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Database: PDB
Entry: 5LW1
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HEADER    DE NOVO PROTEIN                         15-SEP-16   5LW1              
TITLE     CRYSTAL STRUCTURE OF DARPIN-DARPIN RIGID FUSION, VARIANT DD_232_11_D12
TITLE    2 IN COMPLEX JNK1A1 AND JIP1 PEPTIDE                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DD_232_11_D12;                                             
COMPND   3 CHAIN: A, D, G;                                                      
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 8;                        
COMPND   7 CHAIN: B, E, H;                                                      
COMPND   8 SYNONYM: MAPK 8,JNK-46,STRESS-ACTIVATED PROTEIN KINASE 1C,SAPK1C,    
COMPND   9 STRESS-ACTIVATED PROTEIN KINASE JNK1,C-JUN N-TERMINAL KINASE 1;      
COMPND  10 EC: 2.7.11.24;                                                       
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: C-JUN-AMINO-TERMINAL KINASE-INTERACTING PROTEIN 1;         
COMPND  14 CHAIN: C, F, I;                                                      
COMPND  15 SYNONYM: JNK-INTERACTING PROTEIN 1,ISLET-BRAIN 1,IB-1,JNK MAP KINASE 
COMPND  16 SCAFFOLD PROTEIN 1,MITOGEN-ACTIVATED PROTEIN KINASE 8-INTERACTING    
COMPND  17 PROTEIN 1;                                                           
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: PEPSTATIN;                                                 
COMPND  21 CHAIN: L;                                                            
COMPND  22 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE   3 ORGANISM_TAXID: 32630;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE   6 EXPRESSION_SYSTEM_VARIANT: XL1-BLUE;                                 
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 GENE: MAPK8, JNK1, PRKM8, SAPK1, SAPK1C;                             
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE  14 EXPRESSION_SYSTEM_VARIANT: XL1-BLUE;                                 
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606;                                                
SOURCE  20 MOL_ID: 4;                                                           
SOURCE  21 SYNTHETIC: YES;                                                      
SOURCE  22 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  23 ORGANISM_TAXID: 32630                                                
KEYWDS    X-RAY CRYSTALLOGRAPHY; DESIGNED ANKYRIN REPEAT PROTEINS; PROTEIN      
KEYWDS   2 DESIGN; PROTEIN ENGINEERING; RIGID DOMAIN FUSIONS, TRANSFERASE, DE   
KEYWDS   3 NOVO PROTEIN                                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.WU,A.BATYUK,P.R.MITTL,A.HONEGGER,A.PLUECKTHUN                       
REVDAT   3   10-JUL-19 5LW1    1       JRNL                                     
REVDAT   2   13-JUN-18 5LW1    1       REMARK                                   
REVDAT   1   13-DEC-17 5LW1    0                                                
JRNL        AUTH   Y.WU,A.HONEGGER,A.BATYUK,P.R.E.MITTL,A.PLUCKTHUN             
JRNL        TITL   STRUCTURAL BASIS FOR THE SELECTIVE INHIBITION OF C-JUN       
JRNL        TITL 2 N-TERMINAL KINASE 1 DETERMINED BY RIGID DARPIN-DARPIN        
JRNL        TITL 3 FUSIONS.                                                     
JRNL        REF    J.MOL.BIOL.                   V. 430  2128 2018              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   29126898                                                     
JRNL        DOI    10.1016/J.JMB.2017.10.032                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.12_2829: ???)                              
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) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.38                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 58926                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2944                            
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 49.3888 -  8.8127    0.96     2696   135  0.1534 0.1842        
REMARK   3     2  8.8127 -  7.0013    0.99     2734   130  0.1417 0.1654        
REMARK   3     3  7.0013 -  6.1181    0.96     2604   158  0.1645 0.1997        
REMARK   3     4  6.1181 -  5.5596    0.99     2721   123  0.1614 0.2066        
REMARK   3     5  5.5596 -  5.1616    0.99     2718   135  0.1424 0.1836        
REMARK   3     6  5.1616 -  4.8575    0.99     2701   139  0.1363 0.1685        
REMARK   3     7  4.8575 -  4.6144    0.95     2586   123  0.1293 0.1637        
REMARK   3     8  4.6144 -  4.4137    0.97     2623   151  0.1424 0.1628        
REMARK   3     9  4.4137 -  4.2439    0.99     2699   151  0.1498 0.1885        
REMARK   3    10  4.2439 -  4.0975    0.99     2674   135  0.1674 0.2166        
REMARK   3    11  4.0975 -  3.9694    0.99     2679   128  0.1821 0.2256        
REMARK   3    12  3.9694 -  3.8560    0.99     2696   122  0.1886 0.2301        
REMARK   3    13  3.8560 -  3.7545    0.99     2669   169  0.1987 0.2585        
REMARK   3    14  3.7545 -  3.6630    0.99     2710   129  0.2074 0.2255        
REMARK   3    15  3.6630 -  3.5797    0.99     2655   160  0.2332 0.2433        
REMARK   3    16  3.5797 -  3.5036    0.94     2558   140  0.2754 0.3393        
REMARK   3    17  3.5036 -  3.4335    0.98     2628   125  0.2931 0.3307        
REMARK   3    18  3.4335 -  3.3687    0.98     2693   143  0.3010 0.3816        
REMARK   3    19  3.3687 -  3.3086    0.98     2654   140  0.3202 0.3607        
REMARK   3    20  3.3086 -  3.2525    0.98     2648   153  0.3525 0.3781        
REMARK   3    21  3.2525 -  3.2000    0.99     2636   155  0.3818 0.4351        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.500            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.730           
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) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.002          16587                                  
REMARK   3   ANGLE     :  0.494          22485                                  
REMARK   3   CHIRALITY :  0.041           2544                                  
REMARK   3   PLANARITY :  0.004           2870                                  
REMARK   3   DIHEDRAL  : 10.539           9907                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 34                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 6 THROUGH 23 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): 204.2690   7.2402  30.2160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8853 T22:   0.8101                                     
REMARK   3      T33:   1.2104 T12:  -0.0282                                     
REMARK   3      T13:   0.2317 T23:  -0.2734                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9559 L22:   0.0887                                     
REMARK   3      L33:   4.0455 L12:   0.2636                                     
REMARK   3      L13:   1.9521 L23:   0.6447                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5381 S12:  -1.9498 S13:   1.0946                       
REMARK   3      S21:   1.0488 S22:   0.2282 S23:   0.0884                       
REMARK   3      S31:  -0.0714 S32:  -0.1693 S33:   0.5142                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 24 THROUGH 134 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): 224.7486  -2.9631  27.9972              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6201 T22:   0.8772                                     
REMARK   3      T33:   0.6406 T12:  -0.0567                                     
REMARK   3      T13:  -0.0928 T23:  -0.1546                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3003 L22:   2.8075                                     
REMARK   3      L33:   4.5457 L12:  -0.2370                                     
REMARK   3      L13:  -2.4506 L23:   0.4215                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1482 S12:  -0.6076 S13:   0.0882                       
REMARK   3      S21:   0.2702 S22:  -0.1403 S23:   0.0323                       
REMARK   3      S31:   0.4890 S32:   0.0662 S33:   0.2551                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 135 THROUGH 181 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 243.6012  -9.0485  12.9426              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6485 T22:   0.9864                                     
REMARK   3      T33:   0.8519 T12:  -0.0925                                     
REMARK   3      T13:  -0.0239 T23:   0.0182                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4825 L22:   2.9306                                     
REMARK   3      L33:   4.0864 L12:   0.7968                                     
REMARK   3      L13:   1.1634 L23:   3.4556                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2111 S12:   0.2324 S13:   0.2887                       
REMARK   3      S21:  -0.2522 S22:   0.2423 S23:  -0.9179                       
REMARK   3      S31:  -0.4189 S32:   0.5536 S33:  -0.2055                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 182 THROUGH 325 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 230.8307 -25.1994  -6.4433              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5339 T22:   0.6800                                     
REMARK   3      T33:   0.8850 T12:   0.0209                                     
REMARK   3      T13:   0.1263 T23:  -0.0181                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5625 L22:   4.0202                                     
REMARK   3      L33:   8.6290 L12:   0.6572                                     
REMARK   3      L13:   2.3872 L23:   0.1229                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0474 S12:   0.2313 S13:  -0.2248                       
REMARK   3      S21:   0.0264 S22:   0.2502 S23:   0.1198                       
REMARK   3      S31:   0.3013 S32:   0.2419 S33:  -0.2621                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 8 THROUGH 29 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): 278.2535  11.6926  35.9807              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0614 T22:   1.4686                                     
REMARK   3      T33:   1.3406 T12:  -0.2624                                     
REMARK   3      T13:  -0.2877 T23:   0.1463                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4638 L22:   7.2216                                     
REMARK   3      L33:   8.7922 L12:  -0.7881                                     
REMARK   3      L13:  -3.8966 L23:  -2.7880                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7287 S12:  -0.5643 S13:  -0.0682                       
REMARK   3      S21:   0.1451 S22:  -0.0411 S23:  -1.4136                       
REMARK   3      S31:   0.2371 S32:   1.5638 S33:   0.5815                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 30 THROUGH 63 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): 270.2220  14.8826  32.4744              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6950 T22:   1.1387                                     
REMARK   3      T33:   0.7467 T12:  -0.2223                                     
REMARK   3      T13:  -0.1110 T23:   0.2503                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4360 L22:   6.2929                                     
REMARK   3      L33:   5.4146 L12:  -0.1888                                     
REMARK   3      L13:   0.7220 L23:   2.2095                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2264 S12:  -0.3002 S13:  -0.3377                       
REMARK   3      S21:  -0.1083 S22:   0.1030 S23:  -0.5868                       
REMARK   3      S31:  -0.3111 S32:   0.9127 S33:   0.2446                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 64 THROUGH 144 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): 262.0556  20.8310  26.0678              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7639 T22:   0.8647                                     
REMARK   3      T33:   0.6096 T12:  -0.2199                                     
REMARK   3      T13:  -0.1010 T23:   0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9886 L22:   6.4179                                     
REMARK   3      L33:   1.8810 L12:  -3.3966                                     
REMARK   3      L13:  -0.6890 L23:  -0.7200                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1441 S12:  -0.1724 S13:   0.3333                       
REMARK   3      S21:   0.3714 S22:  -0.0153 S23:  -0.6986                       
REMARK   3      S31:  -0.4751 S32:   0.6066 S33:   0.1613                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 145 THROUGH 191 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 253.6025  18.2783  28.5055              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9334 T22:   0.7812                                     
REMARK   3      T33:   0.5866 T12:  -0.1316                                     
REMARK   3      T13:  -0.0932 T23:   0.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4571 L22:   2.7240                                     
