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Database: PDB
Entry: 3G65
LinkDB: 3G65
Original site: 3G65 
HEADER    CELL CYCLE                              06-FEB-09   3G65              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN RAD9-RAD1-HUS1 DNA DAMAGE CHECKPOINT   
TITLE    2 COMPLEX                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL CYCLE CHECKPOINT CONTROL PROTEIN RAD9A;               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-270;                                        
COMPND   5 SYNONYM: HRAD9, DNA REPAIR EXONUCLEASE RAD9 HOMOLOG A;               
COMPND   6 EC: 3.1.11.2;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CELL CYCLE CHECKPOINT PROTEIN RAD1;                        
COMPND  10 CHAIN: B;                                                            
COMPND  11 SYNONYM: HRAD1, DNA REPAIR EXONUCLEASE RAD1 HOMOLOG, RAD1-LIKE DNA   
COMPND  12 DAMAGE CHECKPOINT PROTEIN;                                           
COMPND  13 EC: 3.1.11.2;                                                        
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: CHECKPOINT PROTEIN HUS1;                                   
COMPND  17 CHAIN: C;                                                            
COMPND  18 SYNONYM: HHUS1;                                                      
COMPND  19 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: RAD9, RAD9A;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS;                                
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PFBDM;                                    
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 GENE: RAD1, REC1;                                                    
SOURCE  17 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  18 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  20 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE  21 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS;                                
SOURCE  22 EXPRESSION_SYSTEM_PLASMID: PFBDM;                                    
SOURCE  23 MOL_ID: 3;                                                           
SOURCE  24 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  25 ORGANISM_COMMON: HUMAN;                                              
SOURCE  26 ORGANISM_TAXID: 9606;                                                
SOURCE  27 GENE: HUS1;                                                          
SOURCE  28 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  29 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  30 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  31 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE  32 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS;                                
SOURCE  33 EXPRESSION_SYSTEM_PLASMID: PFBDM                                     
KEYWDS    PCNA, DNA BINDING CLAMP, DNA DAMAGE, DNA REPAIR, EXONUCLEASE,         
KEYWDS   2 HYDROLASE, NUCLEASE, NUCLEUS, PHOSPHOPROTEIN, CELL CYCLE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.S.DORE,M.L.KILKENNY,N.J.RZECHORZEK,L.H.PEARL                        
REVDAT   3   25-SEP-13 3G65    1       REMARK VERSN                             
REVDAT   2   28-JUL-09 3G65    1       JRNL                                     
REVDAT   1   26-MAY-09 3G65    0                                                
JRNL        AUTH   A.S.DORE,M.L.KILKENNY,N.J.RZECHORZEK,L.H.PEARL               
JRNL        TITL   CRYSTAL STRUCTURE OF THE RAD9-RAD1-HUS1 DNA DAMAGE           
JRNL        TITL 2 CHECKPOINT COMPLEX--IMPLICATIONS FOR CLAMP LOADING AND       
JRNL        TITL 3 REGULATION.                                                  
JRNL        REF    MOL.CELL                      V.  34   735 2009              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   19446481                                                     
JRNL        DOI    10.1016/J.MOLCEL.2009.04.027                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 82.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 18445                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.272                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.110                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 942                             
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 82.0425 -  5.5162    1.00     2647   149  0.2306 0.2479        
REMARK   3     2  5.5162 -  4.3784    0.98     2525   146  0.1662 0.2246        
REMARK   3     3  4.3784 -  3.8250    0.97     2534   136  0.1967 0.2330        
REMARK   3     4  3.8250 -  3.4752    0.98     2517   113  0.2138 0.3011        
REMARK   3     5  3.4752 -  3.2261    0.98     2515   138  0.2386 0.3365        
REMARK   3     6  3.2261 -  3.0359    0.98     2533   144  0.2805 0.3341        
REMARK   3     7  3.0359 -  2.9000    0.87     2232   116  0.3048 0.3567        
