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Database: PDB
Entry: 5WLZ
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HEADER    MOTOR PROTEIN                           28-JUL-17   5WLZ              
TITLE     CRYSTAL STRUCTURE OF AMINO ACIDS 1677-1758 OF HUMAN BETA CARDIAC      
TITLE    2 MYOSIN FUSED TO XRCC4                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA REPAIR PROTEIN XRCC4,MYOSIN-7;                         
COMPND   3 CHAIN: C, D, A, B;                                                   
COMPND   4 FRAGMENT: UNP Q13426 RESIDUES 2-132, UNP P12883 RESIDUES 1677-1758;  
COMPND   5 SYNONYM: X-RAY REPAIR CROSS-COMPLEMENTING PROTEIN 4,MYOSIN HEAVY     
COMPND   6 CHAIN 7,MYOSIN HEAVY CHAIN SLOW ISOFORM,MYHC-SLOW,MYOSIN HEAVY CHAIN,
COMPND   7 CARDIAC MUSCLE BETA ISOFORM,MYHC-BETA;                               
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: XRCC4, MYH7, MYHCB;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    MYOSIN, XRCC4, COILED-COIL, MOTOR PROTEIN                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.P.ANDREAS,G.AJAY,J.GELLINGS,I.RAYMENT                               
REVDAT   3   04-DEC-19 5WLZ    1       REMARK                                   
REVDAT   2   27-DEC-17 5WLZ    1       JRNL                                     
REVDAT   1   23-AUG-17 5WLZ    0                                                
JRNL        AUTH   M.P.ANDREAS,G.AJAY,J.A.GELLINGS,I.RAYMENT                    
JRNL        TITL   DESIGN CONSIDERATIONS IN COILED-COIL FUSION CONSTRUCTS FOR   
JRNL        TITL 2 THE STRUCTURAL DETERMINATION OF A PROBLEMATIC REGION OF THE  
JRNL        TITL 3 HUMAN CARDIAC MYOSIN ROD.                                    
JRNL        REF    J. STRUCT. BIOL.              V. 200   219 2017              
JRNL        REFN                   ESSN 1095-8657                               
JRNL        PMID   28743637                                                     
JRNL        DOI    10.1016/J.JSB.2017.07.006                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575)                                 
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.07                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 15666                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.214                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 785                             
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 44.0710 -  6.3550    1.00     2607   138  0.1867 0.2025        
REMARK   3     2  6.3550 -  5.0465    1.00     2490   131  0.2352 0.2615        
REMARK   3     3  5.0465 -  4.4092    1.00     2481   131  0.1823 0.2510        
REMARK   3     4  4.4092 -  4.0064    1.00     2448   128  0.2066 0.2210        
REMARK   3     5  4.0064 -  3.7194    1.00     2434   129  0.2372 0.2928        
REMARK   3     6  3.7194 -  3.5002    0.99     2421   128  0.2654 0.3088        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.900           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           6448                                  
REMARK   3   ANGLE     :  0.423           8663                                  
REMARK   3   CHIRALITY :  0.034            987                                  
REMARK   3   PLANARITY :  0.002           1108                                  
REMARK   3   DIHEDRAL  : 13.055           3965                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID -1 THROUGH 118 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   1.3151  14.0921 -12.4891              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6449 T22:   0.1659                                     
REMARK   3      T33:   0.3108 T12:  -0.0066                                     
REMARK   3      T13:  -0.0373 T23:   0.1956                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8214 L22:   3.5122                                     
REMARK   3      L33:   3.4695 L12:   0.8838                                     
REMARK   3      L13:   0.2645 L23:   1.3414                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0368 S12:  -0.4162 S13:  -0.4916                       
REMARK   3      S21:   0.7877 S22:  -0.0989 S23:   0.0606                       
REMARK   3      S31:   0.4554 S32:  -0.0779 S33:   0.0510                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 119 THROUGH 1748 )                
