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Database: PDB
Entry: 4RA5
LinkDB: 4RA5
Original site: 4RA5 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       09-SEP-14   4RA5              
TITLE     HUMAN PROTEIN KINASE C THETA IN COMPLEX WITH LIGAND COMPOUND 11A (6-  
TITLE    2 [(1,3-DIMETHYL-AZETIDIN-3-YL)-METHYL-AMINO]-4(R)-METHYL-7-PHENYL-2,  
TITLE    3 10-DIHYDRO-9-OXA-1,2,4A-TRIAZA-PHENANTHREN-3-ONE)                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HUMAN PROTEIN KINASE C THETA;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: KINASE DOMAIN;                                             
COMPND   5 SYNONYM: NPKC-THETA;                                                 
COMPND   6 EC: 2.7.11.13;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PRKCQ, PRKCT;                                                  
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    PKC THETA KINASE, KINASE DOMAIN, PROTEROS BIOSTRUCTURES GMBH,         
KEYWDS   2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.ARGIRIADI,D.M.GEORGE                                              
REVDAT   2   04-FEB-15 4RA5    1       JRNL                                     
REVDAT   1   08-OCT-14 4RA5    0                                                
JRNL        AUTH   D.M.GEORGE,E.C.BREINLINGER,M.A.ARGIRIADI,Y.ZHANG,J.WANG,     
JRNL        AUTH 2 P.BANSAL-PAKALA,D.B.DUIGNAN,P.HONORE,Q.LANG,S.MITTELSTADT,   
JRNL        AUTH 3 L.RUNDELL,A.SCHWARTZ,J.SUN,J.J.EDMUNDS                       
JRNL        TITL   OPTIMIZED PROTEIN KINASE C THETA (PKC THETA ) INHIBITORS     
JRNL        TITL 2 REVEAL ONLY MODEST ANTI-INFLAMMATORY EFFICACY IN A RODENT    
JRNL        TITL 3 MODEL OF ARTHRITIS.                                          
JRNL        REF    J.MED.CHEM.                   V.  58   333 2015              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   25254961                                                     
JRNL        DOI    10.1021/JM5013006                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.61 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 73.77                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 25436                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.230                           
REMARK   3   R VALUE            (WORKING SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 912                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.61                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.68                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1853                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.18                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3490                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 74                           
REMARK   3   BIN FREE R VALUE                    : 0.4690                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5375                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 69                                      
REMARK   3   SOLVENT ATOMS            : 24                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 71.68                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 8.66000                                              
REMARK   3    B22 (A**2) : -4.38000                                             
REMARK   3    B33 (A**2) : -4.28000                                             
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.664         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.334         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.281         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.300        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.901                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5395 ; 0.009 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  4728 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7321 ; 1.123 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10907 ; 0.914 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   652 ; 6.004 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   262 ;33.011 ;24.198       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   858 ;13.406 ;15.070       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;15.432 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   761 ; 0.068 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6063 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1178 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   986 ; 0.158 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4457 ; 0.129 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2610 ; 0.161 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2726 ; 0.073 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   109 ; 0.119 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.040 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     4 ; 0.041 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    25 ; 0.094 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.082 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3248 ; 0.822 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1314 ; 0.157 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5186 ; 1.476 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2226 ; 2.228 ; 4.