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Database: PDB
Entry: 3RYT
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Original site: 3RYT 
HEADER    SIGNALING PROTEIN                       11-MAY-11   3RYT              
TITLE     THE PLEXIN A1 INTRACELLULAR REGION IN COMPLEX WITH RAC1               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PLEXIN-A1;                                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: INTRACELLULAR REGION (UNP RESIDUES 1269-1894);             
COMPND   5 SYNONYM: PLEX 1, PLEXIN-1;                                           
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1;                
COMPND   9 CHAIN: C;                                                            
COMPND  10 FRAGMENT: UNP RESIDUES 1-177;                                        
COMPND  11 SYNONYM: RAC1, CELL MIGRATION-INDUCING GENE 5 PROTEIN, RAS-LIKE      
COMPND  12 PROTEIN TC25, P21-RAC1;                                              
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: KIAA4053, PLEXIN A1, PLXNA1;                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ARCTICEXPRESS;                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET28A;                          
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: MIG5, RAC1, TC25;                                              
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;                                  
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET28A                           
KEYWDS    PLEXIN, RASGAP, GTPASE ACTIVATING PROTEIN, RAC, SIGNALING PROTEIN     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.ZHANG,H.HE                                                          
REVDAT   2   01-FEB-12 3RYT    1       JRNL                                     
REVDAT   1   18-JAN-12 3RYT    0                                                
JRNL        AUTH   Y.WANG,H.HE,N.SRIVASTAVA,S.VIKARUNNESSA,Y.B.CHEN,J.JIANG,    
JRNL        AUTH 2 C.W.COWAN,X.ZHANG                                            
JRNL        TITL   PLEXINS ARE GTPASE-ACTIVATING PROTEINS FOR RAP AND ARE       
JRNL        TITL 2 ACTIVATED BY INDUCED DIMERIZATION.                           
JRNL        REF    SCI.SIGNAL.                   V.   5   RA6 2012              
JRNL        REFN                   ESSN 1937-9145                               
JRNL        PMID   22253263                                                     
JRNL        DOI    10.1126/SCISIGNAL.2002636                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.58 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.58                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.54                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 18508                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.270                           
REMARK   3   R VALUE            (WORKING SET) : 0.270                           
REMARK   3   FREE R VALUE                     : 0.340                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.750                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 879                             
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 49.5484 -  6.5049    0.98     3364   163  0.2183 0.2922        
REMARK   3     2  6.5049 -  5.1649    0.95     3098   153  0.3163 0.3859        
REMARK   3     3  5.1649 -  4.5125    0.94     3002   167  0.2431 0.3329        
REMARK   3     4  4.5125 -  4.1002    0.92     2898   115  0.2928 0.3348        
REMARK   3     5  4.1002 -  3.8064    0.87     2729   131  0.3465 0.4100        
REMARK   3     6  3.8064 -  3.5821    0.82     2538   150  0.4381 0.4664        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.33                                          
REMARK   3   B_SOL              : 216.61                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.540            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.860           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.16350                                              
REMARK   3    B22 (A**2) : 6.16350                                              
REMARK   3    B33 (A**2) : -12.32690                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
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      :  0.004           9288                                  
REMARK   3   ANGLE     :  0.494          12682                                  
REMARK   3   CHIRALITY :  0.031           1510                                  
REMARK   3   PLANARITY :  0.002           1617                                  
REMARK   3   DIHEDRAL  : 11.325           3121                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain A and resseq 1472:1657                           
REMARK   3    ORIGIN FOR THE GROUP (A): -56.1463 -32.1374 -12.6168              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.9086 T22:   0.2309                                     
REMARK   3      T33:   1.0862 T12:  -0.4565                                     
REMARK   3      T13:  -0.2309 T23:   0.0354                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3238 L22:   1.0276                                     
REMARK   3      L33:   0.7873 L12:  -1.4690                                     
REMARK   3      L13:  -0.5539 L23:   0.7324                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1031 S12:  -0.0641 S13:  -0.1239                       
REMARK   3      S21:  -1.0778 S22:   0.1830 S23:  -1.6810                       
REMARK   3      S31:   1.5745 S32:   0.3521 S33:   0.1321                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain A and (resseq 1278:1471 and resseq 1676:1890)    
REMARK   3    ORIGIN FOR THE GROUP (A): -47.5292   4.0723  -7.8453              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3405 T22:   0.0066                                     
REMARK   3      T33:   0.3892 T12:  -0.0310                                     
REMARK   3      T13:  -0.1604 T23:   0.0609                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5550 L22:   0.9944                                     
REMARK   3      L33:   3.9151 L12:   2.9228                                     
REMARK   3      L13:  -0.5418 L23:  -0.3100                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2902 S12:  -0.0319 S13:  -0.2859                       
REMARK   3      S21:   0.1953 S22:   0.3814 S23:  -0.1537                       
REMARK   3      S31:   0.0376 S32:  -0.1458 S33:  -0.0617                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain B and resid 1472:1656                            
REMARK   3    ORIGIN FOR THE GROUP (A): -71.4913  24.7354 -41.4615              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4611 T22:   1.8218                                     
REMARK   3      T33:   0.4441 T12:   0.4943                                     
REMARK   3      T13:  -0.8227 T23:  -0.9260                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4986 L22:   2.9867                                     
REMARK   3      L33:   1.1759 L12:  -0.6242                                     
REMARK   3      L13:   0.8165 L23:  -1.1691                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.1208 S12:  -0.6985 S13:  -0.2744                       
REMARK   3      S21:  -1.3412 S22:   0.0313 S23:  -0.3832                       
REMARK   3      S31:  -0.3006 S32:  -0.0808 S33:   0.4416                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain B and (resseq 1277:1471 and resseq 1673:1891)    
REMARK   3    ORIGIN FOR THE GROUP (A): -52.0406  -6.5281 -42.0105              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3988 T22:   0.8747                                     
REMARK   3      T33:   0.2495 T12:   0.1840                                     
REMARK   3      T13:  -0.0650 T23:  -0.1586                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2653 L22:   2.8716                                     
REMARK   3      L33:   0.1744 L12:   1.1466                                     
REMARK   3      L13:   2.8885 L23:   0.9990                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3026 S12:  -0.8799 S13:   0.1479                       
REMARK   3      S21:   0.1616 S22:   0.0723 S23:   0.0330                       
REMARK   3      S31:   0.9385 S32:  -0.2461 S33:   0.2021                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain C and (resseq 2:176 or resname GNP or resname    
REMARK   3               MG)                                                    
REMARK   3    ORIGIN FOR THE GROUP (A): -56.7357 -65.0011 -17.6968              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1781 T22:   0.2233                                     
REMARK   3      T33:   0.4154 T12:   0.2137                                     
REMARK   3      T13:   0.0059 T23:  -0.1205                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4305 L22:   0.4889                                     
REMARK   3      L33:   3.8539 L12:  -1.3415                                     
REMARK   3      L13:  -2.0205 L23:   0.5871                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2384 S12:   0.6741 S13:   0.1663                       
REMARK   3      S21:  -0.1947 S22:  -0.6956 S23:  -0.8286                       
REMARK   3      S31:  -0.8918 S32:   0.3149 S33:   0.1520                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3RYT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAY-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB065545.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97926                            
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK HIGH-RESOLUTION     
REMARK 200                                   DOUBLE-CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20090                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.582                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.568                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10300                            
