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Entry: 4V0C
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HEADER    SIGNALING PROTEIN                       14-SEP-14   4V0C              
TITLE     CRYSTAL STRUCTURE OF THE KV7.1 PROXIMAL C-TERMINAL DOMAIN             
TITLE    2 IN COMPLEX WITH CALMODULIN                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY KQT MEMBER 1;    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: PROXIMAL C-TERMINAL DOMAIN, RESIDUES 352-396 AND RESIDUES  
COMPND   5  502-539;                                                            
COMPND   6 SYNONYM: IKS PRODUCING SLOW VOLTAGE-GATED POTASSIUM CHANNEL SUBUNIT  
COMPND   7  ALPHA KVLQT1, KQT-LIKE 1, VOLTAGE-GATED POTASSIUM CHANNEL SUBUNIT   
COMPND   8  KV7.1, KV7.1 CHANNEL;                                               
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES;                                                       
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: CALMODULIN;                                                
COMPND  13 CHAIN: C, D;                                                         
COMPND  14 FRAGMENT: RESIDUES 1-149;                                            
COMPND  15 SYNONYM: CAM, KV7.1 CHANNEL;                                         
COMPND  16 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET DUET;                                 
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET DUET                                  
KEYWDS    SIGNALING PROTEIN, VOLTAGE-DEPENDENT POTASSIUM CHANNELS, LONG QT      
KEYWDS   2 SYNDROME, CALMODULIN                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.SACHYANI,J.A.HIRSCH                                                 
REVDAT   2   17-DEC-14 4V0C    1       JRNL                                     
REVDAT   1   05-NOV-14 4V0C    0                                                
JRNL        AUTH   D.SACHYANI,M.DVIR,R.STRULOVICH,G.TRIA,W.TOBELAIM,A.PERETZ,   
JRNL        AUTH 2 O.PONGS,D.SVERGUN,B.ATTALI,J.A.HIRSCH                        
JRNL        TITL   STRUCTURAL BASIS OF A KV7.1 POTASSIUM CHANNEL GATING         
JRNL        TITL 2 MODULE: STUDIES OF THE INTRACELLULAR C-TERMINAL DOMAIN IN    
JRNL        TITL 3 COMPLEX WITH CALMODULIN.                                     
JRNL        REF    STRUCTURE                     V.  22  1582 2014              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   25441029                                                     
JRNL        DOI    10.1016/J.STR.2014.07.016                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.86 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT 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) : 2.86                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.784                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.32                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.81                          
REMARK   3   NUMBER OF REFLECTIONS             : 17456                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.2280                          
REMARK   3   R VALUE            (WORKING SET) : 0.2259                          
REMARK   3   FREE R VALUE                     : 0.2679                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 883                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.7913 -  5.1948    1.00     2862   140  0.2018 0.2694        
REMARK   3     2  5.1948 -  4.1239    1.00     2779   139  0.2092 0.2073        
REMARK   3     3  4.1239 -  3.6028    1.00     2736   155  0.2299 0.2824        
REMARK   3     4  3.6028 -  3.2734    1.00     2759   158  0.2679 0.3089        
REMARK   3     5  3.2734 -  3.0388    1.00     2716   151  0.2919 0.3414        
REMARK   3     6  3.0388 -  2.8597    0.99     2721   140  0.2887 0.2825        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.32             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.27            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           3598                                  
REMARK   3   ANGLE     :  1.049           4820                                  
REMARK   3   CHIRALITY :  0.035            531                                  
REMARK   3   PLANARITY :  0.004            646                                  
REMARK   3   DIHEDRAL  : 16.310           1279                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 19                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 330 THROUGH 354 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -61.4027  53.6534  43.2280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8859 T22:   1.4710                                     
REMARK   3      T33:   1.4195 T12:  -0.2852                                     
REMARK   3      T13:  -0.0808 T23:  -0.1213                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6321 L22:   1.9233                                     
REMARK   3      L33:  -0.0070 L12:  -1.2405                                     
REMARK   3      L13:  -0.1001 L23:   0.0441                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5515 S12:   0.7018 S13:   1.0119                       
REMARK   3      S21:  -0.0681 S22:  -0.3984 S23:   0.3398                       
REMARK   3      S31:   0.4095 S32:  -0.0799 S33:   1.5733                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 355 THROUGH 395 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -59.4618  14.0227  13.9016              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4624 T22:   0.4653                                     
REMARK   3      T33:   0.2742 T12:  -0.0833                                     
REMARK   3      T13:  -0.0657 T23:   0.1120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.4699 L22:   8.2808                                     
REMARK   3      L33:   6.9311 L12:  -0.7418                                     
REMARK   3      L13:  -1.2285 L23:   0.0816                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0019 S12:  -0.0653 S13:   0.2388                       
REMARK   3      S21:  -0.3630 S22:   0.2254 S23:   1.5352                       
