
REMARK 620 2 GLU D 196   OE2  89.2                                              
REMARK 620 3 GLU D 203   OE2 107.5  94.1                                        
REMARK 620 4 HOH D1741   O    83.7 172.7  86.5                                  
REMARK 620 5 PO4 D 502   O1  156.1 104.4  91.2  82.8                            
REMARK 620 6 PO4 D 502   O4  102.8  83.6 149.6  99.6  60.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 134   OE1                                                    
REMARK 620 2 GLU E 338   OE1 143.7                                              
REMARK 620 3 ADP E 501   O2B  90.2  96.1                                        
REMARK 620 4 PO4 E 502   O3  100.4 115.2  91.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E 403  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 134   OE1                                                    
REMARK 620 2 GLU E 203   OE2  91.7                                              
REMARK 620 3 ADP E 501   O2A  84.9  94.2                                        
REMARK 620 4 ADP E 501   O3B  98.7 167.3  79.6                                  
REMARK 620 5 HOH E1609   O   174.7  85.3  90.9  83.8                            
REMARK 620 6 PO4 E 502   O1   86.5 100.8 162.9  87.2  98.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 136   OE2                                                    
REMARK 620 2 GLU E 196   OE1  82.7                                              
REMARK 620 3 GLU E 203   OE1 113.9  92.2                                        
REMARK 620 4 PO4 E 502   O1  153.6 109.0  89.8                                  
REMARK 620 5 HOH E1666   O    81.5 163.9  91.4  86.7                            
REMARK 620 6 PO4 E 502   O4   95.8  86.2 149.8  62.6  98.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 404  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B1740   O                                                      
REMARK 620 2 PO4 B 502   O4   93.7                                              
REMARK 620 3 HOH B1738   O    97.4  86.0                                        
REMARK 620 4 HOH B1739   O    96.3 157.9  73.2                                  
REMARK 620 5 HOH B1730   O   176.2  90.1  82.1  79.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D 404  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PO4 D 502   O4                                                     
REMARK 620 2 HOH D1740   O    91.5                                              
REMARK 620 3 HOH D1739   O    91.6 173.3                                        
REMARK 620 4 HOH D1609   O    91.0  99.0  86.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E 404  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PO4 E 502   O4                                                     
REMARK 620 2 HOH E1716   O    93.5                                              
REMARK 620 3 HOH E1717   O    91.7 100.8                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 1404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1502                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1503                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 1504                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 1505                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1506                
DBREF  2OJW A    5   365  UNP    P15104   GLNA_HUMAN       4    364             
DBREF  2OJW B    5   365  UNP    P15104   GLNA_HUMAN       4    364             
DBREF  2OJW C    5   365  UNP    P15104   GLNA_HUMAN       4    364             
DBREF  2OJW D    5   365  UNP    P15104   GLNA_HUMAN       4    364             
DBREF  2OJW E    5   365  UNP    P15104   GLNA_HUMAN       4    364             
SEQADV 2OJW MET A  -18  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS A  -17  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS A  -16  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS A  -15  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS A  -14  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS A  -13  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS A  -12  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW SER A  -11  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW SER A  -10  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW GLY A   -9  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW VAL A   -8  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW ASP A   -7  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW LEU A   -6  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW GLY A   -5  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW THR A   -4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW GLU A   -3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW ASN A   -2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW LEU A   -1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW TYR A    0  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW PHE A    1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW GLN A    2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW SER A    3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW MET A    4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW MET B  -18  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS B  -17  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS B  -16  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS B  -15  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS B  -14  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS B  -13  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS B  -12  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW SER B  -11  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW SER B  -10  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW GLY B   -9  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW VAL B   -8  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW ASP B   -7  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW LEU B   -6  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW GLY B   -5  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW THR B   -4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW GLU B   -3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW ASN B   -2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW LEU B   -1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW TYR B    0  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW PHE B    1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW GLN B    2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW SER B    3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW MET B    4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW MET C  -18  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS C  -17  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS C  -16  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS C  -15  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS C  -14  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS C  -13  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS C  -12  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW SER C  -11  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW SER C  -10  