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) : 3.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 3IG3 AND 1MH1                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG1500, 100 MM SPG BUFFER, PH       
REMARK 280  7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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      132.81400            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       55.39150            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       55.39150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      199.22100            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       55.39150            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       55.39150            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       66.40700            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       55.39150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       55.39150            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      199.22100            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       55.39150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       55.39150            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       66.40700            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      132.81400            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2110 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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  1269                                                      
REMARK 465     ARG A  1270                                                      
REMARK 465     ASP A  1271                                                      
REMARK 465     ALA A  1272                                                      
REMARK 465     ASP A  1273                                                      
REMARK 465     ARG A  1274                                                      
REMARK 465     THR A  1275                                                      
REMARK 465     LEU A  1276                                                      
REMARK 465     LYS A  1277                                                      
REMARK 465     LEU A  1312                                                      
REMARK 465     ASP A  1313                                                      
REMARK 465     GLY A  1314                                                      
REMARK 465     ALA A  1315                                                      
REMARK 465     GLY A  1316                                                      
REMARK 465     GLU A  1342                                                      
REMARK 465     MET A  1343                                                      
REMARK 465     ARG A  1493                                                      
REMARK 465     GLN A  1494                                                      
REMARK 465     GLN A  1495                                                      
REMARK 465     THR A  1603                                                      
REMARK 465     SER A  1604                                                      
REMARK 465     ALA A  1605                                                      
REMARK 465     TYR A  1606                                                      
REMARK 465     ASN A  1607                                                      
REMARK 465     ILE A  1608                                                      
REMARK 465     SER A  1609                                                      
REMARK 465     ASN A  1610                                                      
REMARK 465     SER A  1611                                                      
REMARK 465     SER A  1612                                                      
REMARK 465     THR A  1613                                                      
REMARK 465     PHE A  1614                                                      
REMARK 465     THR A  1615                                                      
REMARK 465     LYS A  1616                                                      
REMARK 465     SER A  1617                                                      
REMARK 465     LEU A  1618                                                      
REMARK 465     SER A  1619                                                      
REMARK 465     ARG A  1620                                                      
REMARK 465     TYR A  1621                                                      
REMARK 465     GLU A  1622                                                      
REMARK 465     SER A  1623                                                      
REMARK 465     MET A  1624                                                      
REMARK 465     LEU A  1625                                                      
REMARK 465     ARG A  1626                                                      
REMARK 465     THR A  1627                                                      
REMARK 465     ALA A  1628                                                      
REMARK 465     SER A  1629                                                      
REMARK 465     SER A  1630                                                      
REMARK 465     PRO A  1631                                                      
REMARK 465     ASP A  1632                                                      
REMARK 465     SER A  1633                                                      
REMARK 465     LEU A  1634                                                      
REMARK 465     ARG A  1635                                                      
REMARK 465     SER A  1636                                                      
REMARK 465     ARG A  1637                                                      
REMARK 465     THR A  1638                                                      
REMARK 465     PRO A  1639                                                      
REMARK 465     MET A  1640                                                      
REMARK 465     ILE A  1641                                                      
REMARK 465     THR A  1642                                                      
REMARK 465     PRO A  1643                                                      
REMARK 465     ASP A  1644                                                      
REMARK 465     LEU A  1645                                                      
REMARK 465     GLU A  1646                                                      
REMARK 465     SER A  1647                                                      
REMARK 465     GLY A  1648                                                      
REMARK 465     THR A  1649                                                      
REMARK 465     LYS A  1650                                                      
REMARK 465     HIS A  1658                                                      
REMARK 465     ASP A  1659                                                      
REMARK 465     HIS A  1660                                                      
REMARK 465     LEU A  1661                                                      
REMARK 465     ASP A  1662                                                      
REMARK 465     GLN A  1663                                                      
REMARK 465     ARG A  1664                                                      
REMARK 465     GLU A  1665                                                      
REMARK 465     GLY A  1666                                                      
REMARK 465     ASP A  1667                                                      
REMARK 465     ARG A  1668                                                      
REMARK 465     GLY A  1669                                                      
REMARK 465     SER A  1670                                                      
REMARK 465     LYS A  1671                                                      
REMARK 465     MET A  1672                                                      
REMARK 465     VAL A  1673                                                      
REMARK 465     SER A  1674                                                      
REMARK 465     GLU A  1675                                                      
REMARK 465     LEU A  1789                                                      
REMARK 465     GLY A  1790                                                      
REMARK 465     LYS A  1791                                                      
REMARK 465     ASP A  1792                                                      
REMARK 465     SER A  1793                                                      
REMARK 465     ALA A  1891                                                      
REMARK 465     LEU A  1892                                                      
REMARK 465     SER A  1893                                                      
REMARK 465     SER A  1894                                                      
REMARK 465     SER B  1269                                                      
REMARK 465     ARG B  1270                                                      
REMARK 465     ASP B  1271                                                      
REMARK 465     ALA B  1272                                                      
REMARK 465     ASP B  1273                                                      
REMARK 465     ARG B  1274                                                      
REMARK 465     THR B  1275                                                      
REMARK 465     LEU B  1276                                                      
REMARK 465     LEU B  1312                                                      
REMARK 465     ASP B  1313                                                      
REMARK 465     GLY B  1314                                                      
REMARK 465     ALA B  1315                                                      
REMARK 465     GLN B  1494                                                      