REMARK   3      S31:   0.6671 S32:  -0.4439 S33:  -0.1670                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 396 THROUGH 535 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -48.7635 -19.7160 -11.1132              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6754 T22:   0.6084                                     
REMARK   3      T33:   0.3906 T12:   0.2225                                     
REMARK   3      T13:  -0.0948 T23:   0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9717 L22:   3.6810                                     
REMARK   3      L33:   7.2153 L12:  -0.6537                                     
REMARK   3      L13:  -0.9902 L23:  -0.2185                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4223 S12:   0.4623 S13:   0.0065                       
REMARK   3      S21:  -0.5095 S22:  -0.0138 S23:  -0.0182                       
REMARK   3      S31:  -0.3922 S32:   0.0250 S33:  -0.1892                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 354 THROUGH 390 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -53.1692 -34.0979  -9.9393              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6213 T22:   0.6270                                     
REMARK   3      T33:   0.5330 T12:   0.1273                                     
REMARK   3      T13:  -0.1697 T23:  -0.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7103 L22:   2.9802                                     
REMARK   3      L33:   5.5891 L12:   2.0609                                     
REMARK   3      L13:   0.8101 L23:  -3.2427                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.9586 S12:   0.2865 S13:  -0.4971                       
REMARK   3      S21:  -0.9792 S22:  -0.9228 S23:   0.6065                       
REMARK   3      S31:  -0.1450 S32:  -1.0300 S33:  -0.0856                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 391 THROUGH 535 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -51.9721   0.5730  14.4453              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0349 T22:   0.4353                                     
REMARK   3      T33:   0.3812 T12:   0.0321                                     
REMARK   3      T13:   0.0020 T23:   0.1264                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3424 L22:   8.8537                                     
REMARK   3      L33:   6.5207 L12:  -1.6926                                     
REMARK   3      L13:  -1.0768 L23:   6.9103                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0954 S12:  -0.2844 S13:  -0.0451                       
REMARK   3      S21:   0.0631 S22:  -0.1079 S23:   0.1038                       
REMARK   3      S31:   0.0790 S32:   0.3930 S33:   0.0441                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 5 THROUGH 72 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -40.4785 -15.5955 -16.1656              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8650 T22:   0.7284                                     
REMARK   3      T33:   0.5037 T12:   0.2396                                     
REMARK   3      T13:   0.0750 T23:   0.0294                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3303 L22:   9.7371                                     
REMARK   3      L33:   7.4936 L12:  -1.1192                                     
REMARK   3      L13:   1.3506 L23:  -2.5211                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2229 S12:   0.4372 S13:  -0.2444                       
REMARK   3      S21:  -0.7157 S22:  -0.0103 S23:  -0.9124                       
REMARK   3      S31:   0.1829 S32:   0.9270 S33:  -0.3118                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 73 THROUGH 81 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -58.4642 -23.0969 -21.1259              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3429 T22:   0.9755                                     
REMARK   3      T33:   1.2772 T12:   0.0946                                     
REMARK   3      T13:  -0.0490 T23:   0.1306                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7105 L22:   6.2280                                     
REMARK   3      L33:   6.0564 L12:  -5.8917                                     
REMARK   3      L13:   3.2979 L23:  -2.5856                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4347 S12:   0.6450 S13:  -1.1254                       
REMARK   3      S21:  -0.2333 S22:   0.4034 S23:   2.2337                       
REMARK   3      S31:   0.9944 S32:   1.2803 S33:  -0.3535                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 82 THROUGH 98 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -62.6759 -37.9565 -12.1793              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7493 T22:   1.2889                                     
REMARK   3      T33:   1.5884 T12:  -0.2815                                     
REMARK   3      T13:  -0.6921 T23:   0.3978                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4648 L22:   8.2123                                     
REMARK   3      L33:   9.7935 L12:  -2.3987                                     
REMARK   3      L13:   4.0062 L23:   3.1764                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.0870 S12:  -1.1644 S13:  -2.2730                       
REMARK   3      S21:  -2.7802 S22:   3.2505 S23:   4.2987                       
REMARK   3      S31:   0.9823 S32:  -5.6300 S33:  -1.0362                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 99 THROUGH 125 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -57.4550 -32.1813   0.4011              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6617 T22:   0.4964                                     
REMARK   3      T33:   1.1044 T12:   0.1107                                     
REMARK   3      T13:   0.2080 T23:   0.1191                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.8997 L22:   8.6401                                     
REMARK   3      L33:   4.1198 L12:   2.2795                                     
REMARK   3      L13:   0.3087 L23:  -2.6748                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1520 S12:  -0.3026 S13:  -0.9477                       
REMARK   3      S21:   1.0552 S22:  -0.1451 S23:   1.5146                       