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              : 0.30                                          
REMARK   3   B_SOL              : 56.89                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.400            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 76.60                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain A and resid 1:126                                
REMARK   3    ORIGIN FOR THE GROUP (A):   1.4351 -17.6938   1.9714              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3819 T22:  -0.3609                                     
REMARK   3      T33:   0.0182 T12:  -0.9277                                     
REMARK   3      T13:   0.2331 T23:   0.0706                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0674 L22:   0.0331                                     
REMARK   3      L33:   0.0990 L12:  -0.0040                                     
REMARK   3      L13:  -0.0154 L23:  -0.0470                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0421 S12:   0.2606 S13:   0.1892                       
REMARK   3      S21:   0.9101 S22:   0.2722 S23:  -0.5650                       
REMARK   3      S31:   0.7344 S32:  -0.4210 S33:   0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain A and resid 127:143                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.1580 -16.3134 -16.4435              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1574 T22:   0.5677                                     
REMARK   3      T33:  -0.0503 T12:  -0.5919                                     
REMARK   3      T13:   0.1586 T23:  -0.4543                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0447 L22:  -0.0480                                     
REMARK   3      L33:  -0.0117 L12:   0.0376                                     
REMARK   3      L13:  -0.0517 L23:   0.0245                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0010 S12:  -0.1444 S13:  -0.0977                       
REMARK   3      S21:  -0.0269 S22:   0.1533 S23:   0.1412                       
REMARK   3      S31:   0.0006 S32:  -0.2121 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain A and resid 144:276                              
REMARK   3    ORIGIN FOR THE GROUP (A):   9.0978  -8.4569 -22.8015              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0979 T22:   0.2748                                     
REMARK   3      T33:   0.2040 T12:  -0.1484                                     
REMARK   3      T13:   0.0365 T23:  -0.0904                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0140 L22:   0.1205                                     
REMARK   3      L33:   0.0795 L12:   0.1921                                     
REMARK   3      L13:  -0.0449 L23:   0.1536                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2454 S12:   0.3025 S13:   0.3743                       
REMARK   3      S21:  -0.1401 S22:  -0.0105 S23:  -0.0753                       
REMARK   3      S31:   0.6754 S32:  -0.4038 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain B and resid 15:135                               
REMARK   3    ORIGIN FOR THE GROUP (A):  29.2192  15.2423  26.6113              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2345 T22:   0.1355                                     
REMARK   3      T33:   0.1499 T12:  -0.0040                                     
REMARK   3      T13:  -0.1004 T23:  -0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0814 L22:   0.0921                                     
REMARK   3      L33:   0.1356 L12:   0.0776                                     
REMARK   3      L13:   0.0083 L23:  -0.0789                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3294 S12:  -0.1862 S13:  -0.0226                       
REMARK   3      S21:   0.2661 S22:   0.2205 S23:   0.0363                       
REMARK   3      S31:  -0.2687 S32:   0.0041 S33:  -0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain B and resid 136:153                              
REMARK   3    ORIGIN FOR THE GROUP (A):  13.0691   9.1619  37.5249              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7605 T22:   0.0779                                     
REMARK   3      T33:  -0.5649 T12:   0.1431                                     
REMARK   3      T13:   0.1758 T23:   0.3123                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0422 L22:  -0.0134                                     
REMARK   3      L33:  -0.0067 L12:   0.0208                                     
REMARK   3      L13:  -0.0251 L23:  -0.0168                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1015 S12:  -0.0553 S13:   0.0627                       
REMARK   3      S21:   0.1559 S22:  -0.2133 S23:  -0.0406                       
REMARK   3      S31:   0.3207 S32:  -0.3077 S33:  -0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain B and resid 154:280                              
