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Database: PDB
Entry: 3R7C
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HEADER    OXIDOREDUCTASE                          22-MAR-11   3R7C              
TITLE     THE STRUCTURE OF A HEXAHESTIDINE-TAGGED FORM OF AUGMENTER OF LIVER    
TITLE    2 REGENERATION REVEALS A NOVEL CD(2)CL(4)O(6) CLUSTER THAT AIDS IN     
TITLE    3 CRYSTAL PACKING                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FAD-LINKED SULFHYDRYL OXIDASE ALR;                         
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: RESIDUES 74-198;                                           
COMPND   5 SYNONYM: AUGMENTER OF LIVER REGENERATION;                            
COMPND   6 EC: 1.8.3.2;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: ALR, GFER, GFER (ALR);                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: JM109;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHRALR                                    
KEYWDS    NOVEL CD(2)CL(4)O(6) CLUSTER, FOUR-HELICAL UP-AND-DOWN BUNDLE, ALL-   
KEYWDS   2 HELICAL FAD BINDING MOTIF, FAD-LINKED SULFHYDRYL OXIDASE, LIVER      
KEYWDS   3 REGENERATION, FAD BINDING, MITOCHONDRIAL INTERMEMBRANE SPACE,        
KEYWDS   4 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.J.FLORENCE,C.-K.WU,J.T.SWINDELL II,B.C.WANG,J.P.ROSE                
REVDAT   2   08-NOV-17 3R7C    1       AUTHOR REMARK                            
REVDAT   1   28-MAR-12 3R7C    0                                                
JRNL        AUTH   Q.J.FLORENCE,C.-K.WU,J.E.HABEL,J.T.SWINDELL II,B.C.WANG,     
JRNL        AUTH 2 J.P.ROSE                                                     
JRNL        TITL   THE STRUCTURE OF A HEXAHESTIDINE-TAGGED FORM OF AUGMENTER OF 
JRNL        TITL 2 LIVER REGENERATION REVEALS A NOVEL CD(2)CL(4)O(6) CLUSTER    
JRNL        TITL 3 THAT AIDS IN CRYSTAL PACKING                                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.-K.WU,T.A.DAILEY,H.A.DAILEY,A.FRANCOVILLA,T.E.STARZL,      
REMARK   1  AUTH 2 B.C.WANG,J.P.ROSE                                            
REMARK   1  TITL   EXPRESSION, PURIFICATION, CRYSTALLIZATION AND PRELIMINARY    
REMARK   1  TITL 2 ANALYSIS OF THE AUGMENTER OF LIVER REGENERATION              
REMARK   1  REF    PROTEIN AND PEPTIDE LETTERS   V.   7    25 2000              
REMARK   1  REFN                   ISSN 0929-8665                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   C.K.WU,T.A.DAILEY,H.A.DAILEY,B.C.WANG,J.P.ROSE               
REMARK   1  TITL   THE CRYSTAL STRUCTURE OF AUGMENTER OF LIVER REGENERATION: A  
REMARK   1  TITL 2 MAMMALIAN FAD -DEPENDENT SULFHYDRYL OXIDASE.                 
REMARK   1  REF    PROTEIN SCI.                  V.  12  1109 2003              
REMARK   1  REFN                   ISSN 0961-8368                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.64                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 41958                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2091                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 19.6381 -  5.8700    1.00     2710   148  0.1806 0.2036        
REMARK   3     2  5.8700 -  4.6799    1.00     2695   146  0.1547 0.1855        
REMARK   3     3  4.6799 -  4.0945    1.00     2688   136  0.1209 0.1518        
REMARK   3     4  4.0945 -  3.7229    1.00     2694   147  0.1429 0.1822        
REMARK   3     5  3.7229 -  3.4576    1.00     2730   132  0.1617 0.2117        
REMARK   3     6  3.4576 -  3.2547    1.00     2656   135  0.1630 0.1869        
REMARK   3     7  3.2547 -  3.0924    0.99     2708   139  0.1563 0.2235        
REMARK   3     8  3.0924 -  2.9582    0.98     2673   149  0.1674 0.2112        
REMARK   3     9  2.9582 -  2.8447    0.98     2623   135  0.1729 0.2595        
REMARK   3    10  2.8447 -  2.7468    0.97     2602   137  0.1729 0.2423        
REMARK   3    11  2.7468 -  2.6611    0.98     2624   136  0.1685 0.2444        
REMARK   3    12  2.6611 -  2.5852    0.97     2653   140  0.1813 0.2330        
REMARK   3    13  2.5852 -  2.5173    0.96     2600   143  0.1876 0.2856        
REMARK   3    14  2.5173 -  2.4560    0.96     2644   133  0.1967 0.2897        
REMARK   3    15  2.4560 -  2.4003    0.95     2567   135  0.1910 0.2561        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.95                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 25.99                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.25270                                             
REMARK   3    B22 (A**2) : -2.25270                                             
REMARK   3    B33 (A**2) : 4.50550                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           3990                                  
REMARK   3   ANGLE     :  1.146           5420                                  
REMARK   3   CHIRALITY :  0.076            515                                  
REMARK   3   PLANARITY :  0.005            691                                  
REMARK   3   DIHEDRAL  : 17.579           1484                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 19                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 14:59)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  43.7887  28.8388  41.4438              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0984 T22:   0.0796                                     
REMARK   3      T33:   0.0728 T12:   0.0013                                     
REMARK   3      T13:   0.0057 T23:  -0.0009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3581 L22:   0.1557                                     
REMARK   3      L33:   0.1276 L12:  -0.0942                                     
REMARK   3      L13:   0.0443 L23:   0.0183                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1103 S12:  -0.0165 S13:  -0.0715                       
REMARK   3      S21:  -0.0613 S22:  -0.0834 S23:  -0.0099                       
REMARK   3      S31:   0.1007 S32:  -0.0073 S33:  -0.0021                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 60:82)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  44.3124  38.5352  47.3434              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0794 T22:   0.1859                                     
REMARK   3      T33:   0.1046 T12:  -0.0421                                     
REMARK   3      T13:  -0.0133 T23:   0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3372 L22:   0.2643                                     
REMARK   3      L33:   0.1152 L12:   0.0669                                     
REMARK   3      L13:   0.1368 L23:   0.1197                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0035 S12:  -0.0111 S13:   0.0683                       
REMARK   3      S21:   0.0321 S22:  -0.1131 S23:   0.0685                       