REMARK   3      S31:  -0.1799 S32:  -0.4328 S33:  -0.0206                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 126 THROUGH 147 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -68.4007 -29.7300  -5.2150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7365 T22:   1.2086                                     
REMARK   3      T33:   2.0410 T12:   0.0441                                     
REMARK   3      T13:  -0.0023 T23:   0.0769                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8132 L22:   8.5752                                     
REMARK   3      L33:   7.3856 L12:  -3.1896                                     
REMARK   3      L13:  -2.3318 L23:  -2.8716                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5181 S12:   0.0161 S13:   0.6498                       
REMARK   3      S21:   0.1893 S22:   1.5322 S23:   3.7299                       
REMARK   3      S31:  -0.1290 S32:  -4.1531 S33:  -1.2034                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 3 THROUGH 38 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -42.5955  -2.6943  20.4466              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7141 T22:   0.5513                                     
REMARK   3      T33:   0.4182 T12:  -0.0305                                     
REMARK   3      T13:  -0.0591 T23:  -0.0022                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.6554 L22:   7.5858                                     
REMARK   3      L33:   8.4195 L12:   1.2957                                     
REMARK   3      L13:   0.4361 L23:  -0.5632                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6693 S12:  -0.3198 S13:  -0.8064                       
REMARK   3      S21:  -1.0929 S22:   0.5918 S23:  -0.8701                       
REMARK   3      S31:   0.8461 S32:   1.1357 S33:  -0.1205                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 39 THROUGH 47 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -43.3964  12.2692  11.4061              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.0144 T22:  -0.0822                                     
REMARK   3      T33:   1.1885 T12:   0.2453                                     
REMARK   3      T13:  -0.3091 T23:   0.0708                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3998 L22:   1.6112                                     
REMARK   3      L33:   0.0233 L12:  -1.4082                                     
REMARK   3      L13:  -0.0818 L23:   0.1185                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8320 S12:   0.7262 S13:   1.5050                       
REMARK   3      S21:  -0.9935 S22:   0.1801 S23:   0.5124                       
REMARK   3      S31:  -1.6148 S32:   0.9848 S33:   1.0361                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 48 THROUGH 64 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -43.1904   8.8300  26.9208              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2618 T22:   0.8054                                     
REMARK   3      T33:   0.7611 T12:  -0.0484                                     
REMARK   3      T13:  -0.2429 T23:  -0.1924                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7639 L22:   6.5701                                     
REMARK   3      L33:   3.0623 L12:  -3.0168                                     
REMARK   3      L13:   0.6061 L23:   2.9460                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5334 S12:  -1.6518 S13:   2.0598                       
REMARK   3      S21:   1.1648 S22:   0.9453 S23:  -0.5656                       
REMARK   3      S31:  -0.6456 S32:   0.9892 S33:  -0.4993                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 65 THROUGH 73 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -48.4110  -0.9821  27.9839              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7196 T22:   0.6730                                     
REMARK   3      T33:   0.3963 T12:  -0.0570                                     
REMARK   3      T13:  -0.1897 T23:   0.2313                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2240 L22:   3.1586                                     
REMARK   3      L33:   1.9967 L12:   3.4188                                     
REMARK   3      L13:   4.3617 L23:   5.1854                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4036 S12:   0.1348 S13:   1.3177                       
REMARK   3      S21:   0.6473 S22:   0.0811 S23:   1.2237                       
REMARK   3      S31:  -2.3867 S32:  -2.6392 S33:  -0.4429                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 74 THROUGH 81 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -62.4913   4.5005  26.7852              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8211 T22:   0.9599                                     
REMARK   3      T33:   0.9170 T12:  -0.6954                                     
REMARK   3      T13:  -0.1942 T23:   0.6666                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0015 L22:   8.5905                                     
REMARK   3      L33:   0.1346 L12:  -0.1974                                     
REMARK   3      L13:  -0.0421 L23:   1.0156                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.0296 S12:  -0.2417 S13:  -0.2147                       
REMARK   3      S21:  -0.2030 S22:   0.8869 S23:   1.7854                       
REMARK   3      S31:   0.6266 S32:  -0.0520 S33:  -1.7005                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 82 THROUGH 92 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -68.4245  15.7529  19.9755              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7780 T22:   0.7804                                     
REMARK   3      T33:   0.7272 T12:  -0.1101                                     
REMARK   3      T13:   0.0619 T23:   0.0992                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5945 L22:   1.9878                                     
REMARK   3      L33:   5.2258 L12:  -3.4943                                     
REMARK   3      L13:   5.7576 L23:  -3.0647                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3536 S12:  -0.9712 S13:  -0.7970                       
REMARK   3      S21:   0.1766 S22:   0.7720 S23:  -0.2872                       