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW GLY C   -9  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW VAL C   -8  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW ASP C   -7  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW LEU C   -6  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW GLY C   -5  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW THR C   -4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW GLU C   -3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW ASN C   -2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW LEU C   -1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW TYR C    0  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW PHE C    1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW GLN C    2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW SER C    3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW MET C    4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW MET D  -18  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS D  -17  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS D  -16  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS D  -15  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS D  -14  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS D  -13  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS D  -12  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW SER D  -11  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW SER D  -10  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW GLY D   -9  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW VAL D   -8  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW ASP D   -7  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW LEU D   -6  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW GLY D   -5  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW THR D   -4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW GLU D   -3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW ASN D   -2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW LEU D   -1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW TYR D    0  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW PHE D    1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW GLN D    2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW SER D    3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW MET D    4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW MET E  -18  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS E  -17  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS E  -16  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS E  -15  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS E  -14  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS E  -13  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW HIS E  -12  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW SER E  -11  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW SER E  -10  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW GLY E   -9  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW VAL E   -8  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW ASP E   -7  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW LEU E   -6  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW GLY E   -5  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW THR E   -4  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW GLU E   -3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW ASN E   -2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW LEU E   -1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW TYR E    0  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW PHE E    1  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW GLN E    2  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW SER E    3  UNP  P15104              EXPRESSION TAG                 
SEQADV 2OJW MET E    4  UNP  P15104              EXPRESSION TAG                 
SEQRES   1 A  384  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  384  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER SER          
SEQRES   3 A  384  HIS LEU ASN LYS GLY ILE LYS GLN VAL TYR MET SER LEU          
SEQRES   4 A  384  PRO GLN GLY GLU LYS VAL GLN ALA MET TYR ILE TRP ILE          
SEQRES   5 A  384  ASP GLY THR GLY GLU GLY LEU ARG CYS LYS THR ARG THR          
SEQRES   6 A  384  LEU ASP SER GLU PRO LYS CYS VAL GLU GLU LEU PRO GLU          
SEQRES   7 A  384  TRP ASN PHE ASP GLY SER SER THR LEU GLN SER GLU GLY          
SEQRES   8 A  384  SER ASN SER ASP MET TYR LEU VAL PRO ALA ALA MET PHE          
SEQRES   9 A  384  ARG ASP PRO PHE ARG LYS ASP PRO ASN LYS LEU VAL LEU          
SEQRES  10 A  384  CYS GLU VAL PHE LYS TYR ASN ARG ARG PRO ALA GLU THR          
SEQRES  11 A  384  ASN LEU ARG HIS THR CYS LYS ARG ILE MET ASP MET VAL          
SEQRES  12 A  384  SER ASN GLN HIS PRO TRP PHE GLY MET GLU GLN GLU TYR          
SEQRES  13 A  384  THR LEU MET GLY THR ASP GLY HIS PRO PHE GLY TRP PRO          
SEQRES  14 A  384  SER ASN GLY PHE PRO GLY PRO GLN GLY PRO TYR TYR CYS          
SEQRES  15 A  384  GLY VAL GLY ALA ASP ARG ALA TYR GLY ARG ASP ILE VAL          
SEQRES  16 A  384  GLU ALA HIS TYR ARG ALA CYS LEU TYR ALA GLY VAL LYS          
SEQRES  17 A  384  ILE ALA GLY THR ASN ALA GLU VAL MET PRO ALA GLN TRP          
SEQRES  18 A  384  GLU PHE GLN ILE GLY PRO CYS GLU GLY ILE SER MET GLY          
SEQRES  19 A  384  ASP HIS LEU TRP VAL ALA ARG PHE ILE LEU HIS ARG VAL          
SEQRES  20 A  384  CYS GLU ASP PHE GLY VAL ILE ALA THR PHE ASP PRO LYS          
SEQRES  21 A  384  PRO ILE PRO GLY ASN TRP ASN GLY ALA GLY CYS HIS THR          
SEQRES  22 A  384  ASN PHE SER THR LYS ALA MET ARG GLU GLU ASN GLY LEU          
SEQRES  23 A  384  LYS TYR ILE GLU GLU ALA ILE GLU LYS LEU SER LYS ARG          
SEQRES  24 A  384  HIS GLN TYR HIS ILE ARG ALA TYR ASP PRO LYS GLY GLY          
SEQRES  25 A  384  LEU ASP ASN ALA ARG ARG LEU THR GLY PHE HIS GLU THR          
SEQRES  26 A  384  SER ASN ILE ASN ASP PHE SER ALA GLY VAL ALA ASN ARG          
SEQRES  27 A  384  SER ALA SER ILE ARG ILE PRO ARG THR VAL GLY GLN GLU          
SEQRES  28 A  384  LYS LYS GLY TYR PHE GLU ASP ARG ARG PRO SER ALA ASN          
SEQRES  29 A  384  CYS ASP PRO PHE SER VAL THR GLU ALA LEU ILE ARG THR          
SEQRES  30 A  384  CYS LEU LEU ASN GLU THR GLY                                  
SEQRES   1 B  384  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  384  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER SER          
SEQRES   3 B  384  HIS LEU ASN LYS GLY ILE LYS GLN VAL TYR MET SER LEU          
SEQRES   4 B  384  PRO GLN GLY GLU LYS VAL GLN ALA MET TYR ILE TRP ILE          
SEQRES   5 B  384  ASP GLY THR GLY GLU GLY LEU ARG CYS LYS THR ARG THR          
SEQRES   6 B  384  LEU ASP SER GLU PRO LYS CYS VAL GLU GLU LEU PRO GLU          
SEQRES   7 B  384  TRP ASN PHE ASP GLY SER SER THR LEU GLN SER GLU GLY          
SEQRES   8 B  384  SER ASN SER ASP MET TYR LEU VAL PRO ALA ALA MET PHE          
SEQRES   9 B  384  ARG ASP PRO PHE ARG LYS ASP PRO ASN LYS LEU VAL LEU          
SEQRES  10 B  384  CYS GLU VAL PHE LYS TYR ASN ARG ARG PRO ALA GLU THR          
SEQRES  11 B  384  ASN LEU ARG HIS THR CYS LYS ARG ILE MET ASP MET VAL          