REMARK   3      L33:   2.5533 L12:  -0.7268                                     
REMARK   3      L13:  -0.6222 L23:  -1.8118                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1303 S12:  -0.0072 S13:  -0.1420                       
REMARK   3      S21:  -0.2457 S22:  -0.3806 S23:   0.1628                       
REMARK   3      S31:  -0.0827 S32:   0.1421 S33:   0.1694                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 192 THROUGH 270 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 234.9298  18.2238  27.5132              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7978 T22:   0.7273                                     
REMARK   3      T33:   0.6175 T12:   0.0550                                     
REMARK   3      T13:  -0.0445 T23:  -0.0408                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3260 L22:   5.5434                                     
REMARK   3      L33:   2.1067 L12:   2.3183                                     
REMARK   3      L13:   0.2288 L23:   0.2863                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2029 S12:  -0.4101 S13:   0.0502                       
REMARK   3      S21:   0.0595 S22:  -0.2181 S23:   0.2905                       
REMARK   3      S31:  -0.2839 S32:  -0.4278 S33:   0.0482                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 271 THROUGH 321 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 240.2289  36.0733  27.1250              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1530 T22:   0.6623                                     
REMARK   3      T33:   0.9521 T12:   0.0461                                     
REMARK   3      T13:  -0.1048 T23:  -0.0680                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1523 L22:   6.6451                                     
REMARK   3      L33:   6.4240 L12:   2.2661                                     
REMARK   3      L13:  -0.9322 L23:  -1.1261                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2547 S12:  -0.3027 S13:   1.1012                       
REMARK   3      S21:   0.2442 S22:  -0.2807 S23:   1.0220                       
REMARK   3      S31:  -1.5174 S32:   0.1641 S33:   0.0488                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 322 THROUGH 362 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 262.5103  15.6041  14.8143              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6168 T22:   0.8633                                     
REMARK   3      T33:   0.6840 T12:  -0.1394                                     
REMARK   3      T13:   0.0340 T23:   0.0601                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8718 L22:   7.1283                                     
REMARK   3      L33:   3.8407 L12:  -1.8128                                     
REMARK   3      L13:   0.3079 L23:  -0.7701                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4190 S12:   0.4184 S13:   0.1400                       
REMARK   3      S21:  -0.7680 S22:  -0.6412 S23:   0.0920                       
REMARK   3      S31:  -0.3001 S32:   0.6853 S33:   0.2750                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 154 THROUGH 162 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 259.0122  40.2076  33.6161              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1527 T22:   1.1382                                     
REMARK   3      T33:   0.8659 T12:  -0.4446                                     
REMARK   3      T13:  -0.1359 T23:  -0.1313                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6188 L22:   4.4208                                     
REMARK   3      L33:   7.6314 L12:  -1.7424                                     
REMARK   3      L13:   2.7866 L23:  -5.7964                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4672 S12:   0.3063 S13:   2.0319                       
REMARK   3      S21:   0.5002 S22:  -0.9695 S23:  -0.1971                       
REMARK   3      S31:  -2.8392 S32:   1.9797 S33:   1.8084                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 13 THROUGH 134 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): 281.3107 -26.9888  49.6597              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0388 T22:   0.7904                                     
REMARK   3      T33:   0.6117 T12:   0.1144                                     
REMARK   3      T13:   0.0969 T23:   0.0861                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5410 L22:   4.7460                                     
REMARK   3      L33:   5.9066 L12:  -0.8251                                     
REMARK   3      L13:   2.3150 L23:  -1.8150                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1232 S12:  -0.2116 S13:  -0.0800                       
REMARK   3      S21:   0.1369 S22:   0.2770 S23:   0.3187                       
REMARK   3      S31:  -0.3072 S32:   0.0088 S33:  -0.4134                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 135 THROUGH 181 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 268.2551 -12.6891  32.0444              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5483 T22:   0.9113                                     
REMARK   3      T33:   0.8469 T12:   0.1324                                     
REMARK   3      T13:  -0.0699 T23:   0.0481                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2763 L22:   2.8907                                     
REMARK   3      L33:   0.9248 L12:  -2.7376                                     
REMARK   3      L13:  -1.4179 L23:   0.1632                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5889 S12:   0.6012 S13:  -0.1906                       
REMARK   3      S21:  -1.3576 S22:  -0.5124 S23:  -0.0685                       
REMARK   3      S31:   0.3614 S32:  -0.1234 S33:  -0.0713                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 182 THROUGH 325 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 251.7870   4.9343  47.3345              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8038 T22:   0.8735                                     
REMARK   3      T33:   0.5927 T12:  -0.0804                                     
REMARK   3      T13:  -0.1402 T23:   0.1016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4885 L22:   7.4012                                     
REMARK   3      L33:   5.1691 L12:  -0.8949                                     
REMARK   3      L13:  -1.3023 L23:   1.8585                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0187 S12:  -0.3325 S13:  -0.0486                       
REMARK   3      S21:   0.4936 S22:  -0.0492 S23:   0.1793                       
REMARK   3      S31:   0.2371 S32:   0.2395 S33:   0.0054                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 8 THROUGH 29 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): 289.6862 -29.9317  -6.7884              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6578 T22:   0.7136                                     
REMARK   3      T33:   1.0600 T12:   0.1853                                     
REMARK   3      T13:   0.1067 T23:  -0.1465                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0999 L22:   6.2063                                     
REMARK   3      L33:   8.4918 L12:  -2.4714                                     
REMARK   3      L13:   2.2236 L23:  -4.9858                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2335 S12:   0.4653 S13:  -0.2004                       
REMARK   3      S21:   0.3051 S22:   0.4780 S23:   0.4937                       
REMARK   3      S31:  -1.9877 S32:   0.0488 S33:  -0.8829                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 30 THROUGH 63 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): 292.9514 -26.0822   1.0384              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6292 T22:   0.6511                                     
REMARK   3      T33:   0.8421 T12:   0.1504                                     
REMARK   3      T13:   0.0260 T23:  -0.0960                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4783 L22:   5.3178                                     
REMARK   3      L33:   7.3609 L12:  -3.1579                                     
REMARK   3      L13:   0.9115 L23:   0.3233                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8626 S12:   0.0217 S13:  -0.5981                       
REMARK   3      S21:   0.2184 S22:  -0.4207 S23:  -0.1723                       
REMARK   3      S31:  -1.8478 S32:   0.1073 S33:  -0.4388                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 64 THROUGH 92 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): 292.8877 -14.8261   7.2676              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.3551 T22:   0.8982                                     
REMARK   3      T33:   0.8112 T12:   0.1684                                     
REMARK   3      T13:   0.2544 T23:  -0.2560                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6700 L22:   5.2591                                     
REMARK   3      L33:   2.4424 L12:  -1.1930                                     
REMARK   3      L13:   1.7638 L23:  -1.7508                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2355 S12:  -0.3404 S13:   0.2753                       
REMARK   3      S21:  -1.9671 S22:   0.0160 S23:   0.7885                       
REMARK   3      S31:  -2.2232 S32:   0.0645 S33:  -0.1224                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 93 THROUGH 114 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): 287.9113 -22.4537  -0.1558              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7867 T22:   0.6726                                     
REMARK   3      T33:   0.9391 T12:   0.2151                                     
REMARK   3      T13:   0.0321 T23:  -0.1380                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6291 L22:   4.0809                                     
REMARK   3      L33:   7.3166 L12:  -1.4712                                     
REMARK   3      L13:   2.0127 L23:  -0.5212                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0337 S12:   0.2420 S13:   0.0850                       
REMARK   3      S21:  -1.0407 S22:   0.1991 S23:   0.5589                       
REMARK   3      S31:  -1.7050 S32:  -0.4940 S33:  -0.1364                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 115 THROUGH 164 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 308.4224 -20.2314  15.8247              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4987 T22:   1.0439                                     
REMARK   3      T33:   1.0141 T12:  -0.4289                                     
REMARK   3      T13:   0.2247 T23:  -0.1848                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3293 L22:   6.0230                                     
REMARK   3      L33:   7.7735 L12:  -2.4014                                     
REMARK   3      L13:   0.5409 L23:   2.1803                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2886 S12:   0.0679 S13:  -0.3293                       
REMARK   3      S21:  -1.0034 S22:   0.0384 S23:  -0.9337                       
REMARK   3      S31:  -0.7198 S32:   1.4590 S33:  -0.2565                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 165 THROUGH 182 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 292.7835 -19.3988  17.3845              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3495 T22:   1.0420                                     
REMARK   3      T33:   1.1505 T12:  -0.0567                                     
REMARK   3      T13:   0.1382 T23:  -0.0088                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7054 L22:   6.2498                                     
REMARK   3      L33:   9.1331 L12:  -3.9950                                     
REMARK   3      L13:  -5.1140 L23:   4.0990                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.9202 S12:  -0.7444 S13:   0.3251                       
REMARK   3      S21:  -0.2136 S22:  -0.2011 S23:   0.6743                       
REMARK   3      S31:  -1.1937 S32:  -0.3828 S33:  -1.0414                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 183 THROUGH 241 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 300.3209 -24.3690  29.4732              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9060 T22:   1.0254                                     
REMARK   3      T33:   0.9022 T12:  -0.0718                                     
REMARK   3      T13:   0.0444 T23:  -0.1218                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7442 L22:   2.3403                                     
REMARK   3      L33:   8.8764 L12:   1.7298                                     
REMARK   3      L13:   0.1293 L23:   1.2650                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0798 S12:  -0.3330 S13:  -0.2381                       
REMARK   3      S21:   0.0711 S22:   0.2011 S23:  -0.1719                       