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1975  -6.7954  26.3727              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1978 T22:   0.2902                                     
REMARK   3      T33:   0.1553 T12:  -0.0619                                     
REMARK   3      T13:   0.0376 T23:   0.0391                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0581 L22:   0.1307                                     
REMARK   3      L33:  -0.0569 L12:   0.0402                                     
REMARK   3      L13:  -0.0952 L23:   0.1093                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1174 S12:   0.4414 S13:  -0.0864                       
REMARK   3      S21:   0.0806 S22:  -0.0450 S23:  -0.0727                       
REMARK   3      S31:   0.1467 S32:  -0.2270 S33:   0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain C and resid 1:134                                
REMARK   3    ORIGIN FOR THE GROUP (A):  29.3513  11.7624 -24.1868              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2001 T22:   0.1681                                     
REMARK   3      T33:   0.2587 T12:  -0.0957                                     
REMARK   3      T13:   0.0583 T23:  -0.0271                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1871 L22:   0.0492                                     
REMARK   3      L33:   0.1576 L12:   0.1055                                     
REMARK   3      L13:   0.0322 L23:  -0.0343                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0417 S12:   0.0050 S13:  -0.4636                       
REMARK   3      S21:  -0.2305 S22:   0.0849 S23:  -0.1206                       
REMARK   3      S31:  -0.3098 S32:   0.1317 S33:   0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain C and resid 135:158                              
REMARK   3    ORIGIN FOR THE GROUP (A):  31.9568  31.3320 -19.5237              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3480 T22:  -0.4477                                     
REMARK   3      T33:  -0.0601 T12:  -0.4544                                     
REMARK   3      T13:   0.0597 T23:   0.3352                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0166 L22:  -0.0241                                     
REMARK   3      L33:   0.0070 L12:   0.0394                                     
REMARK   3      L13:  -0.0113 L23:  -0.0694                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1143 S12:   0.2630 S13:  -0.4203                       
REMARK   3      S21:  -0.8606 S22:  -0.6207 S23:   0.2772                       
REMARK   3      S31:  -0.0006 S32:  -0.0909 S33:   0.0000                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain C and resid 159:280                              
REMARK   3    ORIGIN FOR THE GROUP (A):  35.7856  25.3670   1.6778              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2328 T22:   0.1954                                     
REMARK   3      T33:   0.2096 T12:  -0.1290                                     
REMARK   3      T13:  -0.0291 T23:   0.0603                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0744 L22:   0.1921                                     
REMARK   3      L33:   0.1837 L12:  -0.0886                                     
REMARK   3      L13:   0.1012 L23:  -0.1655                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1602 S12:  -0.0681 S13:   0.0530                       
REMARK   3      S21:   0.0415 S22:  -0.0970 S23:  -0.2808                       
REMARK   3      S31:  -0.5158 S32:   0.3352 S33:  -0.0000                       
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 3G65 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB051471.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-APR-07; NULL                    
REMARK 200  TEMPERATURE           (KELVIN) : NULL; NULL                         
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : ESRF; ESRF                         
REMARK 200  BEAMLINE                       : ID14-1; ID29                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934; 1.0716                      
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210; ADSC QUANTUM     
REMARK 200                                   315R                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18454                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 82.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : 0.11500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 3.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.32600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1AXC                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, 17% PEG 2000-MME, PH      
REMARK 280  8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       35.33650            