SEQRES  12 B  384  SER ASN GLN HIS PRO TRP PHE GLY MET GLU GLN GLU TYR          
SEQRES  13 B  384  THR LEU MET GLY THR ASP GLY HIS PRO PHE GLY TRP PRO          
SEQRES  14 B  384  SER ASN GLY PHE PRO GLY PRO GLN GLY PRO TYR TYR CYS          
SEQRES  15 B  384  GLY VAL GLY ALA ASP ARG ALA TYR GLY ARG ASP ILE VAL          
SEQRES  16 B  384  GLU ALA HIS TYR ARG ALA CYS LEU TYR ALA GLY VAL LYS          
SEQRES  17 B  384  ILE ALA GLY THR ASN ALA GLU VAL MET PRO ALA GLN TRP          
SEQRES  18 B  384  GLU PHE GLN ILE GLY PRO CYS GLU GLY ILE SER MET GLY          
SEQRES  19 B  384  ASP HIS LEU TRP VAL ALA ARG PHE ILE LEU HIS ARG VAL          
SEQRES  20 B  384  CYS GLU ASP PHE GLY VAL ILE ALA THR PHE ASP PRO LYS          
SEQRES  21 B  384  PRO ILE PRO GLY ASN TRP ASN GLY ALA GLY CYS HIS THR          
SEQRES  22 B  384  ASN PHE SER THR LYS ALA MET ARG GLU GLU ASN GLY LEU          
SEQRES  23 B  384  LYS TYR ILE GLU GLU ALA ILE GLU LYS LEU SER LYS ARG          
SEQRES  24 B  384  HIS GLN TYR HIS ILE ARG ALA TYR ASP PRO LYS GLY GLY          
SEQRES  25 B  384  LEU ASP ASN ALA ARG ARG LEU THR GLY PHE HIS GLU THR          
SEQRES  26 B  384  SER ASN ILE ASN ASP PHE SER ALA GLY VAL ALA ASN ARG          
SEQRES  27 B  384  SER ALA SER ILE ARG ILE PRO ARG THR VAL GLY GLN GLU          
SEQRES  28 B  384  LYS LYS GLY TYR PHE GLU ASP ARG ARG PRO SER ALA ASN          
SEQRES  29 B  384  CYS ASP PRO PHE SER VAL THR GLU ALA LEU ILE ARG THR          
SEQRES  30 B  384  CYS LEU LEU ASN GLU THR GLY                                  
SEQRES   1 C  384  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 C  384  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER SER          
SEQRES   3 C  384  HIS LEU ASN LYS GLY ILE LYS GLN VAL TYR MET SER LEU          
SEQRES   4 C  384  PRO GLN GLY GLU LYS VAL GLN ALA MET TYR ILE TRP ILE          
SEQRES   5 C  384  ASP GLY THR GLY GLU GLY LEU ARG CYS LYS THR ARG THR          
SEQRES   6 C  384  LEU ASP SER GLU PRO LYS CYS VAL GLU GLU LEU PRO GLU          
SEQRES   7 C  384  TRP ASN PHE ASP GLY SER SER THR LEU GLN SER GLU GLY          
SEQRES   8 C  384  SER ASN SER ASP MET TYR LEU VAL PRO ALA ALA MET PHE          
SEQRES   9 C  384  ARG ASP PRO PHE ARG LYS ASP PRO ASN LYS LEU VAL LEU          
SEQRES  10 C  384  CYS GLU VAL PHE LYS TYR ASN ARG ARG PRO ALA GLU THR          
SEQRES  11 C  384  ASN LEU ARG HIS THR CYS LYS ARG ILE MET ASP MET VAL          
SEQRES  12 C  384  SER ASN GLN HIS PRO TRP PHE GLY MET GLU GLN GLU TYR          
SEQRES  13 C  384  THR LEU MET GLY THR ASP GLY HIS PRO PHE GLY TRP PRO          
SEQRES  14 C  384  SER ASN GLY PHE PRO GLY PRO GLN GLY PRO TYR TYR CYS          
SEQRES  15 C  384  GLY VAL GLY ALA ASP ARG ALA TYR GLY ARG ASP ILE VAL          
SEQRES  16 C  384  GLU ALA HIS TYR ARG ALA CYS LEU TYR ALA GLY VAL LYS          
SEQRES  17 C  384  ILE ALA GLY THR ASN ALA GLU VAL MET PRO ALA GLN TRP          
SEQRES  18 C  384  GLU PHE GLN ILE GLY PRO CYS GLU GLY ILE SER MET GLY          
SEQRES  19 C  384  ASP HIS LEU TRP VAL ALA ARG PHE ILE LEU HIS ARG VAL          
SEQRES  20 C  384  CYS GLU ASP PHE GLY VAL ILE ALA THR PHE ASP PRO LYS          
SEQRES  21 C  384  PRO ILE PRO GLY ASN TRP ASN GLY ALA GLY CYS HIS THR          
SEQRES  22 C  384  ASN PHE SER THR LYS ALA MET ARG GLU GLU ASN GLY LEU          
SEQRES  23 C  384  LYS TYR ILE GLU GLU ALA ILE GLU LYS LEU SER LYS ARG          
SEQRES  24 C  384  HIS GLN TYR HIS ILE ARG ALA TYR ASP PRO LYS GLY GLY          
SEQRES  25 C  384  LEU ASP ASN ALA ARG ARG LEU THR GLY PHE HIS GLU THR          
SEQRES  26 C  384  SER ASN ILE ASN ASP PHE SER ALA GLY VAL ALA ASN ARG          
SEQRES  27 C  384  SER ALA SER ILE ARG ILE PRO ARG THR VAL GLY GLN GLU          
SEQRES  28 C  384  LYS LYS GLY TYR PHE GLU ASP ARG ARG PRO SER ALA ASN          
SEQRES  29 C  384  CYS ASP PRO PHE SER VAL THR GLU ALA LEU ILE ARG THR          
SEQRES  30 C  384  CYS LEU LEU ASN GLU THR GLY                                  
SEQRES   1 D  384  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 D  384  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER SER          
SEQRES   3 D  384  HIS LEU ASN LYS GLY ILE LYS GLN VAL TYR MET SER LEU          
SEQRES   4 D  384  PRO GLN GLY GLU LYS VAL GLN ALA MET TYR ILE TRP ILE          
SEQRES   5 D  384  ASP GLY THR GLY GLU GLY LEU ARG CYS LYS THR ARG THR          
SEQRES   6 D  384  LEU ASP SER GLU PRO LYS CYS VAL GLU GLU LEU PRO GLU          
SEQRES   7 D  384  TRP ASN PHE ASP GLY SER SER THR LEU GLN SER GLU GLY          
SEQRES   8 D  384  SER ASN SER ASP MET TYR LEU VAL PRO ALA ALA MET PHE          
SEQRES   9 D  384  ARG ASP PRO PHE ARG LYS ASP PRO ASN LYS LEU VAL LEU          
SEQRES  10 D  384  CYS GLU VAL PHE LYS TYR ASN ARG ARG PRO ALA GLU THR          
SEQRES  11 D  384  ASN LEU ARG HIS THR CYS LYS ARG ILE MET ASP MET VAL          
SEQRES  12 D  384  SER ASN GLN HIS PRO TRP PHE GLY MET GLU GLN GLU TYR          
SEQRES  13 D  384  THR LEU MET GLY THR ASP GLY HIS PRO PHE GLY TRP PRO          
SEQRES  14 D  384  SER ASN GLY PHE PRO GLY PRO GLN GLY PRO TYR TYR CYS          
SEQRES  15 D  384  GLY VAL GLY ALA ASP ARG ALA TYR GLY ARG ASP ILE VAL          
SEQRES  16 D  384  GLU ALA HIS TYR ARG ALA CYS LEU TYR ALA GLY VAL LYS          
SEQRES  17 D  384  ILE ALA GLY THR ASN ALA GLU VAL MET PRO ALA GLN TRP          
SEQRES  18 D  384  GLU PHE GLN ILE GLY PRO CYS GLU GLY ILE SER MET GLY          
SEQRES  19 D  384  ASP HIS LEU TRP VAL ALA ARG PHE ILE LEU HIS ARG VAL          
SEQRES  20 D  384  CYS GLU ASP PHE GLY VAL ILE ALA THR PHE ASP PRO LYS          
SEQRES  21 D  384  PRO ILE PRO GLY ASN TRP ASN GLY ALA GLY CYS HIS THR          
SEQRES  22 D  384  ASN PHE SER THR LYS ALA MET ARG GLU GLU ASN GLY LEU          
SEQRES  23 D  384  LYS TYR ILE GLU GLU ALA ILE GLU LYS LEU SER LYS ARG          
SEQRES  24 D  384  HIS GLN TYR HIS ILE ARG ALA TYR ASP PRO LYS GLY GLY          
SEQRES  25 D  384  LEU ASP ASN ALA ARG ARG LEU THR GLY PHE HIS GLU THR          
SEQRES  26 D  384  SER ASN ILE ASN ASP PHE SER ALA GLY VAL ALA ASN ARG          
SEQRES  27 D  384  SER ALA SER ILE ARG ILE PRO ARG THR VAL GLY GLN GLU          
SEQRES  28 D  384  LYS LYS GLY TYR PHE GLU ASP ARG ARG PRO SER ALA ASN          
SEQRES  29 D  384  CYS ASP PRO PHE SER VAL THR GLU ALA LEU ILE ARG THR          
SEQRES  30 D  384  CYS LEU LEU ASN GLU THR GLY                                  
SEQRES   1 E  384  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 E  384  GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER SER          
SEQRES   3 E  384  HIS LEU ASN LYS GLY ILE LYS GLN VAL TYR MET SER LEU          
SEQRES   4 E  384  PRO GLN GLY GLU LYS VAL GLN ALA MET TYR ILE TRP ILE          
SEQRES   5 E  384  ASP GLY THR GLY GLU GLY LEU ARG CYS LYS THR ARG THR          
SEQRES   6 E  384  LEU ASP SER GLU PRO LYS CYS VAL GLU GLU LEU PRO GLU          
SEQRES   7 E  384  TRP ASN PHE ASP GLY SER SER THR LEU GLN SER GLU GLY          
SEQRES   8 E  384  SER ASN SER ASP MET TYR LEU VAL PRO ALA ALA MET PHE          
SEQRES   9 E  384  ARG ASP PRO PHE ARG LYS ASP PRO ASN LYS LEU VAL LEU          
SEQRES  10 E  384  CYS GLU VAL PHE LYS TYR ASN ARG ARG PRO ALA GLU THR          
SEQRES  11 E  384  ASN LEU ARG HIS THR CYS LYS ARG ILE MET ASP MET VAL          
SEQRES  12 E  384  SER ASN GLN HIS PRO TRP PHE GLY MET GLU GLN GLU TYR          
