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Database: PDB
Entry: 3T06
LinkDB: 3T06
Original site: 3T06 
HEADER    SIGNALING PROTEIN                       19-JUL-11   3T06              
TITLE     CRYSTAL STRUCTURE OF THE DH/PH FRAGMENT OF PDZRHOGEF WITH N-TERMINAL  
TITLE    2 REGULATORY ELEMENTS IN COMPLEX WITH HUMAN RHOA                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 11;                 
COMPND   3 CHAIN: A, E;                                                         
COMPND   4 SYNONYM: PDZ-RHOGEF;                                                 
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: TRANSFORMING PROTEIN RHOA;                                 
COMPND   8 CHAIN: B, F;                                                         
COMPND   9 SYNONYM: RHO CDNA CLONE 12, H12;                                     
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ARHGEF11, KIAA0380;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PDEST15;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: ARH12, ARHA, RHO12, RHOA;                                      
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    DH-PH RHOA COMPLEX, PDZRHOGEF, GUANINE NUCLEOTIDE EXCHANGE FACTOR,    
KEYWDS   2 RHOA, SIGNALING PROTEIN                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.BIELNICKI,U.DEREWENDA,Z.S.DEREWENDA                               
REVDAT   4   08-NOV-17 3T06    1       REMARK                                   
REVDAT   3   19-OCT-11 3T06    1       JRNL                                     
REVDAT   2   17-AUG-11 3T06    1       JRNL                                     
REVDAT   1   03-AUG-11 3T06    0                                                
JRNL        AUTH   J.A.BIELNICKI,A.V.SHKUMATOV,U.DEREWENDA,A.V.SOMLYO,          
JRNL        AUTH 2 D.I.SVERGUN,Z.S.DEREWENDA                                    
JRNL        TITL   INSIGHTS INTO THE MOLECULAR ACTIVATION MECHANISM OF THE      
JRNL        TITL 2 RHOA-SPECIFIC GUANINE NUCLEOTIDE EXCHANGE FACTOR, PDZRHOGEF. 
JRNL        REF    J.BIOL.CHEM.                  V. 286 35163 2011              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   21816819                                                     
JRNL        DOI    10.1074/JBC.M111.270918                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.84 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX DEV_818                                       
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.84                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.82                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 36871                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1849                            
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 29.8256 -  6.6555    1.00     2910   171  0.1696 0.1757        
REMARK   3     2  6.6555 -  5.2923    1.00     2902   156  0.2417 0.2608        
REMARK   3     3  5.2923 -  4.6261    1.00     2884   145  0.1679 0.2238        
REMARK   3     4  4.6261 -  4.2044    1.00     2869   158  0.1688 0.2411        
REMARK   3     5  4.2044 -  3.9037    1.00     2926   127  0.1984 0.2477        
REMARK   3     6  3.9037 -  3.6740    1.00     2870   140  0.2049 0.2654        
REMARK   3     7  3.6740 -  3.4903    1.00     2890   138  0.2231 0.2980        
REMARK   3     8  3.4903 -  3.3386    1.00     2866   159  0.2312 0.3035        
REMARK   3     9  3.3386 -  3.2102    0.99     2856   143  0.2573 0.3669        
REMARK   3    10  3.2102 -  3.0996    0.96     2754   162  0.2593 0.3260        
REMARK   3    11  3.0996 -  3.0027    0.87     2461   138  0.2809 0.3131        
REMARK   3    12  3.0027 -  2.9170    0.74     2129   117  0.2964 0.3962        
REMARK   3    13  2.9170 -  2.8400    0.60     1705    95  0.3052 0.3543        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.32                                          
REMARK   3   B_SOL              : 30.43                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.900            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.220           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 16.46500                                             
REMARK   3    B22 (A**2) : -11.40030                                            
REMARK   3    B33 (A**2) : -5.06470                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -12.35140                                            
REMARK   3    B23 (A**2) : 0.00000                                              
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           8802                                  