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.9485  30.0740 -64.5758              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4324 T22:   0.2758                                     
REMARK   3      T33:   0.3406 T12:  -0.1164                                     
REMARK   3      T13:  -0.0400 T23:   0.0104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2608 L22:   0.8683                                     
REMARK   3      L33:   3.0671 L12:   0.3435                                     
REMARK   3      L13:   0.3003 L23:   0.9743                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4339 S12:   0.3745 S13:  -0.1026                       
REMARK   3      S21:  -0.4110 S22:   0.0055 S23:  -0.0995                       
REMARK   3      S31:  -1.2831 S32:   0.3399 S33:   0.2322                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 118 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   4.7497  52.1553 -12.9772              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4178 T22:   0.1448                                     
REMARK   3      T33:   0.2072 T12:  -0.0578                                     
REMARK   3      T13:   0.0550 T23:  -0.1509                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9874 L22:   4.4461                                     
REMARK   3      L33:   3.3496 L12:  -0.9673                                     
REMARK   3      L13:   0.9559 L23:  -1.5343                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1066 S12:  -0.1999 S13:   0.4732                       
REMARK   3      S21:   0.3907 S22:   0.0142 S23:  -0.2095                       
REMARK   3      S31:  -0.0998 S32:   0.2431 S33:  -0.0806                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 119 THROUGH 1745 )                
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.6320  28.9568 -62.1535              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4163 T22:   0.6039                                     
REMARK   3      T33:   0.2126 T12:  -0.1626                                     
REMARK   3      T13:   0.0056 T23:   0.0072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0404 L22:   0.3880                                     
REMARK   3      L33:   4.5555 L12:   0.1872                                     
REMARK   3      L13:   0.3520 L23:   1.1497                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2533 S12:   0.2215 S13:  -0.0974                       
REMARK   3      S21:  -0.0754 S22:  -0.1323 S23:   0.3043                       
REMARK   3      S31:   0.6907 S32:   0.1896 S33:  -0.5890                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 73 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -19.5545  25.4912 -31.6425              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0301 T22:   0.1079                                     
REMARK   3      T33:   0.2857 T12:   0.0628                                     
REMARK   3      T13:   0.0042 T23:   0.0326                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1364 L22:   4.5839                                     
REMARK   3      L33:   3.8526 L12:   0.5980                                     
REMARK   3      L13:   0.3736 L23:   0.4943                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0679 S12:  -0.0555 S13:   0.4678                       
REMARK   3      S21:  -0.1514 S22:  -0.1580 S23:   0.0051                       
REMARK   3      S31:  -0.4503 S32:   0.0869 S33:   0.1293                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 74 THROUGH 118 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -23.2097  27.3535 -24.6098              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4677 T22:   0.1303                                     
REMARK   3      T33:   0.2155 T12:   0.1388                                     
REMARK   3      T13:   0.1496 T23:  -0.0236                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.1729 L22:   8.1664                                     
REMARK   3      L33:   3.8931 L12:   4.8498                                     
REMARK   3      L13:   2.6531 L23:   3.0831                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1760 S12:  -0.6137 S13:   0.3096                       
REMARK   3      S21:   0.3368 S22:  -0.0165 S23:  -0.0368                       
REMARK   3      S31:  -0.3791 S32:  -0.2728 S33:  -0.1430                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 119 THROUGH 1739 )                