REMARK 290   SMTRY3   2  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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4150 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ALA A    64                                                      
REMARK 465     THR A    65                                                      
REMARK 465     PRO A    66                                                      
REMARK 465     GLY A    67                                                      
REMARK 465     GLN A    68                                                      
REMARK 465     ASP A    69                                                      
REMARK 465     LEU A    70                                                      
REMARK 465     LEU A    90                                                      
REMARK 465     GLU A    91                                                      
REMARK 465     LYS A    92                                                      
REMARK 465     THR A    93                                                      
REMARK 465     ARG A   104                                                      
REMARK 465     SER A   105                                                      
REMARK 465     SER A   106                                                      
REMARK 465     GLU A   184                                                      
REMARK 465     GLU A   185                                                      
REMARK 465     ALA A   186                                                      
REMARK 465     ASP A   187                                                      
REMARK 465     SER A   188                                                      
REMARK 465     SER A   274                                                      
REMARK 465     THR A   275                                                      
REMARK 465     SER A   276                                                      
REMARK 465     LEU A   277                                                      
REMARK 465     GLU A   278                                                      
REMARK 465     VAL A   279                                                      
REMARK 465     LEU A   280                                                      
REMARK 465     PHE A   281                                                      
REMARK 465     GLN A   282                                                      
REMARK 465     GLY A   283                                                      
REMARK 465     PRO A   284                                                      
REMARK 465     LEU A   285                                                      
REMARK 465     SER A   286                                                      
REMARK 465     GLY A   287                                                      
REMARK 465     SER A   288                                                      
REMARK 465     GLY A   289                                                      
REMARK 465     GLY A   290                                                      
REMARK 465     HIS A   291                                                      
REMARK 465     HIS A   292                                                      
REMARK 465     HIS A   293                                                      
REMARK 465     HIS A   294                                                      
REMARK 465     HIS A   295                                                      
REMARK 465     HIS A   296                                                      
REMARK 465     MET B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     GLN B     6                                                      
REMARK 465     GLN B     7                                                      
REMARK 465     ILE B     8                                                      
REMARK 465     GLN B     9                                                      
REMARK 465     ASP B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     ASP B    12                                                      
REMARK 465     ASP B    13                                                      
REMARK 465     GLN B    14                                                      
REMARK 465     GLU B   276                                                      
REMARK 465     VAL B   277                                                      
REMARK 465     PRO B   278                                                      
REMARK 465     GLU B   279                                                      
REMARK 465     SER B   280                                                      
REMARK 465     GLU B   281                                                      
REMARK 465     SER B   282                                                      
REMARK 465     LYS C    46                                                      
REMARK 465     LEU C    47                                                      