REMARK   3   ANGLE     :  1.265          11870                                  
REMARK   3   CHIRALITY :  0.080           1345                                  
REMARK   3   PLANARITY :  0.005           1534                                  
REMARK   3   DIHEDRAL  : 19.784           3440                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 3T06 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000066870.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
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 (220)                           
REMARK 200  OPTICS                         : ROSENBAUM-ROCK VERTICAL FOCUSING   
REMARK 200                                   MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36903                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.840                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -4.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.09700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.84                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 59.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BALBES                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1XCG                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15 M DL-MALIC ACID, 20 % W/V PEG       
REMARK 280  3350, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       59.31500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3140 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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     THR A   672                                                      
REMARK 465     PRO A   673                                                      
REMARK 465     LYS A   674                                                      
REMARK 465     MET A   675                                                      
REMARK 465     GLY A   676                                                      
REMARK 465     ARG A   677                                                      
REMARK 465     ARG A   678                                                      
REMARK 465     SER A   679                                                      
REMARK 465     ILE A   680                                                      
REMARK 465     GLU A   681                                                      
REMARK 465     SER A   682                                                      
REMARK 465     PRO A   683                                                      
REMARK 465     SER A   684                                                      
REMARK 465     LEU A   685                                                      
REMARK 465     GLY A   686                                                      
REMARK 465     PHE A   687                                                      
REMARK 465     CYS A   688                                                      
REMARK 465     THR A   689                                                      
REMARK 465     ASP A   690                                                      
REMARK 465     THR A   691                                                      
REMARK 465     LEU A   692                                                      
REMARK 465     LEU A   693                                                      
REMARK 465     PRO A   694                                                      
REMARK 465     HIS A   695                                                      
REMARK 465     LEU A   696                                                      
REMARK 465     LEU A   697                                                      
REMARK 465     GLU A   698                                                      
REMARK 465     ASP A   699                                                      
REMARK 465     ASP A   700                                                      
REMARK 465     LEU A   701                                                      
REMARK 465     GLY A   702                                                      
REMARK 465     GLN A   703                                                      
REMARK 465     LEU A   704                                                      
REMARK 465     SER A   705                                                      
REMARK 465     ASP A   706                                                      
REMARK 465     LEU A   707                                                      
REMARK 465     GLU A   708                                                      
REMARK 465     PRO A   709                                                      
