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Database: PDB
Entry: 2FJU
LinkDB: 2FJU
Original site: 2FJU 
HEADER    SIGNALING PROTEIN,APOPTOSIS/HYDROLASE   03-JAN-06   2FJU              
TITLE     ACTIVATED RAC1 BOUND TO ITS EFFECTOR PHOSPHOLIPASE C BETA 2           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1;                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 1-189;                                            
COMPND   5 SYNONYM: P21-RAC1; RAS-LIKE PROTEIN TC25;                            
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: 1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE                    
COMPND   9 PHOSPHODIESTERASE BETA 2;                                            
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: RESIDUES 1-799;                                            
COMPND  12 SYNONYM: PHOSPHOINOSITIDE PHOSPHOLIPASE C; PHOSPHOLIPASE C-          
COMPND  13 BETA-2; PLC-BETA-2;                                                  
COMPND  14 EC: 3.1.4.11;                                                        
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: RAC1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: PLCB2;                                                         
SOURCE  14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  15 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: SF21;                                      
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PVL1392                                   
KEYWDS    PROTEIN-PROTEIN COMPLEX, SIGNALING PROTEIN,                           
KEYWDS   2 APOPTOSIS/HYDROLASE COMPLEX                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.R.JEZYK,J.T.SNYDER,T.K.HARDEN,J.SONDEK                              
REVDAT   3   24-FEB-09 2FJU    1       VERSN                                    
REVDAT   2   13-FEB-07 2FJU    1       JRNL                                     
REVDAT   1   21-NOV-06 2FJU    0                                                
JRNL        AUTH   M.R.JEZYK,J.T.SNYDER,S.GERSHBERG,D.K.WORTHYLAKE,             
JRNL        AUTH 2 T.K.HARDEN,J.SONDEK                                          
JRNL        TITL   CRYSTAL STRUCTURE OF RAC1 BOUND TO ITS EFFECTOR              
JRNL        TITL 2 PHOSPHOLIPASE C-BETA2.                                       
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  13  1135 2006              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   17115053                                                     
JRNL        DOI    10.1038/NSMB1175                                             
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 93710                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4701                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6994                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 486                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.55                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2FJU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB035962.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-APR-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.009                              
REMARK 200  MONOCHROMATOR                  : SI 220                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 93710                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: MIR, MAD, MR                 
REMARK 200 SOFTWARE USED: SHELX, MLPHARE, DM                                    
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.83                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 3350, PH 8.5, VAPOR               
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       62.54867            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       31.27433            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       31.27433            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       62.54867            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
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 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     SER A   178                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     ASN B     5                                                      
REMARK 465     PRO B     6                                                      
REMARK 465     VAL B     7                                                      