REMARK   3    ORIGIN FOR THE GROUP (A):  23.1879   6.7303 -44.7300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2563 T22:   0.2762                                     
REMARK   3      T33:   0.5692 T12:   0.0650                                     
REMARK   3      T13:   0.0558 T23:  -0.0641                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1581 L22:   0.6620                                     
REMARK   3      L33:   1.4461 L12:   0.3117                                     
REMARK   3      L13:  -0.3734 L23:  -0.2795                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1374 S12:  -0.1933 S13:  -0.4237                       
REMARK   3      S21:  -0.1956 S22:  -0.2408 S23:  -0.4194                       
REMARK   3      S31:   0.0724 S32:   0.7873 S33:  -0.0921                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID -1 THROUGH 86 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -19.1865 -10.7243 -31.8950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2399 T22:   0.0373                                     
REMARK   3      T33:   0.2211 T12:  -0.1389                                     
REMARK   3      T13:   0.1339 T23:  -0.0147                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0289 L22:   4.9213                                     
REMARK   3      L33:   1.9687 L12:  -2.0047                                     
REMARK   3      L13:  -0.1913 L23:  -0.6207                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0249 S12:   0.0347 S13:  -0.3189                       
REMARK   3      S21:  -0.2467 S22:   0.1078 S23:   0.3777                       
REMARK   3      S31:   0.5807 S32:  -0.1927 S33:  -0.0240                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 87 THROUGH 118 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -26.7021 -14.1447 -36.0248              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4356 T22:   0.3964                                     
REMARK   3      T33:   0.6575 T12:  -0.1692                                     
REMARK   3      T13:  -0.2550 T23:  -0.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4208 L22:   5.7297                                     
REMARK   3      L33:   4.0264 L12:  -3.5838                                     
REMARK   3      L13:  -4.7005 L23:   3.4452                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2003 S12:   0.8904 S13:  -0.9649                       
REMARK   3      S21:  -0.4187 S22:  -1.0297 S23:   1.0704                       
REMARK   3      S31:  -0.0472 S32:  -1.0405 S33:   0.4501                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 119 THROUGH 1739 )                
REMARK   3    ORIGIN FOR THE GROUP (A):  21.6568   9.4722 -43.8868              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2373 T22:   0.4397                                     
REMARK   3      T33:   0.4429 T12:   0.1957                                     
REMARK   3      T13:   0.1789 T23:   0.0212                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5481 L22:   0.4018                                     
REMARK   3      L33:   2.2047 L12:  -0.1883                                     
REMARK   3      L13:  -2.5402 L23:   0.1366                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3650 S12:  -0.1285 S13:   0.7778                       
REMARK   3      S21:  -0.2443 S22:  -0.1607 S23:  -0.2730                       
REMARK   3      S31:  -0.3148 S32:   0.7127 S33:  -0.3538                       
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 5WLZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JUL-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229240.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-DEC-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97934                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16299                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 9.500                              
REMARK 200  R MERGE                    (I) : 0.13900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.13900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
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: 1IK9                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8-10% METHYL-ETHER POLYETHYLENE GLYCOL   
REMARK 280  (MEPEG) 5K, 300 MM GLYCINE, BIS-TRIS PROPANE PH 7.0, 1.5-3.0% (W/   
