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Database: PDB
Entry: 4MT7
LinkDB: 4MT7
Original site: 4MT7 
HEADER    PROTEIN BINDING                         19-SEP-13   4MT7              
TITLE     CRYSTAL STRUCTURE OF COLLYBISTIN I                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 9;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 10-493;                                       
COMPND   5 SYNONYM: COLLYBISTIN, RAC/CDC42 GUANINE NUCLEOTIDE EXCHANGE FACTOR 9;
COMPND   6 ENGINEERED: 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: PTXB1                                     
KEYWDS    EXTENDED CONFORMATION, PROTEIN BINDING                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.SCHNEEBERGER,H.SCHINDELIN                                           
REVDAT   2   01-OCT-14 4MT7    1       JRNL                                     
REVDAT   1   13-AUG-14 4MT7    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.    3.50 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) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.89                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 11474                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.540                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 865                             
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 50.8984 -  6.3568    0.99     1871   135  0.1880 0.2125        
REMARK   3     2  6.3568 -  5.0471    1.00     1792   141  0.2457 0.2484        
REMARK   3     3  5.0471 -  4.4095    0.99     1742   146  0.1867 0.2183        
REMARK   3     4  4.4095 -  4.0065    0.99     1767   131  0.2425 0.2763        
REMARK   3     5  4.0065 -  3.7194    0.99     1712   159  0.2946 0.3351        
REMARK   3     6  3.7194 -  3.5002    0.99     1725   153  0.3506 0.3977        
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)     : 0.440            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.970           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 131.69                         
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 120.89                         
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      :  0.005           2917                                  
REMARK   3   ANGLE     :  0.923           3915                                  
REMARK   3   CHIRALITY :  0.072            401                                  
REMARK   3   PLANARITY :  0.003            512                                  
REMARK   3   DIHEDRAL  : 17.056           1128                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 45 through 233 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -22.5157 -18.6597  12.8240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7014 T22:   0.7301                                     
REMARK   3      T33:   0.5593 T12:   0.1668                                     
REMARK   3      T13:   0.0381 T23:   0.4281                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0402 L22:   5.6561                                     
REMARK   3      L33:   5.0792 L12:   0.0146                                     
REMARK   3      L13:  -0.7009 L23:  -2.5188                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0233 S12:   0.9860 S13:   0.9047                       
REMARK   3      S21:  -0.5207 S22:  -0.7310 S23:  -0.6567                       
REMARK   3      S31:  -0.2957 S32:   0.6011 S33:   0.3312                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 234 through 306 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -12.0627 -51.6849  -9.7989              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8435 T22:   0.6035                                     
REMARK   3      T33:   0.6365 T12:   0.1822                                     
REMARK   3      T13:   0.2117 T23:  -0.1698                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6816 L22:   1.9441                                     
REMARK   3      L33:   2.9471 L12:  -0.8335                                     
REMARK   3      L13:   0.0787 L23:  -0.0473                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5578 S12:  -0.2777 S13:  -0.5094                       
REMARK   3      S21:   0.5608 S22:  -0.1518 S23:  -0.0409                       
REMARK   3      S31:   0.5182 S32:  -0.6220 S33:   0.6309                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 307 through 381 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -10.9718 -63.4248  -1.5960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1452 T22:   1.3773                                     
REMARK   3      T33:   1.0322 T12:  -0.4028                                     
REMARK   3      T13:   0.2884 T23:   0.3284                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4005 L22:   4.9392                                     
REMARK   3      L33:   5.4125 L12:  -2.2816                                     
REMARK   3      L13:   0.3881 L23:  -2.1864                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0090 S12:  -0.8511 S13:  -1.8362                       
REMARK   3      S21:   1.0710 S22:  -0.0288 S23:   0.9659                       
REMARK   3      S31:   2.4461 S32:  -0.5688 S33:   0.5333                       
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 4MT7 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 RCSB082334.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JUL-11                          
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   : 11560                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 129.120                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.71400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.71400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
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   (%): 68.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES, 15% PEG 20000, PH 6.5,        