REMARK   3      S31:  -0.7673 S32:   0.9400 S33:  -0.2711                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 242 THROUGH 270 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 297.2050 -19.0104  44.4692              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2721 T22:   1.1839                                     
REMARK   3      T33:   0.6030 T12:  -0.1362                                     
REMARK   3      T13:   0.0032 T23:  -0.2182                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1554 L22:   5.1327                                     
REMARK   3      L33:   7.2001 L12:   0.4217                                     
REMARK   3      L13:  -2.3488 L23:   0.9550                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5777 S12:  -0.7109 S13:   0.0478                       
REMARK   3      S21:   0.6286 S22:  -0.0537 S23:  -0.2330                       
REMARK   3      S31:  -0.9342 S32:   1.2044 S33:  -0.4861                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 271 THROUGH 321 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 316.4456 -17.7381  28.7815              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2261 T22:   1.5911                                     
REMARK   3      T33:   1.3165 T12:  -0.5228                                     
REMARK   3      T13:   0.0179 T23:  -0.3535                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5187 L22:   4.9434                                     
REMARK   3      L33:   2.2960 L12:  -2.2377                                     
REMARK   3      L13:  -0.9660 L23:   0.0607                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1653 S12:  -0.6238 S13:   0.0899                       
REMARK   3      S21:  -0.1789 S22:   0.0909 S23:  -0.7506                       
REMARK   3      S31:  -0.9072 S32:   1.2176 S33:  -0.2539                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 322 THROUGH 362 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 291.3342  -8.9533   9.4950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1176 T22:   1.0509                                     
REMARK   3      T33:   1.1236 T12:   0.1634                                     
REMARK   3      T13:   0.0265 T23:   0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1622 L22:   2.5595                                     
REMARK   3      L33:   5.0030 L12:  -0.7452                                     
REMARK   3      L13:   2.6510 L23:   1.7265                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2171 S12:  -0.6652 S13:   1.0411                       
REMARK   3      S21:  -0.6250 S22:  -0.2334 S23:   0.2089                       
REMARK   3      S31:  -2.2705 S32:  -0.1560 S33:   0.4159                       
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 154 THROUGH 162 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 319.6066 -22.6854   9.1081              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4000 T22:   1.6866                                     
REMARK   3      T33:   1.2976 T12:  -0.3092                                     
REMARK   3      T13:   0.3455 T23:  -0.1941                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2379 L22:   6.2711                                     
REMARK   3      L33:   6.2596 L12:   5.6200                                     
REMARK   3      L13:  -5.5675 L23:  -5.6941                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7259 S12:  -1.3050 S13:  -0.8225                       
REMARK   3      S21:  -3.5047 S22:   1.2022 S23:  -3.3113                       
REMARK   3      S31:  -0.4473 S32:   2.0012 S33:  -0.6948                       
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESID 13 THROUGH 181 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): 259.2815 -43.5705  -2.7402              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8650 T22:   0.8755                                     
REMARK   3      T33:   1.4305 T12:   0.1876                                     
REMARK   3      T13:  -0.0115 T23:   0.0554                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8335 L22:   3.1429                                     
REMARK   3      L33:   6.1149 L12:   1.6969                                     
REMARK   3      L13:   3.0719 L23:   2.3485                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0902 S12:  -0.1617 S13:  -0.1669                       
REMARK   3      S21:  -0.2062 S22:   0.2248 S23:  -0.0905                       
REMARK   3      S31:   0.4529 S32:  -0.0919 S33:  -0.3975                       
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESID 182 THROUGH 326 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 288.5765 -43.2050  19.5477              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6900 T22:   0.6885                                     
REMARK   3      T33:   0.8584 T12:   0.1069                                     
REMARK   3      T13:  -0.0697 T23:  -0.1247                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5078 L22:   5.4336                                     
REMARK   3      L33:   4.9918 L12:  -1.0628                                     
REMARK   3      L13:  -1.2050 L23:   0.8563                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1003 S12:  -0.2605 S13:  -0.2937                       
REMARK   3      S21:   0.0462 S22:   0.1225 S23:  -0.2301                       
REMARK   3      S31:   0.2758 S32:   0.3369 S33:  -0.2434                       
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 8 THROUGH 145 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): 242.6880  -3.3725 -16.6150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5521 T22:   0.7794                                     
REMARK   3      T33:   0.9293 T12:  -0.0895                                     
REMARK   3      T13:   0.0673 T23:   0.1192                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8770 L22:   3.7311                                     
REMARK   3      L33:   3.6219 L12:  -0.8268                                     
REMARK   3      L13:  -0.5008 L23:   0.9930                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0036 S12:   0.2688 S13:   0.4482                       
REMARK   3      S21:   0.2299 S22:  -0.1232 S23:  -0.1029                       
REMARK   3      S31:  -0.0879 S32:   0.0271 S33:   0.1243                       
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 146 THROUGH 191 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 246.9072 -15.3359 -19.6478              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5669 T22:   1.0003                                     
REMARK   3      T33:   0.9465 T12:  -0.0456                                     
REMARK   3      T13:   0.1209 T23:   0.0537                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3215 L22:   5.3431                                     
REMARK   3      L33:   1.3693 L12:  -0.8143                                     
REMARK   3      L13:  -0.8872 L23:   0.6776                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3550 S12:   0.2179 S13:  -0.2076                       
REMARK   3      S21:   0.2882 S22:  -0.1491 S23:  -0.2112                       
REMARK   3      S31:   0.1560 S32:   0.6849 S33:  -0.0747                       
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 192 THROUGH 290 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 251.4248 -30.9695 -27.9150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8024 T22:   0.8658                                     
REMARK   3      T33:   0.9022 T12:   0.1521                                     
REMARK   3      T13:   0.1436 T23:  -0.1583                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0295 L22:   4.2763                                     
REMARK   3      L33:   4.7518 L12:  -1.4615                                     
REMARK   3      L13:   2.2265 L23:  -2.0448                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3547 S12:   0.5073 S13:  -0.4764                       
REMARK   3      S21:  -0.5810 S22:  -0.0477 S23:  -0.3988                       
REMARK   3      S31:   0.5352 S32:   0.2611 S33:  -0.1821                       
REMARK   3   TLS GROUP : 32                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 291 THROUGH 362 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 256.8726 -11.2544 -24.0553              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6712 T22:   1.0262                                     
REMARK   3      T33:   1.0448 T12:   0.0840                                     
REMARK   3      T13:   0.1437 T23:   0.1405                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8278 L22:   2.3652                                     
REMARK   3      L33:   4.5882 L12:  -0.4147                                     
REMARK   3      L13:  -0.5472 L23:   1.7182                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0562 S12:   0.4653 S13:   0.5486                       
REMARK   3      S21:  -0.3158 S22:  -0.0589 S23:  -0.5750                       
REMARK   3      S31:  -0.2386 S32:   0.7363 S33:   0.0690                       
REMARK   3   TLS GROUP : 33                                                     
REMARK   3    SELECTION: CHAIN 'I' AND (RESID 154 THROUGH 163 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 237.6082  -7.5924 -40.8526              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8760 T22:   1.5261                                     
REMARK   3      T33:   1.1303 T12:   0.3215                                     
REMARK   3      T13:   0.2534 T23:   0.2766                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0619 L22:   1.9382                                     
REMARK   3      L33:   7.0686 L12:   2.2832                                     
REMARK   3      L13:  -0.7935 L23:  -0.3774                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4675 S12:   2.5168 S13:   1.5758                       
REMARK   3      S21:  -0.3309 S22:  -0.6725 S23:   0.3902                       
REMARK   3      S31:   1.0120 S32:  -0.7862 S33:   0.2453                       
REMARK   3   TLS GROUP : 34                                                     
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 2 THROUGH 5 )                     
REMARK   3    ORIGIN FOR THE GROUP (A): 264.6813 -28.4630 -10.6279              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1031 T22:   1.4907                                     
REMARK   3      T33:   2.1403 T12:  -0.3748                                     
REMARK   3      T13:   1.0033 T23:  -0.1814                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1055 L22:   2.1949                                     
REMARK   3      L33:   4.4078 L12:  -0.4809                                     
REMARK   3      L13:   0.6821 L23:  -3.1112                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0335 S12:   2.2822 S13:   0.0713                       
REMARK   3      S21:  -0.2804 S22:   0.1196 S23:  -0.7471                       
REMARK   3      S31:  -0.2033 S32:   0.8212 S33:   0.4466                       
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 5LW1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-SEP-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200001070.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-SEP-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000000                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58948                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.383                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.13450                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.2700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.84200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.130                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1SVX CHAIN A AND 1UKH                                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM SULFATE 1.8 M TRIS 0.1 M         
REMARK 280  ADDITIVES (0.002% W/V) ADENOSINE, PEPSTATIN A EPINEPHRINE SODIUM    
REMARK 280  PHENYL PHOSPHATE DIBASIC DEHYDRATE INOSINE 5-TRIPHOSPHATE           
REMARK 280  TRISODIUM SALT PH 8.5, VAPOR DIFFUSION, SITTING DROP,               
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      109.99500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       70.88000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      109.99500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       70.88000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, L                            
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 APPLY THE FOLLOWING TO CHAINS: D, E, F                               
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I                               
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400                                                                      
REMARK 400 THE PEPSTATIN IS OLIGOPEPTIDE, A MEMBER OF ENZYME INHIBITOR CLASS.   
