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Database: PDB
Entry: 4Q9Z
LinkDB: 4Q9Z
Original site: 4Q9Z 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       02-MAY-14   4Q9Z              
TITLE     HUMAN PROTEIN KINASE C THETA IN COMPLEX WITH COMPOUND35 ((1R)-9-      
TITLE    2 (AZETIDIN-3-YLAMINO)-1,8-DIMETHYL-3,5-DIHYDRO[1,2,4]TRIAZINO[3,4-    
TITLE    3 C][1,4]BENZOXAZIN-2(1H)-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 CATALYTIC DOMAIN, TRANSFERASE-TRANSFERASE    
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.ARGIRIADI,D.M.GEORGE                                              
REVDAT   4   21-JAN-15 4Q9Z    1       JRNL                                     
REVDAT   3   17-SEP-14 4Q9Z    1       SOURCE                                   
REVDAT   2   30-JUL-14 4Q9Z    1       JRNL                                     
REVDAT   1   02-JUL-14 4Q9Z    0                                                
JRNL        AUTH   D.M.GEORGE,E.C.BREINLINGER,M.FRIEDMAN,Y.ZHANG,J.WANG,        
JRNL        AUTH 2 M.ARGIRIADI,P.BANSAL-PAKALA,M.BARTH,D.B.DUIGNAN,P.HONORE,    
JRNL        AUTH 3 Q.LANG,S.MITTELSTADT,D.POTIN,L.RUNDELL,J.J.EDMUNDS           
JRNL        TITL   DISCOVERY OF SELECTIVE AND ORALLY BIOAVAILABLE PROTEIN       
JRNL        TITL 2 KINASE C THETA (PKC THETA ) INHIBITORS FROM A FRAGMENT HIT.  
JRNL        REF    J.MED.CHEM.                   V.  58   222 2015              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   25000588                                                     
JRNL        DOI    10.1021/JM500669M                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 73.48                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 26124                          
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) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.219                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 921                             
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1921                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.94                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3570                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 79                           
REMARK   3   BIN FREE R VALUE                    : 0.4040                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5344                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 45                                      
REMARK   3   SOLVENT ATOMS            : 56                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 65.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.15000                                             
REMARK   3    B22 (A**2) : 3.71000                                              
REMARK   3    B33 (A**2) : -1.56000                                             
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): 0.572         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.304         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.240         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.825        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5272 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3708 ; 0.008 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7141 ; 1.077 ; 1.936       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8845 ; 0.994 ; 2.982       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   641 ; 5.444 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   248 ;34.582 ;23.992       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   855 ;12.773 ;15.053       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;16.124 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   756 ; 0.066 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5901 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1147 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  3204 ; 0.820 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1293 ; 0.139 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5121 ; 1.601 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2068 ; 2.459 ; 4.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2016 ; 3.978 ; 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   375        A   460                          
REMARK   3    ORIGIN FOR THE GROUP (A):   14.173   -0.895  -10.560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1914 T22:   0.1311                                     
REMARK   3      T33:   0.2961 T12:   0.1324                                     
REMARK   3      T13:   0.0295 T23:   0.0393                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8300 L22:   3.2733                                     
REMARK   3      L33:   6.4474 L12:   1.0549                                     
REMARK   3      L13:   1.4014 L23:  -1.9060                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0702 S12:   0.0643 S13:   0.6609                       
REMARK   3      S21:   0.1574 S22:   0.0213 S23:   0.2733                       
REMARK   3      S31:  -0.8064 S32:  -0.2182 S33:   0.0489                       
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):   18.590  -20.588   -5.864              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0173 T22:   0.1257                                     
REMARK   3      T33:   0.0846 T12:   0.0214                                     
REMARK   3      T13:   0.0186 T23:  -0.0077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3602 L22:   1.8220                                     
REMARK   3      L33:   2.6108 L12:  -0.3861                                     
REMARK   3      L13:  -0.0476 L23:   0.2368                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0463 S12:   0.0976 S13:   0.1225                       
REMARK   3      S21:   0.0264 S22:   0.0800 S23:  -0.0375                       
REMARK   3      S31:  -0.1173 S32:   0.0076 S33:  -0.0337                       
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   374        B   460                          
REMARK   3    ORIGIN FOR THE GROUP (A):   10.495  -11.756  -46.384              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5450 T22:   0.5370                                     