REMARK 465     ALA C    48                                                      
REMARK 465     ASN C    49                                                      
REMARK 465     VAL C    72                                                      
REMARK 465     SER C    73                                                      
REMARK 465     ALA C    74                                                      
REMARK 465     LEU C   213                                                      
REMARK 465     ALA C   214                                                      
REMARK 465     SER C   215                                                      
REMARK 465     GLU C   216                                                      
REMARK 465     SER C   217                                                      
REMARK 465     THR C   218                                                      
REMARK 465     HIS C   219                                                      
REMARK 465     GLU C   220                                                      
REMARK 465     ASP C   221                                                      
REMARK 465     ARG C   222                                                      
REMARK 465     ASN C   223                                                      
REMARK 465     VAL C   224                                                      
REMARK 465     GLU C   225                                                      
REMARK 465     HIS C   226                                                      
REMARK 465     SER C   280                                                      
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    ILE A  23      -36.22   -144.92                                   
REMARK 500    GLU A  30       97.77   -167.65                                   
REMARK 500    PHE A  53       78.62   -102.20                                   
REMARK 500    PRO A  55       74.91    -19.08                                   
REMARK 500    PHE A  57     -121.75   -153.66                                   
REMARK 500    GLN A  60      144.59   -173.97                                   
REMARK 500    GLN A  62      156.87     66.68                                   
REMARK 500    SER A  86       -6.78   -151.65                                   
REMARK 500    ALA A  88       37.44    -91.60                                   
REMARK 500    PHE A 116       -6.98     69.13                                   
REMARK 500    CYS A 129     -151.99   -132.89                                   
REMARK 500    ASP A 137       70.58    178.95                                   
REMARK 500    GLN A 208       76.63   -114.73                                   
REMARK 500    ASP A 241     -115.92   -126.34                                   
REMARK 500    PRO A 243      106.64    -50.58                                   
REMARK 500    SER A 266     -140.45   -140.32                                   
REMARK 500    ASP A 267      -69.95    -98.53                                   
REMARK 500    SER B  16      -31.62     76.67                                   
REMARK 500    LEU B  17      114.21   -167.09                                   
REMARK 500    THR B  45     -154.07   -125.52                                   
REMARK 500    ALA B  56        9.92     59.90                                   
REMARK 500    GLU B  72       94.13   -173.97                                   
REMARK 500    LYS B  74      118.96   -161.26                                   
REMARK 500    GLU B  77     -123.96     55.27                                   
REMARK 500    GLU B  78     -151.12    -84.40                                   
REMARK 500    PHE B  82      132.80   -171.35                                   
REMARK 500    SER B  94       40.80    -92.04                                   
REMARK 500    PHE B  96       33.16    -82.78                                   
REMARK 500    PRO B 102      104.37    -47.17                                   
REMARK 500    GLU B 140     -117.60     65.40                                   
REMARK 500    GLU B 141       83.52     60.58                                   
REMARK 500    ASP B 146       34.75    -77.72                                   
REMARK 500    ALA B 166      -74.97    -66.98                                   
REMARK 500    LYS B 185      -80.07      6.81                                   
REMARK 500    PHE B 188      102.42   -160.68                                   
REMARK 500    ASP B 246     -168.08   -102.57                                   
REMARK 500    PHE C   3      115.70   -170.36                                   
REMARK 500    LEU C  43      148.91   -172.44                                   
REMARK 500    GLU C  61        4.24    -68.96                                   
REMARK 500    PHE C  63      -54.98   -120.73                                   
REMARK 500    ASN C  76       74.53   -105.34                                   