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2131 ; 3.375 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   374        A   460                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -19.106   -4.777  -26.829              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0771 T22:  -0.0615                                     
REMARK   3      T33:  -0.0250 T12:   0.0871                                     
REMARK   3      T13:  -0.0398 T23:  -0.0895                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4044 L22:   2.2882                                     
REMARK   3      L33:   4.7463 L12:   0.5170                                     
REMARK   3      L13:   0.7783 L23:  -0.8115                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0379 S12:   0.0463 S13:  -0.2119                       
REMARK   3      S21:   0.0189 S22:   0.1089 S23:  -0.5792                       
REMARK   3      S31:   0.1407 S32:   0.6565 S33:  -0.1469                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   461        A   707                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -37.795   -0.638  -31.250              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1353 T22:  -0.2535                                     
REMARK   3      T33:  -0.2140 T12:   0.0298                                     
REMARK   3      T13:  -0.0080 T23:  -0.0236                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7371 L22:   2.2337                                     
REMARK   3      L33:   2.6524 L12:  -0.2393                                     
REMARK   3      L13:  -0.1475 L23:   0.4699                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0433 S12:   0.0624 S13:  -0.0018                       
REMARK   3      S21:  -0.0106 S22:  -0.0172 S23:  -0.1186                       
REMARK   3      S31:   0.0433 S32:   0.0667 S33:  -0.0261                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   375        B   460                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -29.072   -8.260    8.322              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4663 T22:   0.3362                                     
REMARK   3      T33:   0.1320 T12:  -0.3092                                     
REMARK   3      T13:  -0.1321 T23:  -0.0210                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6072 L22:   4.6222                                     
REMARK   3      L33:   4.0346 L12:  -0.3033                                     
REMARK   3      L13:  -1.8143 L23:   0.0822                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2970 S12:  -0.7385 S13:  -0.4829                       
REMARK   3      S21:   0.4763 S22:  -0.2808 S23:   0.4574                       
REMARK   3      S31:   1.0198 S32:  -0.1338 S33:  -0.0161                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   461        B   701                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -29.263   14.938    7.512              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1237 T22:   0.1887                                     
REMARK   3      T33:   0.0929 T12:  -0.1652                                     
REMARK   3      T13:   0.0128 T23:  -0.1078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9696 L22:   4.4229                                     
REMARK   3      L33:   4.1149 L12:   0.8538                                     
REMARK   3      L13:   1.0040 L23:   1.6694                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2489 S12:  -0.1652 S13:   0.0960                       
REMARK   3      S21:   0.4308 S22:  -0.4616 S23:   0.7579                       
REMARK   3      S31:   0.4589 S32:  -0.6504 S33:   0.2126                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4RA5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-SEP-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB087091.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-OCT-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.25                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00001                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26584                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.610                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 73.770                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.04700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.61                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44400                            
