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Database: PDB
Entry: 5LLK
LinkDB: 5LLK
Original site: 5LLK 
HEADER    CELL ADHESION                           27-JUL-16   5LLK              
TITLE     CRYSTAL STRUCTURE OF HUMAN ALPHA-DYSTROGLYCAN                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DYSTROGLYCAN;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 52-315;                                       
COMPND   5 SYNONYM: DYSTROPHIN-ASSOCIATED GLYCOPROTEIN 1;                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: SKELETAL MUSCLE;                                              
SOURCE   6 GENE: DAG1;                                                          
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PLASMID;                                   
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PHIS-TRX                                  
KEYWDS    DYSTROGLYCAN, EXTRAELLULAR MATRIX ADHESION, CELL ADHESION             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.COVACEUSZACH,A.CASSETTA,D.LAMBA,A.BRANCACCIO,M.BOZZI,F.SCIANDRA,    
AUTHOR   2 M.G.BIGOTTI,P.V.KONAREV                                              
REVDAT   2   16-AUG-17 5LLK    1       JRNL                                     
REVDAT   1   12-JUL-17 5LLK    0                                                
JRNL        AUTH   S.COVACEUSZACH,M.BOZZI,M.G.BIGOTTI,F.SCIANDRA,P.V.KONAREV,   
JRNL        AUTH 2 A.BRANCACCIO,A.CASSETTA                                      
JRNL        TITL   STRUCTURAL FLEXIBILITY OF HUMAN ALPHA-DYSTROGLYCAN.          
JRNL        REF    FEBS OPEN BIO                 V.   7  1064 2017              
JRNL        REFN                   ESSN 2211-5463                               
JRNL        PMID   28781947                                                     
JRNL        DOI    10.1002/2211-5463.12259                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (DEV_2328: ???)                               
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.76                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.930                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 25153                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.163                           
REMARK   3   FREE R VALUE                     : 0.195                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1258                            
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 35.7670 -  3.7430    1.00     2680   141  0.1327 0.1567        
REMARK   3     2  3.7430 -  2.9714    1.00     2698   142  0.1535 0.1787        
REMARK   3     3  2.9714 -  2.5959    1.00     2679   142  0.1766 0.2297        
REMARK   3     4  2.5959 -  2.3586    0.99     2673   140  0.1771 0.2188        
REMARK   3     5  2.3586 -  2.1896    1.00     2672   141  0.1706 0.1953        
REMARK   3     6  2.1896 -  2.0605    1.00     2681   140  0.1838 0.1927        
REMARK   3     7  2.0605 -  1.9573    0.99     2667   140  0.2015 0.2777        
REMARK   3     8  1.9573 -  1.8721    0.98     2622   138  0.2487 0.2984        
REMARK   3     9  1.8721 -  1.8001    0.94     2523   134  0.3701 0.3645        
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)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.210           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.00                          
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      :  0.010           1747                                  
REMARK   3   ANGLE     :  1.012           2377                                  
REMARK   3   CHIRALITY :  0.063            277                                  
REMARK   3   PLANARITY :  0.007            305                                  
REMARK   3   DIHEDRAL  : 17.899           1051                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 61 THROUGH 115 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -20.9156 -13.9682  38.0541              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4999 T22:   0.4143                                     
REMARK   3      T33:   0.4416 T12:  -0.0777                                     
REMARK   3      T13:  -0.0429 T23:   0.0322                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4511 L22:   1.2059                                     
REMARK   3      L33:   1.6474 L12:   0.2773                                     
REMARK   3      L13:   0.4354 L23:   0.1272                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0096 S12:  -0.0661 S13:  -0.3679                       
REMARK   3      S21:  -0.0374 S22:  -0.1813 S23:  -0.2286                       
REMARK   3      S31:   0.4306 S32:   0.2714 S33:   0.0002                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 116 THROUGH 143 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -26.1584 -11.4161  39.4008              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3880 T22:   0.3016                                     
REMARK   3      T33:   0.3600 T12:  -0.0462                                     
REMARK   3      T13:  -0.0549 T23:  -0.0126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9656 L22:   0.8343                                     
REMARK   3      L33:   1.0338 L12:   0.0302                                     
REMARK   3      L13:  -0.6708 L23:   0.4401                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0479 S12:   0.0254 S13:  -0.1810                       
REMARK   3      S21:  -0.0593 S22:  -0.2874 S23:  -0.0730                       
REMARK   3      S31:   0.0232 S32:   0.4217 S33:   0.0010                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 144 THROUGH 203 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -23.8242  -3.2110  25.7148              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4632 T22:   0.3464                                     
REMARK   3      T33:   0.3416 T12:  -0.1100                                     
REMARK   3      T13:  -0.0422 T23:   0.0105                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4930 L22:   0.1944                                     
