GenomeNet

Database: PDB
Entry: 2W2X
LinkDB: 2W2X
Original site: 2W2X 
HEADER    SIGNALING PROTEIN/HYDROLASE             04-NOV-08   2W2X              
TITLE     COMPLEX OF RAC2 AND PLCG2 SPPH DOMAIN                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 2;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 2-179;                                            
COMPND   5 SYNONYM: P21-RAC2, SMALL G PROTEIN, GX, RAC2;                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE  
COMPND  10 GAMMA-2;                                                             
COMPND  11 CHAIN: C;                                                            
COMPND  12 FRAGMENT: SPLIT PH DOMAIN, RESIDUES 471-514,841-913;                 
COMPND  13 SYNONYM: PHOSPHOINOSITIDE PHOSPHOLIPASE C, PHOSPHOLIPASE C-GAMMA-2,  
COMPND  14 PLCG2;                                                               
COMPND  15 EC: 3.1.4.11;                                                        
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 3;                                                           
COMPND  18 MOLECULE: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE  
COMPND  19 GAMMA-2;                                                             
COMPND  20 CHAIN: D;                                                            
COMPND  21 FRAGMENT: SPLIT PH DOMAIN, RESIDUES 471-514,841-913;                 
COMPND  22 SYNONYM: PHOSPHOINOSITIDE PHOSPHOLIPASE C, PHOSPHOLIPASE C-GAMMA-2,  
COMPND  23 PLCG2;                                                               
COMPND  24 EC: 3.1.4.11;                                                        
COMPND  25 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  15 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_COMMON: HUMAN;                                              
SOURCE  20 ORGANISM_TAXID: 9606;                                                
SOURCE  21 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  22 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  23 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  24 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    HYDROLASE, PHOSPHOLIPASE C, PHOSPHOINOSITIDES, RHO GTPASES, RAC, SH2  
KEYWDS   2 DOMAIN, SH3 DOMAIN, SIGNALING PROTEIN/HYDROLASE, SIGNALING PROTEIN-  
KEYWDS   3 HYDROLASE COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    O.OPALEYE,T.D.BUNNEY,S.M.ROE,L.H.PEARL                                
REVDAT   2   15-MAY-19 2W2X    1       REMARK                                   
REVDAT   1   05-MAY-09 2W2X    0                                                
JRNL        AUTH   T.D.BUNNEY,O.OPALEYE,S.M.ROE,P.VATTER,R.W.BAXENDALE,         
JRNL        AUTH 2 C.WALLISER,K.L.EVERETT,M.B.JOSEPHS,C.CHRISTOW,               
JRNL        AUTH 3 F.RODRIGUES-LIMA,P.GIERSCHIK,L.H.PEARL,M.KATAN               
JRNL        TITL   STRUCTURAL INSIGHTS INTO FORMATION OF AN ACTIVE SIGNALING    
JRNL        TITL 2 COMPLEX BETWEEN RAC AND PHOSPHOLIPASE C GAMMA 2.             
JRNL        REF    MOL.CELL                      V.  34   223 2009              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   19394299                                                     
JRNL        DOI    10.1016/J.MOLCEL.2009.02.023                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 69.41                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.100                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 83.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 54867                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.237                           
REMARK   3   R VALUE            (WORKING SET) : 0.234                           
REMARK   3   FREE R VALUE                     : 0.294                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2769                            
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 69.4378 -  6.2418    0.79     2495   115  0.2007 0.2259        
REMARK   3     2  6.2418 -  4.9548    0.93     2870   155  0.1769 0.2155        
REMARK   3     3  4.9548 -  4.3286    0.94     2933   172  0.1490 0.1988        
REMARK   3     4  4.3286 -  3.9328    0.95     2958   184  0.1807 0.2320        
REMARK   3     5  3.9328 -  3.6510    0.95     2990   132  0.1997 0.2610        
REMARK   3     6  3.6510 -  3.4357    0.95     2959   175  0.2234 0.2721        
REMARK   3     7  3.4357 -  3.2637    0.95     2979   138  0.2104 0.2763        
REMARK   3     8  3.2637 -  3.1216    0.95     2964   142  0.2467 0.3590        
REMARK   3     9  3.1216 -  3.0014    0.95     2968   172  0.2581 0.4033        
REMARK   3    10  3.0014 -  2.8978    0.95     2964   184  0.2821 0.3368        
REMARK   3    11  2.8978 -  2.8072    0.95     2959   145  0.2836 0.3793        
REMARK   3    12  2.8072 -  2.7270    0.95     2972   166  0.3340 0.4360        
REMARK   3    13  2.7270 -  2.6552    0.94     2961   142  0.3580 0.4819        
REMARK   3    14  2.6552 -  2.5904    0.94     2931   164  0.3499 0.4272        
REMARK   3    15  2.5904 -  2.5315    0.81     2538   113  0.3536 0.3990        
REMARK   3    16  2.5315 -  2.4776    0.69     2152   119  0.3529 0.3856        
REMARK   3    17  2.4776 -  2.4281    0.61     1920    97  0.3269 0.4097        
REMARK   3    18  2.4281 -  2.3823    0.55     1737    88  0.3364 0.4157        
REMARK   3    19  2.3823 -  2.3397    0.50     1546    86  0.3444 0.3749        
REMARK   3    20  2.3397 -  2.3000    0.42     1302    80  0.3438 0.3855        
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              : 0.37                                          