REMARK 400                                                                      
REMARK 400  GROUP: 1                                                            
REMARK 400   NAME: PEPSTATIN                                                    
REMARK 400   CHAIN: L                                                           
REMARK 400   COMPONENT_1: PEPTIDE LIKE POLYMER                                  
REMARK 400   DESCRIPTION: NULL                                                  
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     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     ALA A   326                                                      
REMARK 465     MET B    -9                                                      
REMARK 465     ARG B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     SER B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     ASP B     7                                                      
REMARK 465     LEU B   363                                                      
REMARK 465     ARG C   153                                                      
REMARK 465     PHE C   163                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ARG D     2                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     HIS D     5                                                      
REMARK 465     HIS D     6                                                      
REMARK 465     HIS D     7                                                      
REMARK 465     HIS D     8                                                      
REMARK 465     HIS D     9                                                      
REMARK 465     HIS D    10                                                      
REMARK 465     GLY D    11                                                      
REMARK 465     SER D    12                                                      
REMARK 465     ALA D   326                                                      
REMARK 465     MET E    -9                                                      
REMARK 465     ARG E    -8                                                      
REMARK 465     GLY E    -7                                                      
REMARK 465     SER E    -6                                                      
REMARK 465     HIS E    -5                                                      
REMARK 465     HIS E    -4                                                      
REMARK 465     HIS E    -3                                                      
REMARK 465     HIS E    -2                                                      
REMARK 465     HIS E    -1                                                      
REMARK 465     HIS E     0                                                      
REMARK 465     GLY E     1                                                      
REMARK 465     SER E     2                                                      
REMARK 465     ARG E     3                                                      
REMARK 465     SER E     4                                                      
REMARK 465     LYS E     5                                                      
REMARK 465     ARG E     6                                                      
REMARK 465     ASP E     7                                                      
REMARK 465     LEU E   363                                                      
REMARK 465     ARG F   153                                                      
REMARK 465     PHE F   163                                                      
REMARK 465     MET G     1                                                      
REMARK 465     ARG G     2                                                      
REMARK 465     GLY G     3                                                      
REMARK 465     SER G     4                                                      
REMARK 465     HIS G     5                                                      
REMARK 465     HIS G     6                                                      
REMARK 465     HIS G     7                                                      
REMARK 465     HIS G     8                                                      
REMARK 465     HIS G     9                                                      
REMARK 465     HIS G    10                                                      
REMARK 465     GLY G    11                                                      
REMARK 465     SER G    12                                                      
REMARK 465     MET H    -9                                                      
REMARK 465     ARG H    -8                                                      
REMARK 465     GLY H    -7                                                      
REMARK 465     SER H    -6                                                      
REMARK 465     HIS H    -5                                                      
REMARK 465     HIS H    -4                                                      
REMARK 465     HIS H    -3                                                      
REMARK 465     HIS H    -2                                                      
REMARK 465     HIS H    -1                                                      
REMARK 465     HIS H     0                                                      
REMARK 465     GLY H     1                                                      
REMARK 465     SER H     2                                                      
REMARK 465     ARG H     3                                                      
REMARK 465     SER H     4                                                      
REMARK 465     LYS H     5                                                      
REMARK 465     ARG H     6                                                      
REMARK 465     ASP H     7                                                      
REMARK 465     LEU H   363                                                      
REMARK 465     ARG I   153                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    STA L   4   C   -  N   -  CA  ANGL. DEV. =  18.1 DEGREES          
REMARK 500    STA L   4   CA  -  C   -  N   ANGL. DEV. =  36.5 DEGREES          
REMARK 500    STA L   4   O   -  C   -  N   ANGL. DEV. = -22.2 DEGREES          
REMARK 500    ALA L   5   C   -  N   -  CA  ANGL. DEV. =  25.7 DEGREES          
REMARK 500    ALA L   5   O   -  C   -  N   ANGL. DEV. = -12.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 110     -165.94   -104.80                                   
REMARK 500    ASP A 143     -161.70   -108.91                                   
REMARK 500    HIS A 282       78.85   -106.86                                   
REMARK 500    GLN B 102      -64.23   -138.87                                   
REMARK 500    ASP B 151       28.73   -145.10                                   
REMARK 500    ASN B 322       -8.24    -58.36                                   
REMARK 500    GLU B 331       41.82    -94.37                                   
REMARK 500    GLN B 341       55.80   -104.45                                   
REMARK 500    ASP D 110     -166.67   -103.71                                   
REMARK 500    ASP D 143     -161.72   -107.14                                   
REMARK 500    GLN E 102      -65.54   -139.37                                   
REMARK 500    ASP E 151       30.00   -144.05                                   
REMARK 500    ASN E 322       -7.89    -59.30                                   
REMARK 500    GLU E 331       42.16    -94.25                                   
REMARK 500    GLN E 341       51.40   -104.00                                   
REMARK 500    ASP G 110     -167.41   -101.91                                   
REMARK 500    ASP G 143     -160.17   -108.09                                   
REMARK 500    HIS G 282       78.41   -106.95                                   
REMARK 500    GLN H 102      -64.54   -139.13                                   
REMARK 500    ASP H 151       30.38   -143.88                                   
REMARK 500    LYS H 203     -169.63   -104.82                                   
REMARK 500    ASN H 322       -7.41    -58.71                                   
REMARK 500    GLU H 331       42.98    -92.54                                   
REMARK 500    GLN H 341       52.06   -103.78                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 STA L    4     ALA L    5                 -115.78                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    VAL L   3        -20.00                                           