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: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, MGCL2, SODIUM ACETATE AND      
REMARK 280  SODIUM MALONATE, PH 4.25, VAPOR DIFFUSION, HANGING DROP             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       37.41100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       73.77350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.51300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       73.77350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.41100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.51300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2030 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     LYS B   374                                                      
REMARK 465     CYS B   661                                                      
REMARK 465     SER B   662                                                      
REMARK 465     ASN B   663                                                      
REMARK 465     PHE B   664                                                      
REMARK 465     ASP B   665                                                      
REMARK 465     LYS B   666                                                      
REMARK 465     GLU B   667                                                      
REMARK 465     PHE B   668                                                      
REMARK 465     LEU B   669                                                      
REMARK 465     ASN B   670                                                      
REMARK 465     GLU B   671                                                      
REMARK 465     LYS B   672                                                      
REMARK 465     PHE B   677                                                      
REMARK 465     ALA B   678                                                      
REMARK 465     ASP B   679                                                      
REMARK 465     GLU B   702                                                      
REMARK 465     ARG B   703                                                      
REMARK 465     LEU B   704                                                      
REMARK 465     ILE B   705                                                      
REMARK 465     SER B   706                                                      
REMARK 465     HIS B   707                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A  374   CG   CD   CE   NZ                                   
REMARK 480     LYS A  376   CG   CD   CE   NZ                                   
REMARK 480     ILE A  377   CD1                                                 
REMARK 480     LYS A  384   NZ                                                  
REMARK 480     LYS A  388   CE   NZ                                             
REMARK 480     LYS A  400   CD   CE   NZ                                        
REMARK 480     LYS A  401   CG   CD   CE   NZ                                   
REMARK 480     LYS A  429   NZ                                                  
REMARK 480     GLU A  437   CD   OE1  OE2                                       
REMARK 480     LYS A  451   CG   CD   CE   NZ                                   
REMARK 480     LYS A  498   NZ                                                  
REMARK 480     LYS A  514   CD   CE   NZ                                        
REMARK 480     LYS A  555   NZ                                                  
REMARK 480     ARG A  600   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS A  604   CE   NZ                                             
REMARK 480     GLU A  617   CD   OE1  OE2                                       
REMARK 480     ARG A  625   CZ   NH1  NH2                                       
REMARK 480     ARG A  652   CZ   NH1  NH2                                       
REMARK 480     LYS A  654   CD   CE   NZ                                        
REMARK 480     LYS A  656   CG   CD   CE   NZ                                   
REMARK 480     ASP A  665   CG   OD1  OD2                                       
REMARK 480     GLU A  667   CD   OE1  OE2                                       
REMARK 480     LYS A  672   CD   CE   NZ                                        
REMARK 480     ARG A  680   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLN A  688   CG   CD   OE1  NE2                                  
REMARK 480     ARG A  703   CZ   NH1  NH2                                       