REMARK   3   B_SOL              : 66.45                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.470            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 40.090           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 64.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -9.38640                                             
REMARK   3    B22 (A**2) : 17.09540                                             
REMARK   3    B33 (A**2) : -7.70900                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.44910                                             
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           4382                                  
REMARK   3   ANGLE     :  1.406           5959                                  
REMARK   3   CHIRALITY :  0.095            697                                  
REMARK   3   PLANARITY :  0.007            741                                  
REMARK   3   DIHEDRAL  : 18.736           1484                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  33.6763   3.0504   6.2808              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0995 T22:   0.0229                                     
REMARK   3      T33:   0.1360 T12:   0.1057                                     
REMARK   3      T13:  -0.0356 T23:   0.0219                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7351 L22:   1.9770                                     
REMARK   3      L33:   2.4159 L12:  -0.5386                                     
REMARK   3      L13:  -0.9639 L23:   0.6783                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0293 S12:   0.0329 S13:  -0.0192                       
REMARK   3      S21:  -0.0886 S22:  -0.1099 S23:  -0.1734                       
REMARK   3      S31:  -0.2566 S32:  -0.3147 S33:   0.0091                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  64.0650  -0.3980 -17.4463              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2149 T22:   0.4908                                     
REMARK   3      T33:   0.2763 T12:  -0.0947                                     
REMARK   3      T13:   0.0636 T23:  -0.0215                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.0269 L22:   2.2420                                     
REMARK   3      L33:   0.0014 L12:   3.7428                                     
REMARK   3      L13:   3.7264 L23:   0.7768                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2621 S12:  -0.8905 S13:  -0.1271                       
REMARK   3      S21:   0.0797 S22:  -0.2451 S23:  -0.1018                       
REMARK   3      S31:   0.1002 S32:  -0.1747 S33:  -0.0571                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN C                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  33.0977   0.7523 -27.1112              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2539 T22:   0.4737                                     
REMARK   3      T33:   0.1742 T12:   0.0340                                     
REMARK   3      T13:   0.0047 T23:   0.0666                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2548 L22:   1.8893                                     
REMARK   3      L33:   0.5513 L12:  -0.6442                                     
REMARK   3      L13:   0.0968 L23:  -0.5723                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1091 S12:   0.3737 S13:   0.0120                       
REMARK   3      S21:  -0.0325 S22:   0.0726 S23:  -0.0298                       
REMARK   3      S31:   0.0677 S32:  -0.4746 S33:  -0.0363                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN D                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   4.6977  10.5452  19.7044              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2392 T22:   0.5561                                     
REMARK   3      T33:   0.2213 T12:   0.1149                                     
REMARK   3      T13:   0.0050 T23:   0.0415                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7581 L22:   1.0953                                     
REMARK   3      L33:   0.7050 L12:  -0.4579                                     
REMARK   3      L13:  -0.8607 L23:  -0.0996                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1504 S12:   0.8537 S13:   0.2409                       
REMARK   3      S21:  -0.0797 S22:  -0.1322 S23:   0.0852                       
REMARK   3      S31:   0.0356 S32:  -0.3568 S33:  -0.0715                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 2                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:20 OR RESSEQ 23:44    
REMARK   3                          OR RESSEQ 51:176 )                          
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 2:20 OR RESSEQ 23:44    
REMARK   3                          OR RESSEQ 51:176 )                          
REMARK   3     ATOM PAIRS NUMBER  : 1213                                        
REMARK   3     RMSD               : 0.094                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN C AND (RESSEQ 7:41 OR RESSEQ 51:85    
REMARK   3                          OR RESSEQ 88:96 OR RESSEQ 98:113 )          
REMARK   3     SELECTION          : CHAIN D AND (RESSEQ 7:41 OR RESSEQ 51:85    
REMARK   3                          OR RESSEQ 88:96 OR RESSEQ 98:113 )          
REMARK   3     ATOM PAIRS NUMBER  : 733                                         
REMARK   3     RMSD               : 0.110                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2W2X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-NOV-08.                  