REMARK 465     LEU B     8                                                      
REMARK 465     LEU B     9                                                      
REMARK 465     PRO B    10                                                      
REMARK 465     TYR B   228                                                      
REMARK 465     HIS B   229                                                      
REMARK 465     ALA B   230                                                      
REMARK 465     LYS B   231                                                      
REMARK 465     ALA B   232                                                      
REMARK 465     LYS B   233                                                      
REMARK 465     PRO B   234                                                      
REMARK 465     SER B   252                                                      
REMARK 465     ARG B   253                                                      
REMARK 465     LEU B   254                                                      
REMARK 465     ASN B   255                                                      
REMARK 465     SER B   256                                                      
REMARK 465     LEU B   257                                                      
REMARK 465     LEU B   258                                                      
REMARK 465     PHE B   259                                                      
REMARK 465     PRO B   260                                                      
REMARK 465     PRO B   261                                                      
REMARK 465     ALA B   262                                                      
REMARK 465     ARG B   263                                                      
REMARK 465     PRO B   264                                                      
REMARK 465     ASP B   265                                                      
REMARK 465     GLN B   266                                                      
REMARK 465     VAL B   267                                                      
REMARK 465     GLY B   278                                                      
REMARK 465     ILE B   279                                                      
REMARK 465     ASN B   280                                                      
REMARK 465     ALA B   281                                                      
REMARK 465     GLN B   282                                                      
REMARK 465     ARG B   283                                                      
REMARK 465     ASN B   465                                                      
REMARK 465     GLN B   466                                                      
REMARK 465     PHE B   467                                                      
REMARK 465     SER B   468                                                      
REMARK 465     GLY B   469                                                      
REMARK 465     PRO B   470                                                      
REMARK 465     THR B   471                                                      
REMARK 465     SER B   472                                                      
REMARK 465     SER B   473                                                      
REMARK 465     SER B   474                                                      
REMARK 465     LYS B   475                                                      
REMARK 465     ASP B   476                                                      
REMARK 465     THR B   477                                                      
REMARK 465     GLY B   478                                                      
REMARK 465     GLY B   479                                                      
REMARK 465     GLU B   480                                                      
REMARK 465     ALA B   481                                                      
REMARK 465     GLU B   482                                                      
REMARK 465     GLY B   483                                                      
REMARK 465     SER B   484                                                      
REMARK 465     SER B   485                                                      
REMARK 465     PRO B   486                                                      
REMARK 465     PRO B   487                                                      
REMARK 465     SER B   488                                                      
REMARK 465     ALA B   489                                                      