REMARK 480     LEU A  704   CG   CD1  CD2                                       
REMARK 480     ILE A  705   CG1  CG2  CD1                                       
REMARK 480     LEU B  375   CG   CD1  CD2                                       
REMARK 480     LYS B  376   CG   CD   CE   NZ                                   
REMARK 480     ILE B  377   CD1                                                 
REMARK 480     LYS B  384   CD   CE   NZ                                        
REMARK 480     LYS B  388   CD   CE   NZ                                        
REMARK 480     SER B  390   OG                                                  
REMARK 480     LYS B  400   CG   CD   CE   NZ                                   
REMARK 480     LYS B  401   CG   CD   CE   NZ                                   
REMARK 480     ASN B  403   CG   OD1  ND2                                       
REMARK 480     ILE B  408   CD1                                                 
REMARK 480     LYS B  412   CG   CD   CE   NZ                                   
REMARK 480     LYS B  413   CG   CD   CE   NZ                                   
REMARK 480     ASP B  414   CG   OD1  OD2                                       
REMARK 480     VAL B  416   CG1  CG2                                            
REMARK 480     LEU B  417   CG   CD1  CD2                                       
REMARK 480     MET B  418   CG   SD   CE                                        
REMARK 480     ASP B  419   CG   OD1  OD2                                       
REMARK 480     ASP B  420   CG   OD1  OD2                                       
REMARK 480     VAL B  422   CG1  CG2                                            
REMARK 480     LYS B  429   CG   CD   CE   NZ                                   
REMARK 480     SER B  433   OG                                                  
REMARK 480     GLU B  437   CG   CD   OE1  OE2                                  
REMARK 480     LYS B  451   CG   CD   CE   NZ                                   
REMARK 480     GLU B  452   CD   OE1  OE2                                       
REMARK 480     LEU B  454   CD1  CD2                                            
REMARK 480     ILE B  488   CD1                                                 
REMARK 480     LYS B  498   CG   CD   CE   NZ                                   
REMARK 480     ILE B  500   CD1                                                 
REMARK 480     LYS B  527   CD   CE   NZ                                        
REMARK 480     LEU B  531   CG   CD1  CD2                                       
REMARK 480     LYS B  535   CE   NZ                                             
REMARK 480     LYS B  555   CG   CD   CE   NZ                                   
REMARK 480     LYS B  604   CD   CE   NZ                                        
REMARK 480     GLU B  617   CG   CD   OE1  OE2                                  
REMARK 480     GLU B  619   CG   CD   OE1  OE2                                  
REMARK 480     LYS B  620   CE   NZ                                             
REMARK 480     ARG B  625   CD   NE   CZ   NH1  NH2                             
REMARK 480     GLN B  630   CD   OE1  NE2                                       
REMARK 480     LYS B  654   CG   CD   CE   NZ                                   
REMARK 480     SER B  657   OG                                                  
REMARK 480     ARG B  674   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LEU B  675   CD1  CD2                                            
REMARK 480     ARG B  680   CD   NE   CZ   NH1  NH2                             
REMARK 480     LEU B  682   CG   CD1  CD2                                       
REMARK 480     ILE B  683   CG1  CG2  CD1                                       
REMARK 480     ASN B  684   CG   OD1  ND2                                       
REMARK 480     SER B  685   OG                                                  
REMARK 480     MET B  686   CG   SD   CE                                        
REMARK 480     ASP B  687   CG   OD1  OD2                                       
REMARK 480     GLN B  688   CG   CD   OE1  NE2                                  
REMARK 480     ASN B  689   CG   OD1  ND2                                       
REMARK 480     MET B  690   CG   SD   CE                                        
REMARK 480     PHE B  691   CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 480     ARG B  692   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ASN B  693   CG   OD1  ND2                                       
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    HIS A 474      -39.59     71.18                                   
REMARK 500    ARG A 503       -7.02     72.03                                   
REMARK 500    ASP A 522       80.63     60.37                                   
REMARK 500    ASP A 533       54.87    -92.39                                   