REMARK   3      S31:  -0.0044 S32:   0.0964 S33:   0.0507                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 83:124)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  48.1183  37.3209  31.3697              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1002 T22:   0.1369                                     
REMARK   3      T33:  -0.0087 T12:  -0.0437                                     
REMARK   3      T13:   0.0569 T23:   0.1051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1061 L22:   0.0115                                     
REMARK   3      L33:   0.0127 L12:   0.0323                                     
REMARK   3      L13:   0.0150 L23:  -0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0573 S12:   0.1437 S13:   0.0534                       
REMARK   3      S21:  -0.0608 S22:   0.0477 S23:   0.0077                       
REMARK   3      S31:  -0.0693 S32:   0.0587 S33:  -0.0278                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 14:35)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  22.5283  45.0770  66.7171              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1394 T22:   0.1428                                     
REMARK   3      T33:   0.1169 T12:   0.0048                                     
REMARK   3      T13:  -0.0150 T23:  -0.0161                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1765 L22:   0.8215                                     
REMARK   3      L33:   0.2024 L12:   0.0273                                     
REMARK   3      L13:   0.0181 L23:  -0.2910                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0054 S12:  -0.0144 S13:  -0.0003                       
REMARK   3      S21:   0.1208 S22:  -0.0444 S23:   0.1076                       
REMARK   3      S31:  -0.0295 S32:   0.0259 S33:   0.0171                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 36:59)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  33.9020  48.8279  52.2108              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0767 T22:   0.0815                                     
REMARK   3      T33:   0.1533 T12:  -0.0203                                     
REMARK   3      T13:  -0.0062 T23:  -0.0145                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2162 L22:   0.3264                                     
REMARK   3      L33:   0.1536 L12:   0.0662                                     
REMARK   3      L13:  -0.0377 L23:  -0.1059                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0715 S12:   0.1021 S13:   0.1144                       
REMARK   3      S21:   0.0374 S22:   0.1202 S23:  -0.0535                       
REMARK   3      S31:  -0.0555 S32:   0.0262 S33:   0.0113                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 60:68)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  26.3838  33.5065  63.2314              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1659 T22:   0.1256                                     
REMARK   3      T33:   0.1640 T12:   0.0294                                     
REMARK   3      T13:  -0.0409 T23:   0.0597                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0567 L22:   0.0752                                     
REMARK   3      L33:   0.1716 L12:   0.0377                                     
REMARK   3      L13:  -0.0758 L23:   0.0097                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0670 S12:  -0.0318 S13:  -0.0358                       
REMARK   3      S21:   0.0578 S22:   0.0463 S23:  -0.0053                       
REMARK   3      S31:   0.0291 S32:  -0.0175 S33:  -0.0424                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 69:82)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  30.1464  38.1703  49.9996              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1225 T22:   0.1585                                     
REMARK   3      T33:   0.1189 T12:  -0.0236                                     
REMARK   3      T13:  -0.0078 T23:  -0.0438                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0179 L22:   0.1272                                     
REMARK   3      L33:   0.0260 L12:   0.0471                                     
REMARK   3      L13:  -0.0016 L23:   0.0072                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0134 S12:   0.0012 S13:   0.0396                       
REMARK   3      S21:  -0.0321 S22:   0.0400 S23:  -0.0326                       
REMARK   3      S31:   0.0014 S32:  -0.0446 S33:   0.0028                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 83:101)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.4656  41.6269  52.5848              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0327 T22:   0.0893                                     
REMARK   3      T33:   0.1338 T12:  -0.0188                                     
REMARK   3      T13:  -0.0584 T23:  -0.0679                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1466 L22:   0.0363                                     
REMARK   3      L33:   0.0747 L12:   0.0721                                     
REMARK   3      L13:   0.0801 L23:   0.0409                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0672 S12:   0.0960 S13:   0.0205                       
REMARK   3      S21:  -0.0328 S22:  -0.0098 S23:   0.0330                       
REMARK   3      S31:  -0.0394 S32:   0.0090 S33:  -0.0861                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 102:124)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  12.2734  51.2835  54.7869              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0931 T22:   0.1760                                     
REMARK   3      T33:   0.2355 T12:   0.0438                                     
REMARK   3      T13:  -0.0268 T23:   0.0138                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1705 L22:   0.0642                                     
REMARK   3      L33:   0.1812 L12:   0.0229                                     
REMARK   3      L13:  -0.0361 L23:   0.0458                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0665 S12:  -0.0012 S13:  -0.1023                       
REMARK   3      S21:  -0.0379 S22:   0.0253 S23:   0.1045                       
REMARK   3      S31:  -0.0632 S32:  -0.1050 S33:  -0.0154                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 14:35)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  51.0609  21.0778  37.7690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0929 T22:   0.0661                                     
REMARK   3      T33:   0.1157 T12:   0.0262                                     
REMARK   3      T13:   0.0358 T23:   0.0139                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0356 L22:   0.0229                                     
REMARK   3      L33:   0.0652 L12:   0.0278                                     