SEQRES  13 E  384  THR LEU MET GLY THR ASP GLY HIS PRO PHE GLY TRP PRO          
SEQRES  14 E  384  SER ASN GLY PHE PRO GLY PRO GLN GLY PRO TYR TYR CYS          
SEQRES  15 E  384  GLY VAL GLY ALA ASP ARG ALA TYR GLY ARG ASP ILE VAL          
SEQRES  16 E  384  GLU ALA HIS TYR ARG ALA CYS LEU TYR ALA GLY VAL LYS          
SEQRES  17 E  384  ILE ALA GLY THR ASN ALA GLU VAL MET PRO ALA GLN TRP          
SEQRES  18 E  384  GLU PHE GLN ILE GLY PRO CYS GLU GLY ILE SER MET GLY          
SEQRES  19 E  384  ASP HIS LEU TRP VAL ALA ARG PHE ILE LEU HIS ARG VAL          
SEQRES  20 E  384  CYS GLU ASP PHE GLY VAL ILE ALA THR PHE ASP PRO LYS          
SEQRES  21 E  384  PRO ILE PRO GLY ASN TRP ASN GLY ALA GLY CYS HIS THR          
SEQRES  22 E  384  ASN PHE SER THR LYS ALA MET ARG GLU GLU ASN GLY LEU          
SEQRES  23 E  384  LYS TYR ILE GLU GLU ALA ILE GLU LYS LEU SER LYS ARG          
SEQRES  24 E  384  HIS GLN TYR HIS ILE ARG ALA TYR ASP PRO LYS GLY GLY          
SEQRES  25 E  384  LEU ASP ASN ALA ARG ARG LEU THR GLY PHE HIS GLU THR          
SEQRES  26 E  384  SER ASN ILE ASN ASP PHE SER ALA GLY VAL ALA ASN ARG          
SEQRES  27 E  384  SER ALA SER ILE ARG ILE PRO ARG THR VAL GLY GLN GLU          
SEQRES  28 E  384  LYS LYS GLY TYR PHE GLU ASP ARG ARG PRO SER ALA ASN          
SEQRES  29 E  384  CYS ASP PRO PHE SER VAL THR GLU ALA LEU ILE ARG THR          
SEQRES  30 E  384  CYS LEU LEU ASN GLU THR GLY                                  
HET     MN  A 401       1                                                       
HET     MN  A 402       1                                                       
HET     MN  A 403       1                                                       
HET     MN  A 404       1                                                       
HET    PO4  A 502       5                                                       
HET     MN  B 401       1                                                       
HET     MN  B 402       1                                                       
HET     MN  B 403       1                                                       
HET     MN  B 404       1                                                       
HET    PO4  B 502       5                                                       
HET     MN  C 401       1                                                       
HET     MN  C 402       1                                                       
HET     MN  C 403       1                                                       
HET     MN  C 404       1                                                       
HET    PO4  C 502       5                                                       
HET     MN  D 401       1                                                       
HET     MN  D 402       1                                                       
HET     MN  D 403       1                                                       
HET     MN  D 404       1                                                       
HET    PO4  D 502       5                                                       
HET     MN  E 401       1                                                       
HET     MN  E 402       1                                                       
HET     MN  E 403       1                                                       
HET     MN  E 404       1                                                       
HET    PO4  E 502       5                                                       
HET     CL  B1401       1                                                       
HET     CL  C1402       1                                                       
HET     CL  A1403       1                                                       
HET     CL  D1404       1                                                       
HET     CL  A1405       1                                                       
HET    ADP  A 501      27                                                       
HET    ADP  B 501      27                                                       
HET    ADP  C 501      27                                                       
HET    ADP  D 501      27                                                       
HET    ADP  E 501      27                                                       
HET    GOL  A1501       6                                                       
HET    GOL  B1502       6                                                       
HET    GOL  C1503       6                                                       
HET    GOL  D1504       6                                                       
HET    GOL  E1505       6                                                       
HET    GOL  C1506       6                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   6   MN    20(MN 2+)                                                    
FORMUL  10  PO4    5(O4 P 3-)                                                   
FORMUL  31   CL    5(CL 1-)                                                     
FORMUL  36  ADP    5(C10 H15 N5 O10 P2)                                         
FORMUL  41  GOL    6(C3 H8 O3)                                                  
FORMUL  47  HOH   *1390(H2 O)                                                   
HELIX    1   1 MET A    4  LEU A    9  5                                   6    
HELIX    2   2 ASN A   10  SER A   19  1                                  10    
HELIX    3   3 CYS A   53  LEU A   57  5                                   5    
HELIX    4   4 GLU A   71  ASN A   74  5                                   4    
HELIX    5   5 LEU A  113  VAL A  124  1                                  12    
HELIX    6   6 SER A  125  HIS A  128  5                                   4    
HELIX    7   7 GLY A  172  GLY A  187  1                                  16    
HELIX    8   8 ILE A  212  GLY A  233  1                                  22    
HELIX    9   9 THR A  258  GLU A  263  1                                   6    
HELIX   10  10 GLY A  266  LYS A  279  1                                  14    
HELIX   11  11 ARG A  280  TYR A  288  1                                   9    
HELIX   12  12 ASP A  295  ARG A  299  5                                   5    
HELIX   13  13 PRO A  326  LYS A  333  1                                   8    
HELIX   14  14 ASP A  347  LEU A  360  1                                  14    
HELIX   15  15 MET B    4  LEU B    9  5                                   6    
HELIX   16  16 ASN B   10  SER B   19  1                                  10    
HELIX   17  17 CYS B   53  LEU B   57  5                                   5    
HELIX   18  18 GLU B   71  ASN B   74  5                                   4    
HELIX   19  19 LEU B  113  MET B  123  1                                  11    
HELIX   20  20 VAL B  124  HIS B  128  5                                   5    
HELIX   21  21 GLY B  172  GLY B  187  1                                  16    
HELIX   22  22 ILE B  212  GLY B  233  1                                  22    
HELIX   23  23 THR B  258  GLU B  263  1                                   6    
HELIX   24  24 GLY B  266  LYS B  279  1                                  14    
HELIX   25  25 ARG B  280  TYR B  288  1                                   9    
HELIX   26  26 ASP B  295  ARG B  299  5                                   5    