REMARK   3      S31:  -1.8016 S32:   0.2656 S33:  -0.3850                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 93 THROUGH 126 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -66.0777  13.8507   6.6351              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7285 T22:   0.6079                                     
REMARK   3      T33:   0.8113 T12:  -0.1172                                     
REMARK   3      T13:  -0.2208 T23:  -0.0300                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.0807 L22:   6.4171                                     
REMARK   3      L33:   3.7810 L12:  -1.4293                                     
REMARK   3      L13:   1.0221 L23:  -0.9813                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0975 S12:   1.0723 S13:   0.3511                       
REMARK   3      S21:  -0.6025 S22:  -0.0961 S23:   0.7725                       
REMARK   3      S31:   0.4016 S32:  -0.5766 S33:  -0.0765                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 127 THROUGH 137 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -77.3038  10.2956   6.4145              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -2.2972 T22:   1.6036                                     
REMARK   3      T33:   1.5636 T12:  -1.8309                                     
REMARK   3      T13:   0.1802 T23:  -0.1168                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1089 L22:   3.6722                                     
REMARK   3      L33:   0.6272 L12:  -1.1314                                     
REMARK   3      L13:  -0.9097 L23:  -0.3670                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4158 S12:   0.4634 S13:  -0.5538                       
REMARK   3      S21:  -0.9988 S22:   0.1653 S23:   2.2024                       
REMARK   3      S31:   0.2602 S32:  -0.4369 S33:  -0.1474                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 138 THROUGH 147 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -71.0573   6.1438  16.5149              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1019 T22:   0.8730                                     
REMARK   3      T33:   1.3828 T12:  -0.2588                                     
REMARK   3      T13:   0.0005 T23:   0.1284                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1027 L22:   6.2969                                     
REMARK   3      L33:   7.3081 L12:  -5.5489                                     
REMARK   3      L13:   0.2518 L23:  -4.1454                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.9946 S12:   0.7280 S13:  -1.4302                       
REMARK   3      S21:  -2.8382 S22:  -0.0433 S23:   1.7278                       
REMARK   3      S31:   1.3603 S32:  -0.7877 S33:  -1.2114                       
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 4V0C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-OCT-14.                  
REMARK 100 THE PDBE ID CODE IS EBI-61751.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.924                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17341                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.85                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 15.3                               
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 31.90                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.40                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: PHENIX, SHARP                                         
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.1                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.3 M POTASSIUM THIOCYANATE, 0.1 M       
REMARK 280  SODIUM ACETATE TRIHYDRATE PH=5.6, 5 MM CACL2                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.55333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       18.77667            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       28.16500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        9.38833            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       46.94167            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12120 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 25100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -150.2 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   324                                                      
REMARK 465     GLY A   325                                                      
REMARK 465     SER A   326                                                      
REMARK 465     HIS A   327                                                      
REMARK 465     HIS A   328                                                      
REMARK 465     HIS A   329                                                      
REMARK 465     ASN A   346                                                      
REMARK 465     LEU A   347                                                      
REMARK 465     TYR A   348                                                      
REMARK 465     PHE A   349                                                      
REMARK 465     GLN A   350                                                      
REMARK 465     GLY A   350A                                                     
REMARK 465     TYR A   536                                                      
REMARK 465     ASP A   537                                                      
REMARK 465     VAL A   538                                                      
REMARK 465     ARG A   539                                                      
REMARK 465     MET B   324                                                      
REMARK 465     GLY B   325                                                      
REMARK 465     SER B   326                                                      
REMARK 465     HIS B   327                                                      
REMARK 465     HIS B   328                                                      
REMARK 465     HIS B   329                                                      
REMARK 465     HIS B   330                                                      
REMARK 465     HIS B   331                                                      
REMARK 465     HIS B   332                                                      