REMARK 465     GLU A   710                                                      
REMARK 465     PRO A   711                                                      
REMARK 465     ASP A   712                                                      
REMARK 465     ALA A   713                                                      
REMARK 465     HIS A  1008                                                      
REMARK 465     SER A  1009                                                      
REMARK 465     LYS A  1010                                                      
REMARK 465     THR A  1011                                                      
REMARK 465     ALA A  1012                                                      
REMARK 465     VAL A  1013                                                      
REMARK 465     GLY A  1014                                                      
REMARK 465     SER A  1015                                                      
REMARK 465     SER A  1016                                                      
REMARK 465     ASP A  1017                                                      
REMARK 465     SER A  1018                                                      
REMARK 465     LYS A  1019                                                      
REMARK 465     GLN A  1020                                                      
REMARK 465     HIS A  1082                                                      
REMARK 465     HIS A  1083                                                      
REMARK 465     HIS A  1084                                                      
REMARK 465     HIS A  1085                                                      
REMARK 465     HIS A  1086                                                      
REMARK 465     HIS A  1087                                                      
REMARK 465     HIS A  1088                                                      
REMARK 465     HIS A  1089                                                      
REMARK 465     THR E   672                                                      
REMARK 465     PRO E   673                                                      
REMARK 465     LYS E   674                                                      
REMARK 465     MET E   675                                                      
REMARK 465     GLY E   676                                                      
REMARK 465     ARG E   677                                                      
REMARK 465     ARG E   678                                                      
REMARK 465     SER E   679                                                      
REMARK 465     ILE E   680                                                      
REMARK 465     GLU E   681                                                      
REMARK 465     SER E   682                                                      
REMARK 465     PRO E   683                                                      
REMARK 465     SER E   684                                                      
REMARK 465     LEU E   685                                                      
REMARK 465     GLY E   686                                                      
REMARK 465     PHE E   687                                                      
REMARK 465     CYS E   688                                                      
REMARK 465     THR E   689                                                      
REMARK 465     ASP E   690                                                      
REMARK 465     THR E   691                                                      
REMARK 465     LEU E   692                                                      
REMARK 465     LEU E   693                                                      
REMARK 465     PRO E   694                                                      
REMARK 465     HIS E   695                                                      
REMARK 465     LEU E   696                                                      
REMARK 465     LEU E   697                                                      
REMARK 465     GLU E   698                                                      
REMARK 465     ASP E   699                                                      
REMARK 465     ASP E   700                                                      
REMARK 465     LEU E   701                                                      
REMARK 465     GLY E   702                                                      
REMARK 465     GLN E   703                                                      
REMARK 465     LEU E   704                                                      