REMARK 500    STA L   4         35.90                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ADN B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ADN E 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ADN H 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 I 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide IVA L 1 and VAL L 2    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide VAL L 3 and STA L 4    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide STA L 4 and ALA L 5    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ALA L 5 and STA L 6    
DBREF  5LW1 A    1   326  PDB    5LW1     5LW1             1    326             
DBREF  5LW1 B    2   363  UNP    P45983   MK08_HUMAN       2    363             
DBREF  5LW1 C  153   163  UNP    Q9UQF2   JIP1_HUMAN     157    167             
DBREF  5LW1 D    1   326  PDB    5LW1     5LW1             1    326             
DBREF  5LW1 E    2   363  UNP    P45983   MK08_HUMAN       2    363             
DBREF  5LW1 F  153   163  UNP    Q9UQF2   JIP1_HUMAN     157    167             
DBREF  5LW1 G    1   326  PDB    5LW1     5LW1             1    326             
DBREF  5LW1 H    2   363  UNP    P45983   MK08_HUMAN       2    363             
DBREF  5LW1 I  153   163  UNP    Q9UQF2   JIP1_HUMAN     157    167             
DBREF  5LW1 L    1     6  PDB    5LW1     5LW1             1      6             
SEQADV 5LW1 MET B   -9  UNP  P45983              INITIATING METHIONINE          
SEQADV 5LW1 ARG B   -8  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 GLY B   -7  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 SER B   -6  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 HIS B   -5  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 HIS B   -4  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 HIS B   -3  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 HIS B   -2  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 HIS B   -1  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 HIS B    0  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 GLY B    1  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 MET E   -9  UNP  P45983              INITIATING METHIONINE          
SEQADV 5LW1 ARG E   -8  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 GLY E   -7  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 SER E   -6  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 HIS E   -5  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 HIS E   -4  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 HIS E   -3  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 HIS E   -2  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 HIS E   -1  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 HIS E    0  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 GLY E    1  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 MET H   -9  UNP  P45983              INITIATING METHIONINE          
SEQADV 5LW1 ARG H   -8  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 GLY H   -7  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 SER H   -6  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 HIS H   -5  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 HIS H   -4  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 HIS H   -3  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 HIS H   -2  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 HIS H   -1  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 HIS H    0  UNP  P45983              EXPRESSION TAG                 
SEQADV 5LW1 GLY H    1  UNP  P45983              EXPRESSION TAG                 
SEQRES   1 A  326  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP          
SEQRES   2 A  326  LEU GLY LYS LYS LEU LEU GLU ALA ALA ARG ALA GLY GLN          
SEQRES   3 A  326  ASP ASP GLU VAL ARG ILE LEU MET ALA ASN GLY ALA ASP          
SEQRES   4 A  326  VAL ASN ALA SER ASP GLN LEU GLY ILE THR PRO LEU HIS          
SEQRES   5 A  326  LEU VAL ALA ILE THR GLY HIS LEU GLU ILE VAL GLU VAL          
SEQRES   6 A  326  LEU LEU LYS ASN GLY ALA ASP VAL ASN ALA HIS ASP PHE          
SEQRES   7 A  326  VAL GLY THR THR PRO LEU HIS LEU ALA ALA PHE LEU GLY          
SEQRES   8 A  326  HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS TYR GLY ALA          
SEQRES   9 A  326  ASP VAL ASN ALA VAL ASP ARG ASP GLY LEU THR PRO LEU          
SEQRES  10 A  326  HIS LEU ALA ALA ILE HIS GLY HIS LEU GLU ILE VAL GLU          
SEQRES  11 A  326  VAL LEU LEU LYS HIS GLY ALA LEU VAL LYS ALA LYS ASP          
SEQRES  12 A  326  LYS PHE GLY LYS THR PRO LYS ASP LEU ALA ARG ASP ASN          
SEQRES  13 A  326  GLY ASN GLN PHE ILE TYR GLU LEU LEU GLU LYS ALA GLU          
SEQRES  14 A  326  LEU LEU GLU LYS LEU LEU LEU GLU ALA ALA ARG GLU GLY          
SEQRES  15 A  326  HIS ARG ASP ARG VAL GLU GLU PHE ILE LYS ARG GLY ALA          
SEQRES  16 A  326  ASP VAL ASN THR ALA ASP GLU THR GLY PHE THR PRO LEU          
SEQRES  17 A  326  HIS LEU ALA ALA TRP GLU GLY HIS LEU GLY ILE VAL GLU          
SEQRES  18 A  326  VAL LEU LEU LYS ASN GLY ALA ASP VAL ASN ALA ASN ASP          
SEQRES  19 A  326  GLU ARG GLY HIS THR PRO LEU HIS LEU ALA ALA TYR THR          
SEQRES  20 A  326  GLY HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS ASN GLY          
SEQRES  21 A  326  ALA GLY VAL ASN ALA THR ASP VAL ILE GLY THR ALA PRO          
SEQRES  22 A  326  LEU HIS LEU ALA ALA MET TRP GLY HIS LEU GLU ILE VAL          
SEQRES  23 A  326  GLU VAL LEU LEU LYS HIS GLY ALA ASP VAL ASN ALA GLN          
SEQRES  24 A  326  ASP LYS PHE GLY LYS THR PRO PHE ASP LEU ALA ILE ASP          
SEQRES  25 A  326  ASN GLY ASN GLU ASP ILE ALA GLU VAL LEU GLN LYS ALA          
SEQRES  26 A  326  ALA                                                          
SEQRES   1 B  373  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ARG          
SEQRES   2 B  373  SER LYS ARG ASP ASN ASN PHE TYR SER VAL GLU ILE GLY          
SEQRES   3 B  373  ASP SER THR PHE THR VAL LEU LYS ARG TYR GLN ASN LEU          
SEQRES   4 B  373  LYS PRO ILE GLY SER GLY ALA GLN GLY ILE VAL CYS ALA          
SEQRES   5 B  373  ALA TYR ASP ALA ILE LEU GLU ARG ASN VAL ALA ILE LYS          
SEQRES   6 B  373  LYS LEU SER ARG PRO PHE GLN ASN GLN THR HIS ALA LYS          
SEQRES   7 B  373  ARG ALA TYR ARG GLU LEU VAL LEU MET LYS CYS VAL ASN          
SEQRES   8 B  373  HIS LYS ASN ILE ILE GLY LEU LEU ASN VAL PHE THR PRO          
SEQRES   9 B  373  GLN LYS SER LEU GLU GLU PHE GLN ASP VAL TYR ILE VAL          
SEQRES  10 B  373  MET GLU LEU MET ASP ALA ASN LEU CYS GLN VAL ILE GLN          
SEQRES  11 B  373  MET GLU LEU ASP HIS GLU ARG MET SER TYR LEU LEU TYR          
SEQRES  12 B  373  GLN MET LEU CYS GLY ILE LYS HIS LEU HIS SER ALA GLY          
SEQRES  13 B  373  ILE ILE HIS ARG ASP LEU LYS PRO SER ASN ILE VAL VAL          
SEQRES  14 B  373  LYS SER ASP CYS THR LEU LYS ILE LEU ASP PHE GLY LEU          
SEQRES  15 B  373  ALA ARG THR ALA GLY THR SER PHE MET MET THR PRO TYR          
SEQRES  16 B  373  VAL VAL THR ARG TYR TYR ARG ALA PRO GLU VAL ILE LEU          
SEQRES  17 B  373  GLY MET GLY TYR LYS GLU ASN VAL ASP LEU TRP SER VAL          
SEQRES  18 B  373  GLY CYS ILE MET GLY GLU MET VAL CYS HIS LYS ILE LEU          
SEQRES  19 B  373  PHE PRO GLY ARG ASP TYR ILE ASP GLN TRP ASN LYS VAL          
SEQRES  20 B  373  ILE GLU GLN LEU GLY THR PRO CYS PRO GLU PHE MET LYS          
SEQRES  21 B  373  LYS LEU GLN PRO THR VAL ARG THR TYR VAL GLU ASN ARG          
SEQRES  22 B  373  PRO LYS TYR ALA GLY TYR SER PHE GLU LYS LEU PHE PRO          
SEQRES  23 B  373  ASP VAL LEU PHE PRO ALA ASP SER GLU HIS ASN LYS LEU          
SEQRES  24 B  373  LYS ALA SER GLN ALA ARG ASP LEU LEU SER LYS MET LEU          
SEQRES  25 B  373  VAL ILE ASP ALA SER LYS ARG ILE SER VAL ASP GLU ALA          
SEQRES  26 B  373  LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR ASP PRO SER          
SEQRES  27 B  373  GLU ALA GLU ALA PRO PRO PRO LYS ILE PRO ASP LYS GLN          
SEQRES  28 B  373  LEU ASP GLU ARG GLU HIS THR ILE GLU GLU TRP LYS GLU          
SEQRES  29 B  373  LEU ILE TYR LYS GLU VAL MET ASP LEU                          
SEQRES   1 C   11  ARG PRO LYS ARG PRO THR THR LEU ASN LEU PHE                  
SEQRES   1 D  326  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP          
SEQRES   2 D  326  LEU GLY LYS LYS LEU LEU GLU ALA ALA ARG ALA GLY GLN          
SEQRES   3 D  326  ASP ASP GLU VAL ARG ILE LEU MET ALA ASN GLY ALA ASP          
SEQRES   4 D  326  VAL ASN ALA SER ASP GLN LEU GLY ILE THR PRO LEU HIS          
SEQRES   5 D  326  LEU VAL ALA ILE THR GLY HIS LEU GLU ILE VAL GLU VAL          
SEQRES   6 D  326  LEU LEU LYS ASN GLY ALA ASP VAL ASN ALA HIS ASP PHE          
SEQRES   7 D  326  VAL GLY THR THR PRO LEU HIS LEU ALA ALA PHE LEU GLY          
SEQRES   8 D  326  HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS TYR GLY ALA          
SEQRES   9 D  326  ASP VAL ASN ALA VAL ASP ARG ASP GLY LEU THR PRO LEU          
SEQRES  10 D  326  HIS LEU ALA ALA ILE HIS GLY HIS LEU GLU ILE VAL GLU          
SEQRES  11 D  326  VAL LEU LEU LYS HIS GLY ALA LEU VAL LYS ALA LYS ASP          
SEQRES  12 D  326  LYS PHE GLY LYS THR PRO LYS ASP LEU ALA ARG ASP ASN          