REMARK 465     HIS B   333                                                      
REMARK 465     HIS B   334                                                      
REMARK 465     GLY B   335                                                      
REMARK 465     SER B   336                                                      
REMARK 465     ASP B   337                                                      
REMARK 465     TYR B   338                                                      
REMARK 465     ASP B   339                                                      
REMARK 465     ASP B   340                                                      
REMARK 465     ILE B   341                                                      
REMARK 465     PHE B   342                                                      
REMARK 465     THR B   343                                                      
REMARK 465     THR B   344                                                      
REMARK 465     GLU B   345                                                      
REMARK 465     ASN B   346                                                      
REMARK 465     LEU B   347                                                      
REMARK 465     TYR B   348                                                      
REMARK 465     PHE B   349                                                      
REMARK 465     GLN B   350                                                      
REMARK 465     GLY B   350A                                                     
REMARK 465     SER B   351                                                      
REMARK 465     ALA B   352                                                      
REMARK 465     LEU B   353                                                      
REMARK 465     TYR B   536                                                      
REMARK 465     ASP B   537                                                      
REMARK 465     VAL B   538                                                      
REMARK 465     ARG B   539                                                      
REMARK 465     MET C     0                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     ASP C     2                                                      
REMARK 465     GLN C     3                                                      
REMARK 465     LEU C     4                                                      
REMARK 465     LYS C   148                                                      
REMARK 465     MET D     0                                                      
REMARK 465     ALA D     1                                                      
REMARK 465     ASP D     2                                                      
REMARK 465     LYS D   148                                                      
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     HIS A 330    CG   ND1  CD2  CE1  NE2                             
REMARK 470     HIS A 331    CG   ND1  CD2  CE1  NE2                             
REMARK 470     HIS A 332    CG   ND1  CD2  CE1  NE2                             
REMARK 470     HIS A 334    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TYR A 338    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP A 339    CG   OD1  OD2                                       
REMARK 470     ILE A 341    CG1  CG2  CD1                                       
REMARK 470     PHE A 342    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 345    CG   CD   OE1  OE2                                  
REMARK 470     SER A 351    OG                                                  
REMARK 470     LEU A 353    CG   CD1  CD2                                       
REMARK 470     LYS A 354    CE   NZ                                             
REMARK 470     VAL A 355    CG1  CG2                                            
REMARK 470     GLN A 356    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 358    CG   CD   CE   NZ                                   
REMARK 470     GLN A 359    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 360    CZ   NH1  NH2                                       
REMARK 470     SER A 390    OG                                                  
REMARK 470     GLU A 508    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 534    CG   CD   CE   NZ                                   
REMARK 470     LYS B 354    CG   CD   CE   NZ                                   
REMARK 470     VAL B 355    CG1  CG2                                            
REMARK 470     LYS B 358    CG   CD   CE   NZ                                   
REMARK 470     GLN B 359    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 360    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 362    CG   CD   CE   NZ                                   
REMARK 470     LYS B 527    CG   CD   CE   NZ                                   
REMARK 470     LYS B 534    CG   CD   CE   NZ                                   
REMARK 470     GLU C   6    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  13    CG   CD   CE   NZ                                   
REMARK 470     ASN C  42    CG   OD1  ND2                                       
REMARK 470     GLU C  54    CD   OE1  OE2                                       
REMARK 470     LYS C  75    CG   CD   CE   NZ                                   
REMARK 470     GLU C  83    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  84    CG   CD   OE1  OE2                                  
REMARK 470     ARG C  86    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  94    CG   CD   CE   NZ                                   
REMARK 470     ILE C 100    CG1  CG2  CD1                                       
REMARK 470     GLU C 127    CG   CD   OE1  OE2                                  
REMARK 470     GLN D   3    CG   CD   OE1  NE2                                  
REMARK 470     GLU D   6    CG   CD   OE1  OE2                                  
REMARK 470     GLN D   8    CD   OE1  NE2                                       
REMARK 470     LYS D  30    CG   CD   CE   NZ                                   
REMARK 470     LEU D  39    CG   CD1  CD2                                       
REMARK 470     GLU D  45    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  75    CG   CD   CE   NZ                                   