REMARK 500    ASN C  77       91.35    -61.08                                   
REMARK 500    GLU C  78      138.96   -175.90                                   
REMARK 500    ASN C  97       34.38    -88.53                                   
REMARK 500    ASN C 107       48.64   -163.12                                   
REMARK 500    LYS C 108      -82.29    -60.41                                   
REMARK 500    PRO C 152     -129.58    -65.45                                   
REMARK 500    ILE C 176      -63.73   -100.52                                   
REMARK 500    ASN C 185     -146.21   -101.47                                   
REMARK 500    GLU C 197       37.08    -79.17                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      60 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 322        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH A 331        DISTANCE =  5.61 ANGSTROMS                       
REMARK 525    HOH A 366        DISTANCE = 10.55 ANGSTROMS                       
REMARK 525    HOH A 367        DISTANCE =  7.40 ANGSTROMS                       
REMARK 525    HOH C 325        DISTANCE =  5.34 ANGSTROMS                       
REMARK 525    HOH C 360        DISTANCE =  5.47 ANGSTROMS                       
REMARK 525    HOH C 373        DISTANCE =  7.09 ANGSTROMS                       
DBREF  3G65 A    1   270  UNP    Q99638   RAD9A_HUMAN      1    270             
DBREF  3G65 B    1   282  UNP    O60671   RAD1_HUMAN       1    282             
DBREF  3G65 C    1   280  UNP    O60921   HUS1_HUMAN       1    280             
SEQADV 3G65 GLY A  271  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 THR A  272  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 THR A  273  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 SER A  274  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 THR A  275  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 SER A  276  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 LEU A  277  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 GLU A  278  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 VAL A  279  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 LEU A  280  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 PHE A  281  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 GLN A  282  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 GLY A  283  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 PRO A  284  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 LEU A  285  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 SER A  286  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 GLY A  287  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 SER A  288  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 GLY A  289  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 GLY A  290  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 HIS A  291  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 HIS A  292  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 HIS A  293  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 HIS A  294  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 HIS A  295  UNP  Q99638              EXPRESSION TAG                 
SEQADV 3G65 HIS A  296  UNP  Q99638              EXPRESSION TAG                 
SEQRES   1 A  296  MET LYS CYS LEU VAL THR GLY GLY ASN VAL LYS VAL LEU          
SEQRES   2 A  296  GLY LYS ALA VAL HIS SER LEU SER ARG ILE GLY ASP GLU          
SEQRES   3 A  296  LEU TYR LEU GLU PRO LEU GLU ASP GLY LEU SER LEU ARG          
SEQRES   4 A  296  THR VAL ASN SER SER ARG SER ALA TYR ALA CYS PHE LEU          
SEQRES   5 A  296  PHE ALA PRO LEU PHE PHE GLN GLN TYR GLN ALA ALA THR          
SEQRES   6 A  296  PRO GLY GLN ASP LEU LEU ARG CYS LYS ILE LEU MET LYS          
SEQRES   7 A  296  SER PHE LEU SER VAL PHE ARG SER LEU ALA MET LEU GLU          
SEQRES   8 A  296  LYS THR VAL GLU LYS CYS CYS ILE SER LEU ASN GLY ARG          
SEQRES   9 A  296  SER SER ARG LEU VAL VAL GLN LEU HIS CYS LYS PHE GLY          
SEQRES  10 A  296  VAL ARG LYS THR HIS ASN LEU SER PHE GLN ASP CYS GLU          
SEQRES  11 A  296  SER LEU GLN ALA VAL PHE ASP PRO ALA SER CYS PRO HIS          
SEQRES  12 A  296  MET LEU ARG ALA PRO ALA ARG VAL LEU GLY GLU ALA VAL          
SEQRES  13 A  296  LEU PRO PHE SER PRO ALA LEU ALA GLU VAL THR LEU GLY          
SEQRES  14 A  296  ILE GLY ARG GLY ARG ARG VAL ILE LEU ARG SER TYR HIS          
SEQRES  15 A  296  GLU GLU GLU ALA ASP SER THR ALA LYS ALA MET VAL THR          
SEQRES  16 A  296  GLU MET CYS LEU GLY GLU GLU ASP PHE GLN GLN LEU GLN          
SEQRES  17 A  296  ALA GLN GLU GLY VAL ALA ILE THR PHE CYS LEU LYS GLU          
SEQRES  18 A  296  PHE ARG GLY LEU LEU SER PHE ALA GLU SER ALA ASN LEU          
SEQRES  19 A  296  ASN LEU SER ILE HIS PHE ASP ALA PRO GLY ARG PRO ALA          
SEQRES  20 A  296  ILE PHE THR ILE LYS ASP SER LEU LEU ASP GLY HIS PHE          