SEQRES  13 D  326  GLY ASN GLN PHE ILE TYR GLU LEU LEU GLU LYS ALA GLU          
SEQRES  14 D  326  LEU LEU GLU LYS LEU LEU LEU GLU ALA ALA ARG GLU GLY          
SEQRES  15 D  326  HIS ARG ASP ARG VAL GLU GLU PHE ILE LYS ARG GLY ALA          
SEQRES  16 D  326  ASP VAL ASN THR ALA ASP GLU THR GLY PHE THR PRO LEU          
SEQRES  17 D  326  HIS LEU ALA ALA TRP GLU GLY HIS LEU GLY ILE VAL GLU          
SEQRES  18 D  326  VAL LEU LEU LYS ASN GLY ALA ASP VAL ASN ALA ASN ASP          
SEQRES  19 D  326  GLU ARG GLY HIS THR PRO LEU HIS LEU ALA ALA TYR THR          
SEQRES  20 D  326  GLY HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS ASN GLY          
SEQRES  21 D  326  ALA GLY VAL ASN ALA THR ASP VAL ILE GLY THR ALA PRO          
SEQRES  22 D  326  LEU HIS LEU ALA ALA MET TRP GLY HIS LEU GLU ILE VAL          
SEQRES  23 D  326  GLU VAL LEU LEU LYS HIS GLY ALA ASP VAL ASN ALA GLN          
SEQRES  24 D  326  ASP LYS PHE GLY LYS THR PRO PHE ASP LEU ALA ILE ASP          
SEQRES  25 D  326  ASN GLY ASN GLU ASP ILE ALA GLU VAL LEU GLN LYS ALA          
SEQRES  26 D  326  ALA                                                          
SEQRES   1 E  373  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ARG          
SEQRES   2 E  373  SER LYS ARG ASP ASN ASN PHE TYR SER VAL GLU ILE GLY          
SEQRES   3 E  373  ASP SER THR PHE THR VAL LEU LYS ARG TYR GLN ASN LEU          
SEQRES   4 E  373  LYS PRO ILE GLY SER GLY ALA GLN GLY ILE VAL CYS ALA          
SEQRES   5 E  373  ALA TYR ASP ALA ILE LEU GLU ARG ASN VAL ALA ILE LYS          
SEQRES   6 E  373  LYS LEU SER ARG PRO PHE GLN ASN GLN THR HIS ALA LYS          
SEQRES   7 E  373  ARG ALA TYR ARG GLU LEU VAL LEU MET LYS CYS VAL ASN          
SEQRES   8 E  373  HIS LYS ASN ILE ILE GLY LEU LEU ASN VAL PHE THR PRO          
SEQRES   9 E  373  GLN LYS SER LEU GLU GLU PHE GLN ASP VAL TYR ILE VAL          
SEQRES  10 E  373  MET GLU LEU MET ASP ALA ASN LEU CYS GLN VAL ILE GLN          
SEQRES  11 E  373  MET GLU LEU ASP HIS GLU ARG MET SER TYR LEU LEU TYR          
SEQRES  12 E  373  GLN MET LEU CYS GLY ILE LYS HIS LEU HIS SER ALA GLY          
SEQRES  13 E  373  ILE ILE HIS ARG ASP LEU LYS PRO SER ASN ILE VAL VAL          
SEQRES  14 E  373  LYS SER ASP CYS THR LEU LYS ILE LEU ASP PHE GLY LEU          
SEQRES  15 E  373  ALA ARG THR ALA GLY THR SER PHE MET MET THR PRO TYR          
SEQRES  16 E  373  VAL VAL THR ARG TYR TYR ARG ALA PRO GLU VAL ILE LEU          
SEQRES  17 E  373  GLY MET GLY TYR LYS GLU ASN VAL ASP LEU TRP SER VAL          
SEQRES  18 E  373  GLY CYS ILE MET GLY GLU MET VAL CYS HIS LYS ILE LEU          
SEQRES  19 E  373  PHE PRO GLY ARG ASP TYR ILE ASP GLN TRP ASN LYS VAL          
SEQRES  20 E  373  ILE GLU GLN LEU GLY THR PRO CYS PRO GLU PHE MET LYS          
SEQRES  21 E  373  LYS LEU GLN PRO THR VAL ARG THR TYR VAL GLU ASN ARG          
SEQRES  22 E  373  PRO LYS TYR ALA GLY TYR SER PHE GLU LYS LEU PHE PRO          
SEQRES  23 E  373  ASP VAL LEU PHE PRO ALA ASP SER GLU HIS ASN LYS LEU          
SEQRES  24 E  373  LYS ALA SER GLN ALA ARG ASP LEU LEU SER LYS MET LEU          
SEQRES  25 E  373  VAL ILE ASP ALA SER LYS ARG ILE SER VAL ASP GLU ALA          
SEQRES  26 E  373  LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR ASP PRO SER          
SEQRES  27 E  373  GLU ALA GLU ALA PRO PRO PRO LYS ILE PRO ASP LYS GLN          
SEQRES  28 E  373  LEU ASP GLU ARG GLU HIS THR ILE GLU GLU TRP LYS GLU          
SEQRES  29 E  373  LEU ILE TYR LYS GLU VAL MET ASP LEU                          
SEQRES   1 F   11  ARG PRO LYS ARG PRO THR THR LEU ASN LEU PHE                  
SEQRES   1 G  326  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP          
SEQRES   2 G  326  LEU GLY LYS LYS LEU LEU GLU ALA ALA ARG ALA GLY GLN          
SEQRES   3 G  326  ASP ASP GLU VAL ARG ILE LEU MET ALA ASN GLY ALA ASP          
SEQRES   4 G  326  VAL ASN ALA SER ASP GLN LEU GLY ILE THR PRO LEU HIS          
SEQRES   5 G  326  LEU VAL ALA ILE THR GLY HIS LEU GLU ILE VAL GLU VAL          
SEQRES   6 G  326  LEU LEU LYS ASN GLY ALA ASP VAL ASN ALA HIS ASP PHE          
SEQRES   7 G  326  VAL GLY THR THR PRO LEU HIS LEU ALA ALA PHE LEU GLY          
SEQRES   8 G  326  HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS TYR GLY ALA          
SEQRES   9 G  326  ASP VAL ASN ALA VAL ASP ARG ASP GLY LEU THR PRO LEU          
SEQRES  10 G  326  HIS LEU ALA ALA ILE HIS GLY HIS LEU GLU ILE VAL GLU          
SEQRES  11 G  326  VAL LEU LEU LYS HIS GLY ALA LEU VAL LYS ALA LYS ASP          
SEQRES  12 G  326  LYS PHE GLY LYS THR PRO LYS ASP LEU ALA ARG ASP ASN          
SEQRES  13 G  326  GLY ASN GLN PHE ILE TYR GLU LEU LEU GLU LYS ALA GLU          
SEQRES  14 G  326  LEU LEU GLU LYS LEU LEU LEU GLU ALA ALA ARG GLU GLY          
SEQRES  15 G  326  HIS ARG ASP ARG VAL GLU GLU PHE ILE LYS ARG GLY ALA          
SEQRES  16 G  326  ASP VAL ASN THR ALA ASP GLU THR GLY PHE THR PRO LEU          
SEQRES  17 G  326  HIS LEU ALA ALA TRP GLU GLY HIS LEU GLY ILE VAL GLU          
SEQRES  18 G  326  VAL LEU LEU LYS ASN GLY ALA ASP VAL ASN ALA ASN ASP          
SEQRES  19 G  326  GLU ARG GLY HIS THR PRO LEU HIS LEU ALA ALA TYR THR          
SEQRES  20 G  326  GLY HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS ASN GLY          
SEQRES  21 G  326  ALA GLY VAL ASN ALA THR ASP VAL ILE GLY THR ALA PRO          
SEQRES  22 G  326  LEU HIS LEU ALA ALA MET TRP GLY HIS LEU GLU ILE VAL          
SEQRES  23 G  326  GLU VAL LEU LEU LYS HIS GLY ALA ASP VAL ASN ALA GLN          
SEQRES  24 G  326  ASP LYS PHE GLY LYS THR PRO PHE ASP LEU ALA ILE ASP          
SEQRES  25 G  326  ASN GLY ASN GLU ASP ILE ALA GLU VAL LEU GLN LYS ALA          
SEQRES  26 G  326  ALA                                                          
SEQRES   1 H  373  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ARG          
SEQRES   2 H  373  SER LYS ARG ASP ASN ASN PHE TYR SER VAL GLU ILE GLY          
SEQRES   3 H  373  ASP SER THR PHE THR VAL LEU LYS ARG TYR GLN ASN LEU          
SEQRES   4 H  373  LYS PRO ILE GLY SER GLY ALA GLN GLY ILE VAL CYS ALA          
SEQRES   5 H  373  ALA TYR ASP ALA ILE LEU GLU ARG ASN VAL ALA ILE LYS          
SEQRES   6 H  373  LYS LEU SER ARG PRO PHE GLN ASN GLN THR HIS ALA LYS          
SEQRES   7 H  373  ARG ALA TYR ARG GLU LEU VAL LEU MET LYS CYS VAL ASN          
SEQRES   8 H  373  HIS LYS ASN ILE ILE GLY LEU LEU ASN VAL PHE THR PRO          
SEQRES   9 H  373  GLN LYS SER LEU GLU GLU PHE GLN ASP VAL TYR ILE VAL          
SEQRES  10 H  373  MET GLU LEU MET ASP ALA ASN LEU CYS GLN VAL ILE GLN          
SEQRES  11 H  373  MET GLU LEU ASP HIS GLU ARG MET SER TYR LEU LEU TYR          
SEQRES  12 H  373  GLN MET LEU CYS GLY ILE LYS HIS LEU HIS SER ALA GLY          
SEQRES  13 H  373  ILE ILE HIS ARG ASP LEU LYS PRO SER ASN ILE VAL VAL          
SEQRES  14 H  373  LYS SER ASP CYS THR LEU LYS ILE LEU ASP PHE GLY LEU          
SEQRES  15 H  373  ALA ARG THR ALA GLY THR SER PHE MET MET THR PRO TYR          
SEQRES  16 H  373  VAL VAL THR ARG TYR TYR ARG ALA PRO GLU VAL ILE LEU          
SEQRES  17 H  373  GLY MET GLY TYR LYS GLU ASN VAL ASP LEU TRP SER VAL          
SEQRES  18 H  373  GLY CYS ILE MET GLY GLU MET VAL CYS HIS LYS ILE LEU          
SEQRES  19 H  373  PHE PRO GLY ARG ASP TYR ILE ASP GLN TRP ASN LYS VAL          
SEQRES  20 H  373  ILE GLU GLN LEU GLY THR PRO CYS PRO GLU PHE MET LYS          
SEQRES  21 H  373  LYS LEU GLN PRO THR VAL ARG THR TYR VAL GLU ASN ARG          
SEQRES  22 H  373  PRO LYS TYR ALA GLY TYR SER PHE GLU LYS LEU PHE PRO          
SEQRES  23 H  373  ASP VAL LEU PHE PRO ALA ASP SER GLU HIS ASN LYS LEU          
SEQRES  24 H  373  LYS ALA SER GLN ALA ARG ASP LEU LEU SER LYS MET LEU          
SEQRES  25 H  373  VAL ILE ASP ALA SER LYS ARG ILE SER VAL ASP GLU ALA          
SEQRES  26 H  373  LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR ASP PRO SER          
SEQRES  27 H  373  GLU ALA GLU ALA PRO PRO PRO LYS ILE PRO ASP LYS GLN          
SEQRES  28 H  373  LEU ASP GLU ARG GLU HIS THR ILE GLU GLU TRP LYS GLU          
SEQRES  29 H  373  LEU ILE TYR LYS GLU VAL MET ASP LEU                          
SEQRES   1 I   11  ARG PRO LYS ARG PRO THR THR LEU ASN LEU PHE                  
SEQRES   1 L    6  IVA VAL VAL STA ALA STA                                      
HET    IVA  L   1       6                                                       
HET    STA  L   4      11                                                       
HET    STA  L   6      12                                                       
HET    SO4  A 401       5                                                       
HET    SO4  A 402       5                                                       
HET    ADN  B 401      19                                                       
HET    SO4  B 402       5                                                       
HET    SO4  B 403       5                                                       
