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Database: PDB
Entry: 4MT6
LinkDB: 4MT6
Original site: 4MT6 
HEADER    PROTEIN BINDING                         19-SEP-13   4MT6              
TITLE     CRYSTAL STRUCTURE OF CLOSED INACTIVE COLLYBISTIN                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 9;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: COLLYBISTIN, RAC/CDC42 GUANINE NUCLEOTIDE EXCHANGE FACTOR 9;
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: ARHGEF9;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PTYB12                                    
KEYWDS    CLOSED CONFORMATION, PROTEIN BINDING                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.SCHNEEBERGER,H.SCHINDELIN                                           
REVDAT   2   01-OCT-14 4MT6    1       JRNL                                     
REVDAT   1   13-AUG-14 4MT6    0                                                
JRNL        AUTH   T.SOYKAN,D.SCHNEEBERGER,G.TRIA,C.BUECHNER,N.BADER,D.SVERGUN, 
JRNL        AUTH 2 I.TESSMER,A.POULOPOULOS,T.PAPADOPOULOS,F.VAROQUEAUX,         
JRNL        AUTH 3 H.SCHINDELIN,N.BROSE                                         
JRNL        TITL   A CONFORMATIONAL SWITCH IN COLLYBISTIN DETERMINES THE        
JRNL        TITL 2 DIFFERENTIATION OF INHIBITORY POSTSYNAPSES.                  
JRNL        REF    EMBO J.                       V.  33  2113 2014              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   25082542                                                     
JRNL        DOI    10.15252/EMBJ.201488143                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    5.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 5.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 108.63                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 5694                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.239                           
REMARK   3   R VALUE            (WORKING SET) : 0.237                           
REMARK   3   FREE R VALUE                     : 0.282                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.710                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 268                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1108.6506 -  6.9301    1.00     2752   131  0.2151 0.2614        
REMARK   3     2  6.9301 -  5.5007    1.00     2674   137  0.3199 0.3580        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.910            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 38.440           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 300.13                         
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 177.06                         
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      :  0.004           3372                                  
REMARK   3   ANGLE     :  0.682           4536                                  
REMARK   3   CHIRALITY :  0.047            462                                  
REMARK   3   PLANARITY :  0.003            589                                  
REMARK   3   DIHEDRAL  : 15.531           1278                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain A and resseq 18:72                               
REMARK   3    ORIGIN FOR THE GROUP (A): -22.4396 -35.0715  -6.6584              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6140 T22:   2.6357                                     
REMARK   3      T33:   0.2029 T12:   0.7523                                     
REMARK   3      T13:   0.7429 T23:   0.2887                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0237 L22:   1.0644                                     
REMARK   3      L33:   0.5848 L12:  -0.0116                                     
REMARK   3      L13:  -0.6708 L23:   0.3436                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8403 S12:  -0.4057 S13:  -0.8757                       
REMARK   3      S21:  -0.0986 S22:   0.0332 S23:  -0.0822                       
REMARK   3      S31:   0.5749 S32:  -0.1128 S33:   0.4651                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain A and resseq 106:293                             
REMARK   3    ORIGIN FOR THE GROUP (A): -42.6989 -24.1394  -9.7800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3896 T22:   1.4153                                     
REMARK   3      T33:   1.6232 T12:   0.3592                                     
REMARK   3      T13:  -0.1782 T23:   0.4670                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9649 L22:   2.6656                                     
REMARK   3      L33:   2.6673 L12:   0.1515                                     
REMARK   3      L13:  -0.1981 L23:   0.2683                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4524 S12:   0.4546 S13:  -1.1471                       
REMARK   3      S21:  -1.1204 S22:   0.1639 S23:  -0.3783                       
REMARK   3      S31:  -0.3838 S32:  -0.8042 S33:  -0.2349                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain A and resseq 294:439                             
REMARK   3    ORIGIN FOR THE GROUP (A): -23.9646 -59.0711   4.9860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4607 T22:   1.7060                                     
REMARK   3      T33:   1.4207 T12:  -0.2862                                     
REMARK   3      T13:   0.1180 T23:   0.4218                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4230 L22:   0.7853                                     
REMARK   3      L33:   2.9333 L12:  -0.5080                                     
REMARK   3      L13:  -0.5540 L23:   1.2542                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.0936 S12:  -0.3532 S13:  -2.0853                       
REMARK   3      S21:  -0.0270 S22:   0.4915 S23:   0.4227                       
REMARK   3      S31:   1.3769 S32:  -1.3564 S33:   0.5472                       