REMARK 470     LYS D  77    CG   CD   CE   NZ                                   
REMARK 470     ASP D  78    CG   OD1  OD2                                       
REMARK 470     GLU D  82    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  83    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  94    CG   CD   CE   NZ                                   
REMARK 470     ASN D  97    CG   OD1  ND2                                       
REMARK 470     ILE D 100    CG1  CG2  CD1                                       
REMARK 470     ILE D 125    CG1  CG2  CD1                                       
REMARK 470     GLU D 127    CG   CD   OE1  OE2                                  
REMARK 470     ASP D 129    CG   OD1  OD2                                       
REMARK 470     ILE D 130    CG1  CG2  CD1                                       
REMARK 470     GLN D 135    CG   CD   OE1  NE2                                  
REMARK 470     VAL D 136    CG1  CG2                                            
REMARK 470     GLU D 139    CG   CD   OE1  OE2                                  
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   OD1  ASP C    20     O    THR C    26              2.03            
REMARK 500   OD2  ASP C    22     OE2  GLU C    31              1.84            
REMARK 500   OD2  ASP D    22     OE1  GLU D    31              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    GLY D 134   N   -  CA  -  C   ANGL. DEV. = -20.4 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    THR A 344      178.93    -59.07                                   
REMARK 500    GLN B 356       31.00    -68.14                                   
REMARK 500    SER B 389      100.98    -29.96                                   
REMARK 500    GLU C   7      -58.65    -28.93                                   
REMARK 500    MET C  76      -24.01   -150.66                                   
REMARK 500    ASN C  97     -151.26    -84.26                                   
REMARK 500    LYS C 115     -153.76     54.25                                   
REMARK 500    LEU C 116      143.20    167.51                                   
REMARK 500    ALA C 128      -90.16    -63.38                                   
REMARK 500    ASP C 129       37.05     70.33                                   
REMARK 500    ASP C 131      112.79   -161.59                                   
REMARK 500    ASP C 133      -30.68   -137.85                                   
REMARK 500    ASN D  42       73.43   -119.91                                   
REMARK 500    ALA D  46     -161.49    -73.19                                   
REMARK 500    GLU D  47      -44.61     59.18                                   
REMARK 500    SER D  81      -13.65    159.84                                   
REMARK 500    LYS D 115       87.76     53.51                                   
REMARK 500    GLN D 135      -66.61   -134.73                                   
REMARK 500    VAL D 136       71.69     55.11                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C  26   O                                                      
REMARK 620 2 THR C  26   OG1  83.3                                              
REMARK 620 3 GLU C  31   OE2  81.6 127.3                                        
REMARK 620 4 ASP C  20   OD1  50.6 121.0  85.0                                  
REMARK 620 5 ASP C  22   OD2 104.0 167.8  46.1  70.7                            
REMARK 620 6 ASP C  24   OD1  92.0  77.3 153.0  70.9 111.8                      
REMARK 620 7 ASP C  24   OD2 143.0  73.8 135.4 119.8 104.2  55.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  20   OD1                                                    
REMARK 620 2 ASP D  24   OD1  63.7                                              
REMARK 620 3 ASP D  24   OD2 113.2  54.2                                        
REMARK 620 4 ASP D  22   OD2  90.0 133.8 115.4                                  
REMARK 620 5 THR D  26   O    57.9  83.6 128.7 115.0                            
REMARK 620 6 THR D  26   OG1 105.7  60.8  64.1 163.3  70.5                      
REMARK 620 7 GLU D  31   OE1  66.4 128.8 169.9  55.0  60.4 126.0                
REMARK 620 8 GLU D  31   OE2 116.9 153.0 129.3  72.0  76.0  95.3  53.6          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  58   OD1                                                    
REMARK 620 2 ASP C  56   OD1  75.9                                              
REMARK 620 3 GLU C  67   OE1  82.0  75.1                                        
REMARK 620 4 ASN C  60   OD1  80.4  58.2 132.8                                  
REMARK 620 5 THR C  62   O   131.8  56.0  88.7  71.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR D  62   O                                                      
REMARK 620 2 GLU D  67   OE1  87.5                                              
REMARK 620 3 GLU D  67   OE2 118.3  55.1                                        
REMARK 620 4 HOH D2001   O    65.3  92.7 145.6                                  
REMARK 620 5 ASP D  58   OD2 164.1 102.3  60.4 125.8                            
REMARK 620 6 ASP D  56   OD1  78.6  98.6  63.9 141.6  87.5                      
REMARK 620 7 ASN D  60   OD1  76.9 163.2 138.8  75.3  94.3  84.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA D 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A1536                 
DBREF  4V0C A  352   396  UNP    P51787   KCNQ1_HUMAN    352    396             
DBREF  4V0C A  397   539  UNP    P51787   KCNQ1_HUMAN    502    539             
DBREF  4V0C B  352   396  UNP    P51787   KCNQ1_HUMAN    352    396             
DBREF  4V0C B  397   539  UNP    P51787   KCNQ1_HUMAN    502    539             
DBREF  4V0C C    0   148  UNP    P62158   CALM_HUMAN       1    149             
DBREF  4V0C D    0   148  UNP    P62158   CALM_HUMAN       1    149             