HET    SO4  B 404       5                                                       
HET    SO4  B 405       5                                                       
HET    SO4  B 406       5                                                       
HET    SO4  D 401       5                                                       
HET    SO4  D 402       5                                                       
HET    SO4  D 403       5                                                       
HET    SO4  D 404       5                                                       
HET    ADN  E 401      19                                                       
HET    SO4  E 402       5                                                       
HET    SO4  E 403       5                                                       
HET    SO4  E 404       5                                                       
HET    SO4  E 405       5                                                       
HET    SO4  G 401       5                                                       
HET    SO4  G 402       5                                                       
HET    SO4  G 403       5                                                       
HET    SO4  G 404       5                                                       
HET    ADN  H 401      19                                                       
HET    SO4  H 402       5                                                       
HET    SO4  H 403       5                                                       
HET    SO4  H 404       5                                                       
HET    SO4  H 405       5                                                       
HET    SO4  I 201       5                                                       
HETNAM     IVA ISOVALERIC ACID                                                  
HETNAM     STA STATINE                                                          
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ADN ADENOSINE                                                        
FORMUL  10  IVA    C5 H10 O2                                                    
FORMUL  10  STA    2(C8 H17 N O3)                                               
FORMUL  11  SO4    24(O4 S 2-)                                                  
FORMUL  13  ADN    3(C10 H13 N5 O4)                                             
HELIX    1 AA1 ASP A   13  ALA A   24  1                                  12    
HELIX    2 AA2 GLN A   26  ASN A   36  1                                  11    
HELIX    3 AA3 THR A   49  GLY A   58  1                                  10    
HELIX    4 AA4 HIS A   59  ASN A   69  1                                  11    
HELIX    5 AA5 THR A   82  GLY A   91  1                                  10    
HELIX    6 AA6 HIS A   92  TYR A  102  1                                  11    
HELIX    7 AA7 THR A  115  HIS A  123  1                                   9    
HELIX    8 AA8 HIS A  125  HIS A  135  1                                  11    
HELIX    9 AA9 THR A  148  ASN A  156  1                                   9    
HELIX   10 AB1 ASN A  158  GLY A  182  1                                  25    
HELIX   11 AB2 HIS A  183  ARG A  193  1                                  11    
HELIX   12 AB3 THR A  206  GLY A  215  1                                  10    
HELIX   13 AB4 HIS A  216  ASN A  226  1                                  11    
HELIX   14 AB5 THR A  239  GLY A  248  1                                  10    
HELIX   15 AB6 HIS A  249  ASN A  259  1                                  11    
HELIX   16 AB7 ALA A  272  TRP A  280  1                                   9    
HELIX   17 AB8 HIS A  282  HIS A  292  1                                  11    
HELIX   18 AB9 THR A  305  ASN A  313  1                                   9    
HELIX   19 AC1 ASN A  315  ALA A  325  1                                  11    
HELIX   20 AC2 PRO B   60  GLN B   62  5                                   3    
HELIX   21 AC3 ASN B   63  VAL B   80  1                                  18    
HELIX   22 AC4 LEU B  115  MET B  121  1                                   7    
HELIX   23 AC5 ASP B  124  ALA B  145  1                                  22    
HELIX   24 AC6 LYS B  153  SER B  155  5                                   3    
HELIX   25 AC7 VAL B  187  ARG B  192  5                                   6    
HELIX   26 AC8 ALA B  193  LEU B  198  1                                   6    
HELIX   27 AC9 ASN B  205  HIS B  221  1                                  17    
HELIX   28 AD1 ILE B  231  GLY B  242  1                                  12    
HELIX   29 AD2 CYS B  245  LYS B  250  1                                   6    
HELIX   30 AD3 GLN B  253  ASN B  262  1                                  10    
HELIX   31 AD4 SER B  270  PHE B  275  1                                   6    
HELIX   32 AD5 PRO B  276  PHE B  280  5                                   5    
HELIX   33 AD6 LYS B  290  LEU B  302  1                                  13    
HELIX   34 AD7 SER B  311  GLN B  317  1                                   7    
HELIX   35 AD8 ILE B  321  TYR B  325  5                                   5    
HELIX   36 AD9 ASP B  326  GLU B  331  1                                   6    
HELIX   37 AE1 THR B  348  ASP B  362  1                                  15    
HELIX   38 AE2 LEU D   14  ALA D   24  1                                  11    
HELIX   39 AE3 GLN D   26  ASN D   36  1                                  11    
HELIX   40 AE4 THR D   49  GLY D   58  1                                  10    
HELIX   41 AE5 HIS D   59  ASN D   69  1                                  11    
HELIX   42 AE6 THR D   82  GLY D   91  1                                  10    
HELIX   43 AE7 HIS D   92  TYR D  102  1                                  11    
HELIX   44 AE8 THR D  115  HIS D  123  1                                   9    
HELIX   45 AE9 HIS D  125  HIS D  135  1                                  11    
HELIX   46 AF1 THR D  148  ASN D  156  1                                   9    
HELIX   47 AF2 ASN D  158  GLY D  182  1                                  25    
HELIX   48 AF3 HIS D  183  ARG D  193  1                                  11    
HELIX   49 AF4 THR D  206  GLY D  215  1                                  10    
HELIX   50 AF5 HIS D  216  ASN D  226  1                                  11    
HELIX   51 AF6 THR D  239  GLY D  248  1                                  10    
HELIX   52 AF7 HIS D  249  ASN D  259  1                                  11    
HELIX   53 AF8 ALA D  272  TRP D  280  1                                   9    
HELIX   54 AF9 HIS D  282  HIS D  292  1                                  11    
HELIX   55 AG1 THR D  305  ASN D  313  1                                   9    
HELIX   56 AG2 ASN D  315  LYS D  324  1                                  10    
HELIX   57 AG3 PRO E   60  GLN E   62  5                                   3    
HELIX   58 AG4 ASN E   63  VAL E   80  1                                  18    
HELIX   59 AG5 LEU E  115  MET E  121  1                                   7    
HELIX   60 AG6 ASP E  124  ALA E  145  1                                  22    
HELIX   61 AG7 LYS E  153  SER E  155  5                                   3    
HELIX   62 AG8 VAL E  187  ARG E  192  5                                   6    
HELIX   63 AG9 ALA E  193  LEU E  198  1                                   6    
HELIX   64 AH1 ASN E  205  HIS E  221  1                                  17    
HELIX   65 AH2 ILE E  231  GLY E  242  1                                  12    
HELIX   66 AH3 CYS E  245  LYS E  250  1                                   6    
HELIX   67 AH4 GLN E  253  ASN E  262  1                                  10    
HELIX   68 AH5 SER E  270  PHE E  275  1                                   6    
HELIX   69 AH6 PRO E  276  PHE E  280  5                                   5    
HELIX   70 AH7 LYS E  290  LEU E  302  1                                  13    
HELIX   71 AH8 SER E  311  GLN E  317  1                                   7    
HELIX   72 AH9 ILE E  321  TYR E  325  5                                   5    
HELIX   73 AI1 ASP E  326  GLU E  331  1                                   6    
HELIX   74 AI2 THR E  348  ASP E  362  1                                  15    
HELIX   75 AI3 LEU G   14  ALA G   24  1                                  11    
HELIX   76 AI4 GLN G   26  ASN G   36  1                                  11    
HELIX   77 AI5 THR G   49  GLY G   58  1                                  10    
HELIX   78 AI6 HIS G   59  ASN G   69  1                                  11    
HELIX   79 AI7 THR G   82  GLY G   91  1                                  10    
HELIX   80 AI8 HIS G   92  TYR G  102  1                                  11    
HELIX   81 AI9 THR G  115  HIS G  123  1                                   9    