REMARK 465     ASN B  1512                                                      
REMARK 465     ALA B  1513                                                      
REMARK 465     GLY B  1559                                                      
REMARK 465     ARG B  1560                                                      
REMARK 465     MET B  1561                                                      
REMARK 465     ALA B  1562                                                      
REMARK 465     GLU B  1569                                                      
REMARK 465     ASP B  1570                                                      
REMARK 465     VAL B  1571                                                      
REMARK 465     ASP B  1578                                                      
REMARK 465     GLN B  1602                                                      
REMARK 465     THR B  1603                                                      
REMARK 465     SER B  1604                                                      
REMARK 465     ALA B  1605                                                      
REMARK 465     TYR B  1606                                                      
REMARK 465     ASN B  1607                                                      
REMARK 465     ILE B  1608                                                      
REMARK 465     SER B  1609                                                      
REMARK 465     ASN B  1610                                                      
REMARK 465     SER B  1611                                                      
REMARK 465     SER B  1612                                                      
REMARK 465     THR B  1613                                                      
REMARK 465     PHE B  1614                                                      
REMARK 465     THR B  1615                                                      
REMARK 465     LYS B  1616                                                      
REMARK 465     SER B  1617                                                      
REMARK 465     LEU B  1618                                                      
REMARK 465     SER B  1619                                                      
REMARK 465     ARG B  1620                                                      
REMARK 465     TYR B  1621                                                      
REMARK 465     GLU B  1622                                                      
REMARK 465     SER B  1623                                                      
REMARK 465     MET B  1624                                                      
REMARK 465     LEU B  1625                                                      
REMARK 465     ARG B  1626                                                      
REMARK 465     THR B  1627                                                      
REMARK 465     ALA B  1628                                                      
REMARK 465     SER B  1629                                                      
REMARK 465     SER B  1630                                                      
REMARK 465     PRO B  1631                                                      
REMARK 465     ASP B  1632                                                      
REMARK 465     SER B  1633                                                      
REMARK 465     LEU B  1634                                                      
REMARK 465     ARG B  1635                                                      
REMARK 465     SER B  1636                                                      
REMARK 465     ARG B  1637                                                      
REMARK 465     THR B  1638                                                      
REMARK 465     PRO B  1639                                                      
REMARK 465     MET B  1640                                                      
REMARK 465     ILE B  1641                                                      
REMARK 465     THR B  1642                                                      
REMARK 465     PRO B  1643                                                      
REMARK 465     ASP B  1644                                                      
REMARK 465     LEU B  1645                                                      
REMARK 465     GLU B  1646                                                      
REMARK 465     SER B  1647                                                      
REMARK 465     GLY B  1648                                                      
REMARK 465     THR B  1649                                                      
REMARK 465     LYS B  1650                                                      
REMARK 465     LEU B  1651                                                      
REMARK 465     ASN B  1657                                                      
REMARK 465     HIS B  1658                                                      
REMARK 465     ASP B  1659                                                      
REMARK 465     HIS B  1660                                                      
REMARK 465     LEU B  1661                                                      
REMARK 465     ASP B  1662                                                      
REMARK 465     GLN B  1663                                                      
REMARK 465     ARG B  1664                                                      
REMARK 465     GLU B  1665                                                      
REMARK 465     GLY B  1666                                                      
REMARK 465     ASP B  1667                                                      
REMARK 465     ARG B  1668                                                      
REMARK 465     GLY B  1669                                                      
REMARK 465     SER B  1670                                                      
REMARK 465     LYS B  1671                                                      
REMARK 465     MET B  1672                                                      
REMARK 465     LYS B  1791                                                      
REMARK 465     ASP B  1792                                                      
REMARK 465     SER B  1793                                                      
REMARK 465     LEU B  1892                                                      
REMARK 465     SER B  1893                                                      
REMARK 465     SER B  1894                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     PRO C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     LEU C    61                                                      
REMARK 465     LEU C   177                                                      
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     ARG A1278    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A1279    CG   CD1  CD2                                       
REMARK 470     GLN A1280    CG   CD   OE1  NE2                                  
REMARK 470     GLN A1282    CG   CD   OE1  NE2                                  
REMARK 470     GLU A1287    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1293    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1295    CG   CD   CE   NZ                                   
REMARK 470     GLU A1300    CG   CD   OE1  OE2                                  
REMARK 470     HIS A1306    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A1307    CG   CD   OE1  OE2                                  
REMARK 470     LEU A1308    CG   CD1  CD2                                       
REMARK 470     SER A1310    OG                                                  
REMARK 470     ASP A1311    CG   OD1  OD2                                       
REMARK 470     ARG A1323    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A1344    CG   CD   OE1  OE2                                  
REMARK 470     GLN A1346    CG   CD   OE1  NE2                                  
REMARK 470     ASN A1348    CG   OD1  ND2                                       
REMARK 470     LYS A1351    CG   CD   CE   NZ                                   
REMARK 470     LYS A1362    CG   CD   CE   NZ                                   
REMARK 470     LYS A1363    CG   CD   CE   NZ                                   
REMARK 470     ARG A1371    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A1393    OG1  CG2                                            
REMARK 470     GLU A1398    CG   CD   OE1  OE2                                  
REMARK 470     MET A1399    CG   SD   CE                                        
REMARK 470     GLU A1400    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1419    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1421    CG   CD   CE   NZ                                   
REMARK 470     LEU A1426    CG   CD1  CD2                                       
REMARK 470     ARG A1429    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A1430    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1449    CG   CD   CE   NZ                                   
REMARK 470     GLU A1453    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1457    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1488    CG   CD   OE1  OE2                                  
REMARK 470     ASP A1497    CG   OD1  OD2                                       
REMARK 470     LYS A1499    CG   CD   CE   NZ                                   
REMARK 470     VAL A1506    CG1  CG2                                            
REMARK 470     GLU A1509    CG   CD   OE1  OE2                                  
REMARK 470     ASN A1512    CG   OD1  ND2                                       
REMARK 470     LYS A1519    CG   CD   CE   NZ                                   
REMARK 470     ASP A1524    CG   OD1  OD2                                       
REMARK 470     LYS A1548    CG   CD   CE   NZ                                   
REMARK 470     ASP A1551    CG   OD1  OD2                                       