REMARK   3      L33:   1.8464 L12:  -0.1995                                     
REMARK   3      L13:   0.7350 L23:  -0.0038                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0788 S12:  -0.1206 S13:   0.1124                       
REMARK   3      S21:   0.1731 S22:  -0.1001 S23:  -0.0614                       
REMARK   3      S31:  -0.5043 S32:   0.0623 S33:  -0.0857                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 204 THROUGH 218 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -26.2663 -13.4899  17.5766              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4038 T22:   0.2848                                     
REMARK   3      T33:   0.3176 T12:  -0.0209                                     
REMARK   3      T13:  -0.0429 T23:   0.0220                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2873 L22:   0.3885                                     
REMARK   3      L33:   0.3125 L12:   0.1082                                     
REMARK   3      L13:   0.1393 L23:   0.3147                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2509 S12:  -0.3606 S13:  -0.0117                       
REMARK   3      S21:   0.4518 S22:  -0.0815 S23:  -0.1358                       
REMARK   3      S31:   0.3294 S32:  -0.0942 S33:   0.0003                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 219 THROUGH 292 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -27.7025  -4.4332   7.6753              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2608 T22:   0.2082                                     
REMARK   3      T33:   0.2630 T12:  -0.0018                                     
REMARK   3      T13:  -0.0087 T23:   0.0339                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4857 L22:   2.8537                                     
REMARK   3      L33:   3.1427 L12:   0.7024                                     
REMARK   3      L13:   0.0660 L23:  -0.6079                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0251 S12:   0.0737 S13:   0.1230                       
REMARK   3      S21:  -0.0823 S22:  -0.0810 S23:  -0.1171                       
REMARK   3      S31:  -0.1946 S32:   0.1700 S33:  -0.0001                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 293 THROUGH 304 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -26.5328   0.9806   7.1826              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4063 T22:   0.2606                                     
REMARK   3      T33:   0.3210 T12:  -0.0936                                     
REMARK   3      T13:  -0.0090 T23:   0.0338                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8071 L22:   0.4614                                     
REMARK   3      L33:   0.3311 L12:  -0.6053                                     
REMARK   3      L13:   0.0362 L23:   0.0223                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3030 S12:  -0.2733 S13:   0.3531                       
REMARK   3      S21:   0.2097 S22:  -0.3537 S23:  -0.1587                       
REMARK   3      S31:  -0.5696 S32:   0.2565 S33:   0.0135                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  REFINED: BULK SOLVENT + COORDINATES + TLS + ADP + OCCUPANCIES       
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET: ML                                               
REMARK   3                                                                      
REMARK   3  TLS REFINEMENT: 6 GROUPS                                            
REMARK   3                                                                      
REMARK   3  OCCUPANCIES: SELECTED RESIDUES WITH LOW ELECTRON DENSITY            
REMARK   4                                                                      
REMARK   4 5LLK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JUL-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200000946.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JAN-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8-7.2                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE CRYSTAL             
REMARK 200  OPTICS                         : PT-COATED MIRROR                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25220                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.04600                            
REMARK 200  R SYM                      (I) : 0.04600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.08000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.610                              
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: 1U2C                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8 M SODIUM CITRATE, PH 7.2, VAPOR      
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.76000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       20.64605            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       48.00333            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       35.76000            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       20.64605            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       48.00333            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       35.76000            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       20.64605            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       48.00333            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       41.29209            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       96.00667            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       41.29209            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       96.00667            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       41.29209            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       96.00667            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 370 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 12210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 616  LIES ON A SPECIAL POSITION.                          