HELIX   27  27 PRO B  326  LYS B  333  1                                   8    
HELIX   28  28 ASP B  347  LEU B  360  1                                  14    
HELIX   29  29 ALA C    5  LEU C    9  5                                   5    
HELIX   30  30 ASN C   10  SER C   19  1                                  10    
HELIX   31  31 CYS C   53  LEU C   57  5                                   5    
HELIX   32  32 GLU C   71  ASN C   74  5                                   4    
HELIX   33  33 LEU C  113  VAL C  124  1                                  12    
HELIX   34  34 SER C  125  HIS C  128  5                                   4    
HELIX   35  35 GLY C  172  GLY C  187  1                                  16    
HELIX   36  36 ILE C  212  GLY C  233  1                                  22    
HELIX   37  37 THR C  258  GLU C  263  1                                   6    
HELIX   38  38 GLY C  266  LYS C  279  1                                  14    
HELIX   39  39 ARG C  280  TYR C  288  1                                   9    
HELIX   40  40 GLY C  293  ARG C  298  1                                   6    
HELIX   41  41 PRO C  326  LYS C  333  1                                   8    
HELIX   42  42 ASP C  347  LEU C  360  1                                  14    
HELIX   43  43 ALA D    5  LEU D    9  5                                   5    
HELIX   44  44 ASN D   10  SER D   19  1                                  10    
HELIX   45  45 CYS D   53  LEU D   57  5                                   5    
HELIX   46  46 GLU D   71  ASN D   74  5                                   4    
HELIX   47  47 LEU D  113  VAL D  124  1                                  12    
HELIX   48  48 SER D  125  HIS D  128  5                                   4    
HELIX   49  49 GLY D  172  GLY D  187  1                                  16    
HELIX   50  50 ILE D  212  GLY D  233  1                                  22    
HELIX   51  51 THR D  258  GLU D  263  1                                   6    
HELIX   52  52 GLY D  266  LYS D  279  1                                  14    
HELIX   53  53 ARG D  280  TYR D  288  1                                   9    
HELIX   54  54 ASP D  295  ARG D  299  5                                   5    
HELIX   55  55 PRO D  326  LYS D  333  1                                   8    
HELIX   56  56 ASP D  347  LEU D  360  1                                  14    
HELIX   57  57 ALA E    5  LEU E    9  5                                   5    
HELIX   58  58 ASN E   10  SER E   19  1                                  10    
HELIX   59  59 CYS E   53  LEU E   57  5                                   5    
HELIX   60  60 GLU E   71  ASN E   74  5                                   4    
HELIX   61  61 LEU E  113  MET E  123  1                                  11    
HELIX   62  62 VAL E  124  HIS E  128  5                                   5    
HELIX   63  63 GLY E  172  GLY E  187  1                                  16    
HELIX   64  64 ILE E  212  GLY E  233  1                                  22    
HELIX   65  65 THR E  258  GLU E  263  1                                   6    
HELIX   66  66 GLY E  266  LYS E  279  1                                  14    
HELIX   67  67 ARG E  280  TYR E  288  1                                   9    
HELIX   68  68 ASP E  295  ARG E  299  5                                   5    
HELIX   69  69 PRO E  326  LYS E  333  1                                   8    
HELIX   70  70 ASP E  347  LEU E  360  1                                  14    
SHEET    1   A 9 TRP A  60  ASP A  63  0                                        
SHEET    2   A 9 ASP A  76  ARG A  86 -1  O  LEU A  79   N  TRP A  60           
SHEET    3   A 9 LYS A  95  PHE A 102 -1  O  GLU A 100   N  VAL A  80           
SHEET    4   A 9 VAL A  26  ILE A  33  1  N  ILE A  31   O  VAL A  97           
SHEET    5   A 9 LEU A  40  LEU A  47 -1  O  LEU A  47   N  VAL A  26           
SHEET    6   A 9 ILE B 190  ALA B 195 -1  O  ALA B 191   N  THR A  46           
SHEET    7   A 9 GLN B 201  GLU B 210 -1  O  GLN B 205   N  ALA B 191           
SHEET    8   A 9 TRP B 130  MET B 140 -1  N  PHE B 131   O  CYS B 209           
SHEET    9   A 9 ILE B 235  THR B 237 -1  O  ILE B 235   N  MET B 140           
SHEET    1   B12 TRP A  60  ASP A  63  0                                        
SHEET    2   B12 ASP A  76  ARG A  86 -1  O  LEU A  79   N  TRP A  60           
SHEET    3   B12 LYS A  95  PHE A 102 -1  O  GLU A 100   N  VAL A  80           
SHEET    4   B12 VAL A  26  ILE A  33  1  N  ILE A  31   O  VAL A  97           
SHEET    5   B12 LEU A  40  LEU A  47 -1  O  LEU A  47   N  VAL A  26           
SHEET    6   B12 ILE B 190  ALA B 195 -1  O  ALA B 191   N  THR A  46           
SHEET    7   B12 GLN B 201  GLU B 210 -1  O  GLN B 205   N  ALA B 191           
SHEET    8   B12 TRP B 130  MET B 140 -1  N  PHE B 131   O  CYS B 209           
SHEET    9   B12 CYS B 252  SER B 257 -1  O  ASN B 255   N  GLY B 132           
SHEET   10   B12 PHE B 337  ASP B 339 -1  O  ASP B 339   N  THR B 254           
SHEET   11   B12 ILE B 323  ILE B 325 -1  N  ARG B 324   O  GLU B 338           
SHEET   12   B12 ALA B 314  VAL B 316  1  N  GLY B 315   O  ILE B 323           
SHEET    1   C 6 ILE A 235  THR A 237  0                                        
SHEET    2   C 6 TRP A 130  MET A 140 -1  N  MET A 140   O  ILE A 235           
SHEET    3   C 6 CYS A 252  SER A 257 -1  O  ASN A 255   N  GLY A 132           
SHEET    4   C 6 PHE A 337  ASP A 339 -1  O  ASP A 339   N  THR A 254           
SHEET    5   C 6 ILE A 323  ILE A 325 -1  N  ARG A 324   O  GLU A 338           
SHEET    6   C 6 ALA A 314  VAL A 316  1  N  GLY A 315   O  ILE A 323           
SHEET    1   D 9 ILE A 235  THR A 237  0                                        
SHEET    2   D 9 TRP A 130  MET A 140 -1  N  MET A 140   O  ILE A 235           
SHEET    3   D 9 GLN A 201  GLU A 210 -1  O  CYS A 209   N  PHE A 131           
SHEET    4   D 9 ILE A 190  ALA A 195 -1  N  ALA A 191   O  GLN A 205           
SHEET    5   D 9 LEU E  40  LEU E  47 -1  O  THR E  44   N  THR A 193           
SHEET    6   D 9 VAL E  26  ILE E  33 -1  N  VAL E  26   O  LEU E  47           
SHEET    7   D 9 LYS E  95  PHE E 102  1  O  VAL E  97   N  MET E  29           
SHEET    8   D 9 ASP E  76  ARG E  86 -1  N  ALA E  82   O  LEU E  98           
SHEET    9   D 9 TRP E  60  ASP E  63 -1  N  TRP E  60   O  LEU E  79           
SHEET    1   E 9 TRP B  60  ASP B  63  0                                        
SHEET    2   E 9 ASP B  76  ARG B  86 -1  O  LEU B  79   N  TRP B  60           
SHEET    3   E 9 LYS B  95  PHE B 102 -1  O  LEU B  98   N  ALA B  82           
SHEET    4   E 9 VAL B  26  ILE B  33  1  N  MET B  29   O  LYS B  95           
SHEET    5   E 9 LEU B  40  LEU B  47 -1  O  LEU B  47   N  VAL B  26           
SHEET    6   E 9 ILE C 190  ALA C 195 -1  O  THR C 193   N  THR B  44           
SHEET    7   E 9 GLN C 201  GLU C 210 -1  O  GLN C 205   N  GLY C 192           
SHEET    8   E 9 TRP C 130  MET C 140 -1  N  PHE C 131   O  CYS C 209           
SHEET    9   E 9 ILE C 235  THR C 237 -1  O  ILE C 235   N  MET C 140           
SHEET    1   F12 TRP B  60  ASP B  63  0                                        