REMARK 280  V) JEFFAMINE M-600, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  298K                                                                
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       42.64500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.22850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.47000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.22850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.64500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       51.47000            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13790 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -100.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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     ARG C  1749                                                      
REMARK 465     ASN C  1750                                                      
REMARK 465     ALA C  1751                                                      
REMARK 465     GLU C  1752                                                      
REMARK 465     GLU C  1753                                                      
REMARK 465     LYS C  1754                                                      
REMARK 465     ALA C  1755                                                      
REMARK 465     LYS C  1756                                                      
REMARK 465     LYS C  1757                                                      
REMARK 465     ALA C  1758                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     SER D     0                                                      
REMARK 465     PRO D    80                                                      
REMARK 465     GLN D  1746                                                      
REMARK 465     GLU D  1747                                                      
REMARK 465     CYS D  1748                                                      
REMARK 465     ARG D  1749                                                      
REMARK 465     ASN D  1750                                                      
REMARK 465     ALA D  1751                                                      
REMARK 465     GLU D  1752                                                      
REMARK 465     GLU D  1753                                                      
REMARK 465     LYS D  1754                                                      
REMARK 465     ALA D  1755                                                      
REMARK 465     LYS D  1756                                                      
REMARK 465     LYS D  1757                                                      
REMARK 465     ALA D  1758                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     GLY A     1                                                      
REMARK 465     GLY A    79                                                      
REMARK 465     GLU A  1740                                                      
REMARK 465     VAL A  1741                                                      
REMARK 465     GLU A  1742                                                      
REMARK 465     GLU A  1743                                                      
REMARK 465     ALA A  1744                                                      
REMARK 465     VAL A  1745                                                      
REMARK 465     GLN A  1746                                                      
REMARK 465     GLU A  1747                                                      
REMARK 465     CYS A  1748                                                      
REMARK 465     ARG A  1749                                                      
REMARK 465     ASN A  1750                                                      
REMARK 465     ALA A  1751                                                      
REMARK 465     GLU A  1752                                                      
REMARK 465     GLU A  1753                                                      
REMARK 465     LYS A  1754                                                      
REMARK 465     ALA A  1755                                                      
REMARK 465     LYS A  1756                                                      
REMARK 465     LYS A  1757                                                      
REMARK 465     ALA A  1758                                                      
