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Database: PDB
Entry: 3S4W
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Original site: 3S4W 
HEADER    DNA BINDING PROTEIN                     20-MAY-11   3S4W              
TITLE     STRUCTURE OF THE FANCI-FANCD2 COMPLEX                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FANCONI ANEMIA GROUP I PROTEIN HOMOLOG;                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PROTEIN FACI;                                               
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: FANCONI ANEMIA GROUP D2 PROTEIN HOMOLOG;                   
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: UNP RESIDUES 33-1415;                                      
COMPND  10 SYNONYM: PROTEIN FACD2;                                              
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: FANCI;                                                         
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   8 ORGANISM_COMMON: MOUSE;                                              
SOURCE   9 ORGANISM_TAXID: 10090;                                               
SOURCE  10 GENE: FANCD2                                                         
KEYWDS    DNA REPAIR, DNA BINDING PROTEIN                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.P.PAVLETICH                                                         
REVDAT   2   28-MAR-12 3S4W    1       JRNL                                     
REVDAT   1   27-JUL-11 3S4W    0                                                
JRNL        AUTH   W.JOO,G.XU,N.S.PERSKY,A.SMOGORZEWSKA,D.G.RUDGE,O.BUZOVETSKY, 
JRNL        AUTH 2 S.J.ELLEDGE,N.P.PAVLETICH                                    
JRNL        TITL   STRUCTURE OF THE FANCI-FANCD2 COMPLEX: INSIGHTS INTO THE     
JRNL        TITL 2 FANCONI ANEMIA DNA REPAIR PATHWAY.                           
JRNL        REF    SCIENCE                       V. 333   312 2011              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   21764741                                                     
JRNL        DOI    10.1126/SCIENCE.1205805                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.41 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.1_743)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.41                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.86                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 40654                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.241                           
REMARK   3   R VALUE            (WORKING SET) : 0.240                           
REMARK   3   FREE R VALUE                     : 0.272                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1637                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 19.8586 -  7.6639    0.99     3764   168  0.1699 0.2138        
REMARK   3     2  7.6639 -  6.1423    0.99     3649   169  0.2674 0.2672        
REMARK   3     3  6.1423 -  5.3835    0.98     3590   149  0.2894 0.3135        
REMARK   3     4  5.3835 -  4.8994    0.98     3549   139  0.2396 0.2910        
REMARK   3     5  4.8994 -  4.5528    0.98     3532   158  0.2132 0.2573        
REMARK   3     6  4.5528 -  4.2872    0.97     3489   126  0.2159 0.2402        
REMARK   3     7  4.2872 -  4.0744    0.96     3419   138  0.2405 0.2673        
REMARK   3     8  4.0744 -  3.8984    0.92     3344   121  0.2633 0.3127        
REMARK   3     9  3.8984 -  3.7494    0.89     3145   145  0.2820 0.3014        
REMARK   3    10  3.7494 -  3.6208    0.82     2908   132  0.3102 0.3605        
REMARK   3    11  3.6208 -  3.5082    0.72     2536   116  0.3380 0.3810        
REMARK   3    12  3.5082 -  3.4085    0.58     2092    76  0.3963 0.4010        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.28                                          
REMARK   3   B_SOL              : 58.21                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.830            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.500           
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) : -18.19160                                            
REMARK   3    B22 (A**2) : 11.43630                                             
REMARK   3    B33 (A**2) : 6.75540                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004          18991                                  
REMARK   3   ANGLE     :  0.881          25659                                  
REMARK   3   CHIRALITY :  0.065           3046                                  
REMARK   3   PLANARITY :  0.003           3217                                  
REMARK   3   DIHEDRAL  : 16.670           7068                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 16                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 1:225)                           
REMARK   3    ORIGIN FOR THE GROUP (A): -28.4833  35.5780   9.3600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4738 T22:   1.2901                                     
REMARK   3      T33:   1.1541 T12:  -0.2199                                     
REMARK   3      T13:  -0.5799 T23:   0.1023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3596 L22:   1.9286                                     
REMARK   3      L33:   2.1422 L12:  -1.4362                                     
REMARK   3      L13:   0.8794 L23:   0.2233                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3789 S12:   0.3779 S13:  -0.3783                       
REMARK   3      S21:  -0.5862 S22:  -0.2625 S23:   0.8401                       
REMARK   3      S31:   0.5393 S32:  -0.5732 S33:  -0.0004                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 226:319)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.7783  31.8967  35.7035              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0288 T22:   0.6749                                     
REMARK   3      T33:   0.4087 T12:   0.0528                                     
REMARK   3      T13:  -0.1907 T23:   0.0261                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5057 L22:   2.8681                                     
REMARK   3      L33:   2.3947 L12:   2.2252                                     
REMARK   3      L13:   1.1336 L23:  -0.6073                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2168 S12:   0.1609 S13:  -0.1551                       
REMARK   3      S21:  -0.2755 S22:   0.5281 S23:   0.5021                       
REMARK   3      S31:   0.3181 S32:   0.1540 S33:   0.0048                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 320:469)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  11.5937  36.4364  48.5922              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7060 T22:   0.5006                                     
REMARK   3      T33:   0.4191 T12:  -0.0176                                     
REMARK   3      T13:  -0.1347 T23:   0.1080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7024 L22:   2.2990                                     
REMARK   3      L33:   2.3879 L12:   1.3206                                     
REMARK   3      L13:   1.0128 L23:  -0.3470                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0394 S12:  -0.0005 S13:  -0.1760                       
REMARK   3      S21:  -0.3123 S22:  -0.1621 S23:  -0.1421                       
REMARK   3      S31:   0.0526 S32:   0.1147 S33:   0.0010                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 470:544)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  35.6435  51.5326  51.2479              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8389 T22:   0.9036                                     
REMARK   3      T33:   0.6082 T12:  -0.2023                                     
REMARK   3      T13:  -0.0619 T23:   0.2193                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0946 L22:   0.3523                                     
REMARK   3      L33:   0.5491 L12:   0.5730                                     
REMARK   3      L13:   0.5806 L23:   0.1905                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0375 S12:   0.4534 S13:  -0.4662                       
REMARK   3      S21:  -0.3489 S22:   0.2120 S23:  -0.0053                       
REMARK   3      S31:   0.3112 S32:  -0.5474 S33:  -0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 545:696)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  50.7084  49.6721  64.9391              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3884 T22:   0.1441                                     
REMARK   3      T33:   0.5157 T12:  -0.0167                                     
REMARK   3      T13:   0.0069 T23:   0.0258                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4038 L22:   3.5677                                     
REMARK   3      L33:   5.3468 L12:   0.4608                                     
REMARK   3      L13:  -0.3952 L23:  -2.8719                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0037 S12:   0.2614 S13:   0.2137                       
REMARK   3      S21:  -0.4790 S22:  -0.0196 S23:  -0.3542                       
REMARK   3      S31:   0.4892 S32:   0.1921 S33:  -0.0109                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 697:817)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  44.5178  42.5028  87.5199              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3614 T22:   0.2441                                     
REMARK   3      T33:   0.3655 T12:  -0.0853                                     
REMARK   3      T13:  -0.0354 T23:  -0.0160                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3613 L22:   3.6453                                     
REMARK   3      L33:   3.4653 L12:   1.1936                                     
REMARK   3      L13:  -0.0187 L23:  -0.8146                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0802 S12:  -0.3486 S13:   0.0088                       
REMARK   3      S21:   0.4702 S22:   0.0891 S23:  -0.0157                       
REMARK   3      S31:  -0.2821 S32:  -0.3587 S33:   0.0047                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 818:1186)                        