REMARK 470     GLN A1558    CG   CD   OE1  NE2                                  
REMARK 470     ARG A1560    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A1563    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A1568    CG   OD1  OD2                                       
REMARK 470     GLU A1569    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1574    CG   CD   CE   NZ                                   
REMARK 470     ILE A1575    CG1  CG2  CD1                                       
REMARK 470     ASP A1578    CG   OD1  OD2                                       
REMARK 470     LEU A1582    CG   CD1  CD2                                       
REMARK 470     LEU A1585    CG   CD1  CD2                                       
REMARK 470     VAL A1590    CG1  CG2                                            
REMARK 470     THR A1591    OG1  CG2                                            
REMARK 470     SER A1594    OG                                                  
REMARK 470     VAL A1599    CG1  CG2                                            
REMARK 470     LYS A1601    CG   CD   CE   NZ                                   
REMARK 470     VAL A1655    CG1  CG2                                            
REMARK 470     LYS A1656    CG   CD   CE   NZ                                   
REMARK 470     ILE A1676    CG1  CG2  CD1                                       
REMARK 470     ASP A1694    CG   OD1  OD2                                       
REMARK 470     ARG A1705    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A1728    CG   CD   OE1  NE2                                  
REMARK 470     HIS A1730    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A1786    CG   CD   OE1  OE2                                  
REMARK 470     HIS A1787    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A1788    CG   CD   CE   NZ                                   
REMARK 470     PRO A1794    CG   CD                                             
REMARK 470     SER A1795    OG                                                  
REMARK 470     LYS A1797    CG   CD   CE   NZ                                   
REMARK 470     LYS A1802    CG   CD   CE   NZ                                   
REMARK 470     ASP A1826    CG   OD1  OD2                                       
REMARK 470     ARG A1838    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A1841    CG   CD1  CD2                                       
REMARK 470     MET A1847    CG   SD   CE                                        
REMARK 470     HIS A1851    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A1852    CG   CD   OE1  OE2                                  
REMARK 470     SER A1855    OG                                                  
REMARK 470     TYR A1856    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE A1857    CG1  CG2  CD1                                       
REMARK 470     LYS A1859    CG   CD   CE   NZ                                   
REMARK 470     LYS A1861    CG   CD   CE   NZ                                   
REMARK 470     ASP A1862    CG   OD1  OD2                                       
REMARK 470     GLU A1869    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1870    CG   CD   CE   NZ                                   
REMARK 470     ASP A1871    CG   OD1  OD2                                       
REMARK 470     GLU A1872    CG   CD   OE1  OE2                                  
REMARK 470     GLN A1873    CG   CD   OE1  NE2                                  
REMARK 470     ARG A1875    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A1876    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A1880    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1882    CG   CD   CE   NZ                                   
REMARK 470     LEU A1883    CG   CD1  CD2                                       
REMARK 470     GLN A1885    CG   CD   OE1  NE2                                  
REMARK 470     VAL A1886    CG1  CG2                                            
REMARK 470     MET A1890    CG   SD   CE                                        
REMARK 470     LYS B1277    CG   CD   CE   NZ                                   
REMARK 470     ARG B1278    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B1282    CG   CD   OE1  NE2                                  
REMARK 470     GLU B1293    CG   CD   OE1  OE2                                  
REMARK 470     LYS B1295    CG   CD   CE   NZ                                   
REMARK 470     GLU B1296    CG   CD   OE1  OE2                                  
REMARK 470     GLU B1300    CG   CD   OE1  OE2                                  
REMARK 470     THR B1309    OG1  CG2                                            
REMARK 470     SER B1310    OG                                                  
REMARK 470     ASP B1311    CG   OD1  OD2                                       
REMARK 470     ARG B1328    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B1335    CG   CD   OE1  OE2                                  
REMARK 470     ASP B1336    CG   OD1  OD2                                       
REMARK 470     HIS B1337    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU B1340    CG   CD1  CD2                                       
REMARK 470     GLU B1342    CG   CD   OE1  OE2                                  
REMARK 470     MET B1343    CG   SD   CE                                        
REMARK 470     GLU B1344    CG   CD   OE1  OE2                                  
REMARK 470     VAL B1349    CG1  CG2                                            
REMARK 470     LYS B1351    CG   CD   CE   NZ                                   
REMARK 470     LEU B1355    CG   CD1  CD2                                       
REMARK 470     PHE B1356    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B1362    CG   CD   CE   NZ                                   
REMARK 470     LYS B1363    CG   CD   CE   NZ                                   
REMARK 470     LEU B1366    CG   CD1  CD2                                       
REMARK 470     ILE B1370    CG1  CG2  CD1                                       
REMARK 470     ARG B1371    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B1383    CG   OD1  OD2                                       
REMARK 470     THR B1393    OG1  CG2                                            
REMARK 470     LEU B1395    CG   CD1  CD2                                       
REMARK 470     GLU B1398    CG   CD   OE1  OE2                                  
REMARK 470     LYS B1407    CG   CD   CE   NZ                                   
REMARK 470     GLU B1415    CG   CD   OE1  OE2                                  
REMARK 470     SER B1420    OG                                                  
REMARK 470     LYS B1421    CG   CD   CE   NZ                                   
REMARK 470     LEU B1426    CG   CD1  CD2                                       
REMARK 470     ARG B1429    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B1437    CG   CD   CE   NZ                                   
REMARK 470     LYS B1449    CG   CD   CE   NZ                                   
REMARK 470     GLU B1453    CG   CD   OE1  OE2                                  
REMARK 470     GLU B1457    CG   CD   OE1  OE2                                  
REMARK 470     LYS B1472    CG   CD   CE   NZ                                   
REMARK 470     GLU B1481    CG   CD   OE1  OE2                                  
REMARK 470     ASP B1489    CG   OD1  OD2                                       
REMARK 470     LYS B1490    CG   CD   CE   NZ                                   
REMARK 470     ILE B1492    CG1  CG2  CD1                                       
REMARK 470     ARG B1493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B1495    CG   CD   OE1  NE2                                  
REMARK 470     ILE B1496    CG1  CG2  CD1                                       
REMARK 470     LYS B1499    CG   CD   CE   NZ                                   
REMARK 470     LEU B1503    CG   CD1  CD2                                       
REMARK 470     ASN B1507    CG   OD1  ND2                                       
REMARK 470     GLU B1509    CG   CD   OE1  OE2                                  
REMARK 470     GLU B1511    CG   CD   OE1  OE2                                  
REMARK 470     PRO B1514    CG   CD                                             
REMARK 470     GLU B1515    CG   CD   OE1  OE2                                  
REMARK 470     LYS B1519    CG   CD   CE   NZ                                   
REMARK 470     LEU B1533    CG   CD1  CD2                                       
REMARK 470     LYS B1539    CG   CD   CE   NZ                                   
REMARK 470     LYS B1548    CG   CD   CE   NZ                                   
REMARK 470     ASP B1553    CG   OD1  OD2                                       
REMARK 470     GLU B1555    CG   CD   OE1  OE2                                  
REMARK 470     ARG B1557    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B1558    CG   CD   OE1  NE2                                  
REMARK 470     ARG B1563    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B1564    CG1  CG2  CD1                                       
REMARK 470     ILE B1565    CG1  CG2  CD1                                       
REMARK 470     ASP B1568    CG   OD1  OD2                                       
REMARK 470     ILE B1575    CG1  CG2  CD1                                       
REMARK 470     ASN B1577    CG   OD1  ND2                                       
REMARK 470     LYS B1580    CG   CD   CE   NZ                                   
REMARK 470     LEU B1582    CG   CD1  CD2                                       
REMARK 470     LEU B1585    CG   CD1  CD2                                       
REMARK 470     VAL B1590    CG1  CG2                                            
REMARK 470     THR B1591    OG1  CG2                                            
REMARK 470     SER B1595    OG                                                  
REMARK 470     VAL B1596    CG1  CG2                                            
REMARK 470     LEU B1598    CG   CD1  CD2                                       