REMARK 100 THE DEPOSITION ID IS D_1290038035.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-FEB-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29046                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 70.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.9                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 52.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
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: PDB ENTRY 1UPQ AND 2OVJ                              
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: RAC2(2-177)GTPGS-PLCSPPH(Y495F)          
REMARK 280  COMPLEX WAS CRYSTALLIZED USING A PROTEIN CONCENTRATION OF 25 MG/    
REMARK 280  ML WITH PRECIPITANT (18% PEG1500, 10% GLYCEROL, 100MM SPG PH9)      
REMARK 280  BY MICRO-SEEDING AT A CONSTANT TEMPERATURE OF 4C, PH 7,             
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -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        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       65.78500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.22950            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       65.78500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       42.22950            
REMARK 290   SMTRY3   4  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: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 1070 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.8 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
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: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 1220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.8 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLY 12 TO VAL                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, GLY 12 TO VAL                         
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -5                                                      
REMARK 465     GLY A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     CYS A   178                                                      
REMARK 465     PRO A   179                                                      
REMARK 465     GLY B    -5                                                      
REMARK 465     GLY B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     MET B    45                                                      
REMARK 465     VAL B    46                                                      
REMARK 465     ASP B    47                                                      
REMARK 465     SER B    48                                                      
REMARK 465     LYS B    49                                                      
REMARK 465     PRO B    50                                                      
REMARK 465     CYS B   178                                                      
REMARK 465     PRO B   179                                                      
REMARK 465     GLY C    -5                                                      
REMARK 465     GLY C    -4                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     SER C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     GLY C     0                                                      
REMARK 465     SER C     1                                                      
REMARK 465     LYS C     2                                                      
REMARK 465     LYS C     3                                                      
REMARK 465     ASP C     4                                                      
REMARK 465     GLU C     5                                                      
REMARK 465     HIS C     6                                                      
REMARK 465     ASP C   116                                                      
REMARK 465     THR C   117                                                      
REMARK 465     LYS C   118                                                      
REMARK 465     GLY D    -5                                                      
REMARK 465     GLY D    -4                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     SER D    -2                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     GLY D     0                                                      
REMARK 465     SER D     1                                                      
REMARK 465     LYS D     2                                                      
REMARK 465     LYS D     3                                                      
REMARK 465     ASP D     4                                                      
REMARK 465     GLU D     5                                                      
REMARK 465     HIS D     6                                                      
REMARK 465     GLN D    86                                                      
REMARK 465     GLY D    87                                                      
REMARK 465     LYS D   114                                                      
REMARK 465     ILE D   115                                                      
REMARK 465     ASP D   116                                                      
REMARK 465     THR D   117                                                      
REMARK 465     LYS D   118                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A   1    OG                                                  