REMARK   3      L13:  -0.0242 L23:  -0.0235                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0196 S12:   0.0166 S13:  -0.0707                       
REMARK   3      S21:  -0.0301 S22:   0.0434 S23:  -0.0542                       
REMARK   3      S31:   0.0353 S32:   0.0315 S33:   0.0171                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 36:59)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  41.0728  22.8650  53.4470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1551 T22:   0.0958                                     
REMARK   3      T33:   0.1280 T12:  -0.0400                                     
REMARK   3      T13:   0.0036 T23:   0.0083                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0366 L22:   0.1880                                     
REMARK   3      L33:   0.1680 L12:  -0.0552                                     
REMARK   3      L13:   0.0593 L23:  -0.0278                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0665 S12:   0.0093 S13:   0.0013                       
REMARK   3      S21:   0.1416 S22:  -0.0245 S23:   0.0922                       
REMARK   3      S31:  -0.0260 S32:   0.0544 S33:   0.0096                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 60:75)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  38.4359  13.2671  39.5912              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1843 T22:   0.1839                                     
REMARK   3      T33:   0.2677 T12:  -0.0264                                     
REMARK   3      T13:   0.0744 T23:  -0.0411                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3884 L22:   0.0387                                     
REMARK   3      L33:   1.1113 L12:   0.0900                                     
REMARK   3      L13:  -0.5287 L23:  -0.0609                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1321 S12:   0.0045 S13:  -0.0964                       
REMARK   3      S21:  -0.0167 S22:  -0.1081 S23:  -0.0716                       
REMARK   3      S31:   0.2314 S32:  -0.0744 S33:   0.1553                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 76:107)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.9975  10.4790  48.2591              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1979 T22:   0.0887                                     
REMARK   3      T33:   0.2009 T12:   0.0276                                     
REMARK   3      T13:   0.0386 T23:   0.0170                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0988 L22:   0.0025                                     
REMARK   3      L33:   0.0906 L12:   0.0147                                     
REMARK   3      L13:  -0.0318 L23:   0.0081                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0376 S12:  -0.0328 S13:  -0.1334                       
REMARK   3      S21:   0.0142 S22:  -0.0169 S23:  -0.0272                       
REMARK   3      S31:   0.0791 S32:  -0.0106 S33:   0.0222                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 108:115)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  58.4250  13.3495  50.7709              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1245 T22:   0.2708                                     
REMARK   3      T33:   0.2564 T12:   0.0415                                     
REMARK   3      T13:  -0.0588 T23:   0.0452                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7127 L22:   0.1886                                     
REMARK   3      L33:   0.0821 L12:  -0.2079                                     
REMARK   3      L13:   0.0618 L23:   0.0534                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0074 S12:   0.0258 S13:   0.1308                       
REMARK   3      S21:   0.0453 S22:  -0.0091 S23:  -0.1421                       
REMARK   3      S31:   0.0065 S32:   0.0313 S33:   0.0047                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 116:124)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  66.0245  16.7098  52.3698              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3028 T22:   0.5466                                     
REMARK   3      T33:   0.5802 T12:   0.1091                                     
REMARK   3      T13:  -0.1689 T23:   0.1094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1212 L22:   0.4231                                     
REMARK   3      L33:   0.0513 L12:   0.1652                                     
REMARK   3      L13:  -0.0039 L23:   0.0537                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0443 S12:   0.1702 S13:  -0.1195                       
REMARK   3      S21:  -0.0296 S22:  -0.1930 S23:  -0.2929                       
REMARK   3      S31:   0.0249 S32:   0.1254 S33:   0.1019                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 14:59)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  33.3346  47.9326  65.8725              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1376 T22:   0.1193                                     
REMARK   3      T33:   0.1016 T12:   0.0119                                     
REMARK   3      T13:  -0.0911 T23:  -0.0673                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0943 L22:   0.1705                                     
REMARK   3      L33:   0.1259 L12:  -0.0136                                     
REMARK   3      L13:  -0.0556 L23:  -0.0964                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0149 S12:  -0.0062 S13:   0.0031                       
REMARK   3      S21:   0.0559 S22:   0.1442 S23:  -0.0220                       
REMARK   3      S31:  -0.0310 S32:   0.1108 S33:   0.2087                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 60:72)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  33.1226  61.8031  63.5339              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2220 T22:   0.1190                                     
REMARK   3      T33:   0.3094 T12:  -0.0707                                     
REMARK   3      T13:   0.0877 T23:  -0.0277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9470 L22:   0.2283                                     
REMARK   3      L33:   0.7819 L12:   0.2227                                     
REMARK   3      L13:   0.1441 L23:  -0.3324                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0613 S12:  -0.0470 S13:   0.2951                       
REMARK   3      S21:   0.0300 S22:   0.0548 S23:  -0.1304                       
REMARK   3      S31:  -0.1999 S32:   0.0676 S33:  -0.0595                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 73:82)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  45.1922  50.7010  68.8355              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3965 T22:   0.3660                                     