REMARK   3    ORIGIN FOR THE GROUP (A):  13.3754  17.0080  76.1844              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3778 T22:   0.1408                                     
REMARK   3      T33:   0.5127 T12:   0.0239                                     
REMARK   3      T13:  -0.0432 T23:   0.0971                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6693 L22:   1.6318                                     
REMARK   3      L33:   0.5919 L12:   1.5179                                     
REMARK   3      L13:   0.8137 L23:   0.4714                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1878 S12:  -0.3035 S13:  -0.4482                       
REMARK   3      S21:  -0.0607 S22:  -0.1038 S23:   0.1328                       
REMARK   3      S31:   0.1081 S32:   0.0503 S33:   0.0120                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 1187:1300)                       
REMARK   3    ORIGIN FOR THE GROUP (A): -28.4629  14.1048  72.0244              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6955 T22:   0.7262                                     
REMARK   3      T33:   1.2465 T12:   0.1323                                     
REMARK   3      T13:  -0.1532 T23:  -0.1794                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4779 L22:   1.3361                                     
REMARK   3      L33:   0.2097 L12:   1.7331                                     
REMARK   3      L13:  -0.7994 L23:  -0.2940                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0641 S12:   0.2066 S13:   0.0441                       
REMARK   3      S21:  -0.2442 S22:  -0.3492 S23:   0.4738                       
REMARK   3      S31:  -0.2289 S32:  -0.1910 S33:  -0.0324                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 43:337)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  54.3079  67.3035  51.6432              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7721 T22:   0.6727                                     
REMARK   3      T33:   0.7636 T12:  -0.0479                                     
REMARK   3      T13:   0.1140 T23:   0.1484                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1820 L22:   1.8113                                     
REMARK   3      L33:   2.2070 L12:  -1.3537                                     
REMARK   3      L13:   1.8611 L23:  -0.1639                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1850 S12:   0.1021 S13:   0.6194                       
REMARK   3      S21:  -0.2299 S22:   0.1186 S23:  -0.2738                       
REMARK   3      S31:  -0.1734 S32:  -0.0624 S33:   0.0002                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain 'B' and (resseq 338:565)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   1.2454  61.3348  29.5725              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4253 T22:   0.6634                                     
REMARK   3      T33:   0.1444 T12:   0.1944                                     
REMARK   3      T13:  -0.3399 T23:   0.2315                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3220 L22:   1.3329                                     
REMARK   3      L33:   2.3018 L12:   0.8445                                     
REMARK   3      L13:   2.2217 L23:   0.3126                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0324 S12:   0.1810 S13:  -0.1078                       
REMARK   3      S21:   0.0554 S22:   0.2800 S23:   0.0227                       
REMARK   3      S31:  -0.0361 S32:   0.4305 S33:   0.0555                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: chain 'B' and (resseq 566:662)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -22.4991  60.8542   3.3679              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8871 T22:   0.8808                                     
REMARK   3      T33:   0.4331 T12:   0.0919                                     
REMARK   3      T13:  -0.2855 T23:   0.1397                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8277 L22:   1.1996                                     
REMARK   3      L33:   1.3270 L12:  -0.4037                                     
REMARK   3      L13:   0.5957 L23:   0.3843                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5674 S12:   0.5897 S13:  -0.5592                       
REMARK   3      S21:  -0.5608 S22:  -0.0481 S23:   0.1133                       
REMARK   3      S31:   0.7361 S32:   0.5116 S33:   0.0465                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: chain 'B' and (resseq 663:797)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -38.4480  78.3848   4.9898              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6141 T22:   1.1880                                     
REMARK   3      T33:   0.7429 T12:  -0.0147                                     
REMARK   3      T13:  -0.1368 T23:   0.5550                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6626 L22:   2.9836                                     
REMARK   3      L33:   2.1192 L12:   0.2189                                     
REMARK   3      L13:   1.1799 L23:   0.2058                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0100 S12:   0.4540 S13:   0.3857                       
REMARK   3      S21:   0.1358 S22:   0.0774 S23:   0.2932                       
REMARK   3      S31:  -0.1798 S32:  -0.3664 S33:  -0.0138                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: chain 'B' and (resseq 798:959)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -30.1568  83.1747  14.9608              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5083 T22:   0.8874                                     
REMARK   3      T33:   0.6303 T12:   0.0569                                     
REMARK   3      T13:  -0.2045 T23:   0.4698                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1934 L22:   2.4933                                     
REMARK   3      L33:   3.1798 L12:  -1.3220                                     
REMARK   3      L13:   0.6319 L23:   1.0225                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4155 S12:   0.1214 S13:   0.2424                       
REMARK   3      S21:   0.3987 S22:  -0.0739 S23:  -0.3990                       
REMARK   3      S31:  -0.0128 S32:  -0.1005 S33:  -0.1342                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: chain 'B' and (resseq 960:1090)                        
REMARK   3    ORIGIN FOR THE GROUP (A): -13.9132  90.1663  20.5834              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6297 T22:   0.8301                                     
REMARK   3      T33:   0.7475 T12:  -0.0867                                     
REMARK   3      T13:  -0.3550 T23:   0.3423                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2201 L22:   2.2688                                     
REMARK   3      L33:   2.6108 L12:   1.6752                                     
REMARK   3      L13:   0.5546 L23:   0.1309                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3708 S12:   0.2216 S13:   0.3966                       
REMARK   3      S21:   0.0265 S22:   0.0876 S23:  -0.2021                       
REMARK   3      S31:  -0.0947 S32:   0.5183 S33:  -0.0119                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: chain 'B' and (resseq 1091:1228)                       
REMARK   3    ORIGIN FOR THE GROUP (A): -11.0897 100.8771  37.7690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0652 T22:   0.6910                                     
REMARK   3      T33:   1.1453 T12:  -0.1127                                     
REMARK   3      T13:  -0.5247 T23:   0.0927                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5397 L22:   2.4912                                     
REMARK   3      L33:   2.4501 L12:  -0.5193                                     
REMARK   3      L13:   1.6387 L23:   0.7274                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5841 S12:  -0.2155 S13:   0.9203                       
REMARK   3      S21:   0.4068 S22:   0.1159 S23:  -0.3225                       
REMARK   3      S31:  -0.6619 S32:   0.0595 S33:  -0.0036                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: chain 'B' and (resseq 1229:1391)                       
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.6670  94.9800  66.6158              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3526 T22:   1.0995                                     
REMARK   3      T33:   1.3911 T12:  -0.1409                                     
REMARK   3      T13:  -0.2941 T23:  -0.0873                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2762 L22:   1.6155                                     
REMARK   3      L33:   2.9420 L12:  -0.4898                                     
REMARK   3      L13:   0.3169 L23:   0.8302                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1372 S12:  -0.5856 S13:  -0.5440                       
REMARK   3      S21:   0.2713 S22:   0.0961 S23:  -0.4690                       
REMARK   3      S31:  -0.0323 S32:  -0.0407 S33:   0.0001                       
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 3S4W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB065764.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-DEC-09                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42995                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.09200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.52                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3S51                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MM HEPES-NA, 40 MM POTASSIUM          
REMARK 280  CITRATE, 10 MM DTT, 7 TO 8 % (W/V) PEG 3350, PH 7.4, VAPOR          
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       41.90000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      175.25000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.20000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      175.25000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       41.90000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.20000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 107970 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A   251                                                      