REMARK 500    ASN A 557     -153.26   -123.65                                   
REMARK 500    ASP A 679       92.51    -64.69                                   
REMARK 500    PHE A 691       42.03   -106.56                                   
REMARK 500    LYS B 400      -79.67    -53.43                                   
REMARK 500    ASP B 421       58.13   -105.43                                   
REMARK 500    HIS B 474      -64.53     63.18                                   
REMARK 500    ARG B 503       -2.05     71.71                                   
REMARK 500    ASP B 522       74.37     61.76                                   
REMARK 500    ASN B 557     -161.35   -128.20                                   
REMARK 500    SER B 657       72.71     57.54                                   
REMARK 500    PHE B 691       48.30    -94.45                                   
REMARK 500    PRO B 699      -28.08    -36.20                                   
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                              NA A 802  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 916   O                                                      
REMARK 620 2 HOH A 915   O    78.1                                              
REMARK 620 3 ASP A 594   OD2  60.8  82.4                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3L0 A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3L0 B 801                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4Q9S   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4Q9Z   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4RA4   RELATED DB: PDB                                   
DBREF  4RA5 A  374   706  UNP    Q04759   KPCT_HUMAN     374    706             
DBREF  4RA5 B  374   706  UNP    Q04759   KPCT_HUMAN     374    706             
SEQADV 4RA5 GLU A  381  UNP  Q04759    ILE   381 ENGINEERED MUTATION            
SEQADV 4RA5 GLU A  538  UNP  Q04759    THR   538 ENGINEERED MUTATION            
SEQADV 4RA5 HIS A  707  UNP  Q04759              EXPRESSION TAG                 
SEQADV 4RA5 GLU B  381  UNP  Q04759    ILE   381 ENGINEERED MUTATION            
SEQADV 4RA5 GLU B  538  UNP  Q04759    THR   538 ENGINEERED MUTATION            
SEQADV 4RA5 HIS B  707  UNP  Q04759              EXPRESSION TAG                 
SEQRES   1 A  334  LYS LEU LYS ILE GLU ASP PHE GLU LEU HIS LYS MET LEU          
SEQRES   2 A  334  GLY LYS GLY SER PHE GLY LYS VAL PHE LEU ALA GLU PHE          
SEQRES   3 A  334  LYS LYS THR ASN GLN PHE PHE ALA ILE LYS ALA LEU LYS          
SEQRES   4 A  334  LYS ASP VAL VAL LEU MET ASP ASP ASP VAL GLU CYS THR          
SEQRES   5 A  334  MET VAL GLU LYS ARG VAL LEU SER LEU ALA TRP GLU HIS          
SEQRES   6 A  334  PRO PHE LEU THR HIS MET PHE CYS THR PHE GLN THR LYS          
SEQRES   7 A  334  GLU ASN LEU PHE PHE VAL MET GLU TYR LEU ASN GLY GLY          
SEQRES   8 A  334  ASP LEU MET TYR HIS ILE GLN SER CYS HIS LYS PHE ASP          
SEQRES   9 A  334  LEU SER ARG ALA THR PHE TYR ALA ALA GLU ILE ILE LEU          
SEQRES  10 A  334  GLY LEU GLN PHE LEU HIS SER LYS GLY ILE VAL TYR ARG          
SEQRES  11 A  334  ASP LEU LYS LEU ASP ASN ILE LEU LEU ASP LYS ASP GLY          
SEQRES  12 A  334  HIS ILE LYS ILE ALA ASP PHE GLY MET CYS LYS GLU ASN          
SEQRES  13 A  334  MET LEU GLY ASP ALA LYS THR ASN GLU PHE CYS GLY THR          
SEQRES  14 A  334  PRO ASP TYR ILE ALA PRO GLU ILE LEU LEU GLY GLN LYS          
SEQRES  15 A  334  TYR ASN HIS SER VAL ASP TRP TRP SER PHE GLY VAL LEU          
SEQRES  16 A  334  LEU TYR GLU MET LEU ILE GLY GLN SER PRO PHE HIS GLY          
SEQRES  17 A  334  GLN ASP GLU GLU GLU LEU PHE HIS SER ILE ARG MET ASP          
SEQRES  18 A  334  ASN PRO PHE TYR PRO ARG TRP LEU GLU LYS GLU ALA LYS          
SEQRES  19 A  334  ASP LEU LEU VAL LYS LEU PHE VAL ARG GLU PRO GLU LYS          
SEQRES  20 A  334  ARG LEU GLY VAL ARG GLY ASP ILE ARG GLN HIS PRO LEU          
SEQRES  21 A  334  PHE ARG GLU ILE ASN TRP GLU GLU LEU GLU ARG LYS GLU          
SEQRES  22 A  334  ILE ASP PRO PRO PHE ARG PRO LYS VAL LYS SER PRO PHE          
SEQRES  23 A  334  ASP CYS SER ASN PHE ASP LYS GLU PHE LEU ASN GLU LYS          
SEQRES  24 A  334  PRO ARG LEU SEP PHE ALA ASP ARG ALA LEU ILE ASN SER          
SEQRES  25 A  334  MET ASP GLN ASN MET PHE ARG ASN PHE SEP PHE MET ASN          
SEQRES  26 A  334  PRO GLY MET GLU ARG LEU ILE SER HIS                          
SEQRES   1 B  334  LYS LEU LYS ILE GLU ASP PHE GLU LEU HIS LYS MET LEU          
SEQRES   2 B  334  GLY LYS GLY SER PHE GLY LYS VAL PHE LEU ALA GLU PHE          
SEQRES   3 B  334  LYS LYS THR ASN GLN PHE PHE ALA ILE LYS ALA LEU LYS          
SEQRES   4 B  334  LYS ASP VAL VAL LEU MET ASP ASP ASP VAL GLU CYS THR          
SEQRES   5 B  334  MET VAL GLU LYS ARG VAL LEU SER LEU ALA TRP GLU HIS          