REMARK   3      T33:   0.3422 T12:  -0.0407                                     
REMARK   3      T13:  -0.0832 T23:  -0.0788                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7937 L22:   0.5684                                     
REMARK   3      L33:   1.8865 L12:   0.8308                                     
REMARK   3      L13:   0.0948 L23:   0.5641                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0651 S12:  -0.0715 S13:   0.2456                       
REMARK   3      S21:  -0.0044 S22:   0.0692 S23:   0.0743                       
REMARK   3      S31:   0.0615 S32:   0.0826 S33:  -0.0890                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 83:124)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.3634  50.0495  79.5684              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2523 T22:   0.0766                                     
REMARK   3      T33:   0.1337 T12:   0.0090                                     
REMARK   3      T13:  -0.1758 T23:  -0.0939                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0129 L22:   0.0519                                     
REMARK   3      L33:   0.0324 L12:   0.0106                                     
REMARK   3      L13:   0.0039 L23:   0.0343                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0191 S12:  -0.0618 S13:   0.0182                       
REMARK   3      S21:   0.0769 S22:   0.0161 S23:   0.0042                       
REMARK   3      S31:   0.0514 S32:   0.0017 S33:  -0.0174                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3R7C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000064580.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUN-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : YALE MIRRORS                       
REMARK 200  OPTICS                         : YALE MIRRORS                       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42700                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 30.88                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: CD-SAD                       
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: A TOTAL OF 720 ONE-DEGREE OSCILLATION IMAGES WERE RECORDED   
REMARK 200  FROM A SINGLE CRYSTAL GIVING A BIJVOET REDUNDANCY OF 15.44          
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEGMME 2000, 0.1M NAOAC, 50 MM       
REMARK 280  CDCL(2), SEE REFERENCE 1, PH 4.6, VAPOR DIFFUSION, HANGING DROP,    
REMARK 280  TEMPERATURE 291K (SEE REFERENCE 1).                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X,-Y,Z                                                 
REMARK 290       7555   -Y+1/2,X,Z+3/4                                          
REMARK 290       8555   Y,-X+1/2,Z+1/4                                          
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       49.84400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       49.84400            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.80500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       49.84400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       28.40250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       49.84400            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       85.20750            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       49.84400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       49.84400            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       56.80500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       49.84400            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       85.20750            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       49.84400            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       28.40250            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6780 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -96.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15450 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 19870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -211.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -13                                                      
REMARK 465     GLY A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     MET A    -2                                                      
REMARK 465     ALA A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     ARG A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     ILE A     9                                                      
REMARK 465     LYS A    10                                                      
REMARK 465     PHE A    11                                                      
REMARK 465     ARG A    12                                                      
REMARK 465     GLU A    13                                                      
REMARK 465     ASP A   125                                                      
REMARK 465     MET B   -13                                                      
REMARK 465     GLY B   -12                                                      
REMARK 465     GLY B   -11                                                      
REMARK 465     SER B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     HIS B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     MET B    -2                                                      
REMARK 465     ALA B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     GLN B     4                                                      
REMARK 465     GLN B     5                                                      
REMARK 465     LYS B     6                                                      
REMARK 465     ARG B     7                                                      
REMARK 465     ASP B     8                                                      
REMARK 465     ILE B     9                                                      
REMARK 465     LYS B    10                                                      
REMARK 465     PHE B    11                                                      
REMARK 465     ARG B    12                                                      
REMARK 465     GLU B    13                                                      
REMARK 465     ASP B   125                                                      
REMARK 465     MET C   -13                                                      
REMARK 465     GLY C   -12                                                      
REMARK 465     GLY C   -11                                                      
REMARK 465     SER C   -10                                                      
REMARK 465     HIS C    -9                                                      
REMARK 465     HIS C    -8                                                      