REMARK 465     GLU A   252                                                      
REMARK 465     LEU A   253                                                      
REMARK 465     SER A   254                                                      
REMARK 465     GLU A   255                                                      
REMARK 465     LEU A   256                                                      
REMARK 465     ILE A   257                                                      
REMARK 465     LYS A   402                                                      
REMARK 465     ALA A   403                                                      
REMARK 465     VAL A   404                                                      
REMARK 465     GLU A   405                                                      
REMARK 465     ILE A   406                                                      
REMARK 465     GLY A   407                                                      
REMARK 465     THR A   408                                                      
REMARK 465     SER A   409                                                      
REMARK 465     LEU A   410                                                      
REMARK 465     LEU A   684                                                      
REMARK 465     GLN A   685                                                      
REMARK 465     GLN A   686                                                      
REMARK 465     GLY A   687                                                      
REMARK 465     ASP A   688                                                      
REMARK 465     GLU A   689                                                      
REMARK 465     GLY A   690                                                      
REMARK 465     GLU A   691                                                      
REMARK 465     GLU A   692                                                      
REMARK 465     GLU A   693                                                      
REMARK 465     GLU A   694                                                      
REMARK 465     GLY A   791                                                      
REMARK 465     LYS A   792                                                      
REMARK 465     ALA A   793                                                      
REMARK 465     LYS A   794                                                      
REMARK 465     MET A   795                                                      
REMARK 465     THR A   796                                                      
REMARK 465     SER A   797                                                      
REMARK 465     ILE A   887                                                      
REMARK 465     PRO A   888                                                      
REMARK 465     THR A   889                                                      
REMARK 465     SER A   890                                                      
REMARK 465     VAL A   891                                                      
REMARK 465     GLU A   892                                                      
REMARK 465     GLU A   893                                                      
REMARK 465     SER A   894                                                      
REMARK 465     GLY A   895                                                      
REMARK 465     LYS A   896                                                      
REMARK 465     LYS A   897                                                      
REMARK 465     GLU A   898                                                      
REMARK 465     LYS A   899                                                      
REMARK 465     GLY A   900                                                      
REMARK 465     LYS A   901                                                      
REMARK 465     ASN A  1107                                                      
REMARK 465     GLN A  1108                                                      
REMARK 465     GLU A  1109                                                      
REMARK 465     THR A  1110                                                      
REMARK 465     LEU A  1111                                                      
REMARK 465     SER A  1112                                                      
REMARK 465     ASP A  1113                                                      
REMARK 465     LYS A  1114                                                      
REMARK 465     VAL A  1115                                                      
REMARK 465     THR A  1116                                                      
REMARK 465     PRO A  1117                                                      
REMARK 465     GLU A  1118                                                      
REMARK 465     ASP A  1119                                                      
REMARK 465     ALA A  1120                                                      
REMARK 465     SER A  1121                                                      
REMARK 465     SER A  1122                                                      
REMARK 465     GLN A  1123                                                      
REMARK 465     ALA A  1124                                                      
REMARK 465     VAL A  1125                                                      
REMARK 465     PRO A  1126                                                      
REMARK 465     ASP A  1223                                                      
REMARK 465     ALA A  1224                                                      
REMARK 465     PRO A  1225                                                      
REMARK 465     LYS A  1226                                                      
REMARK 465     CYS A  1227                                                      
REMARK 465     SER A  1228                                                      
REMARK 465     GLU A  1229                                                      
REMARK 465     LYS A  1230                                                      
REMARK 465     GLU A  1231                                                      
REMARK 465     LYS A  1232                                                      
REMARK 465     ALA A  1233                                                      
REMARK 465     ALA A  1234                                                      
REMARK 465     VAL A  1235                                                      
REMARK 465     SER A  1236                                                      
REMARK 465     THR A  1237                                                      
REMARK 465     THR A  1238                                                      
REMARK 465     MET A  1239                                                      
REMARK 465     ALA A  1240                                                      
REMARK 465     LYS A  1241                                                      
REMARK 465     VAL A  1242                                                      
REMARK 465     LEU A  1243                                                      
REMARK 465     ARG A  1244                                                      
REMARK 465     GLU A  1245                                                      
REMARK 465     THR A  1246                                                      
REMARK 465     LYS A  1247                                                      
REMARK 465     GLU A  1301                                                      
REMARK 465     GLU A  1302                                                      
REMARK 465     HIS A  1303                                                      
REMARK 465     HIS A  1304                                                      
REMARK 465     HIS A  1305                                                      
REMARK 465     HIS A  1306                                                      
REMARK 465     HIS A  1307                                                      
REMARK 465     HIS A  1308                                                      
REMARK 465     SER B    33                                                      
REMARK 465     HIS B    34                                                      
REMARK 465     ASN B    35                                                      
REMARK 465     SER B    36                                                      
REMARK 465     HIS B    37                                                      
REMARK 465     GLU B    38                                                      
REMARK 465     VAL B    39                                                      
REMARK 465     GLU B    40                                                      
REMARK 465     GLU B    41                                                      
REMARK 465     ASN B    42                                                      
REMARK 465     LEU B   118                                                      
REMARK 465     GLN B   119                                                      
REMARK 465     ASP B   120                                                      
REMARK 465     GLU B   121                                                      
REMARK 465     GLU B   122                                                      
REMARK 465     ALA B   123                                                      
REMARK 465     SER B   124                                                      
REMARK 465     MET B   125                                                      
REMARK 465     GLY B   126                                                      
REMARK 465     THR B   127                                                      
REMARK 465     GLN B   307                                                      
REMARK 465     PHE B   308                                                      
REMARK 465     ILE B   309                                                      
REMARK 465     LEU B   310                                                      
REMARK 465     PRO B   311                                                      
REMARK 465     SER B   312                                                      