REMARK 465     SER E   705                                                      
REMARK 465     ASP E   706                                                      
REMARK 465     LEU E   707                                                      
REMARK 465     GLU E   708                                                      
REMARK 465     PRO E   709                                                      
REMARK 465     GLU E   710                                                      
REMARK 465     PRO E   711                                                      
REMARK 465     ASP E   712                                                      
REMARK 465     ALA E   713                                                      
REMARK 465     THR E  1011                                                      
REMARK 465     ALA E  1012                                                      
REMARK 465     VAL E  1013                                                      
REMARK 465     GLY E  1014                                                      
REMARK 465     SER E  1015                                                      
REMARK 465     SER E  1016                                                      
REMARK 465     ASP E  1017                                                      
REMARK 465     SER E  1018                                                      
REMARK 465     LYS E  1019                                                      
REMARK 465     GLN E  1020                                                      
REMARK 465     HIS E  1082                                                      
REMARK 465     HIS E  1083                                                      
REMARK 465     HIS E  1084                                                      
REMARK 465     HIS E  1085                                                      
REMARK 465     HIS E  1086                                                      
REMARK 465     HIS E  1087                                                      
REMARK 465     HIS E  1088                                                      
REMARK 465     HIS E  1089                                                      
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   NZ   LYS F    18     OE2  GLU F    64              2.10            
REMARK 500   O    SER E  1064     OD1  ASN E  1068              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (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,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A1053   C   -  N   -  CA  ANGL. DEV. =  15.3 DEGREES          
REMARK 500    PRO A1053   C   -  N   -  CD  ANGL. DEV. = -13.8 DEGREES          
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    THR A 719     -120.63   -101.79                                   
REMARK 500    VAL A 720      149.93    -38.08                                   
REMARK 500    LEU A 758      -71.37    -71.57                                   
REMARK 500    PHE A 760      -76.45   -114.30                                   
REMARK 500    ASN A 781       47.81   -140.02                                   
REMARK 500    GLU A 802       34.46    -75.60                                   
REMARK 500    LYS A 807     -102.56    -76.42                                   
REMARK 500    GLN A 836      -56.40    -28.13                                   
REMARK 500    ALA A 942       57.02   -105.72                                   
REMARK 500    ALA A 944       20.17    -49.91                                   
REMARK 500    ARG A 947      -79.06   -110.91                                   
REMARK 500    ALA A 948     -140.81     94.92                                   
REMARK 500    SER A 949      -62.69   -135.35                                   
REMARK 500    PRO A 951        3.11    -65.92                                   
REMARK 500    PHE A 956       43.80    -99.93                                   
REMARK 500    LEU A 959      -93.78     -5.28                                   
REMARK 500    ASP A 960       93.79     82.00                                   
REMARK 500    ASP A 979       27.95     25.77                                   
REMARK 500    THR A 981     -169.75   -102.03                                   
REMARK 500    LEU A 982      118.70   -173.32                                   
REMARK 500    GLN A 999      -87.30    -72.34                                   
REMARK 500    ASP A1000      -81.84   -129.34                                   
REMARK 500    CYS A1047       99.81    -62.34                                   
REMARK 500    PRO A1053     -149.34    -21.01                                   