REMARK   3      T33:   0.4888 T12:  -0.1950                                     
REMARK   3      T13:  -0.0042 T23:   0.1828                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1414 L22:   2.9324                                     
REMARK   3      L33:   6.1489 L12:  -0.7779                                     
REMARK   3      L13:   1.1706 L23:   3.0916                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0752 S12:  -0.0028 S13:  -0.5905                       
REMARK   3      S21:  -0.6519 S22:  -0.1229 S23:   0.5605                       
REMARK   3      S31:  -0.2975 S32:  -1.0078 S33:   0.1981                       
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   704                          
REMARK   3    ORIGIN FOR THE GROUP (A):   34.407  -10.967  -45.586              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3332 T22:   0.1788                                     
REMARK   3      T33:   0.2878 T12:  -0.0996                                     
REMARK   3      T13:   0.0494 T23:   0.1115                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9838 L22:   2.0034                                     
REMARK   3      L33:   3.2390 L12:   0.8076                                     
REMARK   3      L13:  -1.1756 L23:  -0.6090                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2327 S12:  -0.1219 S13:  -0.4798                       
REMARK   3      S21:  -0.0069 S22:   0.0963 S23:  -0.0194                       
REMARK   3      S31:   0.3922 S32:  -0.1235 S33:   0.1363                       
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   : 1.40                                          
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 4Q9Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB085790.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-FEB-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
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   : 28125                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 73.480                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.04500                            
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) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45000                            
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   (%): 58.54                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       38.47700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       73.48300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.28750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       73.48300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.47700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.28750            
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: 1710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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 A   374                                                      
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     PRO B   673                                                      
REMARK 465     ARG B   674                                                      
REMARK 465     LEU B   675                                                      
REMARK 465     SEP B   676                                                      
REMARK 465     PHE B   677                                                      
REMARK 465     ALA B   678                                                      
REMARK 465     ASP B   679                                                      
REMARK 465     ARG B   680                                                      
REMARK 465     ALA B   681                                                      
REMARK 465     LEU B   682                                                      
REMARK 465     ILE B   683                                                      
REMARK 465     ASN B   684                                                      
REMARK 465     SER B   685                                                      
REMARK 465     MET B   686                                                      
REMARK 465     ASP B   687                                                      
REMARK 465     GLN B   688                                                      
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  376   CG   CD   CE   NZ                                   
REMARK 480     LYS A  384   CE   NZ                                             
REMARK 480     LYS A  388   NZ                                                  
REMARK 480     LYS A  393   NZ                                                  
REMARK 480     LYS A  400   NZ                                                  
REMARK 480     LYS A  401   CG   CD   CE   NZ                                   
REMARK 480     ASN A  403   CG   OD1  ND2                                       
REMARK 480     GLU A  437   CG   CD   OE1  OE2                                  
REMARK 480     LYS A  451   CD   CE   NZ                                        
REMARK 480     LYS A  498   NZ                                                  
REMARK 480     LYS A  555   CE   NZ                                             
REMARK 480     GLN A  582   CD   OE1  NE2                                       
REMARK 480     GLU A  617   CD   OE1  OE2                                       
REMARK 480     GLU A  619   CG   CD   OE1  OE2                                  
REMARK 480     LYS A  620   NZ                                                  
REMARK 480     GLU A  636   CD   OE1  OE2                                       
REMARK 480     ARG A  652   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS A  654   NZ                                                  
REMARK 480     LYS A  656   CD   CE   NZ                                        
REMARK 480     LYS A  666   CD   CE   NZ                                        
REMARK 480     GLU A  667   CG   CD   OE1  OE2                                  
REMARK 480     GLU A  671   CD   OE1  OE2                                       
REMARK 480     LYS A  672   CG   CD   CE   NZ                                   
REMARK 480     ARG A  680   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLN A  688   CD   OE1  NE2                                       