REMARK 465     ARG B   313                                                      
REMARK 465     ILE B   314                                                      
REMARK 465     GLN B   315                                                      
REMARK 465     ALA B   316                                                      
REMARK 465     SER B   317                                                      
REMARK 465     GLN B   318                                                      
REMARK 465     SER B   319                                                      
REMARK 465     LYS B   320                                                      
REMARK 465     LEU B   321                                                      
REMARK 465     LYS B   322                                                      
REMARK 465     SER B   323                                                      
REMARK 465     LYS B   324                                                      
REMARK 465     GLY B   325                                                      
REMARK 465     LEU B   326                                                      
REMARK 465     ALA B   327                                                      
REMARK 465     SER B   328                                                      
REMARK 465     SER B   329                                                      
REMARK 465     SER B   330                                                      
REMARK 465     GLY B   331                                                      
REMARK 465     ASN B   332                                                      
REMARK 465     GLN B   333                                                      
REMARK 465     GLU B   334                                                      
REMARK 465     ASP B   586                                                      
REMARK 465     ARG B   587                                                      
REMARK 465     SER B   588                                                      
REMARK 465     VAL B   589                                                      
REMARK 465     PRO B   590                                                      
REMARK 465     SER B   591                                                      
REMARK 465     ASN B   592                                                      
REMARK 465     SER B   593                                                      
REMARK 465     SER B   594                                                      
REMARK 465     GLN B   595                                                      
REMARK 465     ARG B   596                                                      
REMARK 465     SER B   597                                                      
REMARK 465     ALA B   598                                                      
REMARK 465     ASN B   599                                                      
REMARK 465     VAL B   600                                                      
REMARK 465     SER B   601                                                      
REMARK 465     ASP B   708                                                      
REMARK 465     ALA B   709                                                      
REMARK 465     SER B   710                                                      
REMARK 465     ARG B   711                                                      
REMARK 465     ALA B   712                                                      
REMARK 465     THR B   713                                                      
REMARK 465     SER B   714                                                      
REMARK 465     GLN B   715                                                      
REMARK 465     GLU B   716                                                      
REMARK 465     SER B   717                                                      
REMARK 465     SER B   718                                                      
REMARK 465     GLN B   719                                                      
REMARK 465     ARG B   720                                                      
REMARK 465     SER B   721                                                      
REMARK 465     MET B   722                                                      
REMARK 465     ASP B   906                                                      
REMARK 465     MET B   907                                                      
REMARK 465     MET B   908                                                      
REMARK 465     PRO B   909                                                      
REMARK 465     ARG B   910                                                      
REMARK 465     LYS B   911                                                      
REMARK 465     THR B   912                                                      
REMARK 465     PHE B   913                                                      
REMARK 465     LYS B   941                                                      
REMARK 465     PHE B   942                                                      
REMARK 465     ILE B   943                                                      
REMARK 465     LEU B   944                                                      
REMARK 465     ASP B   945                                                      
REMARK 465     THR B   946                                                      
REMARK 465     GLU B   947                                                      
REMARK 465     MET B   948                                                      
REMARK 465     HIS B   949                                                      
REMARK 465     THR B   950                                                      
REMARK 465     GLU B   951                                                      
REMARK 465     ALA B   952                                                      
REMARK 465     THR B   953                                                      
REMARK 465     GLU B   954                                                      
REMARK 465     VAL B   955                                                      
REMARK 465     VAL B   956                                                      
REMARK 465     GLN B   957                                                      
REMARK 465     ALA B   980                                                      
REMARK 465     PRO B   981                                                      
REMARK 465     PHE B   982                                                      
REMARK 465     ALA B   983                                                      
REMARK 465     LYS B   984                                                      
REMARK 465     ARG B   985                                                      
REMARK 465     ILE B   986                                                      
REMARK 465     CYS B   987                                                      
REMARK 465     CYS B   988                                                      
REMARK 465     PHE B   989                                                      
REMARK 465     LYS B   990                                                      
REMARK 465     ASN B   991                                                      
REMARK 465     LYS B   992                                                      
REMARK 465     GLY B   993                                                      
REMARK 465     ARG B   994                                                      
REMARK 465     GLN B   995                                                      
REMARK 465     ASN B   996                                                      
REMARK 465     ILE B   997                                                      
REMARK 465     GLY B   998                                                      
REMARK 465     GLY B  1036                                                      
REMARK 465     ALA B  1037                                                      
REMARK 465     GLU B  1038                                                      
REMARK 465     HIS B  1039                                                      
REMARK 465     LEU B  1040                                                      
REMARK 465     SER B  1041                                                      
REMARK 465     ALA B  1042                                                      
REMARK 465     ASP B  1043                                                      
REMARK 465     ASP B  1044                                                      
REMARK 465     LYS B  1045                                                      
REMARK 465     ALA B  1046                                                      
REMARK 465     ARG B  1047                                                      
REMARK 465     ALA B  1048                                                      
REMARK 465     ALA B  1144                                                      
REMARK 465     VAL B  1145                                                      
REMARK 465     PRO B  1146                                                      
REMARK 465     ASN B  1147                                                      
REMARK 465     HIS B  1167                                                      
REMARK 465     GLY B  1168                                                      
REMARK 465     GLU B  1169                                                      
REMARK 465     LYS B  1170                                                      
REMARK 465     GLU B  1171                                                      
REMARK 465     LYS B  1214                                                      
REMARK 465     ASP B  1215                                                      
REMARK 465     ALA B  1216                                                      
REMARK 465     ALA B  1217                                                      
REMARK 465     GLN B  1248                                                      
REMARK 465     ALA B  1249                                                      
REMARK 465     GLY B  1250                                                      
REMARK 465     THR B  1251                                                      
REMARK 465     LEU B  1392                                                      