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     GLY A    50                                                      
REMARK 465     SER A    51                                                      
REMARK 465     SER A    52                                                      
REMARK 465     VAL A    53                                                      
REMARK 465     LEU A    54                                                      
REMARK 465     SER A    55                                                      
REMARK 465     ASP A    56                                                      
REMARK 465     LEU A    57                                                      
REMARK 465     HIS A    58                                                      
REMARK 465     GLU A    59                                                      
REMARK 465     ALA A    60                                                      
REMARK 465     GLU A   163                                                      
REMARK 465     LEU A   164                                                      
REMARK 465     GLN A   165                                                      
REMARK 465     SER A   166                                                      
REMARK 465     VAL A   167                                                      
REMARK 465     HIS A   168                                                      
REMARK 465     THR A   169                                                      
REMARK 465     ALA A   170                                                      
REMARK 465     SER A   171                                                      
REMARK 465     PRO A   172                                                      
REMARK 465     ASP A   173                                                      
REMARK 465     PRO A   174                                                      
REMARK 465     GLY A   175                                                      
REMARK 465     GLU A   176                                                      
REMARK 465     VAL A   177                                                      
REMARK 465     VAL A   178                                                      
REMARK 465     SER A   179                                                      
REMARK 465     SER A   180                                                      
REMARK 465     PRO A   305                                                      
REMARK 465     LEU A   306                                                      
REMARK 465     PRO A   307                                                      
REMARK 465     LYS A   308                                                      
REMARK 465     ARG A   309                                                      
REMARK 465     VAL A   310                                                      
REMARK 465     ARG A   311                                                      
REMARK 465     ARG A   312                                                      
REMARK 465     GLN A   313                                                      
REMARK 465     ILE A   314                                                      
REMARK 465     HIS A   315                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP A   237     HZ1  LYS A   302              1.57            
REMARK 500   OD1  ASP A    92     HE   ARG A   137              1.57            
REMARK 500   OD2  ASP A   209     O    HOH A   501              2.01            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 185      -10.85     65.59                                   
REMARK 500    ASN A 232       19.89     56.77                                   
REMARK 500    LEU A 235       35.07    -91.08                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 402                 
DBREF  5LLK A   52   315  UNP    Q14118   DAG1_HUMAN      52    315             
SEQADV 5LLK GLY A   50  UNP  Q14118              EXPRESSION TAG                 
SEQADV 5LLK SER A   51  UNP  Q14118              EXPRESSION TAG                 
SEQADV 5LLK HIS A  168  UNP  Q14118    ARG   168 ENGINEERED MUTATION            
SEQRES   1 A  266  GLY SER SER VAL LEU SER ASP LEU HIS GLU ALA VAL PRO          
SEQRES   2 A  266  THR VAL VAL GLY ILE PRO ASP GLY THR ALA VAL VAL GLY          