REMARK 470     LYS B1601    CG   CD   CE   NZ                                   
REMARK 470     VAL B1655    CG1  CG2                                            
REMARK 470     LYS B1656    CG   CD   CE   NZ                                   
REMARK 470     VAL B1673    CG1  CG2                                            
REMARK 470     GLU B1675    CG   CD   OE1  OE2                                  
REMARK 470     TYR B1677    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU B1678    CG   CD1  CD2                                       
REMARK 470     LYS B1685    CG   CD   CE   NZ                                   
REMARK 470     LEU B1688    CG   CD1  CD2                                       
REMARK 470     LYS B1690    CG   CD   CE   NZ                                   
REMARK 470     GLU B1697    CG   CD   OE1  OE2                                  
REMARK 470     THR B1702    OG1  CG2                                            
REMARK 470     SER B1707    OG                                                  
REMARK 470     LYS B1714    CG   CD   CE   NZ                                   
REMARK 470     GLN B1728    CG   CD   OE1  NE2                                  
REMARK 470     ILE B1729    CG1  CG2  CD1                                       
REMARK 470     LYS B1739    CG   CD   CE   NZ                                   
REMARK 470     LYS B1753    CG   CD   CE   NZ                                   
REMARK 470     VAL B1758    CG1  CG2                                            
REMARK 470     THR B1784    OG1  CG2                                            
REMARK 470     GLU B1786    CG   CD   OE1  OE2                                  
REMARK 470     HIS B1787    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B1788    CG   CD   CE   NZ                                   
REMARK 470     LEU B1789    CG   CD1  CD2                                       
REMARK 470     PRO B1794    CG   CD                                             
REMARK 470     LYS B1797    CG   CD   CE   NZ                                   
REMARK 470     LYS B1802    CG   CD   CE   NZ                                   
REMARK 470     LYS B1808    CG   CD   CE   NZ                                   
REMARK 470     ASP B1826    CG   OD1  OD2                                       
REMARK 470     GLN B1827    CG   CD   OE1  NE2                                  
REMARK 470     ARG B1838    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B1841    CG   CD1  CD2                                       
REMARK 470     SER B1842    OG                                                  
REMARK 470     MET B1847    CG   SD   CE                                        
REMARK 470     LEU B1850    CG   CD1  CD2                                       
REMARK 470     TYR B1854    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER B1855    OG                                                  
REMARK 470     GLU B1863    CG   CD   OE1  OE2                                  
REMARK 470     LYS B1870    CG   CD   CE   NZ                                   
REMARK 470     ASP B1871    CG   OD1  OD2                                       
REMARK 470     GLU B1872    CG   CD   OE1  OE2                                  
REMARK 470     ARG B1876    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B1878    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B1879    CG   CD1  CD2                                       
REMARK 470     SER B1881    OG                                                  
REMARK 470     LYS B1882    CG   CD   CE   NZ                                   
REMARK 470     LEU B1883    CG   CD1  CD2                                       
REMARK 470     GLU B1884    CG   CD   OE1  OE2                                  
REMARK 470     ASP B1888    CG   OD1  OD2                                       
REMARK 470     THR B1889    OG1  CG2                                            
REMARK 470     MET B1890    CG   SD   CE                                        
REMARK 470     GLN C   2    CG   CD   OE1  NE2                                  
REMARK 470     LYS C   5    CG   CD   CE   NZ                                   
REMARK 470     VAL C  46    CG1  CG2                                            
REMARK 470     ASP C  47    CG   OD1  OD2                                       
REMARK 470     ARG C  66    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C  91    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 100    CG   CD   OE1  OE2                                  
REMARK 470     CYS C 105    SG                                                  
REMARK 470     LEU C 119    CG   CD1  CD2                                       
REMARK 470     LYS C 123    CG   CD   CE   NZ                                   
REMARK 470     LYS C 128    CG   CD   CE   NZ                                   
REMARK 470     LYS C 130    CG   CD   CE   NZ                                   
REMARK 470     GLU C 131    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 133    CG   CD   CE   NZ                                   
REMARK 470     THR C 135    OG1  CG2                                            
REMARK 470     GLN C 141    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 147    CG   CD   CE   NZ                                   
REMARK 470     LYS C 153    CG   CD   CE   NZ                                   
REMARK 470     GLU C 156    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 163    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 166    CG   CD   CE   NZ                                   
REMARK 470     ASP C 170    CG   OD1  OD2                                       
REMARK 470     ILE C 173    CG1  CG2  CD1                                       
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 A1794   N   -  CA  -  CB  ANGL. DEV. =   7.2 DEGREES          
REMARK 500    PRO B1514   N   -  CA  -  CB  ANGL. DEV. =   7.8 DEGREES          
REMARK 500    PRO B1794   N   -  CA  -  CB  ANGL. DEV. =   7.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A1309      -14.50   -153.48                                   
REMARK 500    VAL A1339      -46.64   -141.84                                   
REMARK 500    ARG A1377       33.05    -98.77                                   
REMARK 500    GLU A1398       46.86   -160.28                                   
REMARK 500    LEU A1426       56.80   -100.87                                   
REMARK 500    LEU A1427      -61.18   -108.20                                   
REMARK 500    SER A1433     -146.87    -76.61                                   
REMARK 500    CYS A1454      -87.26   -154.48                                   
REMARK 500    GLU A1488       10.39    -67.42                                   
REMARK 500    PRO A1514      146.12    -39.32                                   
REMARK 500    TYR A1538       58.99   -105.22                                   
REMARK 500    PRO A1542     -170.10    -61.53                                   
REMARK 500    SER A1544       20.24    -72.24                                   
REMARK 500    ARG A1560      -84.83   -108.52                                   
REMARK 500    GLU A1569       94.47   -162.16                                   
REMARK 500    ASP A1570     -149.25   -123.68                                   
REMARK 500    ILE A1575      148.04    166.65                                   
REMARK 500    ASP A1576      -66.88   -109.05                                   
REMARK 500    ASP A1578       86.91    -61.24                                   
REMARK 500    THR A1584     -166.34   -118.17                                   
REMARK 500    GLN A1589       81.42     53.81                                   
REMARK 500    HIS A1653      -81.29   -115.16                                   
REMARK 500    LEU A1654      -92.35   -111.54                                   
REMARK 500    PHE A1700       47.31    -98.17                                   
REMARK 500    ASN A1741        1.23    -67.81                                   
REMARK 500    LEU A1743      -67.17    -94.73                                   
REMARK 500    ARG A1746      -51.42   -123.06                                   
REMARK 500    ASN A1764     -168.20    -78.80                                   
REMARK 500    TYR A1800       31.54    -96.52                                   
REMARK 500    LEU A1841      -75.54    -61.99                                   
REMARK 500    SER A1842       48.04    -96.19                                   
REMARK 500    ASN A1845       98.25    -57.47                                   
REMARK 500    TYR A1860       42.24   -108.18                                   
REMARK 500    GLN A1877       31.09    -86.37                                   
REMARK 500    ARG A1878       57.27     26.57                                   
REMARK 500    ASP B1321      151.35    -44.08                                   
REMARK 500    LEU B1340      -78.76   -101.01                                   
REMARK 500    MET B1343       64.95   -154.74                                   
REMARK 500    LEU B1355      -75.95    -54.86                                   
REMARK 500    LYS B1363      -70.68    -44.98                                   
REMARK 500    SER B1378      -78.79    -81.91                                   
REMARK 500    SER B1380     -163.10   -119.42                                   
REMARK 500    ALA B1394      -34.14   -135.49                                   
REMARK 500    LYS B1421       66.02     62.02                                   
REMARK 500    LEU B1427      -72.12   -106.86                                   
REMARK 500    ARG B1429       80.60    -68.97                                   
REMARK 500    ARG B1430       87.55     22.59                                   
REMARK 500    CYS B1454      -69.98   -130.14                                   
REMARK 500    LYS B1490       31.19    -83.58                                   
REMARK 500    GLU B1509      -62.38   -143.80                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      79 RAMACHANDRAN OUTLIERS.                        