REMARK 465     ALA B    78                                                      
REMARK 465     GLY B    79                                                      
REMARK 465     GLU B  1740                                                      
REMARK 465     VAL B  1741                                                      
REMARK 465     GLU B  1742                                                      
REMARK 465     GLU B  1743                                                      
REMARK 465     ALA B  1744                                                      
REMARK 465     VAL B  1745                                                      
REMARK 465     GLN B  1746                                                      
REMARK 465     GLU B  1747                                                      
REMARK 465     CYS B  1748                                                      
REMARK 465     ARG B  1749                                                      
REMARK 465     ASN B  1750                                                      
REMARK 465     ALA B  1751                                                      
REMARK 465     GLU B  1752                                                      
REMARK 465     GLU B  1753                                                      
REMARK 465     LYS B  1754                                                      
REMARK 465     ALA B  1755                                                      
REMARK 465     LYS B  1756                                                      
REMARK 465     LYS B  1757                                                      
REMARK 465     ALA B  1758                                                      
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    SER C   0     -129.03     58.27                                   
REMARK 500    LYS C  26      -68.05     64.71                                   
REMARK 500    HIS C  40      -71.20   -130.18                                   
REMARK 500    ALA C  78       43.02   -159.08                                   
REMARK 500    GLU C  91       29.61     40.16                                   
REMARK 500    ARG C  93       78.79     55.95                                   
REMARK 500    GLU D  25     -149.12    -80.07                                   
REMARK 500    HIS D  40      -55.56   -138.94                                   
REMARK 500    ALA D  73      -61.89    -90.36                                   
REMARK 500    SER D  76       66.29     66.55                                   
REMARK 500    ASP D  82       -7.74     68.67                                   
REMARK 500    LEU D 101     -101.96   -115.10                                   
REMARK 500    LYS D 102      -75.00   -106.90                                   
REMARK 500    LYS A  26      -11.45     70.97                                   
REMARK 500    HIS A  40      -54.26   -120.83                                   
REMARK 500    ALA A  60       73.92     52.27                                   
REMARK 500    ALA A  81       70.30     56.69                                   
REMARK 500    GLU B  25      -85.98    -87.14                                   
REMARK 500    HIS B  40      -60.09   -122.85                                   
REMARK 500    SER B  89      -81.44    -80.00                                   
REMARK 500    LYS B  90      -36.01   -143.48                                   
REMARK 500    GLU B  91       57.44    -59.47                                   
REMARK 500    SER B  92       83.95    -67.66                                   
REMARK 500    LYS B  99       94.50    -65.59                                   
REMARK 500    ASP B 103      -86.71   -144.23                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5WLZ C    2   132  UNP    Q13426   XRCC4_HUMAN      2    132             
DBREF  5WLZ C 1677  1758  UNP    P12883   MYH7_HUMAN    1677   1758             
DBREF  5WLZ D    2   132  UNP    Q13426   XRCC4_HUMAN      2    132             
DBREF  5WLZ D 1677  1758  UNP    P12883   MYH7_HUMAN    1677   1758             
DBREF  5WLZ A    2   132  UNP    Q13426   XRCC4_HUMAN      2    132             
DBREF  5WLZ A 1677  1758  UNP    P12883   MYH7_HUMAN    1677   1758             
DBREF  5WLZ B    2   132  UNP    Q13426   XRCC4_HUMAN      2    132             
DBREF  5WLZ B 1677  1758  UNP    P12883   MYH7_HUMAN    1677   1758             
SEQADV 5WLZ GLY C   -1  UNP  Q13426              EXPRESSION TAG                 