SHEET    2   F12 ASP B  76  ARG B  86 -1  O  LEU B  79   N  TRP B  60           
SHEET    3   F12 LYS B  95  PHE B 102 -1  O  LEU B  98   N  ALA B  82           
SHEET    4   F12 VAL B  26  ILE B  33  1  N  MET B  29   O  LYS B  95           
SHEET    5   F12 LEU B  40  LEU B  47 -1  O  LEU B  47   N  VAL B  26           
SHEET    6   F12 ILE C 190  ALA C 195 -1  O  THR C 193   N  THR B  44           
SHEET    7   F12 GLN C 201  GLU C 210 -1  O  GLN C 205   N  GLY C 192           
SHEET    8   F12 TRP C 130  MET C 140 -1  N  PHE C 131   O  CYS C 209           
SHEET    9   F12 CYS C 252  SER C 257 -1  O  ASN C 255   N  GLY C 132           
SHEET   10   F12 PHE C 337  ASP C 339 -1  O  ASP C 339   N  THR C 254           
SHEET   11   F12 ILE C 323  ILE C 325 -1  N  ARG C 324   O  GLU C 338           
SHEET   12   F12 ALA C 314  VAL C 316  1  N  GLY C 315   O  ILE C 325           
SHEET    1   G 9 TRP C  60  ASP C  63  0                                        
SHEET    2   G 9 ASP C  76  ARG C  86 -1  O  LEU C  79   N  TRP C  60           
SHEET    3   G 9 LYS C  95  PHE C 102 -1  O  LEU C  98   N  ALA C  82           
SHEET    4   G 9 VAL C  26  ILE C  33  1  N  ILE C  31   O  VAL C  97           
SHEET    5   G 9 LEU C  40  LEU C  47 -1  O  LEU C  47   N  VAL C  26           
SHEET    6   G 9 ILE D 190  ALA D 195 -1  O  ALA D 191   N  THR C  46           
SHEET    7   G 9 GLN D 201  GLU D 210 -1  O  GLN D 205   N  ALA D 191           
SHEET    8   G 9 TRP D 130  MET D 140 -1  N  MET D 133   O  ILE D 206           
SHEET    9   G 9 ILE D 235  THR D 237 -1  O  ILE D 235   N  MET D 140           
SHEET    1   H12 TRP C  60  ASP C  63  0                                        
SHEET    2   H12 ASP C  76  ARG C  86 -1  O  LEU C  79   N  TRP C  60           
SHEET    3   H12 LYS C  95  PHE C 102 -1  O  LEU C  98   N  ALA C  82           
SHEET    4   H12 VAL C  26  ILE C  33  1  N  ILE C  31   O  VAL C  97           
SHEET    5   H12 LEU C  40  LEU C  47 -1  O  LEU C  47   N  VAL C  26           
SHEET    6   H12 ILE D 190  ALA D 195 -1  O  ALA D 191   N  THR C  46           
SHEET    7   H12 GLN D 201  GLU D 210 -1  O  GLN D 205   N  ALA D 191           
SHEET    8   H12 TRP D 130  MET D 140 -1  N  MET D 133   O  ILE D 206           
SHEET    9   H12 CYS D 252  SER D 257 -1  O  SER D 257   N  TRP D 130           
SHEET   10   H12 PHE D 337  ASP D 339 -1  O  ASP D 339   N  THR D 254           
SHEET   11   H12 ILE D 323  ILE D 325 -1  N  ARG D 324   O  GLU D 338           
SHEET   12   H12 ALA D 314  VAL D 316  1  N  GLY D 315   O  ILE D 323           
SHEET    1   I 9 TRP D  60  ASP D  63  0                                        
SHEET    2   I 9 ASP D  76  ARG D  86 -1  O  LEU D  79   N  TRP D  60           
SHEET    3   I 9 LYS D  95  PHE D 102 -1  O  LEU D  98   N  ALA D  83           
SHEET    4   I 9 VAL D  26  ILE D  33  1  N  ILE D  31   O  VAL D  97           
SHEET    5   I 9 LEU D  40  LEU D  47 -1  O  LEU D  47   N  VAL D  26           
SHEET    6   I 9 ILE E 190  ALA E 195 -1  O  ALA E 191   N  THR D  46           
SHEET    7   I 9 GLN E 201  GLU E 210 -1  O  GLN E 205   N  ALA E 191           
SHEET    8   I 9 TRP E 130  MET E 140 -1  N  MET E 133   O  ILE E 206           
SHEET    9   I 9 ILE E 235  THR E 237 -1  O  THR E 237   N  THR E 138           
SHEET    1   J12 TRP D  60  ASP D  63  0                                        
SHEET    2   J12 ASP D  76  ARG D  86 -1  O  LEU D  79   N  TRP D  60           
SHEET    3   J12 LYS D  95  PHE D 102 -1  O  LEU D  98   N  ALA D  83           
SHEET    4   J12 VAL D  26  ILE D  33  1  N  ILE D  31   O  VAL D  97           
SHEET    5   J12 LEU D  40  LEU D  47 -1  O  LEU D  47   N  VAL D  26           
SHEET    6   J12 ILE E 190  ALA E 195 -1  O  ALA E 191   N  THR D  46           
SHEET    7   J12 GLN E 201  GLU E 210 -1  O  GLN E 205   N  ALA E 191           
SHEET    8   J12 TRP E 130  MET E 140 -1  N  MET E 133   O  ILE E 206           
SHEET    9   J12 CYS E 252  SER E 257 -1  O  ASN E 255   N  GLY E 132           
SHEET   10   J12 PHE E 337  ASP E 339 -1  O  ASP E 339   N  THR E 254           
SHEET   11   J12 ILE E 323  ILE E 325 -1  N  ARG E 324   O  GLU E 338           
SHEET   12   J12 ALA E 314  VAL E 316  1  N  GLY E 315   O  ILE E 323           
LINK         OE1 GLU A 134                MN    MN A 402     1555   1555  2.17  
LINK         OE1 GLU A 134                MN    MN A 403     1555   1555  2.38  
LINK         OE2 GLU A 136                MN    MN A 401     1555   1555  2.23  
LINK         OE1 GLU A 196                MN    MN A 401     1555   1555  2.34  
LINK         OE1 GLU A 196                MN    MN A 404     1555   1555  2.44  
LINK         OE1 GLU A 203                MN    MN A 401     1555   1555  2.11  
LINK         OE2 GLU A 203                MN    MN A 403     1555   1555  2.25  
LINK         OE2 GLU A 338                MN    MN A 402     1555   1555  2.02  
LINK         OE1 GLU B 134                MN    MN B 402     1555   1555  2.38  
LINK         OE2 GLU B 134                MN    MN B 403     1555   1555  2.19  
LINK         OE2 GLU B 134                MN    MN B 402     1555   1555  2.42  
LINK         OE2 GLU B 136                MN    MN B 401     1555   1555  2.14  
LINK         OE1 GLU B 196                MN    MN B 401     1555   1555  2.24  
LINK         OE1 GLU B 203                MN    MN B 401     1555   1555  2.04  
LINK         OE2 GLU B 203                MN    MN B 403     1555   1555  2.28  
LINK         OE2 GLU B 338                MN    MN B 402     1555   1555  2.05  
LINK         OE1 GLU C 134                MN    MN C 403     1555   1555  2.28  
LINK         OE1 GLU C 134                MN    MN C 402     1555   1555  2.21  
LINK         OE2 GLU C 136                MN    MN C 401     1555   1555  2.11  
LINK         OE1 GLU C 196                MN    MN C 401     1555   1555  2.43  
LINK         OE1 GLU C 196                MN    MN C 404     1555   1555  2.33  
LINK         OE1 GLU C 203                MN    MN C 403     1555   1555  2.28  
LINK         OE2 GLU C 203                MN    MN C 401     1555   1555  2.04  
LINK         OE2 GLU C 338                MN    MN C 402     1555   1555  2.00  
LINK         OE1 GLU D 134                MN    MN D 402     1555   1555  2.31  
LINK         OE1 GLU D 134                MN    MN D 403     1555   1555  2.25  
LINK         OE2 GLU D 136                MN    MN D 401     1555   1555  2.13  
LINK         OE2 GLU D 196                MN    MN D 401     1555   1555  2.27  
LINK         OE1 GLU D 203                MN    MN D 403     1555   1555  2.31  
LINK         OE2 GLU D 203                MN    MN D 401     1555   1555  2.05  
LINK         OE2 GLU D 338                MN    MN D 402     1555   1555  2.19  
LINK         OE1 GLU E 134                MN    MN E 402     1555   1555  2.28  
LINK         OE1 GLU E 134                MN    MN E 403     1555   1555  2.29  
LINK         OE2 GLU E 136                MN    MN E 401     1555   1555  2.22  
LINK         OE1 GLU E 196                MN    MN E 401     1555   1555  2.32  
LINK         OE1 GLU E 203                MN    MN E 401     1555   1555  2.06  
LINK         OE2 GLU E 203                MN    MN E 403     1555   1555  2.32  