REMARK 480     ARG A  703   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LEU A  704   CG   CD1  CD2                                       
REMARK 480     ILE A  705   CD1                                                 
REMARK 480     HIS A  707   CG   ND1  CD2  CE1  NE2                             
REMARK 480     LYS B  374   CG   CD   CE   NZ                                   
REMARK 480     LEU B  375   CD1  CD2                                            
REMARK 480     LYS B  376   CG   CD   CE   NZ                                   
REMARK 480     ILE B  377   CD1                                                 
REMARK 480     GLU B  378   CG   CD   OE1  OE2                                  
REMARK 480     GLU B  381   CG   CD   OE1  OE2                                  
REMARK 480     LYS B  384   NZ                                                  
REMARK 480     LYS B  388   CD   CE   NZ                                        
REMARK 480     SER B  390   OG                                                  
REMARK 480     PHE B  391   CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 480     LYS B  393   CD   CE   NZ                                        
REMARK 480     LYS B  400   CG   CD   CE   NZ                                   
REMARK 480     LYS B  401   CG   CD   CE   NZ                                   
REMARK 480     ILE B  408   CD1                                                 
REMARK 480     LYS B  409   CE   NZ                                             
REMARK 480     LYS B  412   CD   CE   NZ                                        
REMARK 480     ASP B  414   CG   OD1  OD2                                       
REMARK 480     LEU B  417   CG   CD1  CD2                                       
REMARK 480     MET B  418   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   NZ                                                  
REMARK 480     LEU B  434   CD1  CD2                                            
REMARK 480     TRP B  436   CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 480     TRP B  436   CZ3  CH2                                            
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     LYS B  475   CE   NZ                                             
REMARK 480     LYS B  498   CD   CE   NZ                                        
REMARK 480     LYS B  527   NZ                                                  
REMARK 480     ASP B  533   CG   OD1  OD2                                       
REMARK 480     LYS B  535   NZ                                                  
REMARK 480     LYS B  555   CG   CD   CE   NZ                                   
REMARK 480     ARG B  600   CD   NE   CZ   NH1  NH2                             
REMARK 480     GLU B  603   CG   CD   OE1  OE2                                  
REMARK 480     LYS B  604   CD   CE   NZ                                        
REMARK 480     GLU B  605   CD   OE1  OE2                                       
REMARK 480     GLU B  617   CD   OE1  OE2                                       
REMARK 480     GLU B  619   CG   CD   OE1  OE2                                  
REMARK 480     LYS B  620   CG   CD   CE   NZ                                   
REMARK 480     ARG B  625   CD   NE   CZ   NH1  NH2                             
REMARK 480     GLU B  640   CD   OE1  OE2                                       
REMARK 480     LYS B  645   CG   CD   CE   NZ                                   
REMARK 480     GLU B  646   CG   CD   OE1  OE2                                  
REMARK 480     ILE B  647   CD1                                                 
REMARK 480     LYS B  654   CE   NZ                                             
REMARK 480     SER B  662   OG                                                  
REMARK 480     ASN B  663   CG   OD1  ND2                                       
REMARK 480     PHE B  664   CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 480     LYS B  666   CG   CD   CE   NZ                                   
REMARK 480     ASN B  689   CG   OD1  ND2                                       
REMARK 480     ARG B  692   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLU B  702   CG   CD   OE1  OE2                                  
REMARK 480     ARG B  703   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LEU B  704   CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A 652   CG    ARG A 652   CD     -0.154                       
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    LYS A 400     -121.27     57.19                                   
REMARK 500    HIS A 474      -55.57     67.62                                   
REMARK 500    ARG A 503      -13.44     72.84                                   
REMARK 500    ASP A 522       78.05     59.89                                   
REMARK 500    ASN A 557     -152.70   -125.59                                   
REMARK 500    PHE A 614       45.99    -91.86                                   
REMARK 500    PHE A 634       32.46    -99.18                                   
REMARK 500    ASN A 663       49.43    -91.26                                   
REMARK 500    PHE A 691       42.04   -102.94                                   
REMARK 500    LEU A 704       44.92   -102.09                                   
REMARK 500    ILE A 705      -56.10   -138.81                                   
REMARK 500    PHE B 391       31.44    -99.66                                   
REMARK 500    THR B 450     -169.01   -102.89                                   
REMARK 500    HIS B 474      -59.68     68.89                                   
REMARK 500    ARG B 503       -5.88     71.67                                   
REMARK 500    ASP B 522       80.12     60.71                                   
REMARK 500    MET B 530       60.53   -112.74                                   
REMARK 500    ASN B 557     -150.84   -137.94                                   
REMARK 500    PHE B 614       30.57    -88.47                                   
REMARK 500    PHE B 634       44.81    -98.72                                   
REMARK 500    SER B 657       71.23     54.35                                   
REMARK 500    ASN B 663      -97.51    -70.38                                   