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 C 178  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GNP C 179   O2B                                                    
REMARK 620 2 ASP C  57   OD1 126.5                                              
REMARK 620 3 THR C  17   OG1  56.4  88.1                                        
REMARK 620 4 GNP C 179   O1G  73.9 139.4 127.6                                  
REMARK 620 5 GNP C 179   O2G  56.4 167.5  84.6  52.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 178                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP C 179                 
DBREF  3RYT A 1269  1894  UNP    P70206   PLXA1_MOUSE   1269   1894             
DBREF  3RYT B 1269  1894  UNP    P70206   PLXA1_MOUSE   1269   1894             
DBREF  3RYT C    1   177  UNP    P63000   RAC1_HUMAN       1    177             
SEQADV 3RYT GLY C   -2  UNP  P63000              EXPRESSION TAG                 
SEQADV 3RYT PRO C   -1  UNP  P63000              EXPRESSION TAG                 
SEQADV 3RYT HIS C    0  UNP  P63000              EXPRESSION TAG                 
SEQADV 3RYT LEU C   61  UNP  P63000    GLN    61 ENGINEERED MUTATION            
SEQRES   1 A  626  SER ARG ASP ALA ASP ARG THR LEU LYS ARG LEU GLN LEU          
SEQRES   2 A  626  GLN MET ASP ASN LEU GLU SER ARG VAL ALA LEU GLU CYS          
SEQRES   3 A  626  LYS GLU ALA PHE ALA GLU LEU GLN THR ASP ILE HIS GLU          
SEQRES   4 A  626  LEU THR SER ASP LEU ASP GLY ALA GLY ILE PRO PHE LEU          
SEQRES   5 A  626  ASP TYR ARG THR TYR ALA MET ARG VAL LEU PHE PRO GLY          
SEQRES   6 A  626  ILE GLU ASP HIS PRO VAL LEU LYS GLU MET GLU VAL GLN          
SEQRES   7 A  626  ALA ASN VAL GLU LYS SER LEU THR LEU PHE GLY GLN LEU          
SEQRES   8 A  626  LEU THR LYS LYS HIS PHE LEU LEU THR PHE ILE ARG THR          
SEQRES   9 A  626  LEU GLU ALA GLN ARG SER PHE SER MET ARG ASP ARG GLY          
SEQRES  10 A  626  ASN VAL ALA SER LEU ILE MET THR ALA LEU GLN GLY GLU          
SEQRES  11 A  626  MET GLU TYR ALA THR GLY VAL LEU LYS GLN LEU LEU SER          
SEQRES  12 A  626  ASP LEU ILE GLU LYS ASN LEU GLU SER LYS ASN HIS PRO          
SEQRES  13 A  626  LYS LEU LEU LEU ARG ARG THR GLU SER VAL ALA GLU LYS          
SEQRES  14 A  626  MET LEU THR ASN TRP PHE THR PHE LEU LEU TYR LYS PHE          
SEQRES  15 A  626  LEU LYS GLU CYS ALA GLY GLU PRO LEU PHE MET LEU TYR          
SEQRES  16 A  626  CYS ALA ILE LYS GLN GLN MET GLU LYS GLY PRO ILE ASP          
SEQRES  17 A  626  ALA ILE THR GLY GLU ALA ARG TYR SER LEU SER GLU ASP          
SEQRES  18 A  626  LYS LEU ILE ARG GLN GLN ILE ASP TYR LYS THR LEU THR          
SEQRES  19 A  626  LEU ASN CYS VAL ASN PRO GLU HIS GLU ASN ALA PRO GLU          
SEQRES  20 A  626  VAL PRO VAL LYS GLY LEU ASN CYS ASP THR VAL THR GLN          
SEQRES  21 A  626  VAL LYS GLU LYS LEU LEU ASP ALA VAL TYR LYS GLY VAL          
SEQRES  22 A  626  PRO TYR SER GLN ARG PRO LYS ALA GLY ASP MET ASP LEU          
SEQRES  23 A  626  GLU TRP ARG GLN GLY ARG MET ALA ARG ILE ILE LEU GLN          
SEQRES  24 A  626  ASP GLU ASP VAL THR THR LYS ILE ASP ASN ASP TRP LYS          
SEQRES  25 A  626  ARG LEU ASN THR LEU ALA HIS TYR GLN VAL THR ASP GLY          
SEQRES  26 A  626  SER SER VAL ALA LEU VAL PRO LYS GLN THR SER ALA TYR          
SEQRES  27 A  626  ASN ILE SER ASN SER SER THR PHE THR LYS SER LEU SER          
SEQRES  28 A  626  ARG TYR GLU SER MET LEU ARG THR ALA SER SER PRO ASP          
SEQRES  29 A  626  SER LEU ARG SER ARG THR PRO MET ILE THR PRO ASP LEU          
SEQRES  30 A  626  GLU SER GLY THR LYS LEU TRP HIS LEU VAL LYS ASN HIS          
SEQRES  31 A  626  ASP HIS LEU ASP GLN ARG GLU GLY ASP ARG GLY SER LYS          
SEQRES  32 A  626  MET VAL SER GLU ILE TYR LEU THR ARG LEU LEU ALA THR          
SEQRES  33 A  626  LYS GLY THR LEU GLN LYS PHE VAL ASP ASP LEU PHE GLU          
SEQRES  34 A  626  THR ILE PHE SER THR ALA HIS ARG GLY SER ALA LEU PRO          
SEQRES  35 A  626  LEU ALA ILE LYS TYR MET PHE ASP PHE LEU ASP GLU GLN          
SEQRES  36 A  626  ALA ASP LYS HIS GLN ILE HIS ASP SER ASP VAL ARG HIS          
SEQRES  37 A  626  THR TRP LYS SER ASN CYS LEU PRO LEU ARG PHE TRP VAL          
SEQRES  38 A  626  ASN VAL ILE LYS ASN PRO GLN PHE VAL PHE ASP ILE HIS          
SEQRES  39 A  626  LYS ASN SER ILE THR ASP ALA CYS LEU SER VAL VAL ALA          
SEQRES  40 A  626  GLN THR PHE MET ASP SER CYS SER THR SER GLU HIS LYS          
SEQRES  41 A  626  LEU GLY LYS ASP SER PRO SER ASN LYS LEU LEU TYR ALA          
SEQRES  42 A  626  LYS ASP ILE PRO ASN TYR LYS SER TRP VAL GLU ARG TYR          
SEQRES  43 A  626  TYR ALA ASP ILE ALA LYS MET PRO ALA ILE SER ASP GLN          
SEQRES  44 A  626  ASP MET SER ALA TYR LEU ALA GLU GLN SER ARG LEU HIS          
SEQRES  45 A  626  LEU SER GLN PHE ASN SER MET SER ALA LEU HIS GLU ILE          
SEQRES  46 A  626  TYR SER TYR ILE ALA LYS TYR LYS ASP GLU ILE LEU VAL          
SEQRES  47 A  626  ALA LEU GLU LYS ASP GLU GLN ALA ARG ARG GLN ARG LEU          
SEQRES  48 A  626  ARG SER LYS LEU GLU GLN VAL VAL ASP THR MET ALA LEU          
SEQRES  49 A  626  SER SER                                                      
SEQRES   1 B  626  SER ARG ASP ALA ASP ARG THR LEU LYS ARG LEU GLN LEU          
SEQRES   2 B  626  GLN MET ASP ASN LEU GLU SER ARG VAL ALA LEU GLU CYS          
SEQRES   3 B  626  LYS GLU ALA PHE ALA GLU LEU GLN THR ASP ILE HIS GLU          
SEQRES   4 B  626  LEU THR SER ASP LEU ASP GLY ALA GLY ILE PRO PHE LEU          
SEQRES   5 B  626  ASP TYR ARG THR TYR ALA MET ARG VAL LEU PHE PRO GLY          
SEQRES   6 B  626  ILE GLU ASP HIS PRO VAL LEU LYS GLU MET GLU VAL GLN          
SEQRES   7 B  626  ALA ASN VAL GLU LYS SER LEU THR LEU PHE GLY GLN LEU          
SEQRES   8 B  626  LEU THR LYS LYS HIS PHE LEU LEU THR PHE ILE ARG THR          
SEQRES   9 B  626  LEU GLU ALA GLN ARG SER PHE SER MET ARG ASP ARG GLY          
SEQRES  10 B  626  ASN VAL ALA SER LEU ILE MET THR ALA LEU GLN GLY GLU          
SEQRES  11 B  626  MET GLU TYR ALA THR GLY VAL LEU LYS GLN LEU LEU SER          
SEQRES  12 B  626  ASP LEU ILE GLU LYS ASN LEU GLU SER LYS ASN HIS PRO          
SEQRES  13 B  626  LYS LEU LEU LEU ARG ARG THR GLU SER VAL ALA GLU LYS          