REMARK 465     PRO B   490                                                      
REMARK 465     ALA B   491                                                      
REMARK 465     VAL B   492                                                      
REMARK 465     TRP B   493                                                      
REMARK 465     ALA B   494                                                      
REMARK 465     GLY B   495                                                      
REMARK 465     GLU B   496                                                      
REMARK 465     GLU B   497                                                      
REMARK 465     GLY B   498                                                      
REMARK 465     THR B   499                                                      
REMARK 465     GLU B   500                                                      
REMARK 465     LEU B   501                                                      
REMARK 465     GLU B   502                                                      
REMARK 465     GLU B   503                                                      
REMARK 465     GLU B   504                                                      
REMARK 465     GLU B   505                                                      
REMARK 465     VAL B   506                                                      
REMARK 465     GLU B   507                                                      
REMARK 465     GLU B   508                                                      
REMARK 465     GLU B   509                                                      
REMARK 465     GLU B   510                                                      
REMARK 465     GLU B   511                                                      
REMARK 465     ASP B   661                                                      
REMARK 465     LYS B   662                                                      
REMARK 465     GLN B   663                                                      
REMARK 465     PHE B   664                                                      
REMARK 465     ASN B   665                                                      
REMARK 465     PRO B   666                                                      
REMARK 465     PHE B   667                                                      
REMARK 465     SER B   668                                                      
REMARK 465     VAL B   669                                                      
REMARK 465     ASP B   670                                                      
REMARK 465     ARG B   671                                                      
REMARK 465     ILE B   672                                                      
REMARK 465     ASP B   673                                                      
REMARK 465     VAL B   674                                                      
REMARK 465     VAL B   675                                                      
REMARK 465     VAL B   676                                                      
REMARK 465     ALA B   677                                                      
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 B 277    OG                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLY B   193     N    ASN B   195              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    PRO B 191   C     LYS B 192   N       0.381                       
REMARK 500    ASP B 196   C     ALA B 197   N       0.145                       
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 B 191   CA  -  C   -  N   ANGL. DEV. = -13.9 DEGREES          
REMARK 500    PRO B 191   O   -  C   -  N   ANGL. DEV. =  10.9 DEGREES          
REMARK 500    LYS B 192   O   -  C   -  N   ANGL. DEV. = -34.2 DEGREES          
REMARK 500    GLY B 193   C   -  N   -  CA  ANGL. DEV. = -19.5 DEGREES          
REMARK 500    GLY B 193   O   -  C   -  N   ANGL. DEV. = -18.8 DEGREES          
REMARK 500    ASN B 195   O   -  C   -  N   ANGL. DEV. = -21.0 DEGREES          
REMARK 500    ASP B 196   C   -  N   -  CA  ANGL. DEV. =  17.9 DEGREES          
REMARK 500    GLY B 334   C   -  N   -  CA  ANGL. DEV. =  40.1 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    VAL A  36      -60.72   -102.49                                   
REMARK 500    PHE A  37      145.87   -171.08                                   
REMARK 500    ALA A  42      128.21   -171.80                                   
REMARK 500    LYS A  96      -66.38   -124.84                                   