HELIX   82 AJ1 HIS G  125  HIS G  135  1                                  11    
HELIX   83 AJ2 THR G  148  GLY G  157  1                                  10    
HELIX   84 AJ3 ASN G  158  GLY G  182  1                                  25    
HELIX   85 AJ4 HIS G  183  ARG G  193  1                                  11    
HELIX   86 AJ5 THR G  206  GLY G  215  1                                  10    
HELIX   87 AJ6 HIS G  216  ASN G  226  1                                  11    
HELIX   88 AJ7 THR G  239  GLY G  248  1                                  10    
HELIX   89 AJ8 HIS G  249  ASN G  259  1                                  11    
HELIX   90 AJ9 ALA G  272  TRP G  280  1                                   9    
HELIX   91 AK1 HIS G  282  HIS G  292  1                                  11    
HELIX   92 AK2 THR G  305  ASN G  313  1                                   9    
HELIX   93 AK3 ASN G  315  ALA G  325  1                                  11    
HELIX   94 AK4 PRO H   60  GLN H   62  5                                   3    
HELIX   95 AK5 ASN H   63  VAL H   80  1                                  18    
HELIX   96 AK6 LEU H  115  MET H  121  1                                   7    
HELIX   97 AK7 ASP H  124  ALA H  145  1                                  22    
HELIX   98 AK8 VAL H  187  ARG H  192  5                                   6    
HELIX   99 AK9 ALA H  193  LEU H  198  1                                   6    
HELIX  100 AL1 LYS H  203  ASN H  205  5                                   3    
HELIX  101 AL2 VAL H  206  HIS H  221  1                                  16    
HELIX  102 AL3 ILE H  231  GLY H  242  1                                  12    
HELIX  103 AL4 CYS H  245  LYS H  250  1                                   6    
HELIX  104 AL5 GLN H  253  ASN H  262  1                                  10    
HELIX  105 AL6 SER H  270  PHE H  275  1                                   6    
HELIX  106 AL7 PRO H  276  PHE H  280  5                                   5    
HELIX  107 AL8 LYS H  290  LEU H  302  1                                  13    
HELIX  108 AL9 SER H  311  GLN H  317  1                                   7    
HELIX  109 AM1 ILE H  321  TYR H  325  5                                   5    
HELIX  110 AM2 ASP H  326  GLU H  331  1                                   6    
HELIX  111 AM3 THR H  348  ASP H  362  1                                  15    
SHEET    1 AA1 2 PHE B  10  ILE B  15  0                                        
SHEET    2 AA1 2 SER B  18  LEU B  23 -1  O  PHE B  20   N  VAL B  13           
SHEET    1 AA2 5 TYR B  26  SER B  34  0                                        
SHEET    2 AA2 5 ILE B  39  ASP B  45 -1  O  ALA B  42   N  LYS B  30           
SHEET    3 AA2 5 ARG B  50  SER B  58 -1  O  ILE B  54   N  CYS B  41           
SHEET    4 AA2 5 ASP B 103  GLU B 109 -1  O  VAL B 104   N  LEU B  57           
SHEET    5 AA2 5 LEU B  88  PHE B  92 -1  N  LEU B  89   O  VAL B 107           
SHEET    1 AA3 3 ALA B 113  ASN B 114  0                                        
SHEET    2 AA3 3 ILE B 157  VAL B 159 -1  O  VAL B 159   N  ALA B 113           
SHEET    3 AA3 3 LEU B 165  ILE B 167 -1  O  LYS B 166   N  VAL B 158           
SHEET    1 AA4 2 PHE E  10  ILE E  15  0                                        
SHEET    2 AA4 2 SER E  18  LEU E  23 -1  O  PHE E  20   N  VAL E  13           
SHEET    1 AA5 5 TYR E  26  SER E  34  0                                        
SHEET    2 AA5 5 ILE E  39  ASP E  45 -1  O  ALA E  42   N  LYS E  30           
SHEET    3 AA5 5 ARG E  50  SER E  58 -1  O  ILE E  54   N  CYS E  41           
SHEET    4 AA5 5 ASP E 103  GLU E 109 -1  O  VAL E 104   N  LEU E  57           
SHEET    5 AA5 5 LEU E  88  PHE E  92 -1  N  ASN E  90   O  VAL E 107           
SHEET    1 AA6 3 ALA E 113  ASN E 114  0                                        
SHEET    2 AA6 3 ILE E 157  VAL E 159 -1  O  VAL E 159   N  ALA E 113           
SHEET    3 AA6 3 LEU E 165  ILE E 167 -1  O  LYS E 166   N  VAL E 158           
SHEET    1 AA7 2 PHE H  10  ILE H  15  0                                        
SHEET    2 AA7 2 SER H  18  LEU H  23 -1  O  PHE H  20   N  VAL H  13           
SHEET    1 AA8 5 TYR H  26  SER H  34  0                                        
SHEET    2 AA8 5 ILE H  39  ASP H  45 -1  O  ALA H  42   N  LYS H  30           
SHEET    3 AA8 5 ARG H  50  SER H  58 -1  O  ILE H  54   N  CYS H  41           
SHEET    4 AA8 5 ASP H 103  GLU H 109 -1  O  VAL H 104   N  LEU H  57           
SHEET    5 AA8 5 LEU H  88  PHE H  92 -1  N  LEU H  89   O  VAL H 107           
SHEET    1 AA9 3 ALA H 113  ASN H 114  0                                        
SHEET    2 AA9 3 ILE H 157  LYS H 160 -1  O  VAL H 159   N  ALA H 113           
SHEET    3 AA9 3 THR H 164  ILE H 167 -1  O  LYS H 166   N  VAL H 158           
LINK         C   IVA L   1                 N   VAL L   2     1555   1555  1.36  
LINK         C   VAL L   3                 N   STA L   4     1555   1555  1.35  
LINK         C   STA L   4                 N   ALA L   5     1555   1555  1.37  
LINK         C   ALA L   5                 N   STA L   6     1555   1555  1.38  
SITE     1 AC1  3 GLY A 215  LEU A 217  GLY A 218                               
SITE     1 AC2  4 PHE A  89  HIS A 123  HIS A 125  TYR B 230                    
SITE     1 AC3  9 GLY B  33  VAL B  40  ALA B  53  MET B 108                    
SITE     2 AC3  9 GLU B 109  MET B 111  ASN B 114  SER B 155                    
SITE     3 AC3  9 LEU B 168                                                     
SITE     1 AC4  2 LYS B 250  ARG B 257                                          
SITE     1 AC5  1 ARG B 127                                                     
SITE     1 AC6  3 ARG B 189  ARG B 192  TYR B 230                               
SITE     1 AC7  7 MET B 181  THR B 183  VAL B 186  VAL B 187                    
SITE     2 AC7  7 THR B 188  TRP D 213  TYR D 246                               
SITE     1 AC8  2 THR B 348  ILE B 349                                          
SITE     1 AC9  3 HIS D 216  LEU D 217  GLY D 218                               
SITE     1 AD1  4 GLY D 281  HIS D 282  LEU D 283  GLU D 284                    
SITE     1 AD2  2 ARG D 184  GLU D 221                                          
SITE     1 AD3  2 VAL D 263  ASN D 264                                          
SITE     1 AD4  9 GLY E  33  VAL E  40  ALA E  53  ILE E  86                    
SITE     2 AD4  9 MET E 108  GLU E 109  MET E 111  ASN E 114                    
SITE     3 AD4  9 SER E 155                                                     
SITE     1 AD5  3 ARG E 189  ARG E 192  TYR E 230                               
SITE     1 AD6  1 ARG E 257                                                     
SITE     1 AD7  6 THR E 183  VAL E 186  VAL E 187  THR E 188                    
SITE     2 AD7  6 TRP G 213  TYR G 246                                          
SITE     1 AD8  1 SER E  12                                                     
SITE     1 AD9  3 GLY G 215  LEU G 217  GLY G 218                               
SITE     1 AE1  3 LYS G  16  ASP G  44  GLN G  45                               
SITE     1 AE2  4 GLY G 281  HIS G 282  LEU G 283  GLU G 284                    
SITE     1 AE3  2 VAL G 263  ASN G 264                                          
SITE     1 AE4  9 SER H  34  VAL H  40  ALA H  53  MET H 108                    
SITE     2 AE4  9 GLU H 109  MET H 111  ASN H 114  SER H 155                    
SITE     3 AE4  9 LEU H 168                                                     
SITE     1 AE5  3 ARG H 189  ARG H 192  TYR H 230                               
SITE     1 AE6  3 ARG G 111  LYS H 250  ARG H 257                               
SITE     1 AE7  2 LYS H 290  GLN H 293                                          
SITE     1 AE8  2 TYR H  11  SER H  12                                          
SITE     1 AE9  2 ASN A  69  LEU I 160                                          
SITE     1 AF1  3 GLY H 201  VAL L   3  STA L   4                               
SITE     1 AF2  5 LEU G 114  ILE G 122  ASN G 156  VAL L   2                    
SITE     2 AF2  5 ALA L   5                                                     
SITE     1 AF3  8 LEU G 114  ILE G 122  HIS G 123  ASN G 156                    
SITE     2 AF3  8 GLY H 199  VAL L   2  VAL L   3  STA L   6                    
SITE     1 AF4  8 ILE G 122  HIS G 123  ASN G 156  THR H 178                    
SITE     2 AF4  8 GLY H 199  TYR H 230  ILE H 231  STA L   4                    
CRYST1  219.990  141.760  119.850  90.00  97.83  90.00 C 1 2 1      12          
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      0.004546  0.000000  0.000625        0.00000                         
SCALE2      0.000000  0.007054  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008422        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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