SEQADV 4V0C MET A  324  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C GLY A  325  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C SER A  326  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C HIS A  327  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C HIS A  328  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C HIS A  329  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C HIS A  330  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C HIS A  331  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C HIS A  332  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C HIS A  333  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C HIS A  334  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C GLY A  335  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C SER A  336  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C ASP A  337  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C TYR A  338  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C ASP A  339  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C ASP A  340  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C ILE A  341  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C PHE A  342  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C THR A  343  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C THR A  344  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C GLU A  345  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C ASN A  346  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C LEU A  347  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C TYR A  348  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C PHE A  349  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C GLN A  350  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C GLY A  350A UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C SER A  351  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C GLU A  397  UNP  P51787    HIS   502 ENGINEERED MUTATION            
SEQADV 4V0C PHE A  398  UNP  P51787    ILE   503 ENGINEERED MUTATION            
SEQADV 4V0C MET B  324  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C GLY B  325  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C SER B  326  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C HIS B  327  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C HIS B  328  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C HIS B  329  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C HIS B  330  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C HIS B  331  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C HIS B  332  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C HIS B  333  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C HIS B  334  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C GLY B  335  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C SER B  336  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C ASP B  337  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C TYR B  338  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C ASP B  339  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C ASP B  340  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C ILE B  341  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C PHE B  342  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C THR B  343  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C THR B  344  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C GLU B  345  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C ASN B  346  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C LEU B  347  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C TYR B  348  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C PHE B  349  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C GLN B  350  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C GLY B  350A UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C SER B  351  UNP  P51787              EXPRESSION TAG                 
SEQADV 4V0C GLU B  397  UNP  P51787    HIS   502 ENGINEERED MUTATION            
SEQADV 4V0C PHE B  398  UNP  P51787    ILE   503 ENGINEERED MUTATION            
SEQRES   1 A  112  MET GLY SER HIS HIS HIS HIS HIS HIS HIS HIS GLY SER          
SEQRES   2 A  112  ASP TYR ASP ASP ILE PHE THR THR GLU ASN LEU TYR PHE          
SEQRES   3 A  112  GLN GLY SER ALA LEU LYS VAL GLN GLN LYS GLN ARG GLN          
SEQRES   4 A  112  LYS HIS PHE ASN ARG GLN ILE PRO ALA ALA ALA SER LEU          
SEQRES   5 A  112  ILE GLN THR ALA TRP ARG CYS TYR ALA ALA GLU ASN PRO          
SEQRES   6 A  112  ASP SER SER THR TRP LYS ILE TYR ILE GLU PHE SER GLN          
SEQRES   7 A  112  LEU ARG GLU HIS HIS ARG ALA THR ILE LYS VAL ILE ARG          
SEQRES   8 A  112  ARG MET GLN TYR PHE VAL ALA LYS LYS LYS PHE GLN GLN          
SEQRES   9 A  112  ALA ARG LYS PRO TYR ASP VAL ARG                              
SEQRES   1 B  112  MET GLY SER HIS HIS HIS HIS HIS HIS HIS HIS GLY SER          
SEQRES   2 B  112  ASP TYR ASP ASP ILE PHE THR THR GLU ASN LEU TYR PHE          
SEQRES   3 B  112  GLN GLY SER ALA LEU LYS VAL GLN GLN LYS GLN ARG GLN          
SEQRES   4 B  112  LYS HIS PHE ASN ARG GLN ILE PRO ALA ALA ALA SER LEU          
SEQRES   5 B  112  ILE GLN THR ALA TRP ARG CYS TYR ALA ALA GLU ASN PRO          
SEQRES   6 B  112  ASP SER SER THR TRP LYS ILE TYR ILE GLU PHE SER GLN          
SEQRES   7 B  112  LEU ARG GLU HIS HIS ARG ALA THR ILE LYS VAL ILE ARG          
SEQRES   8 B  112  ARG MET GLN TYR PHE VAL ALA LYS LYS LYS PHE GLN GLN          
SEQRES   9 B  112  ALA ARG LYS PRO TYR ASP VAL ARG                              
SEQRES   1 C  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 C  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 C  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 C  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 C  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 C  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 C  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 C  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 C  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 C  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 C  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 C  149  GLN MET MET THR ALA LYS                                      
SEQRES   1 D  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 D  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 D  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 D  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 D  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 D  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 D  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 D  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 D  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 D  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 D  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 D  149  GLN MET MET THR ALA LYS                                      