SEQRES  21 A  296  VAL LEU ALA THR LEU SER ASP THR ASP SER GLY THR THR          
SEQRES  22 A  296  SER THR SER LEU GLU VAL LEU PHE GLN GLY PRO LEU SER          
SEQRES  23 A  296  GLY SER GLY GLY HIS HIS HIS HIS HIS HIS                      
SEQRES   1 B  282  MET PRO LEU LEU THR GLN GLN ILE GLN ASP GLU ASP ASP          
SEQRES   2 B  282  GLN TYR SER LEU VAL ALA SER LEU ASP ASN VAL ARG ASN          
SEQRES   3 B  282  LEU SER THR ILE LEU LYS ALA ILE HIS PHE ARG GLU HIS          
SEQRES   4 B  282  ALA THR CYS PHE ALA THR LYS ASN GLY ILE LYS VAL THR          
SEQRES   5 B  282  VAL GLU ASN ALA LYS CYS VAL GLN ALA ASN ALA PHE ILE          
SEQRES   6 B  282  GLN ALA GLY ILE PHE GLN GLU PHE LYS VAL GLN GLU GLU          
SEQRES   7 B  282  SER VAL THR PHE ARG ILE ASN LEU THR VAL LEU LEU ASP          
SEQRES   8 B  282  CYS LEU SER ILE PHE GLY SER SER PRO MET PRO GLY THR          
SEQRES   9 B  282  LEU THR ALA LEU ARG MET CYS TYR GLN GLY TYR GLY TYR          
SEQRES  10 B  282  PRO LEU MET LEU PHE LEU GLU GLU GLY GLY VAL VAL THR          
SEQRES  11 B  282  VAL CYS LYS ILE ASN THR GLN GLU PRO GLU GLU THR LEU          
SEQRES  12 B  282  ASP PHE ASP PHE CYS SER THR ASN VAL ILE ASN LYS ILE          
SEQRES  13 B  282  ILE LEU GLN SER GLU GLY LEU ARG GLU ALA PHE SER GLU          
SEQRES  14 B  282  LEU ASP MET THR SER GLU VAL LEU GLN ILE THR MET SER          
SEQRES  15 B  282  PRO ASP LYS PRO TYR PHE ARG LEU SER THR PHE GLY ASN          
SEQRES  16 B  282  ALA GLY SER SER HIS LEU ASP TYR PRO LYS ASP SER ASP          
SEQRES  17 B  282  LEU MET GLU ALA PHE HIS CYS ASN GLN THR GLN VAL ASN          
SEQRES  18 B  282  ARG TYR LYS ILE SER LEU LEU LYS PRO SER THR LYS ALA          
SEQRES  19 B  282  LEU VAL LEU SER CYS LYS VAL SER ILE ARG THR ASP ASN          
SEQRES  20 B  282  ARG GLY PHE LEU SER LEU GLN TYR MET ILE ARG ASN GLU          
SEQRES  21 B  282  ASP GLY GLN ILE CYS PHE VAL GLU TYR TYR CYS CYS PRO          
SEQRES  22 B  282  ASP GLU GLU VAL PRO GLU SER GLU SER                          
SEQRES   1 C  280  MET LYS PHE ARG ALA LYS ILE VAL ASP GLY ALA CYS LEU          
SEQRES   2 C  280  ASN HIS PHE THR ARG ILE SER ASN MET ILE ALA LYS LEU          
SEQRES   3 C  280  ALA LYS THR CYS THR LEU ARG ILE SER PRO ASP LYS LEU          
SEQRES   4 C  280  ASN PHE ILE LEU CYS ASP LYS LEU ALA ASN GLY GLY VAL          
SEQRES   5 C  280  SER MET TRP CYS GLU LEU GLU GLN GLU ASN PHE PHE ASN          
SEQRES   6 C  280  GLU PHE GLN MET GLU GLY VAL SER ALA GLU ASN ASN GLU          
SEQRES   7 C  280  ILE TYR LEU GLU LEU THR SER GLU ASN LEU SER ARG ALA          
SEQRES   8 C  280  LEU LYS THR ALA GLN ASN ALA ARG ALA LEU LYS ILE LYS          
SEQRES   9 C  280  LEU THR ASN LYS HIS PHE PRO CYS LEU THR VAL SER VAL          
SEQRES  10 C  280  GLU LEU LEU SER MET SER SER SER SER ARG ILE VAL THR          
SEQRES  11 C  280  HIS ASP ILE PRO ILE LYS VAL ILE PRO ARG LYS LEU TRP          
SEQRES  12 C  280  LYS ASP LEU GLN GLU PRO VAL VAL PRO ASP PRO ASP VAL          
SEQRES  13 C  280  SER ILE TYR LEU PRO VAL LEU LYS THR MET LYS SER VAL          
SEQRES  14 C  280  VAL GLU LYS MET LYS ASN ILE SER ASN HIS LEU VAL ILE          
SEQRES  15 C  280  GLU ALA ASN LEU ASP GLY GLU LEU ASN LEU LYS ILE GLU          
SEQRES  16 C  280  THR GLU LEU VAL CYS VAL THR THR HIS PHE LYS ASP LEU          
SEQRES  17 C  280  GLY ASN PRO PRO LEU ALA SER GLU SER THR HIS GLU ASP          
SEQRES  18 C  280  ARG ASN VAL GLU HIS MET ALA GLU VAL HIS ILE ASP ILE          
SEQRES  19 C  280  ARG LYS LEU LEU GLN PHE LEU ALA GLY GLN GLN VAL ASN          
SEQRES  20 C  280  PRO THR LYS ALA LEU CYS ASN ILE VAL ASN ASN LYS MET          
SEQRES  21 C  280  VAL HIS PHE ASP LEU LEU HIS GLU ASP VAL SER LEU GLN          
SEQRES  22 C  280  TYR PHE ILE PRO ALA LEU SER                                  
FORMUL   4  HOH   *82(H2 O)                                                     
HELIX    1   1 GLY A    7  ARG A   22  1                                  16    
HELIX    2   2 MET A   77  SER A   82  1                                   6    
HELIX    3   3 LYS A  115  GLY A  117  5                                   3    
HELIX    4   4 ASP A  137  CYS A  141  5                                   5    
HELIX    5   5 ALA A  149  VAL A  156  1                                   8    
HELIX    6   6 GLY A  200  PHE A  204  5                                   5    
HELIX    7   7 LEU A  219  ALA A  232  1                                  14    
HELIX    8   8 VAL B   24  ALA B   33  1                                  10    
HELIX    9   9 LEU B   86  SER B   94  1                                   9    
HELIX   10  10 SER B  160  GLU B  169  1                                  10    
HELIX   11  11 LYS B  224  PRO B  230  5                                   7    
HELIX   12  12 SER B  231  VAL B  236  1                                   6    
HELIX   13  13 ASP C    9  ALA C   27  1                                  19    
HELIX   14  14 GLU C   61  PHE C   63  5                                   3    