SEQRES  14 B  626  MET LEU THR ASN TRP PHE THR PHE LEU LEU TYR LYS PHE          
SEQRES  15 B  626  LEU LYS GLU CYS ALA GLY GLU PRO LEU PHE MET LEU TYR          
SEQRES  16 B  626  CYS ALA ILE LYS GLN GLN MET GLU LYS GLY PRO ILE ASP          
SEQRES  17 B  626  ALA ILE THR GLY GLU ALA ARG TYR SER LEU SER GLU ASP          
SEQRES  18 B  626  LYS LEU ILE ARG GLN GLN ILE ASP TYR LYS THR LEU THR          
SEQRES  19 B  626  LEU ASN CYS VAL ASN PRO GLU HIS GLU ASN ALA PRO GLU          
SEQRES  20 B  626  VAL PRO VAL LYS GLY LEU ASN CYS ASP THR VAL THR GLN          
SEQRES  21 B  626  VAL LYS GLU LYS LEU LEU ASP ALA VAL TYR LYS GLY VAL          
SEQRES  22 B  626  PRO TYR SER GLN ARG PRO LYS ALA GLY ASP MET ASP LEU          
SEQRES  23 B  626  GLU TRP ARG GLN GLY ARG MET ALA ARG ILE ILE LEU GLN          
SEQRES  24 B  626  ASP GLU ASP VAL THR THR LYS ILE ASP ASN ASP TRP LYS          
SEQRES  25 B  626  ARG LEU ASN THR LEU ALA HIS TYR GLN VAL THR ASP GLY          
SEQRES  26 B  626  SER SER VAL ALA LEU VAL PRO LYS GLN THR SER ALA TYR          
SEQRES  27 B  626  ASN ILE SER ASN SER SER THR PHE THR LYS SER LEU SER          
SEQRES  28 B  626  ARG TYR GLU SER MET LEU ARG THR ALA SER SER PRO ASP          
SEQRES  29 B  626  SER LEU ARG SER ARG THR PRO MET ILE THR PRO ASP LEU          
SEQRES  30 B  626  GLU SER GLY THR LYS LEU TRP HIS LEU VAL LYS ASN HIS          
SEQRES  31 B  626  ASP HIS LEU ASP GLN ARG GLU GLY ASP ARG GLY SER LYS          
SEQRES  32 B  626  MET VAL SER GLU ILE TYR LEU THR ARG LEU LEU ALA THR          
SEQRES  33 B  626  LYS GLY THR LEU GLN LYS PHE VAL ASP ASP LEU PHE GLU          
SEQRES  34 B  626  THR ILE PHE SER THR ALA HIS ARG GLY SER ALA LEU PRO          
SEQRES  35 B  626  LEU ALA ILE LYS TYR MET PHE ASP PHE LEU ASP GLU GLN          
SEQRES  36 B  626  ALA ASP LYS HIS GLN ILE HIS ASP SER ASP VAL ARG HIS          
SEQRES  37 B  626  THR TRP LYS SER ASN CYS LEU PRO LEU ARG PHE TRP VAL          
SEQRES  38 B  626  ASN VAL ILE LYS ASN PRO GLN PHE VAL PHE ASP ILE HIS          
SEQRES  39 B  626  LYS ASN SER ILE THR ASP ALA CYS LEU SER VAL VAL ALA          
SEQRES  40 B  626  GLN THR PHE MET ASP SER CYS SER THR SER GLU HIS LYS          
SEQRES  41 B  626  LEU GLY LYS ASP SER PRO SER ASN LYS LEU LEU TYR ALA          
SEQRES  42 B  626  LYS ASP ILE PRO ASN TYR LYS SER TRP VAL GLU ARG TYR          
SEQRES  43 B  626  TYR ALA ASP ILE ALA LYS MET PRO ALA ILE SER ASP GLN          
SEQRES  44 B  626  ASP MET SER ALA TYR LEU ALA GLU GLN SER ARG LEU HIS          
SEQRES  45 B  626  LEU SER GLN PHE ASN SER MET SER ALA LEU HIS GLU ILE          
SEQRES  46 B  626  TYR SER TYR ILE ALA LYS TYR LYS ASP GLU ILE LEU VAL          
SEQRES  47 B  626  ALA LEU GLU LYS ASP GLU GLN ALA ARG ARG GLN ARG LEU          
SEQRES  48 B  626  ARG SER LYS LEU GLU GLN VAL VAL ASP THR MET ALA LEU          
SEQRES  49 B  626  SER SER                                                      
SEQRES   1 C  180  GLY PRO HIS MET GLN ALA ILE LYS CYS VAL VAL VAL GLY          
SEQRES   2 C  180  ASP GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR          
SEQRES   3 C  180  THR THR ASN ALA PHE PRO GLY GLU TYR ILE PRO THR VAL          
SEQRES   4 C  180  PHE ASP ASN TYR SER ALA ASN VAL MET VAL ASP GLY LYS          
SEQRES   5 C  180  PRO VAL ASN LEU GLY LEU TRP ASP THR ALA GLY LEU GLU          
SEQRES   6 C  180  ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR          
SEQRES   7 C  180  ASP VAL PHE LEU ILE CYS PHE SER LEU VAL SER PRO ALA          
SEQRES   8 C  180  SER PHE GLU ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL          
SEQRES   9 C  180  ARG HIS HIS CYS PRO ASN THR PRO ILE ILE LEU VAL GLY          
SEQRES  10 C  180  THR LYS LEU ASP LEU ARG ASP ASP LYS ASP THR ILE GLU          
SEQRES  11 C  180  LYS LEU LYS GLU LYS LYS LEU THR PRO ILE THR TYR PRO          
SEQRES  12 C  180  GLN GLY LEU ALA MET ALA LYS GLU ILE GLY ALA VAL LYS          
SEQRES  13 C  180  TYR LEU GLU CYS SER ALA LEU THR GLN ARG GLY LEU LYS          
SEQRES  14 C  180  THR VAL PHE ASP GLU ALA ILE ARG ALA VAL LEU                  
HET     MG  C 178       1                                                       
HET    GNP  C 179      32                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER                      
FORMUL   4   MG    MG 2+                                                        
FORMUL   5  GNP    C10 H17 N6 O13 P3                                            
HELIX    1   1 MET A 1283  VAL A 1290  1                                   8    
HELIX    2   2 VAL A 1290  LEU A 1308  1                                  19    
HELIX    3   3 ASP A 1321  PHE A 1331  1                                  11    
HELIX    4   4 GLN A 1346  THR A 1361  1                                  16    
HELIX    5   5 LYS A 1362  GLN A 1376  1                                  15    
HELIX    6   6 SER A 1380  THR A 1393  1                                  14    
HELIX    7   7 ALA A 1394  GLY A 1397  5                                   4    
HELIX    8   8 GLU A 1398  SER A 1420  1                                  23    
HELIX    9   9 HIS A 1423  LEU A 1427  5                                   5    
HELIX   10  10 SER A 1433  LEU A 1447  1                                  15    
HELIX   11  11 LYS A 1449  CYS A 1454  1                                   6    
HELIX   12  12 ALA A 1455  GLU A 1471  1                                  17    
HELIX   13  13 THR A 1525  TYR A 1538  1                                  14    
HELIX   14  14 THR A 1584  GLN A 1589  1                                   6    
HELIX   15  15 LEU A 1678  LEU A 1688  1                                  11    
HELIX   16  16 LEU A 1688  PHE A 1700  1                                  13    
HELIX   17  17 PRO A 1710  LYS A 1726  1                                  17    
HELIX   18  18 ASP A 1731  ASN A 1741  1                                  11    
HELIX   19  19 PHE A 1747  ASN A 1754  1                                   8    
HELIX   20  20 ASN A 1764  SER A 1783  1                                  20    
HELIX   21  21 PRO A 1794  TYR A 1800  1                                   7    