HET     CA  C 201       1                                                       
HET     CA  C 202       1                                                       
HET     CA  D 201       1                                                       
HET     CA  D 202       1                                                       
HET    SCN  A1536       3                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     SCN THIOCYANATE ION                                                  
FORMUL   5   CA    4(CA 2+)                                                     
FORMUL   6  SCN    C N S 1-                                                     
FORMUL   2  HOH   *4(H2 O)                                                      
HELIX    1   1 LYS A  358  GLU A  385  1                                  28    
HELIX    2   2 THR A  391  ILE A  394  5                                   4    
HELIX    3   3 TYR A  395  LYS A  534  1                                  35    
HELIX    4   4 GLN B  356  ARG B  366  1                                  11    
HELIX    5   5 ARG B  366  GLU B  385  1                                  20    
HELIX    6   6 THR B  391  ILE B  394  5                                   4    
HELIX    7   7 TYR B  395  LYS B  534  1                                  35    
HELIX    8   8 THR C    5  ASP C   20  1                                  16    
HELIX    9   9 THR C   28  LEU C   39  1                                  12    
HELIX   10  10 THR C   44  ASP C   56  1                                  13    
HELIX   11  11 ASP C   64  ALA C   73  1                                  10    
HELIX   12  12 SER C   81  ASP C   93  1                                  13    
HELIX   13  13 ALA C  102  LEU C  112  1                                  11    
HELIX   14  14 THR C  117  ASP C  129  1                                  13    
HELIX   15  15 TYR C  138  THR C  146  1                                   9    
HELIX   16  16 THR D    5  ASP D   20  1                                  16    
HELIX   17  17 THR D   28  LEU D   39  1                                  12    
HELIX   18  18 GLU D   47  ASP D   56  1                                  10    
HELIX   19  19 ASP D   64  ARG D   74  1                                  11    
HELIX   20  20 SER D   81  VAL D   91  1                                  11    
HELIX   21  21 SER D  101  LEU D  112  1                                  12    
HELIX   22  22 THR D  117  ASP D  129  1                                  13    
HELIX   23  23 ASN D  137  THR D  146  1                                  10    
SHEET    1  CA 2 TYR C  99  SER C 101  0                                        
SHEET    2  CA 2 GLN C 135  ASN C 137 -1  O  VAL C 136   N  ILE C 100           
LINK        CA    CA C 201                 O   THR C  26     1555   1555  2.37  
LINK        CA    CA C 201                 OG1 THR C  26     1555   1555  2.37  
LINK        CA    CA C 201                 OE2 GLU C  31     1555   1555  2.37  
LINK        CA    CA C 201                 OD1 ASP C  20     1555   1555  2.37  
LINK        CA    CA C 201                 OD2 ASP C  22     1555   1555  2.35  
LINK        CA    CA C 201                 OD1 ASP C  24     1555   1555  2.35  
LINK        CA    CA C 201                 OD2 ASP C  24     1555   1555  2.38  
LINK        CA    CA C 202                 OD1 ASP C  58     1555   1555  2.36  
LINK        CA    CA C 202                 O   THR C  62     1555   1555  2.37  
LINK        CA    CA C 202                 OD1 ASN C  60     1555   1555  2.38  
LINK        CA    CA C 202                 OE1 GLU C  67     1555   1555  2.36  
LINK        CA    CA C 202                 OD1 ASP C  56     1555   1555  2.37  
LINK        CA    CA D 201                 OG1 THR D  26     1555   1555  2.39  
LINK        CA    CA D 201                 OE1 GLU D  31     1555   1555  2.38  
LINK        CA    CA D 201                 OE2 GLU D  31     1555   1555  2.38  
LINK        CA    CA D 201                 O   THR D  26     1555   1555  2.38  
LINK        CA    CA D 201                 OD2 ASP D  22     1555   1555  2.34  
LINK        CA    CA D 201                 OD2 ASP D  24     1555   1555  2.38  
LINK        CA    CA D 201                 OD1 ASP D  24     1555   1555  2.37  
LINK        CA    CA D 201                 OD1 ASP D  20     1555   1555  2.37  
LINK        CA    CA D 202                 OE1 GLU D  67     1555   1555  2.36  
LINK        CA    CA D 202                 OE2 GLU D  67     1555   1555  2.36  
LINK        CA    CA D 202                 O   HOH D2001     1555   1555  3.14  
LINK        CA    CA D 202                 OD2 ASP D  58     1555   1555  2.36  
LINK        CA    CA D 202                 OD1 ASP D  56     1555   1555  2.36  
LINK        CA    CA D 202                 OD1 ASN D  60     1555   1555  2.38  
LINK        CA    CA D 202                 O   THR D  62     1555   1555  2.37  
CISPEP   1 LEU D   39    GLY D   40          0        -3.77                     
SITE     1 AC1  5 ASP C  20  ASP C  22  ASP C  24  THR C  26                    
SITE     2 AC1  5 GLU C  31                                                     
SITE     1 AC2  5 ASP C  56  ASP C  58  ASN C  60  THR C  62                    
SITE     2 AC2  5 GLU C  67                                                     
SITE     1 AC3  5 ASP D  20  ASP D  22  ASP D  24  THR D  26                    
SITE     2 AC3  5 GLU D  31                                                     
SITE     1 AC4  5 ASP D  56  ASP D  58  ASN D  60  THR D  62                    
SITE     2 AC4  5 GLU D  67                                                     
SITE     1 AC5  2 GLN B 521  GLN D  41                                          
CRYST1  152.092  152.092   56.330  90.00  90.00 120.00 P 65         12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006575  0.003796  0.000000        0.00000                         
SCALE2      0.000000  0.007592  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017753        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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