HELIX   15  15 SER C   85  THR C   94  1                                  10    
HELIX   16  16 PRO C  139  GLN C  147  5                                   9    
HELIX   17  17 VAL C  162  ASN C  175  1                                  14    
HELIX   18  18 ILE C  234  GLN C  244  1                                  11    
SHEET    1   A 8 LYS A   2  THR A   6  0                                        
SHEET    2   A 8 LYS A  96  LEU A 101 -1  O  CYS A  97   N  VAL A   5           
SHEET    3   A 8 LEU A 108  HIS A 113 -1  O  GLN A 111   N  CYS A  98           
SHEET    4   A 8 ARG A 119  LEU A 124 -1  O  LEU A 124   N  LEU A 108           
SHEET    5   A 8 GLY B 197  ASP B 202 -1  O  SER B 198   N  ASN A 123           
SHEET    6   A 8 PHE B 188  PHE B 193 -1  N  LEU B 190   O  LEU B 201           
SHEET    7   A 8 LEU B 177  MET B 181 -1  N  THR B 180   O  ARG B 189           
SHEET    8   A 8 GLN B 219  TYR B 223 -1  O  ASN B 221   N  ILE B 179           
SHEET    1   B 9 CYS A  73  LEU A  76  0                                        
SHEET    2   B 9 GLU A  26  LEU A  32 -1  N  LEU A  27   O  ILE A  75           
SHEET    3   B 9 GLY A  35  VAL A  41 -1  O  ARG A  39   N  TYR A  28           
SHEET    4   B 9 ALA A  47  PHE A  53 -1  O  PHE A  51   N  LEU A  38           
SHEET    5   B 9 ASP A 257  LEU A 262 -1  O  VAL A 261   N  TYR A  48           
SHEET    6   B 9 ALA A 247  LYS A 252 -1  N  PHE A 249   O  PHE A 260           
SHEET    7   B 9 ASN A 235  HIS A 239 -1  N  HIS A 239   O  ILE A 248           
SHEET    8   B 9 MET A 144  PRO A 148 -1  N  ALA A 147   O  LEU A 236           
SHEET    9   B 9 GLN A 206  GLN A 208 -1  O  GLN A 208   N  MET A 144           
SHEET    1   C 7 ALA A 214  CYS A 218  0                                        
SHEET    2   C 7 GLU A 165  GLY A 171 -1  N  LEU A 168   O  ILE A 215           
SHEET    3   C 7 ARG A 175  SER A 180 -1  O  ARG A 179   N  THR A 167           
SHEET    4   C 7 VAL A 194  LEU A 199 -1  O  LEU A 199   N  VAL A 176           
SHEET    5   C 7 ARG C 127  PRO C 134 -1  O  ILE C 128   N  CYS A 198           
SHEET    6   C 7 CYS C 112  LEU C 119 -1  N  VAL C 115   O  HIS C 131           
SHEET    7   C 7 ALA C 100  THR C 106 -1  N  LYS C 104   O  THR C 114           
SHEET    1   D 9 GLU B  72  VAL B  75  0                                        
SHEET    2   D 9 LEU B  17  LEU B  21 -1  N  SER B  20   O  GLU B  72           
SHEET    3   D 9 ALA B 107  CYS B 111 -1  O  LEU B 108   N  LEU B  21           
SHEET    4   D 9 LEU B 119  GLU B 125 -1  O  MET B 120   N  CYS B 111           
SHEET    5   D 9 VAL B 128  ILE B 134 -1  O  ILE B 134   N  LEU B 119           
SHEET    6   D 9 VAL C 199  HIS C 204 -1  O  HIS C 204   N  VAL B 129           
SHEET    7   D 9 LEU C 190  GLU C 195 -1  N  ILE C 194   O  VAL C 201           
SHEET    8   D 9 HIS C 179  ALA C 184 -1  N  GLU C 183   O  ASN C 191           
SHEET    9   D 9 ALA C 228  ASP C 233 -1  O  VAL C 230   N  ILE C 182           
SHEET    1   E 9 VAL B  80  ASN B  85  0                                        
SHEET    2   E 9 HIS B  39  ALA B  44 -1  N  ALA B  40   O  ILE B  84           
SHEET    3   E 9 GLY B  48  ASN B  55 -1  O  THR B  52   N  THR B  41           
SHEET    4   E 9 VAL B  59  GLN B  66 -1  O  ALA B  61   N  VAL B  53           
SHEET    5   E 9 ILE B 264  CYS B 271 -1  O  GLU B 268   N  ASN B  62           
SHEET    6   E 9 LEU B 251  ARG B 258 -1  N  TYR B 255   O  VAL B 267           
SHEET    7   E 9 LYS B 240  ASP B 246 -1  N  SER B 242   O  GLN B 254           
SHEET    8   E 9 VAL B 152  GLN B 159 -1  N  ILE B 156   O  ILE B 243           
SHEET    9   E 9 MET B 210  CYS B 215 -1  O  HIS B 214   N  LYS B 155           
SHEET    1   F 2 LYS C   2  LYS C   6  0                                        
SHEET    2   F 2 GLU C  66  GLU C  70 -1  O  GLN C  68   N  ARG C   4           
SHEET    1   G 8 ILE C  79  THR C  84  0                                        
SHEET    2   G 8 THR C  29  ILE C  34 -1  N  ILE C  34   O  ILE C  79           
SHEET    3   G 8 LYS C  38  CYS C  44 -1  O  ILE C  42   N  THR C  31           
SHEET    4   G 8 SER C  53  GLU C  59 -1  O  LEU C  58   N  LEU C  39           
SHEET    5   G 8 VAL C 270  ILE C 276 -1  O  GLN C 273   N  TRP C  55           
SHEET    6   G 8 MET C 260  HIS C 267 -1  N  PHE C 263   O  TYR C 274           
SHEET    7   G 8 ALA C 251  VAL C 256 -1  N  ASN C 254   O  HIS C 262           
SHEET    8   G 8 VAL C 156  TYR C 159 -1  N  VAL C 156   O  ILE C 255           
CRYST1   73.246   70.673   83.151  90.00  99.51  90.00 P 1 21 1      2          
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      0.013653  0.000000  0.002286        0.00000                         
SCALE2      0.000000  0.014150  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012194        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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