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 4MT6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-SEP-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB082333.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JUL-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8726                             
REMARK 200  MONOCHROMATOR                  : HORIZONTALLY DIFFRACTING SI (111)  
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 5698                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 5.501                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 153.625                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 11.000                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.15500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 5.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 5.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.20                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.01600                            
REMARK 200  R SYM FOR SHELL            (I) : 1.56900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.500                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 84.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 7.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20MM NA-CACODYLATE, 5MM CO(III)          
REMARK 280  HEXAMINE CHLORIDE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,           
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 3                           
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
REMARK 290      13555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      14555   -X,-Y+1/2,Z                                             
REMARK 290      15555   -X+1/2,Y,-Z                                             
REMARK 290      16555   X,-Y,-Z+1/2                                             
REMARK 290      17555   Z+1/2,X+1/2,Y+1/2                                       
REMARK 290      18555   Z,-X,-Y+1/2                                             
REMARK 290      19555   -Z,-X+1/2,Y                                             
REMARK 290      20555   -Z+1/2,X,-Y                                             
REMARK 290      21555   Y+1/2,Z+1/2,X+1/2                                       
REMARK 290      22555   -Y+1/2,Z,-X                                             
REMARK 290      23555   Y,-Z,-X+1/2                                             
REMARK 290      24555   -Y,-Z+1/2,X                                             
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      108.62950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      108.62950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      108.62950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      108.62950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      108.62950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      108.62950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000      108.62950            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000      108.62950            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000      108.62950            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000      108.62950            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000      108.62950            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000      108.62950            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000      108.62950            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000      108.62950            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000      108.62950            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000      108.62950            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000      108.62950            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000      108.62950            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000      108.62950            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000      108.62950            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      108.62950            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000      108.62950            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000      108.62950            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      108.62950            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000      108.62950            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000      108.62950            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000      108.62950            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000      108.62950            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000      108.62950            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000      108.62950            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000      108.62950            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000      108.62950            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000      108.62950            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000      108.62950            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000      108.62950            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000      108.62950            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000        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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLN A     2                                                      
REMARK 465     TRP A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     ARG A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     MET A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     ILE A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     GLY A    14                                                      