REMARK 470     GLU A  31    CG   CD   OE1  OE2                                  
REMARK 470     SER A  48    OG                                                  
REMARK 470     LYS A  49    CG   CD   CE   NZ                                   
REMARK 470     ARG A  66    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 123    CG   CD   CE   NZ                                   
REMARK 470     ASP A 124    CG   OD1  OD2                                       
REMARK 470     GLU A 127    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 128    CG   CD   CE   NZ                                   
REMARK 470     LYS A 130    CG   CD   CE   NZ                                   
REMARK 470     LYS A 132    CG   CD   CE   NZ                                   
REMARK 470     LYS A 133    CG   CD   CE   NZ                                   
REMARK 470     LYS A 147    CG   CD   CE   NZ                                   
REMARK 470     LYS A 166    CG   CD   CE   NZ                                   
REMARK 470     ASP A 170    CG   OD1  OD2                                       
REMARK 470     GLN B   2    CG   CD   OE1  NE2                                  
REMARK 470     ILE B  21    CG1  CG2  CD1                                       
REMARK 470     SER B  22    OG                                                  
REMARK 470     VAL B  44    CG1  CG2                                            
REMARK 470     ARG B  66    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  91    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  94    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  96    CG   CD   CE   NZ                                   
REMARK 470     LYS B 116    CG   CD   CE   NZ                                   
REMARK 470     LYS B 123    CG   CD   CE   NZ                                   
REMARK 470     GLU B 127    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 128    CG   CD   CE   NZ                                   
REMARK 470     LYS B 130    CG   CD   CE   NZ                                   
REMARK 470     GLU B 131    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 132    CG   CD   CE   NZ                                   
REMARK 470     LYS B 133    CG   CD   CE   NZ                                   
REMARK 470     LYS B 147    CG   CD   CE   NZ                                   
REMARK 470     ARG B 163    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 166    CG   CD   CE   NZ                                   
REMARK 470     ASP B 170    CG   OD1  OD2                                       
REMARK 470     GLU B 171    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 177    CG   CD1  CD2                                       
REMARK 470     LYS C   7    CG   CD   CE   NZ                                   
REMARK 470     LYS C  21    CG   CD   CE   NZ                                   
REMARK 470     SER C  35    OG                                                  
REMARK 470     GLU C  41    CG   CD   OE1  OE2                                  
REMARK 470     GLN C  42    CG   CD   OE1  NE2                                  
REMARK 470     THR C  43    OG1  CG2                                            
REMARK 470     GLU C  45    CG   CD   OE1  OE2                                  
REMARK 470     GLN C  74    CG   CD   OE1  NE2                                  
REMARK 470     GLU C  82    CG   CD   OE1  OE2                                  
REMARK 470     SER C 107    OG                                                  
REMARK 470     GLU C 110    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 114    CG   CD   CE   NZ                                   
REMARK 470     LYS D   7    CG   CD   CE   NZ                                   
REMARK 470     LYS D  21    CG   CD   CE   NZ                                   
REMARK 470     ASP D  31    CG   OD1  OD2                                       
REMARK 470     LYS D  33    CG   CD   CE   NZ                                   
REMARK 470     GLU D  45    CG   CD   OE1  OE2                                  
REMARK 470     LEU D  50    CG   CD1  CD2                                       
REMARK 470     GLN D  85    CG   CD   OE1  NE2                                  
REMARK 470     ASP D  88    CG   OD1  OD2                                       
REMARK 470     SER D 107    OG                                                  
REMARK 470     GLU D 110    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR A  32   C     TYR A  32   O       1.374                       
REMARK 500    VAL A  46   CA    VAL A  46   CB      1.337                       
REMARK 500    VAL A  46   C     VAL A  46   O       1.587                       
REMARK 500    SER A  48   C     SER A  48   O       2.453                       
REMARK 500    ASN A  52   C     ASN A  52   O       2.073                       
REMARK 500    SER A  83   CA    SER A  83   CB      2.397                       
REMARK 500    SER A  83   C     SER A  83   O       1.422                       
REMARK 500    SER A  86   CA    SER A  86   CB      1.643                       
REMARK 500    SER A  86   C     SER A  86   O       1.231                       
REMARK 500    ASP A 124   C     ASP A 124   O       2.107                       
REMARK 500    LYS A 130   CA    LYS A 130   CB      1.668                       