REMARK 465     GLN B  1393                                                      
REMARK 465     GLY B  1394                                                      
REMARK 465     GLU B  1395                                                      
REMARK 465     GLU B  1396                                                      
REMARK 465     ILE B  1397                                                      
REMARK 465     ILE B  1398                                                      
REMARK 465     SER B  1399                                                      
REMARK 465     GLN B  1400                                                      
REMARK 465     ASP B  1401                                                      
REMARK 465     PRO B  1402                                                      
REMARK 465     SER B  1403                                                      
REMARK 465     SER B  1404                                                      
REMARK 465     SER B  1405                                                      
REMARK 465     GLU B  1406                                                      
REMARK 465     SER B  1407                                                      
REMARK 465     ASN B  1408                                                      
REMARK 465     ALA B  1409                                                      
REMARK 465     GLU B  1410                                                      
REMARK 465     ASP B  1411                                                      
REMARK 465     SER B  1412                                                      
REMARK 465     GLU B  1413                                                      
REMARK 465     ASP B  1414                                                      
REMARK 465     GLY B  1415                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     THR A 845    OG1  CG2                                            
REMARK 470     GLU A 969    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 970    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 971    CG   OD1  OD2                                       
REMARK 470     ASP A 972    CG   OD1  OD2                                       
REMARK 470     ARG A1189    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A1300    CG   OD1  OD2                                       
REMARK 470     SER B 377    OG                                                  
REMARK 470     SER B 602    OG                                                  
REMARK 470     LEU B 642    CG   CD1  CD2                                       
REMARK 470     SER B 839    OG                                                  
REMARK 470     VAL B 840    CG1  CG2                                            
REMARK 470     ASP B 841    CG   OD1  OD2                                       
REMARK 470     LEU B 842    CG   CD1  CD2                                       
REMARK 470     ASP B 843    CG   OD1  OD2                                       
REMARK 470     THR B 844    OG1  CG2                                            
REMARK 470     LEU B 845    CG   CD1  CD2                                       
REMARK 470     LYS B1172    CG   CD   CE   NZ                                   
REMARK 470     ASP B1254    CG   OD1  OD2                                       
REMARK 470     SER B1255    OG                                                  
REMARK 470     GLN B1256    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    MET B   771     NH1  ARG B   776              2.16            
REMARK 500   O    GLN A    34     N    ALA A    37              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 662   C   -  N   -  CA  ANGL. DEV. =  10.4 DEGREES          
REMARK 500    PRO A1038   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    PRO B1222   C   -  N   -  CA  ANGL. DEV. =  16.1 DEGREES          
REMARK 500    PRO B1222   C   -  N   -  CD  ANGL. DEV. = -14.4 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  11      -72.27    -72.09                                   
REMARK 500    THR A  14     -112.71     60.84                                   
REMARK 500    LEU A  24      -79.33    -92.90                                   
REMARK 500    LYS A  25      -17.86     61.24                                   
REMARK 500    ASP A  26      -76.78    -62.26                                   
REMARK 500    GLN A  34      -60.31   -107.91                                   
REMARK 500    VAL A  38      -70.42    -75.75                                   
REMARK 500    SER A  78      -74.79    -96.38                                   
REMARK 500    ARG A 117      -73.20    -55.89                                   
REMARK 500    VAL A 122      -14.75     66.37                                   
REMARK 500    CYS A 304      -70.32    -85.99                                   
REMARK 500    SER A 374       66.97     67.04                                   
REMARK 500    LYS A 396      -64.43   -131.14                                   
REMARK 500    ILE A 432      -66.01    -96.81                                   
REMARK 500    ARG A 451      -73.93    -77.40                                   
REMARK 500    THR A 452      -22.68     71.78                                   
REMARK 500    ILE A 508      -63.99   -121.77                                   
REMARK 500    VAL A 548      -63.54    -94.51                                   
REMARK 500    VAL A 568      -10.03     66.47                                   
REMARK 500    ARG A 614      -61.34   -104.62                                   
REMARK 500    GLU A 661      137.52     68.70                                   
REMARK 500    LEU A 717      -23.04     61.33                                   
REMARK 500    GLU A 721       71.57     59.99                                   
REMARK 500    ASP A 723     -127.43     63.12                                   
REMARK 500    ALA A 788     -121.71     67.49                                   
REMARK 500    VAL A 799      -70.89    -77.63                                   
REMARK 500    ASP A 819     -144.17     56.66                                   
REMARK 500    SER A 820       35.89     39.86                                   
REMARK 500    ARG A 854      -71.29    -53.92                                   
REMARK 500    ASN A 865       87.86   -150.50                                   
REMARK 500    PHE A 921      -59.70   -128.42                                   
REMARK 500    MET A 936     -120.01     53.99                                   
REMARK 500    THR A 938     -135.35     56.78                                   
REMARK 500    SER A1014      -76.41   -113.94                                   
REMARK 500    GLN A1015       82.19     58.74                                   
REMARK 500    GLU A1016       -8.91    -51.18                                   
REMARK 500    TYR A1035      -73.21   -111.90                                   
REMARK 500    GLN A1058      -23.14     75.11                                   
REMARK 500    GLU A1063      151.51    177.98                                   
REMARK 500    VAL A1071       71.10     71.85                                   
REMARK 500    SER A1188      -56.26   -122.48                                   
REMARK 500    ARG A1189       72.59     70.44                                   
REMARK 500    LEU A1206      -75.34   -109.29                                   
REMARK 500    SER A1270      -88.02   -123.84                                   
REMARK 500    LYS A1271      -71.26   -139.87                                   
REMARK 500    ASP A1285      -69.34   -139.38                                   
REMARK 500    ASN B  62     -179.49    -67.62                                   
REMARK 500    ASP B 289     -169.97    -73.49                                   
REMARK 500    ASP B 416      -70.36    -58.11                                   
REMARK 500    GLN B 438      -71.69    -55.03                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      86 RAMACHANDRAN OUTLIERS.                        
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 ILE A 1062     GLU A 1063                  147.18                    
REMARK 500 THR B  290     THR B  291                  147.31                    
REMARK 500 ASN B 1094     ARG B 1095                  145.14                    
REMARK 500 ASP B 1284     SER B 1285                  139.99                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    HIS A 839        23.1      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3S51   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3S4Z   RELATED DB: PDB                                   
DBREF  3S4W A    1  1302  UNP    Q8K368   FANCI_MOUSE      1   1302             
DBREF  3S4W B   33  1415  UNP    Q80V62   FACD2_MOUSE     33   1415             
SEQADV 3S4W HIS A 1303  UNP  Q8K368              EXPRESSION TAG                 
SEQADV 3S4W HIS A 1304  UNP  Q8K368              EXPRESSION TAG                 
SEQADV 3S4W HIS A 1305  UNP  Q8K368              EXPRESSION TAG                 
SEQADV 3S4W HIS A 1306  UNP  Q8K368              EXPRESSION TAG                 
SEQADV 3S4W HIS A 1307  UNP  Q8K368              EXPRESSION TAG                 
SEQADV 3S4W HIS A 1308  UNP  Q8K368              EXPRESSION TAG                 