REMARK 500    GLU B  29     -141.87   -120.56                                   
REMARK 500    LYS B  54       -0.82     87.33                                   
REMARK 500    ASP B 106     -169.86   -161.06                                   
REMARK 500    LYS B 192       69.78   -103.97                                   
REMARK 500    ASN B 300       68.97   -112.64                                   
REMARK 500    ASN B 328       54.93     32.84                                   
REMARK 500    ALA B 333     -123.27   -125.05                                   
REMARK 500    THR B 377     -159.06   -130.19                                   
REMARK 500    SER B 413      112.42   -160.86                                   
REMARK 500    ASP B 528      -94.28   -119.91                                   
REMARK 500    ASN B 547      -72.64   -140.25                                   
REMARK 500    ALA B 584       53.83   -146.15                                   
REMARK 500    PHE B 689       53.91     38.06                                   
REMARK 500    ASN B 726       55.47   -147.98                                   
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 GLU B   29     THR B   30                  146.58                    
REMARK 500 ALA B  333     GLY B  334                  123.71                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    LYS B 192        -37.01                                           
REMARK 500    GLY B 193         27.51                                           
REMARK 500    ASN B 195        -32.26                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B1466        DISTANCE =  5.85 ANGSTROMS                       
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 A 179  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GSP A2466   O2B                                                    
REMARK 620 2 HOH A1010   O    56.0                                              
REMARK 620 3 THR A  17   OG1  70.6  55.3                                        
REMARK 620 4 THR A  35   OG1 110.4  54.5  68.5                                  
REMARK 620 5 GSP A2466   O2G  73.0  54.8 110.1  71.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B1000  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 359   OD2                                                    
REMARK 620 2 ASP B 359   OD1  49.6                                              
REMARK 620 3 ASN B 328   OD1  79.4  91.2                                        
REMARK 620 4 GLU B 357   OE2 134.1  86.3  91.2                                  
REMARK 620 5 GLU B 408   OE1  94.6  85.4 173.9  93.5                            
REMARK 620 6 HOH B1136   O   143.9 165.8  88.6  79.5  96.0                      
REMARK 620 7 HOH B1073   O    69.0 117.0  90.0 156.6  87.1  77.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 179                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1000                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSP A 2466                
DBREF  2FJU A    1   177  UNP    P63000   RAC1_HUMAN       1    177             
DBREF  2FJU B    1   799  UNP    Q00722   PLCB2_HUMAN      1    799             
SEQADV 2FJU SER A  178  UNP  P63000              INSERTION                      
SEQRES   1 A  178  MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA          
SEQRES   2 A  178  VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN          
SEQRES   3 A  178  ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN          
SEQRES   4 A  178  TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN          
SEQRES   5 A  178  LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 A  178  ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE          
SEQRES   7 A  178  LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU          
SEQRES   8 A  178  ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS          
SEQRES   9 A  178  CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU          
SEQRES  10 A  178  ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS          
SEQRES  11 A  178  GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU          
SEQRES  12 A  178  ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU          
SEQRES  13 A  178  CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE          
SEQRES  14 A  178  ASP GLU ALA ILE ARG ALA VAL LEU SER                          
SEQRES   1 B  799  MET SER LEU LEU ASN PRO VAL LEU LEU PRO PRO LYS VAL          