REMARK 500    LYS A 147   C     LYS A 147   O       1.170                       
REMARK 500    ASP A 170   C     ASP A 170   O       0.973                       
REMARK 500    THR B  25   C     THR B  25   O       1.339                       
REMARK 500    THR B  35   C     THR B  35   O       2.160                       
REMARK 500    VAL B  44   C     VAL B  44   O       3.024                       
REMARK 500    VAL B  51   C     VAL B  51   O       2.550                       
REMARK 500    ASP B 170   C     ASP B 170   O       1.044                       
REMARK 500    LYS C  33   C     LYS C  33   O       0.719                       
REMARK 500    SER C  35   C     SER C  35   O       1.420                       
REMARK 500    GLU C  41   C     GLU C  41   O       2.139                       
REMARK 500    THR C  43   C     THR C  43   O       1.280                       
REMARK 500    SER C  52   CA    SER C  52   CB      1.625                       
REMARK 500    ARG C  55   C     ARG C  55   O       2.000                       
REMARK 500    GLN C  74   C     GLN C  74   O       1.487                       
REMARK 500    GLU C  82   C     GLU C  82   O       0.814                       
REMARK 500    GLU C 103   CA    GLU C 103   CB      1.634                       
REMARK 500    SER C 107   C     SER C 107   O       1.182                       
REMARK 500    ASP D  31   C     ASP D  31   O       1.269                       
REMARK 500    ARG D  55   C     ARG D  55   O       2.085                       
REMARK 500    GLN D  74   C     GLN D  74   O       1.580                       
REMARK 500    ASP D  88   C     ASP D  88   O       1.107                       
REMARK 500    LYS D  97   CA    LYS D  97   CB      1.654                       
REMARK 500    SER D 107   C     SER D 107   O       1.152                       
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    VAL A  46   CA  -  CB  -  CG1 ANGL. DEV. = -18.4 DEGREES          
REMARK 500    SER A  48   CA  -  C   -  O   ANGL. DEV. =  14.2 DEGREES          
REMARK 500    SER A  83   N   -  CA  -  CB  ANGL. DEV. =  11.5 DEGREES          
REMARK 500    SER A  83   CA  -  CB  -  OG  ANGL. DEV. = -92.2 DEGREES          
REMARK 500    SER A  83   CA  -  C   -  O   ANGL. DEV. =  40.8 DEGREES          
REMARK 500    SER A  86   CB  -  CA  -  C   ANGL. DEV. = -19.3 DEGREES          
REMARK 500    SER A  86   N   -  CA  -  CB  ANGL. DEV. =  44.9 DEGREES          
REMARK 500    SER A  86   CA  -  CB  -  OG  ANGL. DEV. = -55.9 DEGREES          
REMARK 500    SER A  86   CA  -  C   -  O   ANGL. DEV. =  17.8 DEGREES          
REMARK 500    ARG A 102   CD  -  NE  -  CZ  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    ARG A 102   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    ARG A 102   NE  -  CZ  -  NH2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    LYS A 130   CB  -  CA  -  C   ANGL. DEV. = -18.3 DEGREES          
REMARK 500    LYS A 147   CA  -  C   -  O   ANGL. DEV. =  40.2 DEGREES          
REMARK 500    ASP A 170   CA  -  C   -  O   ANGL. DEV. =  14.2 DEGREES          
REMARK 500    ARG A 174   CD  -  NE  -  CZ  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ARG A 174   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ARG A 174   NE  -  CZ  -  NH2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    THR B  25   CA  -  C   -  O   ANGL. DEV. = -38.6 DEGREES          
REMARK 500    VAL B  44   CA  -  C   -  O   ANGL. DEV. = -66.1 DEGREES          
REMARK 500    VAL B  51   CA  -  C   -  O   ANGL. DEV. = -66.2 DEGREES          
REMARK 500    ARG B 102   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG B 102   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG B 174   NE  -  CZ  -  NH1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG B 174   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG C  24   CD  -  NE  -  CZ  ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ARG C  24   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ARG C  24   NE  -  CZ  -  NH2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    GLU C  41   CA  -  C   -  O   ANGL. DEV. =  19.9 DEGREES          
REMARK 500    SER C  52   CB  -  CA  -  C   ANGL. DEV. =  38.5 DEGREES          
REMARK 500    SER C  52   N   -  CA  -  CB  ANGL. DEV. = -13.3 DEGREES          
REMARK 500    SER C  52   CA  -  CB  -  OG  ANGL. DEV. = -54.7 DEGREES          
REMARK 500    ARG C  55   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG C  55   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    GLN C  74   CA  -  C   -  O   ANGL. DEV. =  15.4 DEGREES          
REMARK 500    GLU C 103   CB  -  CA  -  C   ANGL. DEV. =  13.1 DEGREES          
REMARK 500    GLU C 103   CA  -  CB  -  CG  ANGL. DEV. = -37.8 DEGREES          
REMARK 500    SER C 107   CA  -  C   -  O   ANGL. DEV. = -15.2 DEGREES          
REMARK 500    ARG D  24   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG D  24   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ARG D  55   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ARG D  55   NE  -  CZ  -  NH2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    GLN D  74   CA  -  C   -  O   ANGL. DEV. =  15.0 DEGREES          
REMARK 500    ASP D  88   CA  -  C   -  O   ANGL. DEV. =  42.6 DEGREES          
REMARK 500    LYS D  97   N   -  CA  -  CB  ANGL. DEV. = -23.9 DEGREES          