SEQADV 5WLZ SER C    0  UNP  Q13426              EXPRESSION TAG                 
SEQADV 5WLZ GLY C    1  UNP  Q13426              EXPRESSION TAG                 
SEQADV 5WLZ LYS C   29  UNP  Q13426    GLU    29 ENGINEERED MUTATION            
SEQADV 5WLZ LYS C   51  UNP  Q13426    GLU    51 ENGINEERED MUTATION            
SEQADV 5WLZ ALA C   57  UNP  Q13426    ASP    57 ENGINEERED MUTATION            
SEQADV 5WLZ THR C   58  UNP  Q13426    ASP    58 ENGINEERED MUTATION            
SEQADV 5WLZ ASN C   62  UNP  Q13426    GLU    62 ENGINEERED MUTATION            
SEQADV 5WLZ ARG C   93  UNP  Q13426    CYS    93 ENGINEERED MUTATION            
SEQADV 5WLZ LYS C   98  UNP  Q13426    GLU    98 ENGINEERED MUTATION            
SEQADV 5WLZ ASP C  128  UNP  Q13426    CYS   128 ENGINEERED MUTATION            
SEQADV 5WLZ ALA C  130  UNP  Q13426    CYS   130 ENGINEERED MUTATION            
SEQADV 5WLZ GLY D   -1  UNP  Q13426              EXPRESSION TAG                 
SEQADV 5WLZ SER D    0  UNP  Q13426              EXPRESSION TAG                 
SEQADV 5WLZ GLY D    1  UNP  Q13426              EXPRESSION TAG                 
SEQADV 5WLZ LYS D   29  UNP  Q13426    GLU    29 ENGINEERED MUTATION            
SEQADV 5WLZ LYS D   51  UNP  Q13426    GLU    51 ENGINEERED MUTATION            
SEQADV 5WLZ ALA D   57  UNP  Q13426    ASP    57 ENGINEERED MUTATION            
SEQADV 5WLZ THR D   58  UNP  Q13426    ASP    58 ENGINEERED MUTATION            
SEQADV 5WLZ ASN D   62  UNP  Q13426    GLU    62 ENGINEERED MUTATION            
SEQADV 5WLZ ARG D   93  UNP  Q13426    CYS    93 ENGINEERED MUTATION            
SEQADV 5WLZ LYS D   98  UNP  Q13426    GLU    98 ENGINEERED MUTATION            
SEQADV 5WLZ ASP D  128  UNP  Q13426    CYS   128 ENGINEERED MUTATION            
SEQADV 5WLZ ALA D  130  UNP  Q13426    CYS   130 ENGINEERED MUTATION            
SEQADV 5WLZ GLY A   -1  UNP  Q13426              EXPRESSION TAG                 
SEQADV 5WLZ SER A    0  UNP  Q13426              EXPRESSION TAG                 
SEQADV 5WLZ GLY A    1  UNP  Q13426              EXPRESSION TAG                 
SEQADV 5WLZ LYS A   29  UNP  Q13426    GLU    29 ENGINEERED MUTATION            
SEQADV 5WLZ LYS A   51  UNP  Q13426    GLU    51 ENGINEERED MUTATION            
SEQADV 5WLZ ALA A   57  UNP  Q13426    ASP    57 ENGINEERED MUTATION            
SEQADV 5WLZ THR A   58  UNP  Q13426    ASP    58 ENGINEERED MUTATION            
SEQADV 5WLZ ASN A   62  UNP  Q13426    GLU    62 ENGINEERED MUTATION            
SEQADV 5WLZ ARG A   93  UNP  Q13426    CYS    93 ENGINEERED MUTATION            
SEQADV 5WLZ LYS A   98  UNP  Q13426    GLU    98 ENGINEERED MUTATION            
SEQADV 5WLZ ASP A  128  UNP  Q13426    CYS   128 ENGINEERED MUTATION            
SEQADV 5WLZ ALA A  130  UNP  Q13426    CYS   130 ENGINEERED MUTATION            
SEQADV 5WLZ GLY B   -1  UNP  Q13426              EXPRESSION TAG                 
SEQADV 5WLZ SER B    0  UNP  Q13426              EXPRESSION TAG                 
SEQADV 5WLZ GLY B    1  UNP  Q13426              EXPRESSION TAG                 
SEQADV 5WLZ LYS B   29  UNP  Q13426    GLU    29 ENGINEERED MUTATION            
SEQADV 5WLZ LYS B   51  UNP  Q13426    GLU    51 ENGINEERED MUTATION            
SEQADV 5WLZ ALA B   57  UNP  Q13426    ASP    57 ENGINEERED MUTATION            
SEQADV 5WLZ THR B   58  UNP  Q13426    ASP    58 ENGINEERED MUTATION            
SEQADV 5WLZ ASN B   62  UNP  Q13426    GLU    62 ENGINEERED MUTATION            
SEQADV 5WLZ ARG B   93  UNP  Q13426    CYS    93 ENGINEERED MUTATION            
SEQADV 5WLZ LYS B   98  UNP  Q13426    GLU    98 ENGINEERED MUTATION            
SEQADV 5WLZ ASP B  128  UNP  Q13426    CYS   128 ENGINEERED MUTATION            
SEQADV 5WLZ ALA B  130  UNP  Q13426    CYS   130 ENGINEERED MUTATION            
SEQRES   1 C  216  GLY SER GLY GLU ARG LYS ILE SER ARG ILE HIS LEU VAL          
SEQRES   2 C  216  SER GLU PRO SER ILE THR HIS PHE LEU GLN VAL SER TRP          
SEQRES   3 C  216  GLU LYS THR LEU LYS SER GLY PHE VAL ILE THR LEU THR          
SEQRES   4 C  216  ASP GLY HIS SER ALA TRP THR GLY THR VAL SER GLU SER          
SEQRES   5 C  216  LYS ILE SER GLN GLU ALA ALA THR MET ALA MET ASN LYS          
SEQRES   6 C  216  GLY LYS TYR VAL GLY GLU LEU ARG LYS ALA LEU LEU SER          
SEQRES   7 C  216  GLY ALA GLY PRO ALA ASP VAL TYR THR PHE ASN PHE SER          
SEQRES   8 C  216  LYS GLU SER ARG TYR PHE PHE PHE LYS LYS ASN LEU LYS          
SEQRES   9 C  216  ASP VAL SER PHE ARG LEU GLY SER PHE ASN LEU GLU LYS          