SEQRES   2 B  799  LYS ALA TYR LEU SER GLN GLY GLU ARG PHE ILE LYS TRP          
SEQRES   3 B  799  ASP ASP GLU THR THR VAL ALA SER PRO VAL ILE LEU ARG          
SEQRES   4 B  799  VAL ASP PRO LYS GLY TYR TYR LEU TYR TRP THR TYR GLN          
SEQRES   5 B  799  SER LYS GLU MET GLU PHE LEU ASP ILE THR SER ILE ARG          
SEQRES   6 B  799  ASP THR ARG PHE GLY LYS PHE ALA LYS MET PRO LYS SER          
SEQRES   7 B  799  GLN LYS LEU ARG ASP VAL PHE ASN MET ASP PHE PRO ASP          
SEQRES   8 B  799  ASN SER PHE LEU LEU LYS THR LEU THR VAL VAL SER GLY          
SEQRES   9 B  799  PRO ASP MET VAL ASP LEU THR PHE HIS ASN PHE VAL SER          
SEQRES  10 B  799  TYR LYS GLU ASN VAL GLY LYS ALA TRP ALA GLU ASP VAL          
SEQRES  11 B  799  LEU ALA LEU VAL LYS HIS PRO LEU THR ALA ASN ALA SER          
SEQRES  12 B  799  ARG SER THR PHE LEU ASP LYS ILE LEU VAL LYS LEU LYS          
SEQRES  13 B  799  MET GLN LEU ASN SER GLU GLY LYS ILE PRO VAL LYS ASN          
SEQRES  14 B  799  PHE PHE GLN MET PHE PRO ALA ASP ARG LYS ARG VAL GLU          
SEQRES  15 B  799  ALA ALA LEU SER ALA CYS HIS LEU PRO LYS GLY LYS ASN          
SEQRES  16 B  799  ASP ALA ILE ASN PRO GLU ASP PHE PRO GLU PRO VAL TYR          
SEQRES  17 B  799  LYS SER PHE LEU MET SER LEU CYS PRO ARG PRO GLU ILE          
SEQRES  18 B  799  ASP GLU ILE PHE THR SER TYR HIS ALA LYS ALA LYS PRO          
SEQRES  19 B  799  TYR MET THR LYS GLU HIS LEU THR LYS PHE ILE ASN GLN          
SEQRES  20 B  799  LYS GLN ARG ASP SER ARG LEU ASN SER LEU LEU PHE PRO          
SEQRES  21 B  799  PRO ALA ARG PRO ASP GLN VAL GLN GLY LEU ILE ASP LYS          
SEQRES  22 B  799  TYR GLU PRO SER GLY ILE ASN ALA GLN ARG GLY GLN LEU          
SEQRES  23 B  799  SER PRO GLU GLY MET VAL TRP PHE LEU CYS GLY PRO GLU          
SEQRES  24 B  799  ASN SER VAL LEU ALA GLN ASP LYS LEU LEU LEU HIS HIS          
SEQRES  25 B  799  ASP MET THR GLN PRO LEU ASN HIS TYR PHE ILE ASN SER          
SEQRES  26 B  799  SER HIS ASN THR TYR LEU THR ALA GLY GLN PHE SER GLY          
SEQRES  27 B  799  LEU SER SER ALA GLU MET TYR ARG GLN VAL LEU LEU SER          
SEQRES  28 B  799  GLY CYS ARG CYS VAL GLU LEU ASP CYS TRP LYS GLY LYS          
SEQRES  29 B  799  PRO PRO ASP GLU GLU PRO ILE ILE THR HIS GLY PHE THR          
SEQRES  30 B  799  MET THR THR ASP ILE PHE PHE LYS GLU ALA ILE GLU ALA          
SEQRES  31 B  799  ILE ALA GLU SER ALA PHE LYS THR SER PRO TYR PRO ILE          
SEQRES  32 B  799  ILE LEU SER PHE GLU ASN HIS VAL ASP SER PRO ARG GLN          
SEQRES  33 B  799  GLN ALA LYS MET ALA GLU TYR CYS ARG THR ILE PHE GLY          
SEQRES  34 B  799  ASP MET LEU LEU THR GLU PRO LEU GLU LYS PHE PRO LEU          
SEQRES  35 B  799  LYS PRO GLY VAL PRO LEU PRO SER PRO GLU ASP LEU ARG          
SEQRES  36 B  799  GLY LYS ILE LEU ILE LYS ASN LYS LYS ASN GLN PHE SER          
SEQRES  37 B  799  GLY PRO THR SER SER SER LYS ASP THR GLY GLY GLU ALA          
SEQRES  38 B  799  GLU GLY SER SER PRO PRO SER ALA PRO ALA VAL TRP ALA          
SEQRES  39 B  799  GLY GLU GLU GLY THR GLU LEU GLU GLU GLU GLU VAL GLU          
SEQRES  40 B  799  GLU GLU GLU GLU GLU GLU SER GLY ASN LEU ASP GLU GLU          
SEQRES  41 B  799  GLU ILE LYS LYS MET GLN SER ASP GLU GLY THR ALA GLY          
SEQRES  42 B  799  LEU GLU VAL THR ALA TYR GLU GLU MET SER SER LEU VAL          
SEQRES  43 B  799  ASN TYR ILE GLN PRO THR LYS PHE VAL SER PHE GLU PHE          
SEQRES  44 B  799  SER ALA GLN LYS ASN ARG SER TYR VAL ILE SER SER PHE          
SEQRES  45 B  799  THR GLU LEU LYS ALA TYR ASP LEU LEU SER LYS ALA SER          
SEQRES  46 B  799  VAL GLN PHE VAL ASP TYR ASN LYS ARG GLN MET SER ARG          
SEQRES  47 B  799  ILE TYR PRO LYS GLY THR ARG MET ASP SER SER ASN TYR          
SEQRES  48 B  799  MET PRO GLN MET PHE TRP ASN ALA GLY CYS GLN MET VAL          
SEQRES  49 B  799  ALA LEU ASN PHE GLN THR MET ASP LEU PRO MET GLN GLN          
SEQRES  50 B  799  ASN MET ALA VAL PHE GLU PHE ASN GLY GLN SER GLY TYR          
SEQRES  51 B  799  LEU LEU LYS HIS GLU PHE MET ARG ARG PRO ASP LYS GLN          
SEQRES  52 B  799  PHE ASN PRO PHE SER VAL ASP ARG ILE ASP VAL VAL VAL          
SEQRES  53 B  799  ALA THR THR LEU SER ILE THR VAL ILE SER GLY GLN PHE          
SEQRES  54 B  799  LEU SER GLU ARG SER VAL ARG THR TYR VAL GLU VAL GLU          
SEQRES  55 B  799  LEU PHE GLY LEU PRO GLY ASP PRO LYS ARG ARG TYR ARG          
SEQRES  56 B  799  THR LYS LEU SER PRO SER THR ASN SER ILE ASN PRO VAL          
SEQRES  57 B  799  TRP LYS GLU GLU PRO PHE VAL PHE GLU LYS ILE LEU MET          
SEQRES  58 B  799  PRO GLU LEU ALA SER LEU ARG VAL ALA VAL MET GLU GLU          