REMARK 500    PRO A1054       74.91    -62.25                                   
REMARK 500    LYS B  18      -66.85    -17.35                                   
REMARK 500    GLN B  29      134.61   -173.56                                   
REMARK 500    GLU B  32      -71.73    -84.05                                   
REMARK 500    ASN B  41      118.32    -35.82                                   
REMARK 500    TYR B  66       70.07   -110.87                                   
REMARK 500    ASP B  67      -25.77    -38.07                                   
REMARK 500    SER B  88       72.14   -161.25                                   
REMARK 500    PRO B  89       -3.63    -58.71                                   
REMARK 500    ASP B 120       13.83    -53.11                                   
REMARK 500    PRO B 138      137.86    -34.51                                   
REMARK 500    THR E 719      -89.27   -104.92                                   
REMARK 500    LYS E 722      -70.30   -163.85                                   
REMARK 500    VAL E 725       -7.26    -51.96                                   
REMARK 500    PHE E 760      -85.75   -109.73                                   
REMARK 500    PHE E 779       69.66   -109.56                                   
REMARK 500    ASN E 781       31.60   -144.05                                   
REMARK 500    LYS E 807     -110.66    -93.26                                   
REMARK 500    SER E 810      -33.20    -33.53                                   
REMARK 500    ALA E 944        7.39    -57.71                                   
REMARK 500    SER E 958       68.77   -112.32                                   
REMARK 500    ASP E 960       97.20     73.55                                   
REMARK 500    THR E 962      -19.65    -40.33                                   
REMARK 500    LEU E 972      135.07   -170.33                                   
REMARK 500    ASP E 979      -36.68     85.08                                   
REMARK 500    GLN E 999      -88.03   -106.24                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      64 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3T06 A  672  1081  UNP    O15085   ARHGB_HUMAN    672   1081             
DBREF  3T06 B    3   180  UNP    P61586   RHOA_HUMAN       3    180             
DBREF  3T06 E  672  1081  UNP    O15085   ARHGB_HUMAN    672   1081             
DBREF  3T06 F    3   180  UNP    P61586   RHOA_HUMAN       3    180             
SEQADV 3T06 HIS A 1082  UNP  O15085              EXPRESSION TAG                 
SEQADV 3T06 HIS A 1083  UNP  O15085              EXPRESSION TAG                 
SEQADV 3T06 HIS A 1084  UNP  O15085              EXPRESSION TAG                 
SEQADV 3T06 HIS A 1085  UNP  O15085              EXPRESSION TAG                 
SEQADV 3T06 HIS A 1086  UNP  O15085              EXPRESSION TAG                 
SEQADV 3T06 HIS A 1087  UNP  O15085              EXPRESSION TAG                 
SEQADV 3T06 HIS A 1088  UNP  O15085              EXPRESSION TAG                 
SEQADV 3T06 HIS A 1089  UNP  O15085              EXPRESSION TAG                 
SEQADV 3T06 ASN B   25  UNP  P61586    PHE    25 ENGINEERED MUTATION            
SEQADV 3T06 HIS E 1082  UNP  O15085              EXPRESSION TAG                 
SEQADV 3T06 HIS E 1083  UNP  O15085              EXPRESSION TAG                 
SEQADV 3T06 HIS E 1084  UNP  O15085              EXPRESSION TAG                 
SEQADV 3T06 HIS E 1085  UNP  O15085              EXPRESSION TAG                 
SEQADV 3T06 HIS E 1086  UNP  O15085              EXPRESSION TAG                 
SEQADV 3T06 HIS E 1087  UNP  O15085              EXPRESSION TAG                 
SEQADV 3T06 HIS E 1088  UNP  O15085              EXPRESSION TAG                 
SEQADV 3T06 HIS E 1089  UNP  O15085              EXPRESSION TAG                 
SEQADV 3T06 ASN F   25  UNP  P61586    PHE    25 ENGINEERED MUTATION            
SEQRES   1 A  418  THR PRO LYS MET GLY ARG ARG SER ILE GLU SER PRO SER          
SEQRES   2 A  418  LEU GLY PHE CYS THR ASP THR LEU LEU PRO HIS LEU LEU          
SEQRES   3 A  418  GLU ASP ASP LEU GLY GLN LEU SER ASP LEU GLU PRO GLU          
SEQRES   4 A  418  PRO ASP ALA GLN ASN TRP GLN HIS THR VAL GLY LYS ASP          
SEQRES   5 A  418  VAL VAL ALA GLY LEU THR GLN ARG GLU ILE ASP ARG GLN          
SEQRES   6 A  418  GLU VAL ILE ASN GLU LEU PHE VAL THR GLU ALA SER HIS          
SEQRES   7 A  418  LEU ARG THR LEU ARG VAL LEU ASP LEU ILE PHE TYR GLN          
SEQRES   8 A  418  ARG MET LYS LYS GLU ASN LEU MET PRO ARG GLU GLU LEU          