SEQRES   3 A  266  ARG SER PHE ARG VAL THR ILE PRO THR ASP LEU ILE ALA          
SEQRES   4 A  266  SER SER GLY ASP ILE ILE LYS VAL SER ALA ALA GLY LYS          
SEQRES   5 A  266  GLU ALA LEU PRO SER TRP LEU HIS TRP ASP SER GLN SER          
SEQRES   6 A  266  HIS THR LEU GLU GLY LEU PRO LEU ASP THR ASP LYS GLY          
SEQRES   7 A  266  VAL HIS TYR ILE SER VAL SER ALA THR ARG LEU GLY ALA          
SEQRES   8 A  266  ASN GLY SER HIS ILE PRO GLN THR SER SER VAL PHE SER          
SEQRES   9 A  266  ILE GLU VAL TYR PRO GLU ASP HIS SER GLU LEU GLN SER          
SEQRES  10 A  266  VAL HIS THR ALA SER PRO ASP PRO GLY GLU VAL VAL SER          
SEQRES  11 A  266  SER ALA CYS ALA ALA ASP GLU PRO VAL THR VAL LEU THR          
SEQRES  12 A  266  VAL ILE LEU ASP ALA ASP LEU THR LYS MET THR PRO LYS          
SEQRES  13 A  266  GLN ARG ILE ASP LEU LEU HIS ARG MET ARG SER PHE SER          
SEQRES  14 A  266  GLU VAL GLU LEU HIS ASN MET LYS LEU VAL PRO VAL VAL          
SEQRES  15 A  266  ASN ASN ARG LEU PHE ASP MET SER ALA PHE MET ALA GLY          
SEQRES  16 A  266  PRO GLY ASN ALA LYS LYS VAL VAL GLU ASN GLY ALA LEU          
SEQRES  17 A  266  LEU SER TRP LYS LEU GLY CYS SER LEU ASN GLN ASN SER          
SEQRES  18 A  266  VAL PRO ASP ILE HIS GLY VAL GLU ALA PRO ALA ARG GLU          
SEQRES  19 A  266  GLY ALA MET SER ALA GLN LEU GLY TYR PRO VAL VAL GLY          
SEQRES  20 A  266  TRP HIS ILE ALA ASN LYS LYS PRO PRO LEU PRO LYS ARG          
SEQRES  21 A  266  VAL ARG ARG GLN ILE HIS                                      
HET    EDO  A 401      10                                                       
HET    EDO  A 402      10                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  EDO    2(C2 H6 O2)                                                  
FORMUL   4  HOH   *129(H2 O)                                                    
HELIX    1 AA1 PRO A   83  ALA A   88  1                                   6    
HELIX    2 AA2 LEU A  122  LYS A  126  5                                   5    
HELIX    3 AA3 PRO A  158  SER A  162  5                                   5    
HELIX    4 AA4 ASP A  198  MET A  202  5                                   5    
HELIX    5 AA5 THR A  203  GLU A  219  1                                  17    
HELIX    6 AA6 GLU A  221  HIS A  223  5                                   3    
HELIX    7 AA7 ILE A  274  GLY A  284  1                                  11    
HELIX    8 AA8 GLY A  284  GLY A  291  1                                   8    
SHEET    1 AA1 4 GLY A  70  VAL A  73  0                                        
SHEET    2 AA1 4 HIS A 144  TYR A 157  1  O  TYR A 157   N  ALA A  72           
SHEET    3 AA1 4 GLY A 127  LEU A 138 -1  N  ILE A 131   O  PHE A 152           
SHEET    4 AA1 4 ILE A  93  ALA A  98 -1  N  ILE A  93   O  THR A 136           
SHEET    1 AA2 3 PHE A  78  THR A  81  0                                        
SHEET    2 AA2 3 THR A 116  GLY A 119 -1  O  LEU A 117   N  VAL A  80           
SHEET    3 AA2 3 LEU A 108  ASP A 111 -1  N  ASP A 111   O  THR A 116           
SHEET    1 AA3 5 MET A 225  PRO A 229  0                                        
SHEET    2 AA3 5 ALA A 256  CYS A 264 -1  O  LEU A 257   N  VAL A 228           
SHEET    3 AA3 5 VAL A 188  LEU A 195 -1  N  LEU A 195   O  ALA A 256           
SHEET    4 AA3 5 VAL A 294  LYS A 302 -1  O  LYS A 302   N  VAL A 188           
SHEET    5 AA3 5 MET A 242  PRO A 245 -1  N  MET A 242   O  ILE A 299           
SSBOND   1 CYS A  182    CYS A  264                          1555   1555  2.05  
SITE     1 AC1  5 ASN A 247  ALA A 285  GLN A 289  HOH A 518                    
SITE     2 AC1  5 HOH A 528                                                     
SITE     1 AC2  5 PHE A 217  SER A 218  TRP A 260  LEU A 262                    
SITE     2 AC2  5 ASP A 273                                                     
CRYST1   71.520   71.520  144.010  90.00  90.00 120.00 H 3           9          
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      0.013982  0.008073  0.000000        0.00000                         
SCALE2      0.000000  0.016145  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006944        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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