SEQRES   6 B  334  PRO PHE LEU THR HIS MET PHE CYS THR PHE GLN THR LYS          
SEQRES   7 B  334  GLU ASN LEU PHE PHE VAL MET GLU TYR LEU ASN GLY GLY          
SEQRES   8 B  334  ASP LEU MET TYR HIS ILE GLN SER CYS HIS LYS PHE ASP          
SEQRES   9 B  334  LEU SER ARG ALA THR PHE TYR ALA ALA GLU ILE ILE LEU          
SEQRES  10 B  334  GLY LEU GLN PHE LEU HIS SER LYS GLY ILE VAL TYR ARG          
SEQRES  11 B  334  ASP LEU LYS LEU ASP ASN ILE LEU LEU ASP LYS ASP GLY          
SEQRES  12 B  334  HIS ILE LYS ILE ALA ASP PHE GLY MET CYS LYS GLU ASN          
SEQRES  13 B  334  MET LEU GLY ASP ALA LYS THR ASN GLU PHE CYS GLY THR          
SEQRES  14 B  334  PRO ASP TYR ILE ALA PRO GLU ILE LEU LEU GLY GLN LYS          
SEQRES  15 B  334  TYR ASN HIS SER VAL ASP TRP TRP SER PHE GLY VAL LEU          
SEQRES  16 B  334  LEU TYR GLU MET LEU ILE GLY GLN SER PRO PHE HIS GLY          
SEQRES  17 B  334  GLN ASP GLU GLU GLU LEU PHE HIS SER ILE ARG MET ASP          
SEQRES  18 B  334  ASN PRO PHE TYR PRO ARG TRP LEU GLU LYS GLU ALA LYS          
SEQRES  19 B  334  ASP LEU LEU VAL LYS LEU PHE VAL ARG GLU PRO GLU LYS          
SEQRES  20 B  334  ARG LEU GLY VAL ARG GLY ASP ILE ARG GLN HIS PRO LEU          
SEQRES  21 B  334  PHE ARG GLU ILE ASN TRP GLU GLU LEU GLU ARG LYS GLU          
SEQRES  22 B  334  ILE ASP PRO PRO PHE ARG PRO LYS VAL LYS SER PRO PHE          
SEQRES  23 B  334  ASP CYS SER ASN PHE ASP LYS GLU PHE LEU ASN GLU LYS          
SEQRES  24 B  334  PRO ARG LEU SEP PHE ALA ASP ARG ALA LEU ILE ASN SER          
SEQRES  25 B  334  MET ASP GLN ASN MET PHE ARG ASN PHE SEP PHE MET ASN          
SEQRES  26 B  334  PRO GLY MET GLU ARG LEU ILE SER HIS                          
MODRES 4RA5 SEP A  676  SER  PHOSPHOSERINE                                      
MODRES 4RA5 SEP A  695  SER  PHOSPHOSERINE                                      
MODRES 4RA5 SEP B  676  SER  PHOSPHOSERINE                                      
MODRES 4RA5 SEP B  695  SER  PHOSPHOSERINE                                      
HET    SEP  A 676      10                                                       
HET    SEP  A 695      10                                                       
HET    SEP  B 676      10                                                       
HET    SEP  B 695      10                                                       
HET    3L0  A 801      30                                                       
HET     NA  A 802       1                                                       
HET    EDO  A 803       4                                                       
HET    EDO  A 804       4                                                       
HET    3L0  B 801      30                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     3L0 (1R)-9-[(1,3-DIMETHYLAZETIDIN-3-YL)(METHYL)AMINO]-1-             
HETNAM   2 3L0  METHYL-8-PHENYL-3,5-DIHYDRO[1,2,4]TRIAZINO[3,4-C][1,            
HETNAM   3 3L0  4]BENZOXAZIN-2(1H)-ONE                                          
HETNAM      NA SODIUM ION                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     3L0 (6-[(1,3-DIMETHYL-AZETIDIN-3-YL)-METHYL-AMINO]-4(R)-             
HETSYN   2 3L0  METHYL-7-PHENYL-2,10-DIHYDRO-9-OXA-1,2,4A-TRIAZA-               
HETSYN   3 3L0  PHENANTHREN-3-ONE)                                              
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  SEP    4(C3 H8 N O6 P)                                              
FORMUL   3  3L0    2(C23 H27 N5 O2)                                             
FORMUL   4   NA    NA 1+                                                        
FORMUL   5  EDO    2(C2 H6 O2)                                                  
FORMUL   8  HOH   *24(H2 O)                                                     
HELIX    1   1 LYS A  376  GLU A  378  5                                   3    
HELIX    2   2 LYS A  413  ASP A  419  1                                   7    
HELIX    3   3 ASP A  421  ALA A  435  1                                  15    
HELIX    4   4 TRP A  436  HIS A  438  5                                   3    
HELIX    5   5 LEU A  466  HIS A  474  1                                   9    
HELIX    6   6 ASP A  477  LYS A  498  1                                  22    
HELIX    7   7 LYS A  506  ASP A  508  5                                   3    
HELIX    8   8 THR A  542  ILE A  546  5                                   5    
HELIX    9   9 ALA A  547  LEU A  552  1                                   6    
HELIX   10  10 HIS A  558  GLY A  575  1                                  18    
HELIX   11  11 ASP A  583  ASP A  594  1                                  12    
HELIX   12  12 GLU A  603  PHE A  614  1                                  12    
HELIX   13  13 GLU A  617  ARG A  621  5                                   5    
HELIX   14  14 ASP A  627  ARG A  635  5                                   9    