REMARK 465     HIS C    -7                                                      
REMARK 465     HIS C    -6                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     MET C    -2                                                      
REMARK 465     ALA C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ARG C     2                                                      
REMARK 465     THR C     3                                                      
REMARK 465     GLN C     4                                                      
REMARK 465     GLN C     5                                                      
REMARK 465     LYS C     6                                                      
REMARK 465     ARG C     7                                                      
REMARK 465     ASP C     8                                                      
REMARK 465     ILE C     9                                                      
REMARK 465     LYS C    10                                                      
REMARK 465     PHE C    11                                                      
REMARK 465     ARG C    12                                                      
REMARK 465     GLU C    13                                                      
REMARK 465     ASP C   125                                                      
REMARK 465     MET D   -13                                                      
REMARK 465     GLY D   -12                                                      
REMARK 465     GLY D   -11                                                      
REMARK 465     SER D   -10                                                      
REMARK 465     HIS D    -9                                                      
REMARK 465     HIS D    -8                                                      
REMARK 465     HIS D    -7                                                      
REMARK 465     HIS D    -6                                                      
REMARK 465     HIS D    -5                                                      
REMARK 465     HIS D    -4                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     MET D    -2                                                      
REMARK 465     ALA D    -1                                                      
REMARK 465     SER D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ARG D     2                                                      
REMARK 465     THR D     3                                                      
REMARK 465     GLN D     4                                                      
REMARK 465     GLN D     5                                                      
REMARK 465     LYS D     6                                                      
REMARK 465     ARG D     7                                                      
REMARK 465     ASP D     8                                                      
REMARK 465     ILE D     9                                                      
REMARK 465     LYS D    10                                                      
REMARK 465     PHE D    11                                                      
REMARK 465     ARG D    12                                                      
REMARK 465     GLU D    13                                                      
REMARK 465     ASP D   125                                                      
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     GLU A  63    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU A  64    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU B  63    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU B  64    CB   CG   CD   OE1  OE2                             
REMARK 470     ARG B 110    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C  63    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU C  64    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU D  63    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU D  64    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU D  67    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS D  71    CB   CG   CD   CE   NZ                              
REMARK 470     ARG D  72    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     ASP D  74    CB   CG   OD1  OD2                                  
REMARK 470     ARG D  75    CB   CG   CD   NE   CZ   NH1  NH2                   
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    CYS A  62       65.61   -156.02                                   
REMARK 500    SER A  76       79.32   -104.70                                   
REMARK 500    ARG B 116      -66.13   -121.64                                   
REMARK 500    ARG C 116      -64.71   -130.74                                   
REMARK 500    CYS D  62       95.68   -166.77                                   
REMARK 500    GLU D  64        7.19     88.31                                   
REMARK 500    ARG D  75      -52.12    167.06                                   
REMARK 500    ARG D 116      -57.52   -144.23                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     SO4 D  127                                                       
REMARK 610     SO4 D  129                                                       
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                              CD A 500  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1  CL A 502  CL                                                      
REMARK 620 2  CL A 503  CL    88.8                                              
REMARK 620 3  CL A 504  CL    99.4  97.3                                        
REMARK 620 4 HOH A 506   O    86.5 158.8 103.8                                  
REMARK 620 5 ASP A  74   OD1 103.8  90.5 155.6  70.7                            
REMARK 620 6 ASP A  74   OD2 156.1  88.2 104.5  87.8  52.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 501  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1  CL A 502  CL                                                      
REMARK 620 2  CL A 503  CL    87.5                                              
REMARK 620 3  CL A 505  CL    97.3 104.6                                        
REMARK 620 4 HOH A 507   O   168.4  89.1  94.3                                  
REMARK 620 5 ASP B  74   OD1  87.7 104.7 150.5  82.4                            
REMARK 620 6 ASP B  74   OD2  93.5 157.4  97.6  85.4  52.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD B 130  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 113   OE1                                                    
REMARK 620 2 HOH B 138   O    95.3                                              
REMARK 620 3 HOH B 139   O   118.5 107.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD C 127  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 129   O                                                      