LINK         OE1 GLU E 338                MN    MN E 402     1555   1555  2.02  
LINK        MN    MN A 401                 O4  PO4 A 502     1555   1555  2.37  
LINK        MN    MN A 401                 O2  PO4 A 502     1555   1555  2.24  
LINK        MN    MN A 401                 O   HOH A1686     1555   1555  2.34  
LINK        MN    MN A 402                 O3B ADP A 501     1555   1555  2.12  
LINK        MN    MN A 402                 O1  PO4 A 502     1555   1555  2.18  
LINK        MN    MN A 403                 O2A ADP A 501     1555   1555  2.19  
LINK        MN    MN A 403                 O1B ADP A 501     1555   1555  2.00  
LINK        MN    MN A 403                 O   HOH A1635     1555   1555  2.29  
LINK        MN    MN A 403                 O2  PO4 A 502     1555   1555  2.23  
LINK        MN    MN A 404                 O4  PO4 A 502     1555   1555  2.24  
LINK        MN    MN A 404                 O   HOH A1730     1555   1555  1.95  
LINK        MN    MN A 404                 O   HOH A1729     1555   1555  2.15  
LINK        MN    MN A 404                 O   HOH A1731     1555   1555  2.45  
LINK        MN    MN B 401                 O3  PO4 B 502     1555   1555  2.36  
LINK        MN    MN B 401                 O   HOH B1747     1555   1555  2.29  
LINK        MN    MN B 401                 O4  PO4 B 502     1555   1555  2.44  
LINK        MN    MN B 402                 O2B ADP B 501     1555   1555  2.26  
LINK        MN    MN B 402                 O2  PO4 B 502     1555   1555  2.24  
LINK        MN    MN B 403                 O2A ADP B 501     1555   1555  2.20  
LINK        MN    MN B 403                 O3B ADP B 501     1555   1555  2.18  
LINK        MN    MN B 403                 O   HOH B1616     1555   1555  2.14  
LINK        MN    MN B 403                 O3  PO4 B 502     1555   1555  2.13  
LINK        MN    MN B 404                 O   HOH B1740     1555   1555  2.31  
LINK        MN    MN B 404                 O4  PO4 B 502     1555   1555  2.35  
LINK        MN    MN B 404                 O   HOH B1738     1555   1555  2.31  
LINK        MN    MN B 404                 O   HOH B1739     1555   1555  2.17  
LINK        MN    MN B 404                 O   HOH B1730     1555   1555  2.20  
LINK        MN    MN C 401                 O1  PO4 C 502     1555   1555  2.29  
LINK        MN    MN C 401                 O   HOH C1745     1555   1555  2.37  
LINK        MN    MN C 401                 O4  PO4 C 502     1555   1555  2.16  
LINK        MN    MN C 402                 O2B ADP C 501     1555   1555  2.09  
LINK        MN    MN C 402                 O3  PO4 C 502     1555   1555  2.27  
LINK        MN    MN C 403                 O2A ADP C 501     1555   1555  2.10  
LINK        MN    MN C 403                 O   HOH C1604     1555   1555  2.33  
LINK        MN    MN C 403                 O3B ADP C 501     1555   1555  2.11  
LINK        MN    MN C 403                 O1  PO4 C 502     1555   1555  2.13  
LINK        MN    MN C 404                 O4  PO4 C 502     1555   1555  2.17  
LINK        MN    MN C 404                 O   HOH B1741     1555   1555  2.30  
LINK        MN    MN C 404                 O   HOH C1718     1555   1555  2.27  
LINK        MN    MN C 404                 O   HOH C1719     1555   1555  2.22  
LINK        MN    MN D 401                 O   HOH D1741     1555   1555  2.19  
LINK        MN    MN D 401                 O1  PO4 D 502     1555   1555  2.37  
LINK        MN    MN D 401                 O4  PO4 D 502     1555   1555  2.28  
LINK        MN    MN D 402                 O2B ADP D 501     1555   1555  2.05  
LINK        MN    MN D 402                 O3  PO4 D 502     1555   1555  2.16  
LINK        MN    MN D 403                 O2A ADP D 501     1555   1555  2.06  
LINK        MN    MN D 403                 O   HOH D1615     1555   1555  2.16  
LINK        MN    MN D 403                 O3B ADP D 501     1555   1555  2.14  
LINK        MN    MN D 403                 O1  PO4 D 502     1555   1555  2.16  
LINK        MN    MN D 404                 O4  PO4 D 502     1555   1555  2.17  
LINK        MN    MN D 404                 O   HOH D1740     1555   1555  2.08  
LINK        MN    MN D 404                 O   HOH D1739     1555   1555  2.12  
LINK        MN    MN D 404                 O   HOH D1609     1555   1555  2.34  
LINK        MN    MN E 401                 O1  PO4 E 502     1555   1555  2.39  
LINK        MN    MN E 401                 O   HOH E1666     1555   1555  2.39  
LINK        MN    MN E 401                 O4  PO4 E 502     1555   1555  2.31  
LINK        MN    MN E 402                 O2B ADP E 501     1555   1555  2.08  
LINK        MN    MN E 402                 O3  PO4 E 502     1555   1555  2.20  
LINK        MN    MN E 403                 O2A ADP E 501     1555   1555  2.04  
LINK        MN    MN E 403                 O3B ADP E 501     1555   1555  2.33  
LINK        MN    MN E 403                 O   HOH E1609     1555   1555  2.30  
LINK        MN    MN E 403                 O1  PO4 E 502     1555   1555  2.04  
LINK        MN    MN E 404                 O4  PO4 E 502     1555   1555  2.23  
LINK        MN    MN E 404                 O   HOH E1716     1555   1555  2.12  
LINK        MN    MN E 404                 O   HOH E1717     1555   1555  2.14  
CISPEP   1 ASP B   92    PRO B   93          0        -3.72                     
SITE     1 AC1  6 GLU A 136  GLU A 196  GLU A 203   MN A 404                    
SITE     2 AC1  6 PO4 A 502  HOH A1686                                          
SITE     1 AC2  6 GLU A 134  HIS A 253  GLU A 338  ARG A 340                    
SITE     2 AC2  6 ADP A 501  PO4 A 502                                          
SITE     1 AC3  5 GLU A 134  GLU A 203  ADP A 501  PO4 A 502                    
SITE     2 AC3  5 HOH A1635                                                     
SITE     1 AC4  6 GLU A 196   MN A 401  PO4 A 502  HOH A1729                    
SITE     2 AC4  6 HOH A1730  HOH A1731                                          
SITE     1 AC5 16 GLU A 134  GLU A 136  GLU A 196  GLU A 203                    
SITE     2 AC5 16 HIS A 253  ARG A 319  GLU A 338  ARG A 340                    
SITE     3 AC5 16  MN A 401   MN A 402   MN A 403   MN A 404                    
SITE     4 AC5 16 ADP A 501  HOH A1686  HOH A1730  HOH A1786                    
SITE     1 AC6  6 GLU B 136  GLU B 196  GLU B 203   MN B 404                    
SITE     2 AC6  6 PO4 B 502  HOH B1747                                          
SITE     1 AC7  6 GLU B 134  HIS B 253  GLU B 338  ARG B 340                    
SITE     2 AC7  6 ADP B 501  PO4 B 502                                          
SITE     1 AC8  5 GLU B 134  GLU B 203  ADP B 501  PO4 B 502                    
SITE     2 AC8  5 HOH B1616                                                     
SITE     1 AC9  7 GLU B 196   MN B 401  PO4 B 502  HOH B1730                    
SITE     2 AC9  7 HOH B1738  HOH B1739  HOH B1740                               
SITE     1 BC1 15 GLU B 134  GLU B 136  GLU B 196  GLU B 203                    
SITE     2 BC1 15 HIS B 253  ARG B 319  GLU B 338  ARG B 340                    
SITE     3 BC1 15  MN B 401   MN B 402   MN B 403   MN B 404                    
SITE     4 BC1 15 ADP B 501  HOH B1616  HOH B1740                               