REMARK 500    SER D 107   CA  -  C   -  O   ANGL. DEV. = -14.8 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    GLN A   2      109.82     67.43                                   
REMARK 500    ASN A  26       21.01     43.79                                   
REMARK 500    GLU A  31      -90.15     13.68                                   
REMARK 500    VAL A  36      -68.24    -97.11                                   
REMARK 500    GLN A  74       -2.85     76.18                                   
REMARK 500    VAL A 176      -62.23    -98.77                                   
REMARK 500    ALA B  13       17.32     55.53                                   
REMARK 500    GLU B  31     -121.45     56.23                                   
REMARK 500    GLN B  74       -4.01     76.76                                   
REMARK 500    SER B  86       87.35   -151.22                                   
REMARK 500    LYS B 116       32.07     70.83                                   
REMARK 500    LYS B 153      149.87   -174.47                                   
REMARK 500    GLN B 162        7.41     81.83                                   
REMARK 500    VAL B 176      -60.13    -99.57                                   
REMARK 500    ASP C  31     -103.03     46.78                                   
REMARK 500    ASP C  47      100.47     27.39                                   
REMARK 500    LYS C  72      134.94   -170.04                                   
REMARK 500    LYS C 114       70.98    163.59                                   
REMARK 500    GLU D  46      113.52    -17.80                                   
REMARK 500    LEU D  50     -134.40     -5.12                                   
REMARK 500    LYS D  72      136.42   -172.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY A   30     GLU A   31                  117.58                    
REMARK 500 GLU A   31     TYR A   32                 -108.87                    
REMARK 500 GLY B   30     GLU B   31                   66.09                    
REMARK 500 GLU B   31     TYR B   32                  -52.56                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1179  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  35   OG1                                                    
REMARK 620 2 THR A  17   OG1  80.2                                              
REMARK 620 3 GSP A1178   O2G  71.1 123.4                                        
REMARK 620 4 GSP A1178   O2B 144.3  81.6  94.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1179  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B  35   OG1                                                    
REMARK 620 2 GSP B1178   O2G  76.0                                              
REMARK 620 3 GSP B1178   O1B 136.4  84.1                                        
REMARK 620 4 THR B  17   OG1  73.8 120.7  84.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSP A 1178                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSP B 1178                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1179                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1179                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2W2V   RELATED DB: PDB                                   
REMARK 900 RAC2 (G12V) IN COMPLEX WITH GTPGS                                    
REMARK 900 RELATED ID: 2W2W   RELATED DB: PDB                                   
REMARK 900 PLCG2 SPLIT PLECKSTRIN HOMOLOGY (PH) DOMAIN                          
REMARK 900 RELATED ID: 2W2T   RELATED DB: PDB                                   
REMARK 900 RAC2 (G12V) IN COMPLEX WITH GDP                                      
REMARK 900 RELATED ID: 1DS6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A RAC-RHOGDI COMPLEX                            
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THERE IS A LEADING LINKER SEQUENCE GGGSGGS (NOT SEEN IN              
REMARK 999 STRUCTURE) AND G12V MUTATION                                         
REMARK 999 THERE IS A LEADING LINKER SEQUENCE GGGSGGS (NOT SEEN IN              
REMARK 999 STRUCTURE) AND TWO SH2 DOMAINS EXCISED FROM SEQUENCE AND             
REMARK 999 CHAIN REJOINED.                                                      
DBREF  2W2X A   -5     1  PDB    2W2X     2W2X            -5      1             
DBREF  2W2X A    2   179  UNP    P15153   RAC2_HUMAN       2    179             
DBREF  2W2X B   -5     1  PDB    2W2X     2W2X            -5      1             
DBREF  2W2X B    2   179  UNP    P15153   RAC2_HUMAN       2    179             
DBREF  2W2X C   -5     1  PDB    2W2X     2W2X            -5      1             
DBREF  2W2X C    2    45  UNP    P16885   PLCG2_HUMAN    471    514             
DBREF  2W2X C   46   118  UNP    P16885   PLCG2_HUMAN    841    913             
DBREF  2W2X D   -5     1  PDB    2W2X     2W2X            -5      1             
DBREF  2W2X D    2    45  UNP    P16885   PLCG2_HUMAN    471    514             
DBREF  2W2X D   46   118  UNP    P16885   PLCG2_HUMAN    841    913             
SEQADV 2W2X VAL A   12  UNP  P15153    GLY    12 ENGINEERED MUTATION            
SEQADV 2W2X VAL B   12  UNP  P15153    GLY    12 ENGINEERED MUTATION            
SEQADV 2W2X PHE C   26  UNP  P16885    TYR   495 CONFLICT                       
SEQADV 2W2X ASP C   88  UNP  P16885    TYR   883 CONFLICT                       
SEQADV 2W2X PHE D   26  UNP  P16885    TYR   495 CONFLICT                       