SEQRES  59 B  799  GLY ASN LYS PHE LEU GLY HIS ARG ILE ILE PRO ILE ASN          
SEQRES  60 B  799  ALA LEU ASN SER GLY TYR HIS HIS LEU CYS LEU HIS SER          
SEQRES  61 B  799  GLU SER ASN MET PRO LEU THR MET PRO ALA LEU PHE ILE          
SEQRES  62 B  799  PHE LEU GLU MET LYS ASP                                      
HET     MG  A 179       1                                                       
HET     CA  B1000       1                                                       
HET    GSP  A2466      32                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CA CALCIUM ION                                                      
HETNAM     GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE                       
FORMUL   3   MG    MG 2+                                                        
FORMUL   4   CA    CA 2+                                                        
FORMUL   5  GSP    C10 H16 N5 O13 P3 S                                          
FORMUL   6  HOH   *486(H2 O)                                                    
HELIX    1   1 GLY A   15  ASN A   26  1                                  12    
HELIX    2   2 GLN A   61  ASP A   65  5                                   5    
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  LYS A  132  1                                  11    
HELIX    8   8 THR A  138  GLY A  150  1                                  13    
HELIX    9   9 GLY A  164  ALA A  175  1                                  12    
HELIX   10  10 LYS B   14  GLY B   20  1                                   7    
HELIX   11  11 LYS B   71  ALA B   73  5                                   3    
HELIX   12  12 SER B   78  PHE B   85  1                                   8    
HELIX   13  13 SER B   93  LEU B   96  5                                   4    
HELIX   14  14 ASN B  121  LYS B  135  1                                  15    
HELIX   15  15 HIS B  136  ASN B  141  1                                   6    
HELIX   16  16 SER B  143  GLN B  158  1                                  16    
HELIX   17  17 VAL B  167  PHE B  174  1                                   8    
HELIX   18  18 ASP B  177  CYS B  188  1                                  12    
HELIX   19  19 ASN B  199  PHE B  203  5                                   5    
HELIX   20  20 PRO B  206  CYS B  216  1                                  11    
HELIX   21  21 ARG B  218  SER B  227  1                                  10    
HELIX   22  22 THR B  237  LYS B  248  1                                  12    
HELIX   23  23 GLN B  268  GLU B  275  1                                   8    
HELIX   24  24 SER B  287  GLY B  297  1                                  11    
HELIX   25  25 ALA B  304  LEU B  309  5                                   6    
HELIX   26  26 PRO B  317  ASN B  319  5                                   3    
HELIX   27  27 ALA B  342  SER B  351  1                                  10    
HELIX   28  28 PHE B  384  ALA B  395  1                                  12    
HELIX   29  29 SER B  413  GLY B  429  1                                  17    
HELIX   30  30 ASP B  430  LEU B  432  5                                   3    
HELIX   31  31 GLU B  529  LEU B  534  5                                   6    
HELIX   32  32 TYR B  539  SER B  544  1                                   6    
HELIX   33  33 SER B  556  ASN B  564  1                                   9    
HELIX   34  34 GLU B  574  GLN B  595  1                                  22    
HELIX   35  35 PRO B  613  ALA B  619  1                                   7    
HELIX   36  36 ASP B  632  PHE B  642  1                                  11    
HELIX   37  37 GLU B  643  SER B  648  5                                   6    
HELIX   38  38 HIS B  654  ARG B  658  5                                   5    
HELIX   39  39 MET B  741  LEU B  744  5                                   4    
HELIX   40  40 ASN B  767  LEU B  769  5                                   3    
SHEET    1   A 6 PHE A  37  MET A  45  0                                        
SHEET    2   A 6 PRO A  50  THR A  58 -1  O  LEU A  55   N  TYR A  40           
SHEET    3   A 6 GLN A   2  GLY A  10  1  N  CYS A   6   O  TRP A  56           
SHEET    4   A 6 VAL A  77  SER A  83  1  O  CYS A  81   N  VAL A   9           
SHEET    5   A 6 ILE A 110  THR A 115  1  O  VAL A 113   N  ILE A  80           
SHEET    6   A 6 LYS A 153  GLU A 156  1  O  LEU A 155   N  GLY A 114           
SHEET    1   B 7 MET B  56  ASP B  60  0                                        