REMARK 465     ASP A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     ILE A    17                                                      
REMARK 465     VAL A    73                                                      
REMARK 465     ASN A    74                                                      
REMARK 465     GLN A    75                                                      
REMARK 465     GLU A    76                                                      
REMARK 465     ASP A    77                                                      
REMARK 465     GLY A    78                                                      
REMARK 465     VAL A    79                                                      
REMARK 465     GLU A    80                                                      
REMARK 465     GLU A    81                                                      
REMARK 465     GLY A    82                                                      
REMARK 465     PRO A    83                                                      
REMARK 465     SER A    84                                                      
REMARK 465     ASP A    85                                                      
REMARK 465     VAL A    86                                                      
REMARK 465     GLN A    87                                                      
REMARK 465     ASN A    88                                                      
REMARK 465     GLY A    89                                                      
REMARK 465     HIS A    90                                                      
REMARK 465     LEU A    91                                                      
REMARK 465     ASP A    92                                                      
REMARK 465     PRO A    93                                                      
REMARK 465     ASN A    94                                                      
REMARK 465     SER A    95                                                      
REMARK 465     ASP A    96                                                      
REMARK 465     CYS A    97                                                      
REMARK 465     LEU A    98                                                      
REMARK 465     CYS A    99                                                      
REMARK 465     LEU A   100                                                      
REMARK 465     GLY A   101                                                      
REMARK 465     ARG A   102                                                      
REMARK 465     PRO A   103                                                      
REMARK 465     LEU A   104                                                      
REMARK 465     GLN A   105                                                      
REMARK 465     ILE A   440                                                      
REMARK 465     GLY A   441                                                      
REMARK 465     PHE A   442                                                      
REMARK 465     GLU A   443                                                      
REMARK 465     ILE A   444                                                      
REMARK 465     SER A   445                                                      
REMARK 465     GLU A   446                                                      
REMARK 465     ASN A   447                                                      
REMARK 465     GLN A   448                                                      
REMARK 465     LYS A   449                                                      
REMARK 465     ARG A   450                                                      
REMARK 465     GLN A   451                                                      
REMARK 465     ALA A   452                                                      
REMARK 465     ALA A   453                                                      
REMARK 465     MET A   454                                                      
REMARK 465     THR A   455                                                      
REMARK 465     VAL A   456                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A  296   CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ASN A   292     N    LYS A   295              1.77            
REMARK 500   O    ASN A   292     N    ARG A   294              1.95            
REMARK 500   O    LEU A   263     OG1  THR A   267              2.09            
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    LEU A  45      -61.64    -92.79                                   
REMARK 500    PHE A 156      -63.28   -104.77                                   
REMARK 500    GLN A 236       61.64     72.38                                   
REMARK 500    ASP A 239       38.56    -76.76                                   
REMARK 500    ALA A 241     -166.80    -67.65                                   
REMARK 500    VAL A 250       -8.58    -59.44                                   
REMARK 500    ASN A 292      -88.18    -69.09                                   
REMARK 500    GLU A 293      -38.69     -9.60                                   
REMARK 500    SER A 324       26.35   -177.47                                   
REMARK 500    GLU A 325      132.11   -170.33                                   
REMARK 500    TYR A 339       -7.67     77.36                                   
REMARK 500    HIS A 352      -22.03    100.86                                   
REMARK 500    ASP A 385      163.76    -48.83                                   
REMARK 500    ASP A 390      106.45    -23.01                                   
REMARK 500    PHE A 391      -95.09     12.66                                   
REMARK 500    ASN A 392       56.79     96.44                                   
REMARK 500    ASN A 397       64.11     61.48                                   
REMARK 500    LYS A 415      -70.69    -89.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4MT7   RELATED DB: PDB                                   