REMARK 620 2 ASP C 107   OD1 111.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD B 131  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 141   O                                                      
REMARK 620 2 GLN B  47   OE1  89.0                                              
REMARK 620 3 GLU B  44   OE2 116.3  87.5                                        
REMARK 620 4 HOH A 133   O   106.7  88.3 136.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 126                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 130                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 131                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 126                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 130                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 131                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 132                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 133                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD C 126                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 127                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 128                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD D 126                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 127                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 128                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 129                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 505                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1OQC   RELATED DB: PDB                                   
REMARK 900 THE NATIVE ALR CRYSTAL STRUCTURE                                     
DBREF  3R7C A    1   125  UNP    Q63042   ALR_RAT         74    198             
DBREF  3R7C B    1   125  UNP    Q63042   ALR_RAT         74    198             
DBREF  3R7C C    1   125  UNP    Q63042   ALR_RAT         74    198             
DBREF  3R7C D    1   125  UNP    Q63042   ALR_RAT         74    198             
SEQADV 3R7C MET A  -13  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C GLY A  -12  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C GLY A  -11  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C SER A  -10  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS A   -9  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS A   -8  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS A   -7  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS A   -6  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS A   -5  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS A   -4  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C GLY A   -3  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C MET A   -2  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C ALA A   -1  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C SER A    0  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C MET B  -13  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C GLY B  -12  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C GLY B  -11  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C SER B  -10  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS B   -9  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS B   -8  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS B   -7  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS B   -6  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS B   -5  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS B   -4  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C GLY B   -3  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C MET B   -2  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C ALA B   -1  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C SER B    0  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C MET C  -13  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C GLY C  -12  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C GLY C  -11  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C SER C  -10  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS C   -9  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS C   -8  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS C   -7  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS C   -6  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS C   -5  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS C   -4  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C GLY C   -3  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C MET C   -2  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C ALA C   -1  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C SER C    0  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C MET D  -13  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C GLY D  -12  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C GLY D  -11  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C SER D  -10  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS D   -9  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS D   -8  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS D   -7  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS D   -6  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS D   -5  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C HIS D   -4  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C GLY D   -3  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C MET D   -2  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C ALA D   -1  UNP  Q63042              EXPRESSION TAG                 
SEQADV 3R7C SER D    0  UNP  Q63042              EXPRESSION TAG                 
SEQRES   1 A  139  MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA          
SEQRES   2 A  139  SER MET ARG THR GLN GLN LYS ARG ASP ILE LYS PHE ARG          
SEQRES   3 A  139  GLU ASP CYS PRO GLN ASP ARG GLU GLU LEU GLY ARG ASN          
SEQRES   4 A  139  THR TRP ALA PHE LEU HIS THR LEU ALA ALA TYR TYR PRO          
SEQRES   5 A  139  ASP MET PRO THR PRO GLU GLN GLN GLN ASP MET ALA GLN          
SEQRES   6 A  139  PHE ILE HIS ILE PHE SER LYS PHE TYR PRO CYS GLU GLU          
SEQRES   7 A  139  CYS ALA GLU ASP ILE ARG LYS ARG ILE ASP ARG SER GLN          
SEQRES   8 A  139  PRO ASP THR SER THR ARG VAL SER PHE SER GLN TRP LEU          
SEQRES   9 A  139  CYS ARG LEU HIS ASN GLU VAL ASN ARG LYS LEU GLY LYS          
SEQRES  10 A  139  PRO ASP PHE ASP CYS SER ARG VAL ASP GLU ARG TRP ARG          
SEQRES  11 A  139  ASP GLY TRP LYS ASP GLY SER CYS ASP                          
SEQRES   1 B  139  MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA          
SEQRES   2 B  139  SER MET ARG THR GLN GLN LYS ARG ASP ILE LYS PHE ARG          
SEQRES   3 B  139  GLU ASP CYS PRO GLN ASP ARG GLU GLU LEU GLY ARG ASN          
SEQRES   4 B  139  THR TRP ALA PHE LEU HIS THR LEU ALA ALA TYR TYR PRO          