SHEET    2   B 7 TYR B  46  TYR B  51 -1  N  LEU B  47   O  LEU B  59           
SHEET    3   B 7 ALA B  33  VAL B  40 -1  N  ARG B  39   O  TYR B  48           
SHEET    4   B 7 GLU B  21  TRP B  26 -1  N  LYS B  25   O  SER B  34           
SHEET    5   B 7 THR B 111  SER B 117 -1  O  VAL B 116   N  ILE B  24           
SHEET    6   B 7 THR B  98  SER B 103 -1  N  LEU B  99   O  PHE B 115           
SHEET    7   B 7 ILE B  64  PHE B  69 -1  N  ARG B  65   O  VAL B 102           
SHEET    1   C 2 ILE B 165  PRO B 166  0                                        
SHEET    2   C 2 ALA B 197  ILE B 198 -1  O  ILE B 198   N  ILE B 165           
SHEET    1   D 2 TYR B 321  ILE B 323  0                                        
SHEET    2   D 2 TYR B 650  LEU B 652 -1  O  LEU B 651   N  PHE B 322           
SHEET    1   E 5 ILE B 382  PHE B 383  0                                        
SHEET    2   E 5 ILE B 371  ILE B 372 -1  N  ILE B 372   O  ILE B 382           
SHEET    3   E 5 CYS B 355  TRP B 361 -1  N  TRP B 361   O  ILE B 371           
SHEET    4   E 5 ILE B 403  ASN B 409  1  O  SER B 406   N  VAL B 356           
SHEET    5   E 5 ILE B 458  LYS B 461  1  O  LEU B 459   N  LEU B 405           
SHEET    1   F 4 GLN B 550  PRO B 551  0                                        
SHEET    2   F 4 VAL B 568  THR B 573  1  O  ILE B 569   N  GLN B 550           
SHEET    3   F 4 MET B 596  TYR B 600  1  O  ARG B 598   N  PHE B 572           
SHEET    4   F 4 MET B 623  VAL B 624  1  O  MET B 623   N  ILE B 599           
SHEET    1   G 4 PHE B 734  PHE B 736  0                                        
SHEET    2   G 4 THR B 679  GLN B 688 -1  N  LEU B 680   O  PHE B 736           
SHEET    3   G 4 PRO B 785  LYS B 798 -1  O  LYS B 798   N  THR B 679           
SHEET    4   G 4 GLY B 772  HIS B 779 -1  N  LEU B 776   O  LEU B 791           
SHEET    1   H 4 TYR B 714  ARG B 715  0                                        
SHEET    2   H 4 THR B 697  PHE B 704 -1  N  VAL B 701   O  TYR B 714           
SHEET    3   H 4 SER B 746  GLU B 753 -1  O  MET B 752   N  TYR B 698           
SHEET    4   H 4 LYS B 757  PRO B 765 -1  O  GLY B 760   N  VAL B 751           
LINK        MG    MG A 179                 O2B GSP A2466     1555   1555  2.64  
LINK        MG    MG A 179                 O   HOH A1010     1555   1555  3.02  
LINK        MG    MG A 179                 OG1 THR A  17     1555   1555  2.45  
LINK        MG    MG A 179                 OG1 THR A  35     1555   1555  2.51  
LINK        MG    MG A 179                 O2G GSP A2466     1555   1555  2.43  
LINK        CA    CA B1000                 OD2 ASP B 359     1555   1555  2.67  
LINK        CA    CA B1000                 OD1 ASP B 359     1555   1555  2.58  
LINK        CA    CA B1000                 OD1 ASN B 328     1555   1555  2.44  
LINK        CA    CA B1000                 OE2 GLU B 357     1555   1555  2.47  
LINK        CA    CA B1000                 OE1 GLU B 408     1555   1555  2.43  
LINK        CA    CA B1000                 O   HOH B1136     1555   1555  2.60  
LINK        CA    CA B1000                 O   HOH B1073     1555   1555  2.54  
CISPEP   1 GLU B  205    PRO B  206          0         0.35                     
CISPEP   2 PRO B  365    PRO B  366          0         0.30                     
SITE     1 AC1  5 THR A  17  ILE A  33  THR A  35  HOH A1010                    
SITE     2 AC1  5 GSP A2466                                                     
SITE     1 AC2  6 ASN B 328  GLU B 357  ASP B 359  GLU B 408                    
SITE     2 AC2  6 HOH B1073  HOH B1136                                          
SITE     1 AC3 21 GLY A  12  ALA A  13  VAL A  14  GLY A  15                    
SITE     2 AC3 21 LYS A  16  THR A  17  CYS A  18  PHE A  28                    
SITE     3 AC3 21 TYR A  32  THR A  35  GLY A  60  LYS A 116                    
SITE     4 AC3 21 ASP A 118  LEU A 119  SER A 158  ALA A 159                    
SITE     5 AC3 21 LEU A 160   MG A 179  HOH A1010  HOH A1233                    
SITE     6 AC3 21 HOH A1245                                                     
CRYST1  185.822  185.822   93.823  90.00  90.00 120.00 P 32 2 1      6          
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      0.005381  0.003107  0.000000        0.00000                         
SCALE2      0.000000  0.006214  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010658        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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