SEQRES   9 A  418  ALA ARG LEU PHE PRO ASN LEU PRO GLU LEU ILE GLU ILE          
SEQRES  10 A  418  HIS ASN SER TRP CYS GLU ALA MET LYS LYS LEU ARG GLU          
SEQRES  11 A  418  GLU GLY PRO ILE ILE LYS GLU ILE SER ASP LEU MET LEU          
SEQRES  12 A  418  ALA ARG PHE ASP GLY PRO ALA ARG GLU GLU LEU GLN GLN          
SEQRES  13 A  418  VAL ALA ALA GLN PHE CYS SER TYR GLN SER ILE ALA LEU          
SEQRES  14 A  418  GLU LEU ILE LYS THR LYS GLN ARG LYS GLU SER ARG PHE          
SEQRES  15 A  418  GLN LEU PHE MET GLN GLU ALA GLU SER HIS PRO GLN CYS          
SEQRES  16 A  418  ARG ARG LEU GLN LEU ARG ASP LEU ILE ILE SER GLU MET          
SEQRES  17 A  418  GLN ARG LEU THR LYS TYR PRO LEU LEU LEU GLU SER ILE          
SEQRES  18 A  418  ILE LYS HIS THR GLU GLY GLY THR SER GLU HIS GLU LYS          
SEQRES  19 A  418  LEU CYS ARG ALA ARG ASP GLN CYS ARG GLU ILE LEU LYS          
SEQRES  20 A  418  TYR VAL ASN GLU ALA VAL LYS GLN THR GLU ASN ARG HIS          
SEQRES  21 A  418  ARG LEU GLU GLY TYR GLN LYS ARG LEU ASP ALA THR ALA          
SEQRES  22 A  418  LEU GLU ARG ALA SER ASN PRO LEU ALA ALA GLU PHE LYS          
SEQRES  23 A  418  SER LEU ASP LEU THR THR ARG LYS MET ILE HIS GLU GLY          
SEQRES  24 A  418  PRO LEU THR TRP ARG ILE SER LYS ASP LYS THR LEU ASP          
SEQRES  25 A  418  LEU HIS VAL LEU LEU LEU GLU ASP LEU LEU VAL LEU LEU          
SEQRES  26 A  418  GLN LYS GLN ASP GLU LYS LEU LEU LEU LYS CYS HIS SER          
SEQRES  27 A  418  LYS THR ALA VAL GLY SER SER ASP SER LYS GLN THR PHE          
SEQRES  28 A  418  SER PRO VAL LEU LYS LEU ASN ALA VAL LEU ILE ARG SER          
SEQRES  29 A  418  VAL ALA THR ASP LYS ARG ALA PHE PHE ILE ILE CYS THR          
SEQRES  30 A  418  SER LYS LEU GLY PRO PRO GLN ILE TYR GLU LEU VAL ALA          
SEQRES  31 A  418  LEU THR SER SER ASP LYS ASN THR TRP MET GLU LEU LEU          
SEQRES  32 A  418  GLU GLU ALA VAL ARG ASN ALA HIS HIS HIS HIS HIS HIS          
SEQRES  33 A  418  HIS HIS                                                      
SEQRES   1 B  178  ALA ILE ARG LYS LYS LEU VAL ILE VAL GLY ASP GLY ALA          
SEQRES   2 B  178  CYS GLY LYS THR CYS LEU LEU ILE VAL ASN SER LYS ASP          
SEQRES   3 B  178  GLN PHE PRO GLU VAL TYR VAL PRO THR VAL PHE GLU ASN          
SEQRES   4 B  178  TYR VAL ALA ASP ILE GLU VAL ASP GLY LYS GLN VAL GLU          
SEQRES   5 B  178  LEU ALA LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 B  178  ARG LEU ARG PRO LEU SER TYR PRO ASP THR ASP VAL ILE          
SEQRES   7 B  178  LEU MET CYS PHE SER ILE ASP SER PRO ASP SER LEU GLU          
SEQRES   8 B  178  ASN ILE PRO GLU LYS TRP THR PRO GLU VAL LYS HIS PHE          
SEQRES   9 B  178  CYS PRO ASN VAL PRO ILE ILE LEU VAL GLY ASN LYS LYS          
SEQRES  10 B  178  ASP LEU ARG ASN ASP GLU HIS THR ARG ARG GLU LEU ALA          
SEQRES  11 B  178  LYS MET LYS GLN GLU PRO VAL LYS PRO GLU GLU GLY ARG          
SEQRES  12 B  178  ASP MET ALA ASN ARG ILE GLY ALA PHE GLY TYR MET GLU          
SEQRES  13 B  178  CYS SER ALA LYS THR LYS ASP GLY VAL ARG GLU VAL PHE          
SEQRES  14 B  178  GLU MET ALA THR ARG ALA ALA LEU GLN                          
SEQRES   1 E  418  THR PRO LYS MET GLY ARG ARG SER ILE GLU SER PRO SER          
SEQRES   2 E  418  LEU GLY PHE CYS THR ASP THR LEU LEU PRO HIS LEU LEU          
SEQRES   3 E  418  GLU ASP ASP LEU GLY GLN LEU SER ASP LEU GLU PRO GLU          
SEQRES   4 E  418  PRO ASP ALA GLN ASN TRP GLN HIS THR VAL GLY LYS ASP          
SEQRES   5 E  418  VAL VAL ALA GLY LEU THR GLN ARG GLU ILE ASP ARG GLN          
SEQRES   6 E  418  GLU VAL ILE ASN GLU LEU PHE VAL THR GLU ALA SER HIS          
SEQRES   7 E  418  LEU ARG THR LEU ARG VAL LEU ASP LEU ILE PHE TYR GLN          
SEQRES   8 E  418  ARG MET LYS LYS GLU ASN LEU MET PRO ARG GLU GLU LEU          
SEQRES   9 E  418  ALA ARG LEU PHE PRO ASN LEU PRO GLU LEU ILE GLU ILE          
SEQRES  10 E  418  HIS ASN SER TRP CYS GLU ALA MET LYS LYS LEU ARG GLU          
SEQRES  11 E  418  GLU GLY PRO ILE ILE LYS GLU ILE SER ASP LEU MET LEU          
SEQRES  12 E  418  ALA ARG PHE ASP GLY PRO ALA ARG GLU GLU LEU GLN GLN          
SEQRES  13 E  418  VAL ALA ALA GLN PHE CYS SER TYR GLN SER ILE ALA LEU          
SEQRES  14 E  418  GLU LEU ILE LYS THR LYS GLN ARG LYS GLU SER ARG PHE          
SEQRES  15 E  418  GLN LEU PHE MET GLN GLU ALA GLU SER HIS PRO GLN CYS          
SEQRES  16 E  418  ARG ARG LEU GLN LEU ARG ASP LEU ILE ILE SER GLU MET          
SEQRES  17 E  418  GLN ARG LEU THR LYS TYR PRO LEU LEU LEU GLU SER ILE          
SEQRES  18 E  418  ILE LYS HIS THR GLU GLY GLY THR SER GLU HIS GLU LYS          
SEQRES  19 E  418  LEU CYS ARG ALA ARG ASP GLN CYS ARG GLU ILE LEU LYS          