SEQADV 3S4W     B       UNP  Q80V62    SER   851 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    SER   852 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    SER   853 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    ALA   854 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    VAL   855 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    ALA   856 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    ALA   857 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    LYS   858 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    ASN   859 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    ARG   860 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    ASN   861 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    LYS   862 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    GLY   863 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    LYS   864 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    THR   865 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    GLY   866 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    GLY   867 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    LYS   868 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    LYS   869 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    GLN   870 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    LYS   871 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    ALA   872 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    ASP   873 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    SER   874 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    ASN   875 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    LYS   876 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    ALA   877 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    SER   878 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    CYS   879 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    SER   880 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    ASP   881 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    THR   882 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    LEU   883 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    LEU   884 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    THR   885 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    GLU   886 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    ASP   887 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    THR   888 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    SER   889 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    GLU   890 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    CYS   891 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    ASP   892 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    MET   893 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    ALA   894 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    PRO   895 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    SER   896 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    GLY   897 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    ARG   898 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    SER   899 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    HIS   900 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    VAL   901 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    ASP   902 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    LYS   903 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    GLU   904 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    SER   905 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    THR   906 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    GLY   907 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    LYS   908 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    GLU   909 DELETION                       
SEQADV 3S4W     B       UNP  Q80V62    GLY   910 DELETION                       
SEQRES   1 A 1308  MET ASP LEU LYS ILE LEU SER LEU ALA THR ASP LYS THR          
SEQRES   2 A 1308  THR ASP LYS LEU GLN GLU PHE LEU GLN THR LEU LYS ASP          
SEQRES   3 A 1308  ASP ASP LEU ALA SER LEU LEU GLN ASN GLN ALA VAL LYS          
SEQRES   4 A 1308  GLY ARG ALA VAL GLY THR LEU LEU ARG ALA VAL LEU LYS          
SEQRES   5 A 1308  GLY SER PRO CYS SER GLU GLU ASP GLY ALA LEU ARG ARG          
SEQRES   6 A 1308  TYR LYS ILE TYR SER CYS CYS ILE GLN LEU VAL GLU SER          
SEQRES   7 A 1308  GLY ASP LEU GLN GLN ASP VAL ALA SER GLU ILE ILE GLY          
SEQRES   8 A 1308  LEU LEU MET LEU GLU VAL HIS HIS PHE PRO GLY PRO LEU          
SEQRES   9 A 1308  LEU VAL ASP LEU ALA SER ASP PHE VAL GLY ALA VAL ARG          
SEQRES  10 A 1308  GLU ASP ARG LEU VAL ASN GLY LYS SER LEU GLU LEU LEU          
SEQRES  11 A 1308  PRO ILE ILE LEU THR ALA LEU ALA THR LYS LYS GLU VAL          
SEQRES  12 A 1308  LEU ALA CYS GLY LYS GLY ASP LEU ASN GLY GLU GLU TYR          
SEQRES  13 A 1308  LYS ARG GLN LEU ILE ASP THR LEU CYS SER VAL ARG TRP          
SEQRES  14 A 1308  PRO GLN ARG TYR MET ILE GLN LEU THR SER VAL PHE LYS          
SEQRES  15 A 1308  ASP VAL CYS LEU THR PRO GLU GLU MET ASN LEU VAL VAL          
SEQRES  16 A 1308  ALA LYS VAL LEU THR MET PHE SER LYS LEU ASN LEU GLN          
SEQRES  17 A 1308  GLU ILE PRO PRO LEU VAL TYR GLN LEU LEU VAL LEU SER          
SEQRES  18 A 1308  SER LYS GLY SER ARG ARG SER VAL LEU ASP GLY ILE ILE          
SEQRES  19 A 1308  ALA PHE PHE ARG GLU LEU ASP LYS GLN HIS ARG GLU GLU          
SEQRES  20 A 1308  GLN SER SER ASP GLU LEU SER GLU LEU ILE THR ALA PRO          
SEQRES  21 A 1308  ALA ASP GLU LEU TYR HIS VAL GLU GLY THR VAL ILE LEU          
SEQRES  22 A 1308  HIS ILE VAL PHE ALA ILE LYS LEU ASP CYS GLU LEU GLY          
SEQRES  23 A 1308  ARG GLU LEU LEU LYS HIS LEU LYS ALA GLY GLN GLN GLY          
SEQRES  24 A 1308  ASP PRO SER LYS CYS LEU CYS PRO PHE SER ILE ALA LEU          
SEQRES  25 A 1308  LEU LEU SER LEU THR ARG ILE GLN ARG PHE GLU GLU GLN          
SEQRES  26 A 1308  VAL PHE ASP LEU LEU LYS THR SER VAL VAL LYS SER PHE          
SEQRES  27 A 1308  LYS ASP LEU GLN LEU LEU GLN GLY SER LYS PHE LEU GLN          
SEQRES  28 A 1308  THR LEU VAL PRO GLN ARG THR CYS VAL SER THR MET ILE          
SEQRES  29 A 1308  LEU GLU VAL VAL ARG ASN SER VAL HIS SER TRP ASP HIS          
SEQRES  30 A 1308  VAL THR GLN GLY LEU ILE GLU PHE GLY PHE ILE LEU MET          
SEQRES  31 A 1308  ASP SER TYR GLY PRO LYS LYS ILE LEU ASP GLY LYS ALA          
SEQRES  32 A 1308  VAL GLU ILE GLY THR SER LEU SER LYS MET THR ASN GLN          
SEQRES  33 A 1308  HIS ALA CYS LYS LEU GLY ALA ASN ILE LEU LEU GLU THR          
SEQRES  34 A 1308  PHE LYS ILE HIS GLU MET ILE ARG GLN GLU ILE LEU GLU          
SEQRES  35 A 1308  GLN VAL LEU ASN ARG VAL VAL THR ARG THR SER SER PRO          
SEQRES  36 A 1308  ILE ASN HIS PHE LEU ASP LEU PHE SER ASP ILE ILE MET          
SEQRES  37 A 1308  TYR ALA PRO LEU ILE LEU GLN ASN CYS SER LYS VAL THR          
SEQRES  38 A 1308  GLU THR PHE ASP TYR LEU THR PHE LEU PRO LEU GLN THR          
SEQRES  39 A 1308  VAL GLN GLY LEU LEU LYS ALA VAL GLN PRO LEU LEU LYS          
SEQRES  40 A 1308  ILE SER MET SER MET ARG ASP SER LEU ILE LEU VAL LEU          
SEQRES  41 A 1308  ARG LYS ALA MET PHE ALA SER GLN LEU ASP ALA ARG LYS          
SEQRES  42 A 1308  SER ALA VAL ALA GLY PHE LEU LEU LEU LEU LYS ASN PHE          
SEQRES  43 A 1308  LYS VAL LEU GLY SER LEU PRO SER SER GLN CYS THR GLN          
SEQRES  44 A 1308  SER ILE GLY VAL THR GLN VAL ARG VAL ASP VAL HIS SER          
SEQRES  45 A 1308  ARG TYR SER ALA VAL ALA ASN GLU THR PHE CYS LEU GLU          
SEQRES  46 A 1308  ILE ILE ASP SER LEU LYS ARG SER LEU GLY GLN GLN ALA          
SEQRES  47 A 1308  ASP ILE ARG LEU MET LEU TYR ASP GLY PHE TYR ASP VAL          
SEQRES  48 A 1308  LEU ARG ARG ASN SER GLN LEU ALA SER SER ILE MET GLN          
SEQRES  49 A 1308  THR LEU PHE SER GLN LEU LYS GLN PHE TYR GLU PRO GLU          
SEQRES  50 A 1308  PRO ASP LEU LEU PRO PRO LEU LYS LEU GLY ALA CYS VAL          
SEQRES  51 A 1308  LEU THR GLN GLY SER GLN ILE PHE LEU GLN GLU PRO LEU          
SEQRES  52 A 1308  ASP HIS LEU LEU SER CYS ILE GLN HIS CYS LEU ALA TRP          
SEQRES  53 A 1308  TYR LYS SER ARG VAL VAL PRO LEU GLN GLN GLY ASP GLU          
SEQRES  54 A 1308  GLY GLU GLU GLU GLU GLU GLU LEU TYR SER GLU LEU ASP          
SEQRES  55 A 1308  ASP MET LEU GLU SER ILE THR VAL ARG MET ILE LYS SER          
SEQRES  56 A 1308  GLU LEU GLU ASP PHE GLU LEU ASP LYS SER ALA ASP PHE          
SEQRES  57 A 1308  SER GLN ASN THR ASN VAL GLY ILE LYS ASN ASN ILE CYS          
SEQRES  58 A 1308  ALA CYS LEU ILE MET GLY VAL CYS GLU VAL LEU MET GLU          
SEQRES  59 A 1308  TYR ASN PHE SER ILE SER ASN PHE SER LYS SER LYS PHE          
SEQRES  60 A 1308  GLU GLU ILE LEU SER LEU PHE THR CYS TYR LYS LYS PHE          
SEQRES  61 A 1308  SER ASP ILE LEU SER GLU LYS ALA GLY LYS GLY LYS ALA          
SEQRES  62 A 1308  LYS MET THR SER LYS VAL SER ASP SER LEU LEU SER LEU          
SEQRES  63 A 1308  LYS PHE VAL SER ASP LEU LEU THR ALA LEU PHE ARG ASP          
SEQRES  64 A 1308  SER ILE GLN SER HIS GLU GLU SER LEU SER VAL LEU ARG          
SEQRES  65 A 1308  SER SER GLY GLU PHE MET HIS TYR ALA VAL ASN VAL THR          
SEQRES  66 A 1308  LEU GLN LYS ILE GLN GLN LEU ILE ARG THR GLY HIS VAL          
SEQRES  67 A 1308  SER GLY PRO ASP GLY GLN ASN PRO ASP LYS ILE PHE GLN          
SEQRES  68 A 1308  ASN LEU CYS ASP ILE THR ARG VAL LEU LEU TRP ARG TYR          
SEQRES  69 A 1308  THR SER ILE PRO THR SER VAL GLU GLU SER GLY LYS LYS          
SEQRES  70 A 1308  GLU LYS GLY LYS SER ILE SER LEU LEU CYS LEU GLU GLY          
SEQRES  71 A 1308  LEU GLN LYS THR PHE SER VAL VAL LEU GLN PHE TYR GLN          
SEQRES  72 A 1308  PRO LYS VAL GLN GLN PHE LEU GLN ALA LEU ASP VAL MET          
SEQRES  73 A 1308  GLY THR GLU GLU GLU GLU ALA GLY VAL THR VAL THR GLN          
SEQRES  74 A 1308  ARG ALA SER PHE GLN ILE ARG GLN PHE GLN ARG SER LEU          
SEQRES  75 A 1308  LEU ASN LEU LEU SER SER GLU GLU ASP ASP PHE ASN SER          
SEQRES  76 A 1308  LYS GLU ALA LEU LEU LEU ILE ALA VAL LEU SER THR LEU          
SEQRES  77 A 1308  SER ARG LEU LEU GLU PRO THR SER PRO GLN PHE VAL GLN          
SEQRES  78 A 1308  MET LEU SER TRP THR SER LYS ILE CYS LYS GLU TYR SER          
SEQRES  79 A 1308  GLN GLU ASP ALA SER PHE CYS LYS SER LEU MET ASN LEU          
SEQRES  80 A 1308  PHE PHE SER LEU HIS VAL LEU TYR LYS SER PRO VAL THR          
SEQRES  81 A 1308  LEU LEU ARG ASP LEU SER GLN ASP ILE HIS GLY GLN LEU          
SEQRES  82 A 1308  GLY ASP ILE ASP GLN ASP VAL GLU ILE GLU LYS THR ASP          
SEQRES  83 A 1308  HIS PHE ALA VAL VAL ASN LEU ARG THR ALA ALA PRO THR          
SEQRES  84 A 1308  VAL CYS LEU LEU VAL LEU SER GLN ALA GLU LYS VAL LEU          
SEQRES  85 A 1308  GLU GLU VAL ASP TRP LEU ILE ALA LYS ILE LYS GLY SER          
SEQRES  86 A 1308  ALA ASN GLN GLU THR LEU SER ASP LYS VAL THR PRO GLU          
SEQRES  87 A 1308  ASP ALA SER SER GLN ALA VAL PRO PRO THR LEU LEU ILE          
SEQRES  88 A 1308  GLU LYS ALA ILE VAL MET GLN LEU GLY THR LEU VAL THR          
SEQRES  89 A 1308  PHE PHE HIS GLU LEU VAL GLN THR ALA LEU PRO SER GLY          
SEQRES  90 A 1308  SER CYS VAL ASP THR LEU LEU LYS GLY LEU SER LYS ILE          