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.56000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       64.56000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       41.46500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       82.71500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       41.46500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       82.71500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       64.56000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       41.46500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       82.71500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       64.56000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       41.46500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       82.71500            
REMARK 290   SMTRY3   8  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: 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   -50                                                      
REMARK 465     LEU A   -49                                                      
REMARK 465     ILE A   -48                                                      
REMARK 465     THR A   -47                                                      
REMARK 465     GLY A   -46                                                      
REMARK 465     ASP A   -45                                                      
REMARK 465     SER A   -44                                                      
REMARK 465     ILE A   -43                                                      
REMARK 465     VAL A   -42                                                      
REMARK 465     SER A   -41                                                      
REMARK 465     ALA A   -40                                                      
REMARK 465     GLU A   -39                                                      
REMARK 465     ALA A   -38                                                      
REMARK 465     VAL A   -37                                                      
REMARK 465     TRP A   -36                                                      
REMARK 465     ASP A   -35                                                      
REMARK 465     HIS A   -34                                                      
REMARK 465     VAL A   -33                                                      
REMARK 465     THR A   -32                                                      
REMARK 465     MET A   -31                                                      
REMARK 465     ALA A   -30                                                      
REMARK 465     ASN A   -29                                                      
REMARK 465     ARG A   -28                                                      
REMARK 465     GLY A   -27                                                      
REMARK 465     VAL A   -26                                                      
REMARK 465     ALA A   -25                                                      
REMARK 465     PHE A   -24                                                      
REMARK 465     LYS A   -23                                                      
REMARK 465     ALA A   -22                                                      
REMARK 465     GLY A   -21                                                      
REMARK 465     ASP A   -20                                                      
REMARK 465     VAL A   -19                                                      
REMARK 465     ILE A   -18                                                      
REMARK 465     LYS A   -17                                                      
REMARK 465     VAL A   -16                                                      
REMARK 465     LEU A   -15                                                      
REMARK 465     ASP A   -14                                                      
REMARK 465     ALA A   -13                                                      
REMARK 465     SER A   -12                                                      
REMARK 465     ASN A   -11                                                      
REMARK 465     LYS A   -10                                                      
REMARK 465     ASP A    -9                                                      
REMARK 465     TRP A    -8                                                      
REMARK 465     TRP A    -7                                                      
REMARK 465     TRP A    -6                                                      
REMARK 465     GLY A    -5                                                      
REMARK 465     GLN A    -4                                                      
REMARK 465     ILE A    -3                                                      
REMARK 465     ASP A    -2                                                      
REMARK 465     ASP A    -1                                                      
REMARK 465     GLU A     0                                                      
REMARK 465     GLU A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     TRP A     3                                                      
REMARK 465     PHE A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     PHE A     8                                                      
REMARK 465     VAL A     9                                                      
REMARK 465     ARG A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     TRP A    12                                                      
REMARK 465     VAL A    13                                                      
REMARK 465     ASN A    14                                                      
REMARK 465     GLN A    15                                                      
REMARK 465     GLU A    16                                                      
REMARK 465     ASP A    17                                                      
REMARK 465     GLY A    18                                                      
REMARK 465     VAL A    19                                                      
REMARK 465     GLU A    20                                                      
REMARK 465     GLU A    21                                                      
REMARK 465     GLY A    22                                                      
REMARK 465     PRO A    23                                                      
REMARK 465     SER A    24                                                      
REMARK 465     ASP A    25                                                      
REMARK 465     VAL A    26                                                      