HELIX   22  22 ASP A 1803  MET A 1821  1                                  19    
HELIX   23  23 SER A 1825  LEU A 1839  1                                  15    
HELIX   24  24 ASN A 1845  ALA A 1858  1                                  14    
HELIX   25  25 TYR A 1860  LEU A 1868  1                                   9    
HELIX   26  26 ASP A 1871  GLN A 1877  1                                   7    
HELIX   27  27 ARG A 1878  MET A 1890  1                                  13    
HELIX   28  28 LEU B 1279  SER B 1310  1                                  32    
HELIX   29  29 ASP B 1321  PHE B 1331  1                                  11    
HELIX   30  30 VAL B 1349  LYS B 1362  1                                  14    
HELIX   31  31 LYS B 1362  ALA B 1375  1                                  14    
HELIX   32  32 SER B 1380  ILE B 1391  1                                  12    
HELIX   33  33 ALA B 1394  GLY B 1397  5                                   4    
HELIX   34  34 GLU B 1398  GLU B 1419  1                                  22    
HELIX   35  35 SER B 1433  LEU B 1447  1                                  15    
HELIX   36  36 LYS B 1449  CYS B 1454  1                                   6    
HELIX   37  37 ALA B 1455  LYS B 1472  1                                  18    
HELIX   38  38 THR B 1525  TYR B 1538  1                                  14    
HELIX   39  39 GLU B 1675  ARG B 1680  1                                   6    
HELIX   40  40 LEU B 1681  LEU B 1688  1                                   8    
HELIX   41  41 LEU B 1688  PHE B 1700  1                                  13    
HELIX   42  42 PRO B 1710  LYS B 1726  1                                  17    
HELIX   43  43 ASP B 1731  LEU B 1743  1                                  13    
HELIX   44  44 ARG B 1746  ASN B 1754  1                                   9    
HELIX   45  45 PRO B 1755  VAL B 1758  5                                   4    
HELIX   46  46 ASN B 1764  SER B 1783  1                                  20    
HELIX   47  47 SER B 1795  TYR B 1800  1                                   6    
HELIX   48  48 ASP B 1803  MET B 1821  1                                  19    
HELIX   49  49 SER B 1825  HIS B 1840  1                                  16    
HELIX   50  50 ASN B 1845  LYS B 1859  1                                  15    
HELIX   51  51 LYS B 1861  GLU B 1869  1                                   9    
HELIX   52  52 ASP B 1871  GLN B 1877  1                                   7    
HELIX   53  53 ARG B 1878  ALA B 1891  1                                  14    
HELIX   54  54 GLY C   15  THR C   25  1                                  11    
HELIX   55  55 LEU C   67  TYR C   72  5                                   6    
HELIX   56  56 SER C   86  LYS C   96  1                                  11    
HELIX   57  57 LYS C   96  CYS C  105  1                                  10    
HELIX   58  58 LYS C  116  ARG C  120  5                                   5    
HELIX   59  59 LYS C  123  GLU C  131  1                                   9    
HELIX   60  60 THR C  138  GLY C  150  1                                  13    
HELIX   61  61 GLY C  164  ALA C  175  1                                  12    
SHEET    1   A 5 VAL A1516  LEU A1521  0                                        
SHEET    2   A 5 THR A1500  CYS A1505 -1  N  CYS A1505   O  VAL A1516           
SHEET    3   A 5 SER A1595  PRO A1600  1  O  VAL A1596   N  ASN A1504           
SHEET    4   A 5 MET A1552  GLN A1558 -1  N  ASP A1553   O  VAL A1599           
SHEET    5   A 5 ALA A1562  LEU A1566 -1  O  ALA A1562   N  GLN A1558           
SHEET    1   B 2 THR B1500  VAL B1506  0                                        
SHEET    2   B 2 GLU B1515  LEU B1521 -1  O  VAL B1516   N  CYS B1505           
SHEET    1   C 3 ILE B1564  LEU B1566  0                                        
SHEET    2   C 3 MET B1552  ARG B1557 -1  N  LEU B1554   O  LEU B1566           
SHEET    3   C 3 SER B1595  PRO B1600 -1  O  ALA B1597   N  GLU B1555           
SHEET    1   D 4 ALA C  42  MET C  45  0                                        
SHEET    2   D 4 PRO C  50  ASP C  57 -1  O  LEU C  53   N  ALA C  42           
SHEET    3   D 4 ALA C   3  VAL C   8  1  N  VAL C   8   O  TRP C  56           
SHEET    4   D 4 VAL C  77  PHE C  78  1  O  VAL C  77   N  VAL C   7           
SHEET    1   E 3 CYS C  81  SER C  83  0                                        
SHEET    2   E 3 VAL C 113  THR C 115  1  O  THR C 115   N  PHE C  82           
SHEET    3   E 3 LEU C 155  GLU C 156  1  O  LEU C 155   N  GLY C 114           
LINK        MG    MG C 178                 O2B GNP C 179     1555   1555  2.83  
LINK         OD1 ASP C  57                MG    MG C 178     1555   1555  2.88  
LINK         OG1 THR C  17                MG    MG C 178     1555   1555  2.90  
LINK        MG    MG C 178                 O1G GNP C 179     1555   1555  2.92  
LINK        MG    MG C 178                 O2G GNP C 179     1555   1555  2.92  
CISPEP   1 HIS A 1337    PRO A 1338          0        -0.43                     
CISPEP   2 ARG A 1429    ARG A 1430          0        -5.24                     
CISPEP   3 ARG B 1705    GLY B 1706          0         0.18                     
SITE     1 AC1  5 THR C  17  THR C  35  ASP C  57  THR C  58                    
SITE     2 AC1  5 GNP C 179                                                     
SITE     1 AC2 18 GLY C  12  ALA C  13  VAL C  14  GLY C  15                    
SITE     2 AC2 18 LYS C  16  THR C  17  CYS C  18  PHE C  28                    
SITE     3 AC2 18 GLY C  30  TYR C  32  PRO C  34  THR C  35                    
SITE     4 AC2 18 LYS C 116  ASP C 118  SER C 158  ALA C 159                    
SITE     5 AC2 18 LEU C 160   MG C 178                                          
CRYST1  110.783  110.783  265.628  90.00  90.00  90.00 P 43 21 2    16          
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      0.009027  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009027  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003765        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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