SEQRES  91 A 1308  TYR SER THR LEU THR ALA PHE VAL LYS TYR TYR LEU GLN          
SEQRES  92 A 1308  VAL CYS GLN SER SER ARG GLY ILE PRO ASN THR VAL GLU          
SEQRES  93 A 1308  LYS LEU VAL LYS LEU SER GLY SER HIS LEU THR PRO VAL          
SEQRES  94 A 1308  CYS TYR SER PHE ILE SER TYR VAL GLN ASN LYS SER SER          
SEQRES  95 A 1308  ASP ALA PRO LYS CYS SER GLU LYS GLU LYS ALA ALA VAL          
SEQRES  96 A 1308  SER THR THR MET ALA LYS VAL LEU ARG GLU THR LYS PRO          
SEQRES  97 A 1308  ILE PRO ASN LEU VAL PHE ALA ILE GLU GLN TYR GLU LYS          
SEQRES  98 A 1308  PHE LEU ILE GLN LEU SER LYS LYS SER LYS VAL ASN LEU          
SEQRES  99 A 1308  MET GLN HIS MET LYS LEU SER THR SER ARG ASP PHE LYS          
SEQRES 100 A 1308  ILE LYS GLY SER VAL LEU ASP MET VAL LEU ARG GLU ASP          
SEQRES 101 A 1308  GLU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 B 1323  SER HIS ASN SER HIS GLU VAL GLU GLU ASN GLY SER VAL          
SEQRES   2 B 1323  PHE VAL LYS LEU LEU LYS ALA SER GLY LEU THR LEU LYS          
SEQRES   3 B 1323  THR GLY GLU ASN GLN ASN GLN LEU GLY VAL ASP GLN VAL          
SEQRES   4 B 1323  ILE PHE GLN ARG LYS LEU PHE GLN ALA LEU ARG LYS HIS          
SEQRES   5 B 1323  PRO ALA TYR PRO LYS VAL ILE GLU GLU PHE VAL ASN GLY          
SEQRES   6 B 1323  LEU GLU SER TYR THR GLU ASP SER GLU SER LEU ARG ASN          
SEQRES   7 B 1323  CYS LEU LEU SER CYS GLU ARG LEU GLN ASP GLU GLU ALA          
SEQRES   8 B 1323  SER MET GLY THR PHE TYR SER LYS SER LEU ILE LYS LEU          
SEQRES   9 B 1323  LEU LEU GLY ILE ASP ILE LEU GLN PRO ALA ILE ILE LYS          
SEQRES  10 B 1323  MET LEU PHE GLU LYS VAL PRO GLN PHE LEU PHE GLU SER          
SEQRES  11 B 1323  GLU ASN ARG ASP GLY ILE ASN MET ALA ARG LEU ILE ILE          
SEQRES  12 B 1323  ASN GLN LEU LYS TRP LEU ASP ARG ILE VAL ASP GLY LYS          
SEQRES  13 B 1323  ASP LEU THR ALA GLN MET MET GLN LEU ILE SER VAL ALA          
SEQRES  14 B 1323  PRO VAL ASN LEU GLN HIS ASP PHE ILE THR SER LEU PRO          
SEQRES  15 B 1323  GLU ILE LEU GLY ASP SER GLN HIS ALA ASN VAL GLY LYS          
SEQRES  16 B 1323  GLU LEU GLY GLU LEU LEU VAL GLN ASN THR SER LEU THR          
SEQRES  17 B 1323  VAL PRO ILE LEU ASP VAL PHE SER SER LEU ARG LEU ASP          
SEQRES  18 B 1323  PRO ASN PHE LEU SER LYS ILE ARG GLN LEU VAL MET GLY          
SEQRES  19 B 1323  LYS LEU SER SER VAL ARG LEU GLU ASP PHE PRO VAL ILE          
SEQRES  20 B 1323  VAL LYS PHE LEU LEU HIS SER VAL THR ASP THR THR SER          
SEQRES  21 B 1323  LEU GLU VAL ILE ALA GLU LEU ARG GLU ASN LEU ASN VAL          
SEQRES  22 B 1323  GLN GLN PHE ILE LEU PRO SER ARG ILE GLN ALA SER GLN          
SEQRES  23 B 1323  SER LYS LEU LYS SER LYS GLY LEU ALA SER SER SER GLY          
SEQRES  24 B 1323  ASN GLN GLU ASN SER ASP LYS ASP CYS ILE VAL LEU VAL          
SEQRES  25 B 1323  PHE ASP VAL ILE LYS SER ALA ILE ARG TYR GLU LYS THR          
SEQRES  26 B 1323  ILE SER GLU ALA TRP PHE LYS ALA ILE GLU ARG ILE GLU          
SEQRES  27 B 1323  SER ALA ALA GLU HIS LYS SER LEU ASP VAL VAL MET LEU          
SEQRES  28 B 1323  LEU ILE ILE TYR SER THR SER THR GLN THR LYS LYS GLY          
SEQRES  29 B 1323  VAL GLU LYS LEU LEU ARG ASN LYS ILE GLN SER ASP CYS          
SEQRES  30 B 1323  ILE GLN GLU GLN LEU LEU ASP SER ALA PHE SER THR HIS          
SEQRES  31 B 1323  TYR LEU VAL LEU LYS ASP ILE CYS PRO SER ILE LEU LEU          
SEQRES  32 B 1323  LEU ALA GLN THR LEU PHE HIS SER GLN ASP GLN ARG ILE          
SEQRES  33 B 1323  ILE LEU PHE GLY SER LEU LEU TYR LYS TYR ALA PHE LYS          
SEQRES  34 B 1323  PHE PHE ASP THR TYR CYS GLN GLN GLU VAL VAL GLY ALA          
SEQRES  35 B 1323  LEU VAL THR HIS VAL CYS SER GLY THR GLU ALA GLU VAL          
SEQRES  36 B 1323  ASP THR ALA LEU ASP VAL LEU LEU GLU LEU ILE VAL LEU          
SEQRES  37 B 1323  ASN ALA SER ALA MET ARG LEU ASN ALA ALA PHE VAL LYS          
SEQRES  38 B 1323  GLY ILE LEU ASP TYR LEU GLU ASN MET SER PRO GLN GLN          
SEQRES  39 B 1323  ILE ARG LYS ILE PHE CYS ILE LEU SER THR LEU ALA PHE          
SEQRES  40 B 1323  SER GLN GLN PRO GLY THR SER ASN HIS ILE GLN ASP ASP          
SEQRES  41 B 1323  MET HIS LEU VAL ILE ARG LYS GLN LEU SER SER THR VAL          
SEQRES  42 B 1323  PHE LYS TYR LYS LEU ILE GLY ILE ILE GLY ALA VAL THR          
SEQRES  43 B 1323  MET ALA GLY ILE MET ALA GLU ASP ARG SER VAL PRO SER          
SEQRES  44 B 1323  ASN SER SER GLN ARG SER ALA ASN VAL SER SER GLU GLN          
SEQRES  45 B 1323  ARG THR GLN VAL THR SER LEU LEU GLN LEU VAL HIS SER          
SEQRES  46 B 1323  CYS THR GLU HIS SER PRO TRP ALA SER SER LEU TYR TYR          
SEQRES  47 B 1323  ASP GLU PHE ALA ASN LEU ILE GLN GLU ARG LYS LEU ALA          
SEQRES  48 B 1323  PRO LYS THR LEU GLU TRP VAL GLY GLN THR ILE PHE ASN          
SEQRES  49 B 1323  ASP PHE GLN ASP ALA PHE VAL VAL ASP PHE CYS ALA ALA          
SEQRES  50 B 1323  PRO GLU GLY ASP PHE PRO PHE PRO VAL LYS ALA LEU TYR          
SEQRES  51 B 1323  GLY LEU GLU GLU TYR SER THR GLN ASP GLY ILE VAL ILE          
SEQRES  52 B 1323  ASN LEU LEU PRO LEU PHE TYR GLN GLU CYS ALA LYS ASP          
SEQRES  53 B 1323  ALA SER ARG ALA THR SER GLN GLU SER SER GLN ARG SER          
SEQRES  54 B 1323  MET SER SER LEU CYS LEU ALA SER HIS PHE ARG LEU LEU          
SEQRES  55 B 1323  ARG LEU CYS VAL ALA ARG GLN HIS ASP GLY ASN LEU ASP          
SEQRES  56 B 1323  GLU ILE ASP GLY LEU LEU ASP CYS PRO LEU PHE LEU PRO          
SEQRES  57 B 1323  ASP LEU GLU PRO GLY GLU LYS LEU GLU SER MET SER ALA          
SEQRES  58 B 1323  LYS ASP ARG SER LEU MET CYS SER LEU THR PHE LEU THR          
SEQRES  59 B 1323  PHE ASN TRP PHE ARG GLU VAL VAL ASN ALA PHE CYS GLN          
SEQRES  60 B 1323  GLN THR SER PRO GLU MET LYS GLY LYS VAL LEU SER ARG          
SEQRES  61 B 1323  LEU LYS ASP LEU VAL GLU LEU GLN GLY ILE LEU GLU LYS          
SEQRES  62 B 1323  TYR LEU ALA VAL ILE PRO ASP TYR VAL PRO PRO PHE ALA          
SEQRES  63 B 1323  SER VAL ASP LEU ASP THR LEU ASP MET MET PRO ARG LYS          
SEQRES  64 B 1323  THR PHE VAL SER LEU GLN ASN TYR ARG ALA PHE PHE ARG          
SEQRES  65 B 1323  GLU LEU ASP ILE GLU VAL PHE SER ILE LEU HIS SER GLY          
SEQRES  66 B 1323  LEU VAL THR LYS PHE ILE LEU ASP THR GLU MET HIS THR          
SEQRES  67 B 1323  GLU ALA THR GLU VAL VAL GLN LEU GLY PRO ALA GLU LEU          
SEQRES  68 B 1323  LEU PHE LEU LEU GLU ASP LEU SER GLN LYS LEU GLU ASN          
SEQRES  69 B 1323  MET LEU THR ALA PRO PHE ALA LYS ARG ILE CYS CYS PHE          
SEQRES  70 B 1323  LYS ASN LYS GLY ARG GLN ASN ILE GLY PHE SER HIS LEU          
SEQRES  71 B 1323  HIS GLN ARG SER VAL GLN ASP ILE VAL HIS CYS VAL VAL          
SEQRES  72 B 1323  GLN LEU LEU THR PRO MET CYS ASN HIS LEU GLU ASN ILE          
SEQRES  73 B 1323  HIS ASN PHE PHE GLN CYS LEU GLY ALA GLU HIS LEU SER          
SEQRES  74 B 1323  ALA ASP ASP LYS ALA ARG ALA THR ALA GLN GLU GLN HIS          
SEQRES  75 B 1323  THR MET ALA CYS CYS TYR GLN LYS LEU LEU GLN VAL LEU          
SEQRES  76 B 1323  HIS ALA LEU PHE ALA TRP LYS GLY PHE THR HIS GLN SER          
SEQRES  77 B 1323  LYS HIS ARG LEU LEU HIS SER ALA LEU GLU VAL LEU SER          
SEQRES  78 B 1323  ASN ARG LEU LYS GLN MET GLU GLN ASP GLN PRO LEU GLU          
SEQRES  79 B 1323  GLU LEU VAL SER GLN SER PHE SER TYR LEU GLN ASN PHE          
SEQRES  80 B 1323  HIS HIS SER VAL PRO SER PHE GLN CYS GLY LEU TYR LEU          
SEQRES  81 B 1323  LEU ARG LEU LEU MET ALA LEU LEU GLU LYS SER ALA VAL          
SEQRES  82 B 1323  PRO ASN GLN LYS LYS GLU LYS LEU ALA SER LEU ALA LYS          
SEQRES  83 B 1323  GLN LEU LEU CYS ARG ALA TRP PRO HIS GLY GLU LYS GLU          
SEQRES  84 B 1323  LYS ASN PRO THR PHE ASN ASP HIS LEU HIS ASP VAL LEU          
SEQRES  85 B 1323  TYR ILE TYR LEU GLU HIS THR ASP ASN VAL LEU LYS ALA          
SEQRES  86 B 1323  ILE GLU GLU ILE THR GLY VAL GLY VAL PRO GLU LEU VAL          
SEQRES  87 B 1323  SER ALA PRO LYS ASP ALA ALA SER SER THR PHE PRO THR          
SEQRES  88 B 1323  LEU THR ARG HIS THR PHE VAL ILE PHE PHE ARG VAL MET          
SEQRES  89 B 1323  MET ALA GLU LEU GLU LYS THR VAL LYS GLY LEU GLN ALA          
SEQRES  90 B 1323  GLY THR ALA ALA ASP SER GLN GLN VAL HIS GLU GLU LYS          
SEQRES  91 B 1323  LEU LEU TYR TRP ASN MET ALA VAL ARG ASP PHE SER ILE          
SEQRES  92 B 1323  LEU LEU ASN LEU MET LYS VAL PHE ASP SER TYR PRO VAL          
SEQRES  93 B 1323  LEU HIS VAL CYS LEU LYS TYR GLY ARG ARG PHE VAL GLU          
SEQRES  94 B 1323  ALA PHE LEU LYS GLN CYS MET PRO LEU LEU ASP PHE SER          
SEQRES  95 B 1323  PHE ARG LYS HIS ARG GLU ASP VAL LEU SER LEU LEU GLN          
SEQRES  96 B 1323  THR LEU GLN LEU ASN THR ARG LEU LEU HIS HIS LEU CYS          
SEQRES  97 B 1323  GLY HIS SER LYS ILE ARG GLN ASP THR ARG LEU THR LYS          
SEQRES  98 B 1323  HIS VAL PRO LEU LEU LYS LYS SER LEU GLU LEU LEU VAL          
SEQRES  99 B 1323  CYS ARG VAL LYS ALA MET LEU VAL LEU ASN ASN CYS ARG          
SEQRES 100 B 1323  GLU ALA PHE TRP LEU GLY THR LEU LYS ASN ARG ASP LEU          
SEQRES 101 B 1323  GLN GLY GLU GLU ILE ILE SER GLN ASP PRO SER SER SER          
SEQRES 102 B 1323  GLU SER ASN ALA GLU ASP SER GLU ASP GLY                      
HELIX    1   1 MET A    1  ALA A    9  1                                   9    
HELIX    2   2 THR A   14  THR A   23  1                                  10    
HELIX    3   3 ASP A   28  LYS A   39  1                                  12    
HELIX    4   4 GLY A   40  GLY A   53  1                                  14    
HELIX    5   5 GLU A   58  GLY A   79  1                                  22    
HELIX    6   6 GLN A   82  VAL A   97  1                                  16    
HELIX    7   7 PRO A  101  GLU A  118  1                                  18    
HELIX    8   8 ASN A  123  LEU A  127  5                                   5    
HELIX    9   9 GLU A  128  ALA A  138  1                                  11    
HELIX   10  10 ASN A  152  VAL A  167  1                                  16    
HELIX   11  11 TYR A  173  LYS A  182  1                                  10    
HELIX   12  12 THR A  187  MET A  201  1                                  15    
HELIX   13  13 PHE A  202  LEU A  205  5                                   4    
HELIX   14  14 ASN A  206  GLN A  208  5                                   3    
HELIX   15  15 GLU A  209  SER A  222  1                                  14    