SEQRES   5 B  139  ASP MET PRO THR PRO GLU GLN GLN GLN ASP MET ALA GLN          
SEQRES   6 B  139  PHE ILE HIS ILE PHE SER LYS PHE TYR PRO CYS GLU GLU          
SEQRES   7 B  139  CYS ALA GLU ASP ILE ARG LYS ARG ILE ASP ARG SER GLN          
SEQRES   8 B  139  PRO ASP THR SER THR ARG VAL SER PHE SER GLN TRP LEU          
SEQRES   9 B  139  CYS ARG LEU HIS ASN GLU VAL ASN ARG LYS LEU GLY LYS          
SEQRES  10 B  139  PRO ASP PHE ASP CYS SER ARG VAL ASP GLU ARG TRP ARG          
SEQRES  11 B  139  ASP GLY TRP LYS ASP GLY SER CYS ASP                          
SEQRES   1 C  139  MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA          
SEQRES   2 C  139  SER MET ARG THR GLN GLN LYS ARG ASP ILE LYS PHE ARG          
SEQRES   3 C  139  GLU ASP CYS PRO GLN ASP ARG GLU GLU LEU GLY ARG ASN          
SEQRES   4 C  139  THR TRP ALA PHE LEU HIS THR LEU ALA ALA TYR TYR PRO          
SEQRES   5 C  139  ASP MET PRO THR PRO GLU GLN GLN GLN ASP MET ALA GLN          
SEQRES   6 C  139  PHE ILE HIS ILE PHE SER LYS PHE TYR PRO CYS GLU GLU          
SEQRES   7 C  139  CYS ALA GLU ASP ILE ARG LYS ARG ILE ASP ARG SER GLN          
SEQRES   8 C  139  PRO ASP THR SER THR ARG VAL SER PHE SER GLN TRP LEU          
SEQRES   9 C  139  CYS ARG LEU HIS ASN GLU VAL ASN ARG LYS LEU GLY LYS          
SEQRES  10 C  139  PRO ASP PHE ASP CYS SER ARG VAL ASP GLU ARG TRP ARG          
SEQRES  11 C  139  ASP GLY TRP LYS ASP GLY SER CYS ASP                          
SEQRES   1 D  139  MET GLY GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA          
SEQRES   2 D  139  SER MET ARG THR GLN GLN LYS ARG ASP ILE LYS PHE ARG          
SEQRES   3 D  139  GLU ASP CYS PRO GLN ASP ARG GLU GLU LEU GLY ARG ASN          
SEQRES   4 D  139  THR TRP ALA PHE LEU HIS THR LEU ALA ALA TYR TYR PRO          
SEQRES   5 D  139  ASP MET PRO THR PRO GLU GLN GLN GLN ASP MET ALA GLN          
SEQRES   6 D  139  PHE ILE HIS ILE PHE SER LYS PHE TYR PRO CYS GLU GLU          
SEQRES   7 D  139  CYS ALA GLU ASP ILE ARG LYS ARG ILE ASP ARG SER GLN          
SEQRES   8 D  139  PRO ASP THR SER THR ARG VAL SER PHE SER GLN TRP LEU          
SEQRES   9 D  139  CYS ARG LEU HIS ASN GLU VAL ASN ARG LYS LEU GLY LYS          
SEQRES  10 D  139  PRO ASP PHE ASP CYS SER ARG VAL ASP GLU ARG TRP ARG          
SEQRES  11 D  139  ASP GLY TRP LYS ASP GLY SER CYS ASP                          
HET    FAD  A 126      53                                                       
HET     CL  A 130       1                                                       
HET     CL  A 131       1                                                       
HET     CD  A 500       1                                                       
HET     CD  A 501       1                                                       
HET     CL  A 502       1                                                       
HET     CL  A 503       1                                                       
HET     CL  A 504       1                                                       
HET     CL  A 505       1                                                       
HET    FAD  B 126      53                                                       
HET     CD  B 130       1                                                       
HET     CD  B 131       1                                                       
HET     CL  B 132       1                                                       
HET     CL  B 133       1                                                       
HET    FAD  C 126      53                                                       
HET     CD  C 127       1                                                       
HET     CL  C 128       1                                                       
HET    FAD  D 126      53                                                       
HET    SO4  D 127       1                                                       
HET     CL  D 128       1                                                       
HET    SO4  D 129       1                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM      CD CADMIUM ION                                                      
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5  FAD    4(C27 H33 N9 O15 P2)                                         
FORMUL   6   CL    10(CL 1-)                                                    
FORMUL   8   CD    5(CD 2+)                                                     
FORMUL  23  SO4    2(O4 S 2-)                                                   
FORMUL  26  HOH   *237(H2 O)                                                    
HELIX    1   1 ASP A   18  TYR A   36  1                                  19    
HELIX    2   2 THR A   42  TYR A   60  1                                  19    
HELIX    3   3 ASP A   68  SER A   76  1                                   9    
HELIX    4   4 THR A   82  GLY A  102  1                                  21    
HELIX    5   5 ASP A  107  SER A  109  5                                   3    
HELIX    6   6 ARG A  110  ARG A  116  1                                   7    
HELIX    7   7 ASP B   18  TYR B   36  1                                  19    
HELIX    8   8 THR B   42  TYR B   60  1                                  19    
HELIX    9   9 ASP B   68  SER B   76  1                                   9    
HELIX   10  10 THR B   82  LEU B  101  1                                  20    
HELIX   11  11 ASP B  107  SER B  109  5                                   3    
HELIX   12  12 ARG B  110  ARG B  116  1                                   7    
HELIX   13  13 ASP C   18  TYR C   36  1                                  19    
HELIX   14  14 THR C   42  TYR C   60  1                                  19    
HELIX   15  15 CYS C   62  SER C   76  1                                  15    
HELIX   16  16 THR C   82  GLY C  102  1                                  21    
HELIX   17  17 ASP C  107  SER C  109  5                                   3    
HELIX   18  18 ARG C  110  ARG C  116  1                                   7    
HELIX   19  19 ASP D   18  TYR D   36  1                                  19    
HELIX   20  20 THR D   42  TYR D   60  1                                  19    
HELIX   21  21 ASP D   68  ILE D   73  1                                   6    
HELIX   22  22 THR D   82  LEU D  101  1                                  20    
HELIX   23  23 ASP D  107  SER D  109  5                                   3    
HELIX   24  24 ARG D  110  ARG D  116  1                                   7    
SSBOND   1 CYS A   15    CYS C  124                          1555   1555  2.03  
SSBOND   2 CYS A   62    CYS A   65                          1555   1555  2.03  
SSBOND   3 CYS A   91    CYS A  108                          1555   1555  2.04  
SSBOND   4 CYS A  124    CYS C   15                          1555   1555  2.03  
SSBOND   5 CYS B   15    CYS D  124                          1555   1555  2.03  