REMARK 465     GLN A    27                                                      
REMARK 465     ASN A    28                                                      
REMARK 465     GLY A    29                                                      
REMARK 465     HIS A    30                                                      
REMARK 465     LEU A    31                                                      
REMARK 465     ASP A    32                                                      
REMARK 465     PRO A    33                                                      
REMARK 465     ASN A    34                                                      
REMARK 465     SER A    35                                                      
REMARK 465     ASP A    36                                                      
REMARK 465     CYS A    37                                                      
REMARK 465     LEU A    38                                                      
REMARK 465     CYS A    39                                                      
REMARK 465     LEU A    40                                                      
REMARK 465     GLY A    41                                                      
REMARK 465     ARG A    42                                                      
REMARK 465     PRO A    43                                                      
REMARK 465     LEU A    44                                                      
REMARK 465     PHE A   382                                                      
REMARK 465     GLU A   383                                                      
REMARK 465     ILE A   384                                                      
REMARK 465     SER A   385                                                      
REMARK 465     GLU A   386                                                      
REMARK 465     ASN A   387                                                      
REMARK 465     GLN A   388                                                      
REMARK 465     LYS A   389                                                      
REMARK 465     ARG A   390                                                      
REMARK 465     GLN A   391                                                      
REMARK 465     ALA A   392                                                      
REMARK 465     ALA A   393                                                      
REMARK 465     MET A   394                                                      
REMARK 465     THR A   395                                                      
REMARK 465     VAL A   396                                                      
REMARK 465     ARG A   397                                                      
REMARK 465     LYS A   398                                                      
REMARK 465     ALA A   399                                                      
REMARK 465     SER A   400                                                      
REMARK 465     LYS A   401                                                      
REMARK 465     GLN A   402                                                      
REMARK 465     LYS A   403                                                      
REMARK 465     GLY A   404                                                      
REMARK 465     ARG A   405                                                      
REMARK 465     VAL A   406                                                      
REMARK 465     GLY A   407                                                      
REMARK 465     GLU A   408                                                      
REMARK 465     GLU A   409                                                      
REMARK 465     GLU A   410                                                      
REMARK 465     ASN A   411                                                      
REMARK 465     GLN A   412                                                      
REMARK 465     SER A   413                                                      
REMARK 465     LEU A   414                                                      
REMARK 465     GLU A   415                                                      
REMARK 465     LEU A   416                                                      
REMARK 465     LYS A   417                                                      
REMARK 465     ARG A   418                                                      
REMARK 465     ALA A   419                                                      
REMARK 465     CYS A   420                                                      
REMARK 465     GLU A   421                                                      
REMARK 465     VAL A   422                                                      
REMARK 465     LEU A   423                                                      
REMARK 465     GLN A   424                                                      
REMARK 465     ARG A   425                                                      
REMARK 465     LEU A   426                                                      
REMARK 465     TRP A   427                                                      
REMARK 465     SER A   428                                                      
REMARK 465     PRO A   429                                                      
REMARK 465     GLY A   430                                                      
REMARK 465     LYS A   431                                                      
REMARK 465     LYS A   432                                                      
REMARK 465     SER A   433                                                      
REMARK 465     CYS A   434                                                      
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    ASN A  46       50.99     35.50                                   
REMARK 500    ARG A  47      -48.71    169.62                                   
REMARK 500    SER A  88     -175.80    -66.61                                   
REMARK 500    ASN A  98       32.94    -90.74                                   
REMARK 500    ASN A 147       31.96    -95.31                                   
REMARK 500    LEU A 260       11.40    -68.50                                   