HELIX   16  16 SER A  225  SER A  249  1                                  25    
HELIX   17  17 PRO A  260  ASP A  282  1                                  23    
HELIX   18  18 CYS A  283  LYS A  294  1                                  12    
HELIX   19  19 GLY A  299  LEU A  305  1                                   7    
HELIX   20  20 CYS A  306  THR A  317  1                                  12    
HELIX   21  21 ARG A  321  GLN A  345  1                                  25    
HELIX   22  22 SER A  347  VAL A  354  1                                   8    
HELIX   23  23 CYS A  359  ASN A  370  1                                  12    
HELIX   24  24 SER A  371  SER A  374  5                                   4    
HELIX   25  25 TRP A  375  GLY A  394  1                                  20    
HELIX   26  26 SER A  411  HIS A  433  1                                  23    
HELIX   27  27 ILE A  436  ARG A  451  1                                  16    
HELIX   28  28 ILE A  456  ALA A  470  1                                  15    
HELIX   29  29 ALA A  470  GLN A  475  1                                   6    
HELIX   30  30 CYS A  477  THR A  483  1                                   7    
HELIX   31  31 PHE A  484  TYR A  486  5                                   3    
HELIX   32  32 PRO A  491  VAL A  502  1                                  12    
HELIX   33  33 VAL A  502  LYS A  507  1                                   6    
HELIX   34  34 SER A  509  MET A  524  1                                  16    
HELIX   35  35 GLN A  528  ASN A  545  1                                  18    
HELIX   36  36 ASN A  545  GLY A  550  1                                   6    
HELIX   37  37 SER A  554  SER A  560  1                                   7    
HELIX   38  38 HIS A  571  ARG A  592  1                                  22    
HELIX   39  39 SER A  593  GLN A  596  5                                   4    
HELIX   40  40 GLN A  597  ASN A  615  1                                  19    
HELIX   41  41 LEU A  618  TYR A  634  1                                  17    
HELIX   42  42 LEU A  646  ALA A  648  5                                   3    
HELIX   43  43 PRO A  662  ARG A  680  1                                  19    
HELIX   44  44 GLU A  696  SER A  715  1                                  20    
HELIX   45  45 THR A  732  SER A  760  1                                  29    
HELIX   46  46 SER A  763  LYS A  787  1                                  25    
HELIX   47  47 SER A  805  ARG A  818  1                                  14    
HELIX   48  48 GLN A  822  SER A  827  5                                   6    
HELIX   49  49 LEU A  828  SER A  833  1                                   6    
HELIX   50  50 GLY A  835  THR A  855  1                                  21    
HELIX   51  51 ASN A  865  SER A  886  1                                  22    
HELIX   52  52 SER A  902  PHE A  921  1                                  20    
HELIX   53  53 TYR A  922  PRO A  924  5                                   3    
HELIX   54  54 LYS A  925  LEU A  933  1                                   9    
HELIX   55  55 THR A  946  SER A  968  1                                  23    
HELIX   56  56 ASN A  974  ARG A  990  1                                  17    
HELIX   57  57 SER A  996  TYR A 1013  1                                  18    
HELIX   58  58 ASP A 1017  VAL A 1033  1                                  17    
HELIX   59  59 PRO A 1038  GLY A 1054  1                                  17    
HELIX   60  60 ASN A 1072  ALA A 1077  1                                   6    
HELIX   61  61 PRO A 1078  GLY A 1104  1                                  27    
HELIX   62  62 PRO A 1127  VAL A 1150  1                                  24    
HELIX   63  63 SER A 1158  CYS A 1185  1                                  28    
HELIX   64  64 PRO A 1192  LYS A 1200  1                                   9    
HELIX   65  65 LEU A 1201  LEU A 1206  1                                   6    
HELIX   66  66 LEU A 1206  SER A 1222  1                                  17    
HELIX   67  67 PRO A 1248  SER A 1270  1                                  23    
HELIX   68  68 SER A 1291  ARG A 1298  1                                   8    
HELIX   69  69 SER B   44  SER B   53  1                                  10    
HELIX   70  70 VAL B   71  HIS B   84  1                                  14    
HELIX   71  71 ALA B   86  THR B  102  1                                  17    
HELIX   72  72 ASP B  104  LEU B  112  1                                   9    
HELIX   73  73 SER B  132  ILE B  140  1                                   9    
HELIX   74  74 LEU B  143  PHE B  160  1                                  18    
HELIX   75  75 ASN B  169  ASN B  176  1                                   8    
HELIX   76  76 GLN B  177  LYS B  179  5                                   3    
HELIX   77  77 ASP B  186  ALA B  201  1                                  16    
HELIX   78  78 LEU B  205  SER B  212  1                                   8    
HELIX   79  79 SER B  212  LEU B  217  1                                   6    
HELIX   80  80 GLY B  218  SER B  220  5                                   3    
HELIX   81  81 GLN B  221  ASN B  236  1                                  16    
HELIX   82  82 LEU B  239  LEU B  250  1                                  12    
HELIX   83  83 ASP B  253  LYS B  267  1                                  15    
HELIX   84  84 GLU B  274  SER B  286  1                                  13    
HELIX   85  85 THR B  291  VAL B  305  1                                  15    
HELIX   86  86 ASN B  335  GLU B  355  1                                  21    
HELIX   87  87 GLU B  355  ILE B  369  1                                  15    
HELIX   88  88 GLU B  370  ALA B  372  5                                   3    
HELIX   89  89 SER B  377  SER B  390  1                                  14    
HELIX   90  90 SER B  390  GLN B  406  1                                  17    
HELIX   91  91 GLN B  411  LYS B  427  1                                  17    
HELIX   92  92 ILE B  429  HIS B  442  1                                  14    
HELIX   93  93 ASP B  445  PHE B  462  1                                  18    
HELIX   94  94 ASP B  464  GLY B  482  1                                  19    
HELIX   95  95 THR B  483  ASN B  501  1                                  19    
HELIX   96  96 ASN B  501  ASN B  508  1                                   8    
HELIX   97  97 ASN B  508  GLY B  514  1                                   7    
HELIX   98  98 ILE B  515  MET B  522  5                                   8    
HELIX   99  99 SER B  523  GLN B  542  1                                  20    
HELIX  100 100 ASN B  547  SER B  562  1                                  16    
HELIX  101 101 VAL B  565  MET B  583  1                                  19    
HELIX  102 102 SER B  602  GLU B  620  1                                  19    
HELIX  103 103 SER B  622  ARG B  640  1                                  19    
HELIX  104 104 ALA B  643  PHE B  662  1                                  20    
HELIX  105 105 ASN B  696  LYS B  707  1                                  12    
HELIX  106 106 CYS B  726  ASP B  743  1                                  18    
HELIX  107 107 ILE B  749  LEU B  753  5                                   5    
HELIX  108 108 ALA B  773  CYS B  798  1                                  26    
HELIX  109 109 SER B  802  ALA B  828  1                                  27    
HELIX  110 110 SER B  915  ARG B  920  1                                   6    
HELIX  111 111 ASP B  927  SER B  936  5                                  10    
HELIX  112 112 GLY B  959  THR B  979  1                                  21    
HELIX  113 113 SER B 1006  LEU B 1035  1                                  30    
HELIX  114 114 THR B 1049  ALA B 1072  1                                  24    
HELIX  115 115 LYS B 1081  VAL B 1091  1                                  11    
HELIX  116 116 PRO B 1104  ASN B 1118  1                                  15    
HELIX  117 117 PHE B 1119  VAL B 1123  5                                   5    
HELIX  118 118 SER B 1125  GLU B 1141  1                                  17    
HELIX  119 119 GLN B 1148  LEU B 1161  1                                  14    
HELIX  120 120 ASN B 1173  THR B 1191  1                                  19    
HELIX  121 121 ASN B 1193  VAL B 1204  1                                  12    
HELIX  122 122 VAL B 1206  SER B 1211  1                                   6    
HELIX  123 123 THR B 1225  LYS B 1245  1                                  21    
HELIX  124 124 ALA B 1253  LYS B 1281  1                                  29    
HELIX  125 125 TYR B 1286  GLN B 1306  1                                  21    
HELIX  126 126 GLN B 1306  PHE B 1315  1                                  10    
HELIX  127 127 HIS B 1318  GLY B 1341  1                                  24    
HELIX  128 128 SER B 1343  GLN B 1347  5                                   5    
HELIX  129 129 ASP B 1348  LYS B 1353  5                                   6    
HELIX  130 130 HIS B 1354  VAL B 1374  1                                  21    
HELIX  131 131 CYS B 1378  LYS B 1388  1                                  11    
SHEET    1   A 2 VAL A 650  GLN A 653  0                                        
SHEET    2   A 2 GLN A 656  LEU A 659 -1  O  PHE A 658   N  LEU A 651           
SHEET    1   B 2 LEU B  55  THR B  56  0                                        
SHEET    2   B 2 GLN B  65  LEU B  66 -1  O  GLN B  65   N  THR B  56           
SHEET    1   C 2 VAL B 663  VAL B 664  0                                        
SHEET    2   C 2 VAL B 694  ILE B 695 -1  O  VAL B 694   N  VAL B 664           
SHEET    1   D 2 LYS B 679  LEU B 681  0                                        
SHEET    2   D 2 LEU B 757  LEU B 759 -1  O  LEU B 757   N  LEU B 681           
CRYST1   83.800  110.400  350.500  90.00  90.00  90.00 P 21 21 21    4          
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      0.011933  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009058  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002853        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system