SSBOND   6 CYS B   62    CYS B   65                          1555   1555  2.02  
SSBOND   7 CYS B   91    CYS B  108                          1555   1555  2.03  
SSBOND   8 CYS B  124    CYS D   15                          1555   1555  2.02  
SSBOND   9 CYS C   62    CYS C   65                          1555   1555  2.04  
SSBOND  10 CYS C   91    CYS C  108                          1555   1555  2.04  
SSBOND  11 CYS D   62    CYS D   65                          1555   1555  2.02  
SSBOND  12 CYS D   91    CYS D  108                          1555   1555  2.04  
LINK        CD    CD A 500                CL    CL A 502     1555   1555  2.58  
LINK        CD    CD A 500                CL    CL A 503     1555   1555  2.70  
LINK        CD    CD A 500                CL    CL A 504     1555   1555  2.49  
LINK        CD    CD A 500                 O   HOH A 506     1555   1555  2.29  
LINK         OD1 ASP A  74                CD    CD A 500     1555   1555  2.56  
LINK         OD2 ASP A  74                CD    CD A 500     1555   1555  2.37  
LINK        CD    CD A 501                CL    CL A 502     1555   1555  2.74  
LINK        CD    CD A 501                CL    CL A 503     1555   1555  2.59  
LINK        CD    CD A 501                CL    CL A 505     1555   1555  2.40  
LINK        CD    CD A 501                 O   HOH A 507     1555   1555  2.51  
LINK         OD1 ASP B  74                CD    CD A 501     1555   1555  2.48  
LINK         OD2 ASP B  74                CD    CD A 501     1555   1555  2.49  
LINK         OE1 GLU B 113                CD    CD B 130     1555   1555  2.42  
LINK        CD    CD C 127                 O   HOH C 129     1555   1555  2.52  
LINK        CD    CD B 130                 O   HOH B 138     1555   1555  2.53  
LINK        CD    CD B 130                 O   HOH B 139     1555   1555  2.55  
LINK        CD    CD B 131                 O   HOH B 141     1555   1555  2.55  
LINK         OE1 GLN B  47                CD    CD B 131     1555   1555  2.60  
LINK         OD1 ASP C 107                CD    CD C 127     1555   1555  2.62  
LINK         OE2 GLU B  44                CD    CD B 131     1555   1555  2.69  
LINK        CD    CD B 131                 O   HOH A 133     1555   1555  2.69  
CISPEP   1 GLU B   63    GLU B   64          0        -0.81                     
SITE     1 AC1 30 ARG A  19  GLU A  20  GLY A  23  ARG A  24                    
SITE     2 AC1 30 TRP A  27  HIS A  31  TYR A  60  CYS A  62                    
SITE     3 AC1 30 CYS A  65  ALA A  66  GLU A  67  CYS A  91                    
SITE     4 AC1 30 HIS A  94  ASN A  95  VAL A  97  ASN A  98                    
SITE     5 AC1 30 LEU A 101  LYS A 103  PHE A 106  ARG A 114                    
SITE     6 AC1 30 TRP A 115  HOH A 141  HOH A 143  HOH A 156                    
SITE     7 AC1 30 HOH A 162  HOH A 165  HOH A 171  HOH A 189                    
SITE     8 AC1 30 ASP C  14  HOH C 144                                          
SITE     1 AC2  5 GLU A  44  GLN A  47  HOH A 168  HOH A 223                    
SITE     2 AC2  5 HOH B 222                                                     
SITE     1 AC3  5 GLU A  44  ASP A  48  ARG B  75  LYS C  58                    
SITE     2 AC3  5 HOH C 150                                                     
SITE     1 AC4 30 ARG B  19  GLU B  20  GLY B  23  ARG B  24                    
SITE     2 AC4 30 TRP B  27  HIS B  31  TYR B  60  CYS B  62                    
SITE     3 AC4 30 CYS B  65  ALA B  66  GLU B  67  CYS B  91                    
SITE     4 AC4 30 HIS B  94  ASN B  95  VAL B  97  ASN B  98                    
SITE     5 AC4 30 LEU B 101  LYS B 103  PHE B 106  ARG B 114                    
SITE     6 AC4 30 TRP B 115  HOH B 135  HOH B 144  HOH B 151                    
SITE     7 AC4 30 HOH B 163  HOH B 172  HOH B 173  HOH B 179                    
SITE     8 AC4 30 HOH B 181  HOH B 190                                          
SITE     1 AC5  4 GLU B 113  HOH B 138  HOH B 139  HOH D 137                    
SITE     1 AC6  5 HOH A 133  HOH A 199  GLU B  44  GLN B  47                    
SITE     2 AC6  5 HOH B 141                                                     
SITE     1 AC7  4 CYS B  15  GLN B  17  HOH B 174  HOH B 185                    
SITE     1 AC8  1 ARG B  92                                                     
SITE     1 AC9 21 GLU C  20  GLY C  23  ARG C  24  TRP C  27                    
SITE     2 AC9 21 HIS C  31  TYR C  60  CYS C  65  ILE C  69                    
SITE     3 AC9 21 CYS C  91  HIS C  94  ASN C  95  VAL C  97                    
SITE     4 AC9 21 ASN C  98  LYS C 100  LEU C 101  LYS C 103                    
SITE     5 AC9 21 PHE C 106  VAL C 111  ARG C 114  TRP C 115                    
SITE     6 AC9 21 HOH C 145                                                     
SITE     1 BC1  4 ASP C 107  SER C 109  HOH C 129  HOH C 131                    
SITE     1 BC2  2 GLN C  17  ASN C  25                                          
SITE     1 BC3 24 ARG D  19  GLU D  20  GLY D  23  ARG D  24                    
SITE     2 BC3 24 TRP D  27  HIS D  31  TYR D  60  CYS D  65                    
SITE     3 BC3 24 ALA D  66  GLU D  67  ILE D  69  CYS D  91                    
SITE     4 BC3 24 HIS D  94  ASN D  95  VAL D  97  ASN D  98                    
SITE     5 BC3 24 LEU D 101  LYS D 103  PHE D 106  ARG D 114                    
SITE     6 BC3 24 TRP D 115  HOH D 130  HOH D 138  HOH D 187                    
SITE     1 BC4  3 ASP B 105  ASP D 112  HOH D 173                               
SITE     1 BC5  2 GLU D  21  HOH D 148                                          
SITE     1 BC6  2 GLN D  17  ASN D  25                                          
SITE     1 BC7  5 ASP A  74   CL A 502   CL A 503   CL A 504                    
SITE     2 BC7  5 HOH A 506                                                     
SITE     1 BC8  5  CL A 502   CL A 503   CL A 505  HOH A 507                    
SITE     2 BC8  5 ASP B  74                                                     
SITE     1 BC9  6 HIS A  54  LYS A  58   CD A 500   CD A 501                    
SITE     2 BC9  6  CL A 503  ASP B  74                                          
SITE     1 CC1  6 ASP A  74   CD A 500   CD A 501   CL A 502                    
SITE     2 CC1  6 HIS B  54  LYS B  58                                          
SITE     1 CC2  4 LYS A  58  ARG A  70   CD A 500  LYS B  58                    
SITE     1 CC3  4 LYS A  58   CD A 501  ARG B  70  ASP B  74                    
CRYST1   99.688   99.688  113.610  90.00  90.00  90.00 I 41         32          
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      0.010031  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010031  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008802        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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