SEQRES  20 E  418  TYR VAL ASN GLU ALA VAL LYS GLN THR GLU ASN ARG HIS          
SEQRES  21 E  418  ARG LEU GLU GLY TYR GLN LYS ARG LEU ASP ALA THR ALA          
SEQRES  22 E  418  LEU GLU ARG ALA SER ASN PRO LEU ALA ALA GLU PHE LYS          
SEQRES  23 E  418  SER LEU ASP LEU THR THR ARG LYS MET ILE HIS GLU GLY          
SEQRES  24 E  418  PRO LEU THR TRP ARG ILE SER LYS ASP LYS THR LEU ASP          
SEQRES  25 E  418  LEU HIS VAL LEU LEU LEU GLU ASP LEU LEU VAL LEU LEU          
SEQRES  26 E  418  GLN LYS GLN ASP GLU LYS LEU LEU LEU LYS CYS HIS SER          
SEQRES  27 E  418  LYS THR ALA VAL GLY SER SER ASP SER LYS GLN THR PHE          
SEQRES  28 E  418  SER PRO VAL LEU LYS LEU ASN ALA VAL LEU ILE ARG SER          
SEQRES  29 E  418  VAL ALA THR ASP LYS ARG ALA PHE PHE ILE ILE CYS THR          
SEQRES  30 E  418  SER LYS LEU GLY PRO PRO GLN ILE TYR GLU LEU VAL ALA          
SEQRES  31 E  418  LEU THR SER SER ASP LYS ASN THR TRP MET GLU LEU LEU          
SEQRES  32 E  418  GLU GLU ALA VAL ARG ASN ALA HIS HIS HIS HIS HIS HIS          
SEQRES  33 E  418  HIS HIS                                                      
SEQRES   1 F  178  ALA ILE ARG LYS LYS LEU VAL ILE VAL GLY ASP GLY ALA          
SEQRES   2 F  178  CYS GLY LYS THR CYS LEU LEU ILE VAL ASN SER LYS ASP          
SEQRES   3 F  178  GLN PHE PRO GLU VAL TYR VAL PRO THR VAL PHE GLU ASN          
SEQRES   4 F  178  TYR VAL ALA ASP ILE GLU VAL ASP GLY LYS GLN VAL GLU          
SEQRES   5 F  178  LEU ALA LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 F  178  ARG LEU ARG PRO LEU SER TYR PRO ASP THR ASP VAL ILE          
SEQRES   7 F  178  LEU MET CYS PHE SER ILE ASP SER PRO ASP SER LEU GLU          
SEQRES   8 F  178  ASN ILE PRO GLU LYS TRP THR PRO GLU VAL LYS HIS PHE          
SEQRES   9 F  178  CYS PRO ASN VAL PRO ILE ILE LEU VAL GLY ASN LYS LYS          
SEQRES  10 F  178  ASP LEU ARG ASN ASP GLU HIS THR ARG ARG GLU LEU ALA          
SEQRES  11 F  178  LYS MET LYS GLN GLU PRO VAL LYS PRO GLU GLU GLY ARG          
SEQRES  12 F  178  ASP MET ALA ASN ARG ILE GLY ALA PHE GLY TYR MET GLU          
SEQRES  13 F  178  CYS SER ALA LYS THR LYS ASP GLY VAL ARG GLU VAL PHE          
SEQRES  14 F  178  GLU MET ALA THR ARG ALA ALA LEU GLN                          
HELIX    1   1 THR A  729  PHE A  760  1                                  32    
HELIX    2   2 PHE A  760  GLU A  767  1                                   8    
HELIX    3   3 PRO A  771  PHE A  779  1                                   9    
HELIX    4   4 ASN A  781  ARG A  800  1                                  20    
HELIX    5   5 GLU A  801  GLY A  803  5                                   3    
HELIX    6   6 ILE A  809  ASP A  818  1                                  10    
HELIX    7   7 GLY A  819  TYR A  835  1                                  17    
HELIX    8   8 TYR A  835  GLU A  850  1                                  16    
HELIX    9   9 GLU A  850  GLU A  861  1                                  12    
HELIX   10  10 HIS A  863  ARG A  867  5                                   5    
HELIX   11  11 GLN A  870  ILE A  875  1                                   6    
HELIX   12  12 ILE A  876  HIS A  895  1                                  20    
HELIX   13  13 THR A  900  ARG A  939  1                                  40    
HELIX   14  14 ASP A  960  ARG A  964  5                                   5    
HELIX   15  15 THR A 1063  ASN A 1080  1                                  18    
HELIX   16  16 GLY B   17  ASP B   28  1                                  12    
HELIX   17  17 LEU B   69  TYR B   74  5                                   6    
HELIX   18  18 SER B   88  LYS B   98  1                                  11    
HELIX   19  19 LYS B   98  CYS B  107  1                                  10    
HELIX   20  20 LYS B  118  ARG B  122  5                                   5    
HELIX   21  21 ASP B  124  MET B  134  1                                  11    
HELIX   22  22 LYS B  140  ILE B  151  1                                  12    
HELIX   23  23 GLY B  166  GLN B  180  1                                  15    
HELIX   24  24 ASP E  723  LEU E  728  5                                   6    
HELIX   25  25 GLN E  730  PHE E  760  1                                  31    
HELIX   26  26 PHE E  760  GLU E  767  1                                   8    
HELIX   27  27 PRO E  771  PHE E  779  1                                   9    
HELIX   28  28 ASN E  781  GLU E  802  1                                  22    
HELIX   29  29 ILE E  809  ASP E  818  1                                  10    
HELIX   30  30 GLY E  819  TYR E  835  1                                  17    