SEQADV 2W2X ASP D   88  UNP  P16885    TYR   883 CONFLICT                       
SEQADV 2W2X LYS D   97  UNP  P16885    ARG   892 CONFLICT                       
SEQRES   1 A  185  GLY GLY GLY SER GLY GLY SER GLN ALA ILE LYS CYS VAL          
SEQRES   2 A  185  VAL VAL GLY ASP VAL ALA VAL GLY LYS THR CYS LEU LEU          
SEQRES   3 A  185  ILE SER TYR THR THR ASN ALA PHE PRO GLY GLU TYR ILE          
SEQRES   4 A  185  PRO THR VAL PHE ASP ASN TYR SER ALA ASN VAL MET VAL          
SEQRES   5 A  185  ASP SER LYS PRO VAL ASN LEU GLY LEU TRP ASP THR ALA          
SEQRES   6 A  185  GLY GLN GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR          
SEQRES   7 A  185  PRO GLN THR ASP VAL PHE LEU ILE CYS PHE SER LEU VAL          
SEQRES   8 A  185  SER PRO ALA SER TYR GLU ASN VAL ARG ALA LYS TRP PHE          
SEQRES   9 A  185  PRO GLU VAL ARG HIS HIS CYS PRO SER THR PRO ILE ILE          
SEQRES  10 A  185  LEU VAL GLY THR LYS LEU ASP LEU ARG ASP ASP LYS ASP          
SEQRES  11 A  185  THR ILE GLU LYS LEU LYS GLU LYS LYS LEU ALA PRO ILE          
SEQRES  12 A  185  THR TYR PRO GLN GLY LEU ALA LEU ALA LYS GLU ILE ASP          
SEQRES  13 A  185  SER VAL LYS TYR LEU GLU CYS SER ALA LEU THR GLN ARG          
SEQRES  14 A  185  GLY LEU LYS THR VAL PHE ASP GLU ALA ILE ARG ALA VAL          
SEQRES  15 A  185  LEU CYS PRO                                                  
SEQRES   1 B  185  GLY GLY GLY SER GLY GLY SER GLN ALA ILE LYS CYS VAL          
SEQRES   2 B  185  VAL VAL GLY ASP VAL ALA VAL GLY LYS THR CYS LEU LEU          
SEQRES   3 B  185  ILE SER TYR THR THR ASN ALA PHE PRO GLY GLU TYR ILE          
SEQRES   4 B  185  PRO THR VAL PHE ASP ASN TYR SER ALA ASN VAL MET VAL          
SEQRES   5 B  185  ASP SER LYS PRO VAL ASN LEU GLY LEU TRP ASP THR ALA          
SEQRES   6 B  185  GLY GLN GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR          
SEQRES   7 B  185  PRO GLN THR ASP VAL PHE LEU ILE CYS PHE SER LEU VAL          
SEQRES   8 B  185  SER PRO ALA SER TYR GLU ASN VAL ARG ALA LYS TRP PHE          
SEQRES   9 B  185  PRO GLU VAL ARG HIS HIS CYS PRO SER THR PRO ILE ILE          
SEQRES  10 B  185  LEU VAL GLY THR LYS LEU ASP LEU ARG ASP ASP LYS ASP          
SEQRES  11 B  185  THR ILE GLU LYS LEU LYS GLU LYS LYS LEU ALA PRO ILE          
SEQRES  12 B  185  THR TYR PRO GLN GLY LEU ALA LEU ALA LYS GLU ILE ASP          
SEQRES  13 B  185  SER VAL LYS TYR LEU GLU CYS SER ALA LEU THR GLN ARG          
SEQRES  14 B  185  GLY LEU LYS THR VAL PHE ASP GLU ALA ILE ARG ALA VAL          
SEQRES  15 B  185  LEU CYS PRO                                                  
SEQRES   1 C  124  GLY GLY GLY SER GLY GLY SER LYS LYS ASP GLU HIS LYS          
SEQRES   2 C  124  GLN GLN GLY GLU LEU TYR MET TRP ASP SER ILE ASP GLN          
SEQRES   3 C  124  LYS TRP THR ARG HIS PHE CYS ALA ILE ALA ASP ALA LYS          
SEQRES   4 C  124  LEU SER PHE SER ASP ASP ILE GLU GLN THR MET GLU GLU          
SEQRES   5 C  124  ASP ASN PRO LEU GLY SER LEU CYS ARG GLY ILE LEU ASP          
SEQRES   6 C  124  LEU ASN THR TYR ASN VAL VAL LYS ALA PRO GLN GLY LYS          
SEQRES   7 C  124  ASN GLN LYS SER PHE VAL PHE ILE LEU GLU PRO LYS GLN          
SEQRES   8 C  124  GLN GLY ASP PRO PRO VAL GLU PHE ALA THR ASP ARG VAL          
SEQRES   9 C  124  GLU GLU LEU PHE GLU TRP PHE GLN SER ILE ARG GLU ILE          
SEQRES  10 C  124  THR TRP LYS ILE ASP THR LYS                                  
SEQRES   1 D  124  GLY GLY GLY SER GLY GLY SER LYS LYS ASP GLU HIS LYS          
SEQRES   2 D  124  GLN GLN GLY GLU LEU TYR MET TRP ASP SER ILE ASP GLN          
SEQRES   3 D  124  LYS TRP THR ARG HIS PHE CYS ALA ILE ALA ASP ALA LYS          
SEQRES   4 D  124  LEU SER PHE SER ASP ASP ILE GLU GLN THR MET GLU GLU          
SEQRES   5 D  124  ASP ASN PRO LEU GLY SER LEU CYS ARG GLY ILE LEU ASP          
SEQRES   6 D  124  LEU ASN THR TYR ASN VAL VAL LYS ALA PRO GLN GLY LYS          
SEQRES   7 D  124  ASN GLN LYS SER PHE VAL PHE ILE LEU GLU PRO LYS GLN          
SEQRES   8 D  124  GLN GLY ASP PRO PRO VAL GLU PHE ALA THR ASP LYS VAL          
SEQRES   9 D  124  GLU GLU LEU PHE GLU TRP PHE GLN SER ILE ARG GLU ILE          
SEQRES  10 D  124  THR TRP LYS ILE ASP THR LYS                                  
HET    GSP  A1178      32                                                       
HET     MG  A1179       1                                                       
HET    GSP  B1178      32                                                       
HET     MG  B1179       1                                                       
HETNAM     GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE                       
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   5  GSP    2(C10 H16 N5 O13 P3 S)                                       
FORMUL   6   MG    2(MG 2+)                                                     
FORMUL   9  HOH   *37(H2 O)                                                     
HELIX    1   1 GLY A   15  ASN A   26  1                                  12    
HELIX    2   2 GLN A   61  ARG A   66  5                                   6    
HELIX    3   3 LEU A   67  TYR A   72  5                                   6    
HELIX    4   4 SER A   86  LYS A   96  1                                  11    
HELIX    5   5 LYS A   96  CYS A  105  1                                  10    
HELIX    6   6 LYS A  116  ARG A  120  5                                   5    