SITE     1 BC2  6 GLU C 136  GLU C 196  GLU C 203   MN C 404                    
SITE     2 BC2  6 PO4 C 502  HOH C1745                                          
SITE     1 BC3  6 GLU C 134  HIS C 253  GLU C 338  ARG C 340                    
SITE     2 BC3  6 ADP C 501  PO4 C 502                                          
SITE     1 BC4  5 GLU C 134  GLU C 203  ADP C 501  PO4 C 502                    
SITE     2 BC4  5 HOH C1604                                                     
SITE     1 BC5  6 HOH B1741  GLU C 196   MN C 401  PO4 C 502                    
SITE     2 BC5  6 HOH C1718  HOH C1719                                          
SITE     1 BC6 17 HOH B1741  GLU C 134  GLU C 136  GLU C 196                    
SITE     2 BC6 17 GLU C 203  HIS C 253  ARG C 319  GLU C 338                    
SITE     3 BC6 17 ARG C 340   MN C 401   MN C 402   MN C 403                    
SITE     4 BC6 17  MN C 404  ADP C 501  HOH C1707  HOH C1718                    
SITE     5 BC6 17 HOH C1745                                                     
SITE     1 BC7  6 GLU D 136  GLU D 196  GLU D 203   MN D 404                    
SITE     2 BC7  6 PO4 D 502  HOH D1741                                          
SITE     1 BC8  6 GLU D 134  HIS D 253  GLU D 338  ARG D 340                    
SITE     2 BC8  6 ADP D 501  PO4 D 502                                          
SITE     1 BC9  5 GLU D 134  GLU D 203  ADP D 501  PO4 D 502                    
SITE     2 BC9  5 HOH D1615                                                     
SITE     1 CC1  6 GLU D 196   MN D 401  PO4 D 502  HOH D1609                    
SITE     2 CC1  6 HOH D1739  HOH D1740                                          
SITE     1 CC2 17 GLU D 134  GLU D 136  GLU D 196  GLU D 203                    
SITE     2 CC2 17 HIS D 253  ARG D 319  GLU D 338  ARG D 340                    
SITE     3 CC2 17  MN D 401   MN D 402   MN D 403   MN D 404                    
SITE     4 CC2 17 ADP D 501  HOH D1598  HOH D1739  HOH D1740                    
SITE     5 CC2 17 HOH D1741                                                     
SITE     1 CC3  6 GLU E 136  GLU E 196  GLU E 203   MN E 404                    
SITE     2 CC3  6 PO4 E 502  HOH E1666                                          
SITE     1 CC4  6 GLU E 134  HIS E 253  GLU E 338  ARG E 340                    
SITE     2 CC4  6 ADP E 501  PO4 E 502                                          
SITE     1 CC5  5 GLU E 134  GLU E 203  ADP E 501  PO4 E 502                    
SITE     2 CC5  5 HOH E1609                                                     
SITE     1 CC6  7 GLU E 136  GLU E 196   MN E 401  PO4 E 502                    
SITE     2 CC6  7 HOH E1611  HOH E1716  HOH E1717                               
SITE     1 CC7 15 GLU E 134  GLU E 136  GLU E 196  GLU E 203                    
SITE     2 CC7 15 HIS E 253  ARG E 319  GLU E 338  ARG E 340                    
SITE     3 CC7 15  MN E 401   MN E 402   MN E 403   MN E 404                    
SITE     4 CC7 15 ADP E 501  HOH E1699  HOH E1716                               
SITE     1 CC8  2 THR B  44  THR C 193                                          
SITE     1 CC9  3 MET C  29  THR C  44  THR D 193                               
SITE     1 DC1  2 THR A 193  THR E  44                                          
SITE     1 DC2  3 THR D  44  THR E 193  HOH E1531                               
SITE     1 DC3  2 THR A  44  THR B 193                                          
SITE     1 DC4 23 TRP A 130  GLY A 132  GLU A 134  GLU A 203                    
SITE     2 DC4 23 GLN A 205  GLY A 207  PRO A 208  ASN A 255                    
SITE     3 DC4 23 SER A 257  ARG A 319  ARG A 324  TYR A 336                    
SITE     4 DC4 23 GLU A 338   MN A 402   MN A 403  PO4 A 502                    
SITE     5 DC4 23 HOH A1540  HOH A1587  HOH A1619  HOH A1620                    
SITE     6 DC4 23 HOH A1635  HOH A1664  HOH E1513                               
SITE     1 DC5 23 HOH A1575  TRP B 130  GLY B 132  GLU B 134                    
SITE     2 DC5 23 GLU B 203  GLN B 205  GLY B 207  PRO B 208                    
SITE     3 DC5 23 ASN B 255  SER B 257  ARG B 319  ARG B 324                    
SITE     4 DC5 23 TYR B 336  GLU B 338   MN B 402   MN B 403                    
SITE     5 DC5 23 PO4 B 502  HOH B1560  HOH B1570  HOH B1589                    
SITE     6 DC5 23 HOH B1616  HOH B1693  HOH B1753                               
SITE     1 DC6 23 TRP C 130  GLY C 132  GLU C 134  GLU C 203                    
SITE     2 DC6 23 GLN C 205  GLY C 207  PRO C 208  ASN C 255                    
SITE     3 DC6 23 SER C 257  ARG C 319  ARG C 324  TYR C 336                    
SITE     4 DC6 23 GLU C 338   MN C 402   MN C 403  PO4 C 502                    
SITE     5 DC6 23 HOH C1584  HOH C1600  HOH C1603  HOH C1604                    
SITE     6 DC6 23 HOH C1656  HOH C1674  HOH C1681                               
SITE     1 DC7 24 TRP D 130  GLY D 132  GLU D 134  GLU D 203                    
SITE     2 DC7 24 GLN D 205  GLY D 207  PRO D 208  ASN D 255                    
SITE     3 DC7 24 SER D 257  ARG D 319  ARG D 324  TYR D 336                    
SITE     4 DC7 24 GLU D 338   MN D 402   MN D 403  PO4 D 502                    
SITE     5 DC7 24 HOH D1585  HOH D1597  HOH D1615  HOH D1628                    
SITE     6 DC7 24 HOH D1631  HOH D1636  HOH D1716  HOH D1750                    
SITE     1 DC8 23 HOH D1617  TRP E 130  GLY E 132  GLU E 134                    
SITE     2 DC8 23 GLU E 203  GLN E 205  GLY E 207  PRO E 208                    
SITE     3 DC8 23 ASN E 255  SER E 257  ARG E 262  ARG E 319                    
SITE     4 DC8 23 ARG E 324  TYR E 336  GLU E 338   MN E 402                    
SITE     5 DC8 23  MN E 403  PO4 E 502  HOH E1540  HOH E1555                    
SITE     6 DC8 23 HOH E1609  HOH E1636  HOH E1644                               
SITE     1 DC9  6 LYS A  14  PRO A  88  PHE A  89  HOH A1543                    
SITE     2 DC9  6 HOH A1665  HOH A1694                                          
SITE     1 EC1  8 TYR A  17  LYS B  14  PRO B  88  PHE B  89                    
SITE     2 EC1  8 HOH B1548  HOH B1674  HOH B1748  HOH B1756                    
SITE     1 EC2  5 LYS C  14  PRO C  88  PHE C  89  HOH C1557                    
SITE     2 EC2  5 HOH C1734                                                     
SITE     1 EC3  5 LYS D  14  PRO D  88  PHE D  89  HOH D1601                    
SITE     2 EC3  5 HOH D1752                                                     
SITE     1 EC4  7 VAL D  16  LYS E  14  PRO E  88  PHE E  89                    
SITE     2 EC4  7 HOH E1557  HOH E1594  HOH E1642                               
SITE     1 EC5  5 ALA C  82  SER C 213  ASP C 216  HIS C 217                    
SITE     2 EC5  5 HOH C1781                                                     
CRYST1  177.600  122.600  126.600  90.00 130.60  90.00 C 1 2 1      20          
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      0.005631  0.000000  0.004826        0.00000                         
SCALE2      0.000000  0.008157  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010403        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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