SEQRES  10 C  216  VAL GLU ASN PRO ALA GLU VAL ILE ARG GLU LEU ILE ASP          
SEQRES  11 C  216  TYR ALA LEU ASP ARG ASN ASN LEU LEU GLN ALA GLU LEU          
SEQRES  12 C  216  GLU GLU LEU ARG ALA VAL VAL GLU GLN THR GLU ARG SER          
SEQRES  13 C  216  ARG LYS LEU ALA GLU GLN GLU LEU ILE GLU THR SER GLU          
SEQRES  14 C  216  ARG VAL GLN LEU LEU HIS SER GLN ASN THR SER LEU ILE          
SEQRES  15 C  216  ASN GLN LYS LYS LYS MET ASP ALA ASP LEU SER GLN LEU          
SEQRES  16 C  216  GLN THR GLU VAL GLU GLU ALA VAL GLN GLU CYS ARG ASN          
SEQRES  17 C  216  ALA GLU GLU LYS ALA LYS LYS ALA                              
SEQRES   1 D  216  GLY SER GLY GLU ARG LYS ILE SER ARG ILE HIS LEU VAL          
SEQRES   2 D  216  SER GLU PRO SER ILE THR HIS PHE LEU GLN VAL SER TRP          
SEQRES   3 D  216  GLU LYS THR LEU LYS SER GLY PHE VAL ILE THR LEU THR          
SEQRES   4 D  216  ASP GLY HIS SER ALA TRP THR GLY THR VAL SER GLU SER          
SEQRES   5 D  216  LYS ILE SER GLN GLU ALA ALA THR MET ALA MET ASN LYS          
SEQRES   6 D  216  GLY LYS TYR VAL GLY GLU LEU ARG LYS ALA LEU LEU SER          
SEQRES   7 D  216  GLY ALA GLY PRO ALA ASP VAL TYR THR PHE ASN PHE SER          
SEQRES   8 D  216  LYS GLU SER ARG TYR PHE PHE PHE LYS LYS ASN LEU LYS          
SEQRES   9 D  216  ASP VAL SER PHE ARG LEU GLY SER PHE ASN LEU GLU LYS          
SEQRES  10 D  216  VAL GLU ASN PRO ALA GLU VAL ILE ARG GLU LEU ILE ASP          
SEQRES  11 D  216  TYR ALA LEU ASP ARG ASN ASN LEU LEU GLN ALA GLU LEU          
SEQRES  12 D  216  GLU GLU LEU ARG ALA VAL VAL GLU GLN THR GLU ARG SER          
SEQRES  13 D  216  ARG LYS LEU ALA GLU GLN GLU LEU ILE GLU THR SER GLU          
SEQRES  14 D  216  ARG VAL GLN LEU LEU HIS SER GLN ASN THR SER LEU ILE          
SEQRES  15 D  216  ASN GLN LYS LYS LYS MET ASP ALA ASP LEU SER GLN LEU          
SEQRES  16 D  216  GLN THR GLU VAL GLU GLU ALA VAL GLN GLU CYS ARG ASN          
SEQRES  17 D  216  ALA GLU GLU LYS ALA LYS LYS ALA                              
SEQRES   1 A  216  GLY SER GLY GLU ARG LYS ILE SER ARG ILE HIS LEU VAL          
SEQRES   2 A  216  SER GLU PRO SER ILE THR HIS PHE LEU GLN VAL SER TRP          
SEQRES   3 A  216  GLU LYS THR LEU LYS SER GLY PHE VAL ILE THR LEU THR          
SEQRES   4 A  216  ASP GLY HIS SER ALA TRP THR GLY THR VAL SER GLU SER          
SEQRES   5 A  216  LYS ILE SER GLN GLU ALA ALA THR MET ALA MET ASN LYS          
SEQRES   6 A  216  GLY LYS TYR VAL GLY GLU LEU ARG LYS ALA LEU LEU SER          
SEQRES   7 A  216  GLY ALA GLY PRO ALA ASP VAL TYR THR PHE ASN PHE SER          
SEQRES   8 A  216  LYS GLU SER ARG TYR PHE PHE PHE LYS LYS ASN LEU LYS          
SEQRES   9 A  216  ASP VAL SER PHE ARG LEU GLY SER PHE ASN LEU GLU LYS          
SEQRES  10 A  216  VAL GLU ASN PRO ALA GLU VAL ILE ARG GLU LEU ILE ASP          
SEQRES  11 A  216  TYR ALA LEU ASP ARG ASN ASN LEU LEU GLN ALA GLU LEU          
SEQRES  12 A  216  GLU GLU LEU ARG ALA VAL VAL GLU GLN THR GLU ARG SER          
SEQRES  13 A  216  ARG LYS LEU ALA GLU GLN GLU LEU ILE GLU THR SER GLU          
SEQRES  14 A  216  ARG VAL GLN LEU LEU HIS SER GLN ASN THR SER LEU ILE          
SEQRES  15 A  216  ASN GLN LYS LYS LYS MET ASP ALA ASP LEU SER GLN LEU          
SEQRES  16 A  216  GLN THR GLU VAL GLU GLU ALA VAL GLN GLU CYS ARG ASN          
SEQRES  17 A  216  ALA GLU GLU LYS ALA LYS LYS ALA                              
SEQRES   1 B  216  GLY SER GLY GLU ARG LYS ILE SER ARG ILE HIS LEU VAL          
SEQRES   2 B  216  SER GLU PRO SER ILE THR HIS PHE LEU GLN VAL SER TRP          
SEQRES   3 B  216  GLU LYS THR LEU LYS SER GLY PHE VAL ILE THR LEU THR          
SEQRES   4 B  216  ASP GLY HIS SER ALA TRP THR GLY THR VAL SER GLU SER          
SEQRES   5 B  216  LYS ILE SER GLN GLU ALA ALA THR MET ALA MET ASN LYS          
SEQRES   6 B  216  GLY LYS TYR VAL GLY GLU LEU ARG LYS ALA LEU LEU SER          
SEQRES   7 B  216  GLY ALA GLY PRO ALA ASP VAL TYR THR PHE ASN PHE SER          
SEQRES   8 B  216  LYS GLU SER ARG TYR PHE PHE PHE LYS LYS ASN LEU LYS          
SEQRES   9 B  216  ASP VAL SER PHE ARG LEU GLY SER PHE ASN LEU GLU LYS          
SEQRES  10 B  216  VAL GLU ASN PRO ALA GLU VAL ILE ARG GLU LEU ILE ASP          
SEQRES  11 B  216  TYR ALA LEU ASP ARG ASN ASN LEU LEU GLN ALA GLU LEU          
SEQRES  12 B  216  GLU GLU LEU ARG ALA VAL VAL GLU GLN THR GLU ARG SER          
SEQRES  13 B  216  ARG LYS LEU ALA GLU GLN GLU LEU ILE GLU THR SER GLU          
SEQRES  14 B  216  ARG VAL GLN LEU LEU HIS SER GLN ASN THR SER LEU ILE          