REMARK 500    PHE B 664      -58.96   -162.67                                   
REMARK 500    ASP B 665     -135.80     39.63                                   
REMARK 500    PHE B 691       47.00   -105.26                                   
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 948   O                                                      
REMARK 620 2 HOH A 947   O   108.2                                              
REMARK 620 3 HOH A 946   O    89.2  66.6                                        
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 PZW 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 PZW B 801                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4Q9S   RELATED DB: PDB                                   
DBREF  4Q9Z A  374   706  UNP    Q04759   KPCT_HUMAN     374    706             
DBREF  4Q9Z B  374   706  UNP    Q04759   KPCT_HUMAN     374    706             
SEQADV 4Q9Z GLU A  381  UNP  Q04759    ILE   381 ENGINEERED MUTATION            
SEQADV 4Q9Z GLU A  538  UNP  Q04759    THR   538 ENGINEERED MUTATION            
SEQADV 4Q9Z HIS A  707  UNP  Q04759              EXPRESSION TAG                 
SEQADV 4Q9Z GLU B  381  UNP  Q04759    ILE   381 ENGINEERED MUTATION            
SEQADV 4Q9Z GLU B  538  UNP  Q04759    THR   538 ENGINEERED MUTATION            
SEQADV 4Q9Z 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 4Q9Z SEP A  676  SER  PHOSPHOSERINE                                      
MODRES 4Q9Z SEP A  695  SER  PHOSPHOSERINE                                      
MODRES 4Q9Z SEP B  695  SER  PHOSPHOSERINE                                      
HET    SEP  A 676      10                                                       
HET    SEP  A 695      10                                                       
HET    SEP  B 695      10                                                       
HET    PZW  A 801      22                                                       
HET     NA  A 802       1                                                       
HET    PZW  B 801      22                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     PZW (1R)-9-(AZETIDIN-3-YLAMINO)-1,8-DIMETHYL-3,5-DIHYDRO[1,          
HETNAM   2 PZW  2,4]TRIAZINO[3,4-C][1,4]BENZOXAZIN-2(1H)-ONE                    
HETNAM      NA SODIUM ION                                                       
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  SEP    3(C3 H8 N O6 P)                                              
FORMUL   3  PZW    2(C15 H19 N5 O2)                                             
FORMUL   4   NA    NA 1+                                                        
FORMUL   6  HOH   *56(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 LEU A  466  HIS A  474  1                                   9    
HELIX    5   5 ASP A  477  LYS A  498  1                                  22    
HELIX    6   6 LYS A  506  ASP A  508  5                                   3    
HELIX    7   7 THR A  542  ILE A  546  5                                   5    
HELIX    8   8 ALA A  547  LEU A  552  1                                   6    
HELIX    9   9 HIS A  558  GLY A  575  1                                  18    
HELIX   10  10 ASP A  583  ASP A  594  1                                  12    
HELIX   11  11 GLU A  603  PHE A  614  1                                  12    
HELIX   12  12 GLU A  617  ARG A  621  5                                   5    
HELIX   13  13 ASP A  627  ARG A  635  5                                   9    
HELIX   14  14 ASN A  638  ARG A  644  1                                   7    
HELIX   15  15 ASP A  665  ASN A  670  1                                   6    
HELIX   16  16 ASP A  679  MET A  686  1                                   8    
HELIX   17  17 ASP A  687  ARG A  692  5                                   6    
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  ALA B  435  1                                  15    
HELIX   22  22 LEU B  466  HIS B  474  1                                   9    
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 ASN B  698  LEU B  704  1                                   7    
SHEET    1   A 6 PHE A 380  GLY A 389  0                                        
SHEET    2   A 6 GLY A 392  PHE A 399 -1  O  VAL A 394   N  GLY A 387           
SHEET    3   A 6 PHE A 405  LYS A 412 -1  O  ALA A 410   N  LYS A 393           
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  CYS A 446   O  VAL A 457           
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  GLY B 389  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  ILE B 408   N  PHE B 395           
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  CYS B 446   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 3 GLY B 464  ASP B 465  0                                        
SHEET    2   D 3 ILE B 510  LEU B 512 -1  O  LEU B 512   N  GLY B 464           
SHEET    3   D 3 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   PHE B 694                 N   SEP B 695     1555   1555  1.33  
LINK         C   SEP B 695                 N   PHE B 696     1555   1555  1.33  
LINK        NA    NA A 802                 O   HOH A 948     1555   1555  2.34  
LINK        NA    NA A 802                 O   HOH A 947     1555   1555  2.34  
LINK        NA    NA A 802                 O   HOH A 946     1555   1555  2.68  
SITE     1 AC1 12 LEU A 386  PHE A 391  VAL A 394  ALA A 407                    
SITE     2 AC1 12 MET A 458  GLU A 459  LEU A 461  ASP A 508                    
SITE     3 AC1 12 ASN A 509  LEU A 511  ASP A 522  PHE A 664                    
SITE     1 AC2  5 GLU A 586  ASP A 594  HOH A 946  HOH A 947                    
SITE     2 AC2  5 HOH A 948                                                     
SITE     1 AC3 10 VAL B 394  ALA B 407  MET B 458  GLU B 459                    
SITE     2 AC3 10 LEU B 461  ASP B 508  ASN B 509  LEU B 511                    
SITE     3 AC3 10 ASP B 522  PHE B 659                                          
CRYST1   76.954   78.575  146.966  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      0.012995  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012727  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006804        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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