REMARK 500    SER A 264       49.06   -176.92                                   
REMARK 500    GLU A 265      127.27    169.10                                   
REMARK 500    ILE A 267      -71.11    -78.88                                   
REMARK 500    HIS A 292      -34.68     84.00                                   
REMARK 500    ILE A 302      -55.06   -123.32                                   
REMARK 500    PHE A 331      -87.36     22.03                                   
REMARK 500    ASN A 332       68.94     86.78                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    PHE A 331        23.6      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4MT6   RELATED DB: PDB                                   
DBREF  4MT7 A  -50   433  UNP    Q9QX73   ARHG9_RAT       10    493             
SEQADV 4MT7 CYS A  434  UNP  Q9QX73              EXPRESSION TAG                 
SEQRES   1 A  485  MET LEU ILE THR GLY ASP SER ILE VAL SER ALA GLU ALA          
SEQRES   2 A  485  VAL TRP ASP HIS VAL THR MET ALA ASN ARG GLY VAL ALA          
SEQRES   3 A  485  PHE LYS ALA GLY ASP VAL ILE LYS VAL LEU ASP ALA SER          
SEQRES   4 A  485  ASN LYS ASP TRP TRP TRP GLY GLN ILE ASP ASP GLU GLU          
SEQRES   5 A  485  GLY TRP PHE PRO ALA SER PHE VAL ARG LEU TRP VAL ASN          
SEQRES   6 A  485  GLN GLU ASP GLY VAL GLU GLU GLY PRO SER ASP VAL GLN          
SEQRES   7 A  485  ASN GLY HIS LEU ASP PRO ASN SER ASP CYS LEU CYS LEU          
SEQRES   8 A  485  GLY ARG PRO LEU GLN ASN ARG ASP GLN MET ARG ALA ASN          
SEQRES   9 A  485  VAL ILE ASN GLU ILE MET SER THR GLU ARG HIS TYR ILE          
SEQRES  10 A  485  LYS HIS LEU LYS ASP ILE CYS GLU GLY TYR LEU LYS GLN          
SEQRES  11 A  485  CYS ARG LYS ARG ARG ASP MET PHE SER ASP GLU GLN LEU          
SEQRES  12 A  485  LYS VAL ILE PHE GLY ASN ILE GLU ASP ILE TYR ARG PHE          
SEQRES  13 A  485  GLN MET GLY PHE VAL ARG ASP LEU GLU LYS GLN TYR ASN          
SEQRES  14 A  485  ASN ASP ASP PRO HIS LEU SER GLU ILE GLY PRO CYS PHE          
SEQRES  15 A  485  LEU GLU HIS GLN ASP GLY PHE TRP ILE TYR SER GLU TYR          
SEQRES  16 A  485  CYS ASN ASN HIS LEU ASP ALA CYS MET GLU LEU SER LYS          
SEQRES  17 A  485  LEU MET LYS ASP SER ARG TYR GLN HIS PHE PHE GLU ALA          
SEQRES  18 A  485  CYS ARG LEU LEU GLN GLN MET ILE ASP ILE ALA ILE ASP          
SEQRES  19 A  485  GLY PHE LEU LEU THR PRO VAL GLN LYS ILE CYS LYS TYR          
SEQRES  20 A  485  PRO LEU GLN LEU ALA GLU LEU LEU LYS TYR THR ALA GLN          
SEQRES  21 A  485  ASP HIS SER ASP TYR ARG TYR VAL ALA ALA ALA LEU ALA          
SEQRES  22 A  485  VAL MET ARG ASN VAL THR GLN GLN ILE ASN GLU ARG LYS          
SEQRES  23 A  485  ARG ARG LEU GLU ASN ILE ASP LYS ILE ALA GLN TRP GLN          
SEQRES  24 A  485  ALA SER VAL LEU ASP TRP GLU GLY ASP ASP ILE LEU ASP          
SEQRES  25 A  485  ARG SER SER GLU LEU ILE TYR THR GLY GLU MET ALA TRP          
SEQRES  26 A  485  ILE TYR GLN PRO TYR GLY ARG ASN GLN GLN ARG VAL PHE          
SEQRES  27 A  485  PHE LEU PHE ASP HIS GLN MET VAL LEU CYS LYS LYS ASP          
SEQRES  28 A  485  LEU ILE ARG ARG ASP ILE LEU TYR TYR LYS GLY ARG ILE          
SEQRES  29 A  485  ASP MET ASP LYS TYR GLU VAL ILE ASP ILE GLU ASP GLY          
SEQRES  30 A  485  ARG ASP ASP ASP PHE ASN VAL SER MET LYS ASN ALA PHE          
SEQRES  31 A  485  LYS LEU HIS ASN LYS GLU THR GLU GLU VAL HIS LEU PHE          
SEQRES  32 A  485  PHE ALA LYS LYS LEU GLU GLU LYS ILE ARG TRP LEU ARG          
SEQRES  33 A  485  ALA PHE ARG GLU GLU ARG LYS MET VAL GLN GLU ASP GLU          
SEQRES  34 A  485  LYS ILE GLY PHE GLU ILE SER GLU ASN GLN LYS ARG GLN          
SEQRES  35 A  485  ALA ALA MET THR VAL ARG LYS ALA SER LYS GLN LYS GLY          
SEQRES  36 A  485  ARG VAL GLY GLU GLU GLU ASN GLN SER LEU GLU LEU LYS          
SEQRES  37 A  485  ARG ALA CYS GLU VAL LEU GLN ARG LEU TRP SER PRO GLY          
SEQRES  38 A  485  LYS LYS SER CYS                                              
HELIX    1   1 GLN A   49  TYR A   76  1                                  28    
HELIX    2   2 TYR A   76  ARG A   83  1                                   8    
HELIX    3   3 SER A   88  GLY A   97  1                                  10    
HELIX    4   4 ASN A   98  GLN A  116  1                                  19    
HELIX    5   5 ASP A  121  SER A  125  5                                   5    
HELIX    6   6 ILE A  127  HIS A  134  1                                   8    
HELIX    7   7 ASP A  136  PHE A  138  5                                   3    
HELIX    8   8 TRP A  139  ASN A  147  1                                   9    
HELIX    9   9 ASN A  147  MET A  159  1                                  13    
HELIX   10  10 ASP A  161  GLN A  175  1                                  15    
HELIX   11  11 ALA A  181  LEU A  186  1                                   6    
HELIX   12  12 LEU A  187  TYR A  206  1                                  20    
HELIX   13  13 ASP A  213  VAL A  251  1                                  39    
HELIX   14  14 ASP A  258  ARG A  262  5                                   5    
HELIX   15  15 LYS A  356  GLY A  381  1                                  26    
SHEET    1   A 7 LEU A 307  ASP A 314  0                                        
SHEET    2   A 7 GLN A 293  LYS A 299 -1  N  LEU A 296   O  GLY A 311           
SHEET    3   A 7 GLN A 283  PHE A 290 -1  N  PHE A 288   O  VAL A 295           
SHEET    4   A 7 LEU A 266  ILE A 275 -1  N  TYR A 268   O  LEU A 289           
SHEET    5   A 7 VAL A 349  PHE A 353 -1  O  PHE A 353   N  ALA A 273           
SHEET    6   A 7 ALA A 338  ASN A 343 -1  N  PHE A 339   O  PHE A 352           
SHEET    7   A 7 TYR A 318  ASP A 322 -1  N  GLU A 319   O  HIS A 342           
SHEET    1   B 2 GLY A 326  ARG A 327  0                                        
SHEET    2   B 2 SER A 334  MET A 335 -1  O  MET A 335   N  GLY A 326           
CISPEP   1 ASP A  330    PHE A  331          0        -6.02                     
CRYST1   82.930  165.430  129.120  90.00  90.00  90.00 C 2 2 21      8          
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      0.012058  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006045  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007745        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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