HELIX    7   7 ASP A  122  GLU A  131  1                                  10    
HELIX    8   8 THR A  138  ASP A  150  1                                  13    
HELIX    9   9 GLY A  164  ASP A  170  1                                   7    
HELIX   10  10 GLY B   15  THR B   25  1                                  11    
HELIX   11  11 GLN B   61  ARG B   66  5                                   6    
HELIX   12  12 LEU B   67  TYR B   72  5                                   6    
HELIX   13  13 SER B   86  LYS B   96  1                                  11    
HELIX   14  14 LYS B   96  CYS B  105  1                                  10    
HELIX   15  15 LEU B  117  ARG B  120  5                                   4    
HELIX   16  16 ASP B  122  GLU B  131  1                                  10    
HELIX   17  17 THR B  138  ASP B  150  1                                  13    
HELIX   18  18 GLY B  164  ASP B  170  1                                   7    
HELIX   19  19 ARG C   97  TRP C  113  1                                  17    
HELIX   20  20 ILE D   40  GLU D   46  1                                   7    
HELIX   21  21 VAL D   98  TRP D  113  1                                  16    
SHEET    1  AA 6 PHE A  37  MET A  45  0                                        
SHEET    2  AA 6 PRO A  50  THR A  58 -1  O  VAL A  51   N  VAL A  44           
SHEET    3  AA 6 LYS A   5  GLY A  10  1  O  CYS A   6   N  TRP A  56           
SHEET    4  AA 6 VAL A  77  SER A  83  1  O  VAL A  77   N  VAL A   7           
SHEET    5  AA 6 ILE A 110  THR A 115  1  O  ILE A 111   N  ILE A  80           
SHEET    6  AA 6 LYS A 153  GLU A 156  1  O  LYS A 153   N  LEU A 112           
SHEET    1  BA 6 PHE B  37  ALA B  42  0                                        
SHEET    2  BA 6 LEU B  53  THR B  58 -1  O  LEU B  53   N  ALA B  42           
SHEET    3  BA 6 ILE B   4  GLY B  10  1  O  ILE B   4   N  GLY B  54           
SHEET    4  BA 6 VAL B  77  SER B  83  1  O  VAL B  77   N  VAL B   7           
SHEET    5  BA 6 ILE B 110  THR B 115  1  O  ILE B 111   N  ILE B  80           
SHEET    6  BA 6 LYS B 153  CYS B 157  1  O  LYS B 153   N  LEU B 112           
SHEET    1  CA 7 GLY C  56  ASP C  59  0                                        
SHEET    2  CA 7 LYS C  33  PHE C  36 -1  O  LEU C  34   N  LEU C  58           
SHEET    3  CA 7 LYS C  21  ALA C  30 -1  O  ALA C  28   N  SER C  35           
SHEET    4  CA 7 GLN C   9  ASP C  16 -1  O  GLY C  10   N  CYS C  27           
SHEET    5  CA 7 VAL C  91  THR C  95 -1  O  GLU C  92   N  TRP C  15           
SHEET    6  CA 7 PHE C  77  PRO C  83 -1  O  PHE C  77   N  THR C  95           
SHEET    7  CA 7 TYR C  63  LYS C  67 -1  O  ASN C  64   N  GLU C  82           
SHEET    1  DA 7 GLY D  56  ASP D  59  0                                        
SHEET    2  DA 7 LYS D  33  ASP D  39 -1  O  LEU D  34   N  LEU D  58           
SHEET    3  DA 7 LYS D  21  ALA D  30 -1  O  PHE D  26   N  SER D  37           
SHEET    4  DA 7 GLN D   9  ASP D  16 -1  O  GLY D  10   N  CYS D  27           
SHEET    5  DA 7 VAL D  91  THR D  95 -1  O  GLU D  92   N  TRP D  15           
SHEET    6  DA 7 PHE D  77  PRO D  83 -1  O  PHE D  77   N  THR D  95           
SHEET    7  DA 7 TYR D  63  LYS D  67 -1  O  ASN D  64   N  GLU D  82           
LINK        MG    MG A1179                 OG1 THR A  35     1555   1555  2.31  
LINK        MG    MG A1179                 OG1 THR A  17     1555   1555  2.20  
LINK        MG    MG A1179                 O2G GSP A1178     1555   1555  2.33  
LINK        MG    MG A1179                 O2B GSP A1178     1555   1555  2.45  
LINK        MG    MG B1179                 OG1 THR B  35     1555   1555  2.56  
LINK        MG    MG B1179                 O2G GSP B1178     1555   1555  2.41  
LINK        MG    MG B1179                 O1B GSP B1178     1555   1555  2.65  
LINK        MG    MG B1179                 OG1 THR B  17     1555   1555  2.25  
CISPEP   1 LYS C  114    ILE C  115          0        -6.30                     
SITE     1 AC1 18 ASP A  11  ALA A  13  VAL A  14  GLY A  15                    
SITE     2 AC1 18 LYS A  16  THR A  17  CYS A  18  PHE A  28                    
SITE     3 AC1 18 TYR A  32  PRO A  34  THR A  35  GLY A  60                    
SITE     4 AC1 18 LYS A 116  ASP A 118  LEU A 119  ALA A 159                    
SITE     5 AC1 18 LEU A 160   MG A1179                                          
SITE     1 AC2 17 ASP B  11  ALA B  13  VAL B  14  GLY B  15                    
SITE     2 AC2 17 LYS B  16  THR B  17  CYS B  18  PHE B  28                    
SITE     3 AC2 17 TYR B  32  THR B  35  GLY B  60  ASP B 118                    
SITE     4 AC2 17 LEU B 119  SER B 158  ALA B 159  LEU B 160                    
SITE     5 AC2 17  MG B1179                                                     
SITE     1 AC3  4 THR A  17  THR A  35  ASP A  57  GSP A1178                    
SITE     1 AC4  4 THR B  17  THR B  35  ASP B  57  GSP B1178                    
CRYST1  131.570   84.459   74.196  90.00 112.21  90.00 C 1 2 1       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      0.007601  0.000000  0.003103        0.00000                         
SCALE2      0.000000  0.011840  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014558        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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