HELIX   15  15 ASN A  638  ARG A  644  1                                   7    
HELIX   16  16 ASP A  665  GLU A  671  1                                   7    
HELIX   17  17 ASP A  679  MET A  686  1                                   8    
HELIX   18  18 ASN A  698  HIS A  707  1                                  10    
HELIX   19  19 LYS B  376  GLU B  378  5                                   3    
HELIX   20  20 LYS B  413  ASP B  420  1                                   8    
HELIX   21  21 ASP B  421  TRP B  436  1                                  16    
HELIX   22  22 ASP B  465  HIS B  474  1                                  10    
HELIX   23  23 ASP B  477  LYS B  498  1                                  22    
HELIX   24  24 LYS B  506  ASP B  508  5                                   3    
HELIX   25  25 THR B  542  ILE B  546  5                                   5    
HELIX   26  26 ALA B  547  LEU B  552  1                                   6    
HELIX   27  27 HIS B  558  GLY B  575  1                                  18    
HELIX   28  28 ASP B  583  ASP B  594  1                                  12    
HELIX   29  29 GLU B  603  PHE B  614  1                                  12    
HELIX   30  30 GLU B  617  ARG B  621  5                                   5    
HELIX   31  31 ASP B  627  ARG B  635  5                                   9    
HELIX   32  32 ASN B  638  ARG B  644  1                                   7    
HELIX   33  33 ALA B  681  SER B  685  1                                   5    
HELIX   34  34 ASP B  687  ARG B  692  5                                   6    
SHEET    1   A 6 PHE A 380  LYS A 388  0                                        
SHEET    2   A 6 LYS A 393  PHE A 399 -1  O  GLU A 398   N  GLU A 381           
SHEET    3   A 6 PHE A 405  LYS A 412 -1  O  PHE A 406   N  ALA A 397           
SHEET    4   A 6 ASN A 453  MET A 458 -1  O  MET A 458   N  ALA A 407           
SHEET    5   A 6 MET A 444  GLN A 449 -1  N  PHE A 448   O  PHE A 455           
SHEET    6   A 6 PHE A 696  MET A 697 -1  O  PHE A 696   N  THR A 447           
SHEET    1   B 3 GLY A 464  ASP A 465  0                                        
SHEET    2   B 3 ILE A 510  LEU A 512 -1  O  LEU A 512   N  GLY A 464           
SHEET    3   B 3 ILE A 518  ILE A 520 -1  O  LYS A 519   N  LEU A 511           
SHEET    1   C 6 PHE B 380  LYS B 388  0                                        
SHEET    2   C 6 GLY B 392  PHE B 399 -1  O  LEU B 396   N  LYS B 384           
SHEET    3   C 6 PHE B 405  LYS B 412 -1  O  PHE B 406   N  ALA B 397           
SHEET    4   C 6 ASN B 453  MET B 458 -1  O  MET B 458   N  ALA B 407           
SHEET    5   C 6 MET B 444  GLN B 449 -1  N  PHE B 445   O  VAL B 457           
SHEET    6   C 6 PHE B 696  MET B 697 -1  O  PHE B 696   N  THR B 447           
SHEET    1   D 2 ILE B 510  LEU B 512  0                                        
SHEET    2   D 2 ILE B 518  ILE B 520 -1  O  LYS B 519   N  LEU B 511           
LINK         C   LEU A 675                 N   SEP A 676     1555   1555  1.33  
LINK         C   SEP A 676                 N   PHE A 677     1555   1555  1.33  
LINK         C   PHE A 694                 N   SEP A 695     1555   1555  1.33  
LINK         C   SEP A 695                 N   PHE A 696     1555   1555  1.33  
LINK         C   LEU B 675                 N   SEP B 676     1555   1555  1.33  
LINK         C   PHE B 694                 N   SEP B 695     1555   1555  1.34  
LINK         C   SEP B 695                 N   PHE B 696     1555   1555  1.33  
LINK        NA    NA A 802                 O   HOH A 916     1555   1555  2.36  
LINK        NA    NA A 802                 O   HOH A 915     1555   1555  2.38  
LINK         OD2 ASP A 594                NA    NA A 802     1555   1555  2.89  
SITE     1 AC1 12 LEU A 386  GLY A 387  LYS A 388  VAL A 394                    
SITE     2 AC1 12 ALA A 407  MET A 458  GLU A 459  LEU A 461                    
SITE     3 AC1 12 ASP A 508  LEU A 511  ASP A 522  PHE A 664                    
SITE     1 AC2  3 ASP A 594  HOH A 915  HOH A 916                               
SITE     1 AC3  4 ASP A 504  LYS A 506  ASP A 508  ASP A 522                    
SITE     1 AC4  2 GLY A 389  SER A 390                                          
SITE     1 AC5  9 LEU B 386  LYS B 388  THR B 442  MET B 458                    
SITE     2 AC5  9 GLU B 459  LEU B 461  ASP B 465  ASP B 508                    
SITE     3 AC5  9 ASP B 522                                                     
CRYST1   74.822   77.026  147.547  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013365  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012983  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006778        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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