SEQRES  15 B  216  ASN GLN LYS LYS LYS MET ASP ALA ASP LEU SER GLN LEU          
SEQRES  16 B  216  GLN THR GLU VAL GLU GLU ALA VAL GLN GLU CYS ARG ASN          
SEQRES  17 B  216  ALA GLU GLU LYS ALA LYS LYS ALA                              
HELIX    1 AA1 GLU C   49  MET C   59  1                                  11    
HELIX    2 AA2 ASN C   62  LEU C   75  1                                  14    
HELIX    3 AA3 ASN C  100  VAL C  104  5                                   5    
HELIX    4 AA4 ASN C  118  GLN C 1746  1                                  85    
HELIX    5 AA5 THR D   27  LYS D   29  5                                   3    
HELIX    6 AA6 GLU D   49  MET D   59  1                                  11    
HELIX    7 AA7 ASN D   62  LEU D   75  1                                  14    
HELIX    8 AA8 ASN D  118  ALA D 1744  1                                  83    
HELIX    9 AA9 THR A   27  SER A   30  5                                   4    
HELIX   10 AB1 SER A   48  MET A   59  1                                  12    
HELIX   11 AB2 ASN A   62  LEU A   74  1                                  13    
HELIX   12 AB3 ASN A  118  THR A 1739  1                                  78    
HELIX   13 AB4 THR B   27  LYS B   29  5                                   3    
HELIX   14 AB5 GLU B   49  THR B   58  1                                  10    
HELIX   15 AB6 ASN B   62  LEU B   75  1                                  14    
HELIX   16 AB7 ASN B  118  LEU B 1737  1                                  76    
SHEET    1 AA1 5 GLU C   2  ILE C   8  0                                        
SHEET    2 AA1 5 HIS C  18  TRP C  24 -1  O  LEU C  20   N  SER C   6           
SHEET    3 AA1 5 GLY C  31  THR C  37 -1  O  THR C  35   N  GLN C  21           
SHEET    4 AA1 5 ALA C  42  SER C  48 -1  O  GLY C  45   N  ILE C  34           
SHEET    5 AA1 5 GLU C 114  LYS C 115 -1  O  GLU C 114   N  THR C  44           
SHEET    1 AA2 3 ASP C  82  PHE C  86  0                                        
SHEET    2 AA2 3 TYR C  94  LYS C  98 -1  O  PHE C  97   N  VAL C  83           
SHEET    3 AA2 3 ARG C 107  PHE C 111 -1  O  PHE C 111   N  TYR C  94           
SHEET    1 AA3 5 GLU D   2  ILE D   8  0                                        
SHEET    2 AA3 5 HIS D  18  TRP D  24 -1  O  LEU D  20   N  SER D   6           
SHEET    3 AA3 5 GLY D  31  THR D  37 -1  O  VAL D  33   N  SER D  23           
SHEET    4 AA3 5 ALA D  42  SER D  48 -1  O  TRP D  43   N  LEU D  36           
SHEET    5 AA3 5 GLU D 114  LYS D 115 -1  O  GLU D 114   N  THR D  44           
SHEET    1 AA4 3 TYR D  84  SER D  89  0                                        
SHEET    2 AA4 3 TYR D  94  ASN D 100 -1  O  PHE D  96   N  ASN D  87           
SHEET    3 AA4 3 SER D 105  ASN D 112 -1  O  PHE D 111   N  PHE D  95           
SHEET    1 AA5 5 ARG A   3  ILE A   8  0                                        
SHEET    2 AA5 5 HIS A  18  TRP A  24 -1  O  LEU A  20   N  SER A   6           
SHEET    3 AA5 5 PHE A  32  THR A  37 -1  O  VAL A  33   N  SER A  23           
SHEET    4 AA5 5 ALA A  42  VAL A  47 -1  O  TRP A  43   N  LEU A  36           
SHEET    5 AA5 5 GLU A 114  LYS A 115 -1  O  GLU A 114   N  THR A  44           
SHEET    1 AA6 3 TYR A  84  SER A  89  0                                        
SHEET    2 AA6 3 TYR A  94  LEU A 101 -1  O  LYS A  98   N  THR A  85           
SHEET    3 AA6 3 VAL A 104  ASN A 112 -1  O  PHE A 111   N  PHE A  95           
SHEET    1 AA7 5 GLU B   2  ILE B   8  0                                        
SHEET    2 AA7 5 HIS B  18  TRP B  24 -1  O  HIS B  18   N  ILE B   8           
SHEET    3 AA7 5 GLY B  31  THR B  37 -1  O  THR B  35   N  GLN B  21           
SHEET    4 AA7 5 ALA B  42  SER B  48 -1  O  TRP B  43   N  LEU B  36           
SHEET    5 AA7 5 GLU B 114  LYS B 115 -1  O  GLU B 114   N  THR B  44           
SHEET    1 AA8 3 VAL B  83  THR B  85  0                                        
SHEET    2 AA8 3 ARG B  93  PHE B  97 -1  O  PHE B  97   N  VAL B  83           
SHEET    3 AA8 3 ARG B 107  ASN B 112 -1  O  PHE B 111   N  TYR B  94           
CRYST1   85.290  102.940  136.457  90.00  90.00  90.00 P 21 21 21   16          
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      0.011725  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009714  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007328        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system