DBREF  4MT6 A    1   456  UNP    Q9QX73   ARHG9_RAT        1    456             
SEQADV 4MT6 GLU A   33  UNP  Q9QX73    GLY    33 ENGINEERED MUTATION            
SEQADV 4MT6 LEU A   34  UNP  Q9QX73    VAL    34 ENGINEERED MUTATION            
SEQRES   1 A  456  MET GLN TRP ILE ARG GLY GLY SER GLY MET LEU ILE THR          
SEQRES   2 A  456  GLY ASP SER ILE VAL SER ALA GLU ALA VAL TRP ASP HIS          
SEQRES   3 A  456  VAL THR MET ALA ASN ARG GLU LEU ALA PHE LYS ALA GLY          
SEQRES   4 A  456  ASP VAL ILE LYS VAL LEU ASP ALA SER ASN LYS ASP TRP          
SEQRES   5 A  456  TRP TRP GLY GLN ILE ASP ASP GLU GLU GLY TRP PHE PRO          
SEQRES   6 A  456  ALA SER PHE VAL ARG LEU TRP VAL ASN GLN GLU ASP GLY          
SEQRES   7 A  456  VAL GLU GLU GLY PRO SER ASP VAL GLN ASN GLY HIS LEU          
SEQRES   8 A  456  ASP PRO ASN SER ASP CYS LEU CYS LEU GLY ARG PRO LEU          
SEQRES   9 A  456  GLN ASN ARG ASP GLN MET ARG ALA ASN VAL ILE ASN GLU          
SEQRES  10 A  456  ILE MET SER THR GLU ARG HIS TYR ILE LYS HIS LEU LYS          
SEQRES  11 A  456  ASP ILE CYS GLU GLY TYR LEU LYS GLN CYS ARG LYS ARG          
SEQRES  12 A  456  ARG ASP MET PHE SER ASP GLU GLN LEU LYS VAL ILE PHE          
SEQRES  13 A  456  GLY ASN ILE GLU ASP ILE TYR ARG PHE GLN MET GLY PHE          
SEQRES  14 A  456  VAL ARG ASP LEU GLU LYS GLN TYR ASN ASN ASP ASP PRO          
SEQRES  15 A  456  HIS LEU SER GLU ILE GLY PRO CYS PHE LEU GLU HIS GLN          
SEQRES  16 A  456  ASP GLY PHE TRP ILE TYR SER GLU TYR CYS ASN ASN HIS          
SEQRES  17 A  456  LEU ASP ALA CYS MET GLU LEU SER LYS LEU MET LYS ASP          
SEQRES  18 A  456  SER ARG TYR GLN HIS PHE PHE GLU ALA CYS ARG LEU LEU          
SEQRES  19 A  456  GLN GLN MET ILE ASP ILE ALA ILE ASP GLY PHE LEU LEU          
SEQRES  20 A  456  THR PRO VAL GLN LYS ILE CYS LYS TYR PRO LEU GLN LEU          
SEQRES  21 A  456  ALA GLU LEU LEU LYS TYR THR ALA GLN ASP HIS SER ASP          
SEQRES  22 A  456  TYR ARG TYR VAL ALA ALA ALA LEU ALA VAL MET ARG ASN          
SEQRES  23 A  456  VAL THR GLN GLN ILE ASN GLU ARG LYS ARG ARG LEU GLU          
SEQRES  24 A  456  ASN ILE ASP LYS ILE ALA GLN TRP GLN ALA SER VAL LEU          
SEQRES  25 A  456  ASP TRP GLU GLY ASP ASP ILE LEU ASP ARG SER SER GLU          
SEQRES  26 A  456  LEU ILE TYR THR GLY GLU MET ALA TRP ILE TYR GLN PRO          
SEQRES  27 A  456  TYR GLY ARG ASN GLN GLN ARG VAL PHE PHE LEU PHE ASP          
SEQRES  28 A  456  HIS GLN MET VAL LEU CYS LYS LYS ASP LEU ILE ARG ARG          
SEQRES  29 A  456  ASP ILE LEU TYR TYR LYS GLY ARG ILE ASP MET ASP LYS          
SEQRES  30 A  456  TYR GLU VAL ILE ASP ILE GLU ASP GLY ARG ASP ASP ASP          
SEQRES  31 A  456  PHE ASN VAL SER MET LYS ASN ALA PHE LYS LEU HIS ASN          
SEQRES  32 A  456  LYS GLU THR GLU GLU VAL HIS LEU PHE PHE ALA LYS LYS          
SEQRES  33 A  456  LEU GLU GLU LYS ILE ARG TRP LEU ARG ALA PHE ARG GLU          
SEQRES  34 A  456  GLU ARG LYS MET VAL GLN GLU ASP GLU LYS ILE GLY PHE          
SEQRES  35 A  456  GLU ILE SER GLU ASN GLN LYS ARG GLN ALA ALA MET THR          
SEQRES  36 A  456  VAL                                                          
HELIX    1   1 PRO A   65  SER A   67  5                                   3    
HELIX    2   2 ARG A  107  TYR A  136  1                                  30    
HELIX    3   3 TYR A  136  ARG A  143  1                                   8    
HELIX    4   4 SER A  148  PHE A  156  1                                   9    
HELIX    5   5 ASN A  158  TYR A  177  1                                  20    
HELIX    6   6 ASP A  181  SER A  185  5                                   5    
HELIX    7   7 ILE A  187  HIS A  194  1                                   8    
HELIX    8   8 TRP A  199  ASN A  207  1                                   9    
HELIX    9   9 ASN A  207  LYS A  220  1                                  14    
HELIX   10  10 ASP A  221  GLN A  235  1                                  15    
HELIX   11  11 ALA A  241  LEU A  246  1                                   6    
HELIX   12  12 THR A  248  TYR A  266  1                                  19    
HELIX   13  13 ASP A  273  ASN A  300  1                                  28    
HELIX   14  14 ILE A  301  ALA A  309  1                                   9    
HELIX   15  15 ASP A  318  ARG A  322  5                                   5    
HELIX   16  16 LYS A  416  LYS A  439  1                                  24    
SHEET    1   A 5 GLU A  61  PHE A  64  0                                        
SHEET    2   A 5 TRP A  53  GLN A  56 -1  N  GLY A  55   O  GLY A  62           
SHEET    3   A 5 VAL A  41  VAL A  44 -1  N  LYS A  43   O  GLN A  56           
SHEET    4   A 5 SER A  19  ALA A  22 -1  N  ALA A  20   O  ILE A  42           
SHEET    5   A 5 VAL A  69  LEU A  71 -1  O  ARG A  70   N  GLU A  21           
SHEET    1   B 7 LEU A 367  ASP A 374  0                                        
SHEET    2   B 7 GLN A 353  LYS A 359 -1  N  MET A 354   O  ILE A 373           
SHEET    3   B 7 GLN A 343  PHE A 350 -1  N  PHE A 350   O  GLN A 353           
SHEET    4   B 7 LEU A 326  ILE A 335 -1  N  ILE A 327   O  LEU A 349           
SHEET    5   B 7 VAL A 409  PHE A 413 -1  O  PHE A 413   N  ALA A 333           
SHEET    6   B 7 ALA A 398  ASN A 403 -1  N  PHE A 399   O  PHE A 412           
SHEET    7   B 7 TYR A 378  ILE A 381 -1  N  ILE A 381   O  LYS A 400           
SHEET    1   C 2 GLY A 386  ARG A 387  0                                        
SHEET    2   C 2 SER A 394  MET A 395 -1  O  MET A 395   N  GLY A 386           
CISPEP   1 ASP A  390    PHE A  391          0        -0.19                     
CRYST1  217.259  217.259  217.259  90.00  90.00  90.00 I 21 3       24          
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      0.004603  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004603  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004603        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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