HELIX   31  31 TYR E  835  GLU E  850  1                                  16    
HELIX   32  32 GLU E  850  SER E  862  1                                  13    
HELIX   33  33 HIS E  863  ARG E  867  5                                   5    
HELIX   34  34 GLN E  870  ILE E  875  1                                   6    
HELIX   35  35 ILE E  876  HIS E  895  1                                  20    
HELIX   36  36 THR E  900  GLN E  937  1                                  38    
HELIX   37  37 LYS E  938  LEU E  940  5                                   3    
HELIX   38  38 ASN E  950  GLU E  955  1                                   6    
HELIX   39  39 ASP E  960  ARG E  964  5                                   5    
HELIX   40  40 ASN E 1029  VAL E 1031  5                                   3    
HELIX   41  41 THR E 1063  ASN E 1080  1                                  18    
HELIX   42  42 GLY F   17  ASP F   28  1                                  12    
HELIX   43  43 LEU F   69  SER F   73  5                                   5    
HELIX   44  44 SER F   88  LYS F   98  1                                  11    
HELIX   45  45 LYS F   98  CYS F  107  1                                  10    
HELIX   46  46 LYS F  118  ARG F  122  5                                   5    
HELIX   47  47 ASP F  124  LYS F  133  1                                  10    
HELIX   48  48 LYS F  140  ILE F  151  1                                  12    
HELIX   49  49 GLY F  166  GLN F  180  1                                  15    
SHEET    1   A 4 LEU A 940  ASP A 941  0                                        
SHEET    2   A 4 LEU A1003  LEU A1004  1  O  LEU A1003   N  ASP A 941           
SHEET    3   A 4 LEU A 992  LYS A 998 -1  N  GLN A 997   O  LEU A1004           
SHEET    4   A 4 VAL A1025  LYS A1027 -1  O  LEU A1026   N  LEU A 993           
SHEET    1   B 8 LEU A 940  ASP A 941  0                                        
SHEET    2   B 8 LEU A1003  LEU A1004  1  O  LEU A1003   N  ASP A 941           
SHEET    3   B 8 LEU A 992  LYS A 998 -1  N  GLN A 997   O  LEU A1004           
SHEET    4   B 8 ASP A 983  LEU A 989 -1  N  LEU A 989   O  LEU A 992           
SHEET    5   B 8 MET A 966  TRP A 974 -1  N  LEU A 972   O  LEU A 984           
SHEET    6   B 8 ILE A1056  VAL A1060 -1  O  VAL A1060   N  THR A 973           
SHEET    7   B 8 ALA A1042  CYS A1047 -1  N  PHE A1043   O  LEU A1059           
SHEET    8   B 8 VAL A1031  SER A1035 -1  N  LEU A1032   O  ILE A1046           
SHEET    1   C 6 TYR B  42  VAL B  48  0                                        
SHEET    2   C 6 LYS B  51  ASP B  59 -1  O  LEU B  57   N  TYR B  42           
SHEET    3   C 6 ILE B   4  GLY B  12  1  N  LEU B   8   O  ALA B  56           
SHEET    4   C 6 VAL B  79  SER B  85  1  O  CYS B  83   N  VAL B  11           
SHEET    5   C 6 ILE B 112  ASN B 117  1  O  ILE B 113   N  ILE B  80           
SHEET    6   C 6 GLY B 155  GLU B 158  1  O  MET B 157   N  LEU B 114           
SHEET    1   D 3 LEU E1003  LEU E1004  0                                        
SHEET    2   D 3 LEU E 992  LYS E 998 -1  N  GLN E 997   O  LEU E1004           
SHEET    3   D 3 VAL E1025  LYS E1027 -1  O  LEU E1026   N  LEU E 993           
SHEET    1   E 7 LEU E1003  LEU E1004  0                                        
SHEET    2   E 7 LEU E 992  LYS E 998 -1  N  GLN E 997   O  LEU E1004           
SHEET    3   E 7 THR E 981  LEU E 989 -1  N  HIS E 985   O  LEU E 996           
SHEET    4   E 7 MET E 966  ARG E 975 -1  N  HIS E 968   O  LEU E 988           
SHEET    5   E 7 GLN E1055  VAL E1060 -1  O  VAL E1060   N  THR E 973           
SHEET    6   E 7 ALA E1042  CYS E1047 -1  N  ILE E1045   O  TYR E1057           
SHEET    7   E 7 ILE E1033  SER E1035 -1  N  ARG E1034   O  PHE E1044           
SHEET    1   F 6 TYR F  42  VAL F  48  0                                        
SHEET    2   F 6 LYS F  51  ASP F  59 -1  O  LEU F  55   N  ALA F  44           
SHEET    3   F 6 ILE F   4  GLY F  12  1  N  LYS F   6   O  ALA F  56           
SHEET    4   F 6 VAL F  79  SER F  85  1  O  CYS F  83   N  VAL F  11           
SHEET    5   F 6 ILE F 112  ASN F 117  1  O  ILE F 113   N  MET F  82           
SHEET    6   F 6 GLY F 155  GLU F 158  1  O  MET F 157   N  GLY F 116           
CRYST1   84.370  118.630   92.443  90.00 113.61  90.00 P 1 21 1      4          
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      0.011853  0.000000  0.005181        0.00000                         
SCALE2      0.000000  0.008430  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011806        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system