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Database: PDB
Entry: 5T8P
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Original site: 5T8P 
HEADER    TRANSFERASE                             08-SEP-16   5T8P              
TITLE     CRYSTAL STRUCTURE OF MURINE NF-KAPPAB INDUCING KINASE (NIK) BOUND TO  
TITLE    2 BENZOXEPIN COMPOUND 2                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 14;         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 329-675;                                      
COMPND   5 SYNONYM: NF-KAPPA-BETA-INDUCING KINASE,SERINE/THREONINE-PROTEIN      
COMPND   6 KINASE NIK;                                                          
COMPND   7 EC: 2.7.11.25;                                                       
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: MAP3K14, NIK;                                                  
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF9                                     
KEYWDS    PROTEIN SERINE/THREONINE KINASE, NF-KAPPAB, MAP3K14, TRANSFERASE      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.SMITH,P.A.MCEWAN                                                  
REVDAT   3   08-FEB-17 5T8P    1       JRNL                                     
REVDAT   2   25-JAN-17 5T8P    1       JRNL                                     
REVDAT   1   11-JAN-17 5T8P    0                                                
JRNL        AUTH   G.M.CASTANEDO,N.BLAQUIERE,M.BERESINI,B.BRAVO,H.BRIGHTBILL,   
JRNL        AUTH 2 J.CHEN,H.F.CUI,C.EIGENBROT,C.EVERETT,J.FENG,R.GODEMANN,      
JRNL        AUTH 3 E.GOGOL,S.HYMOWITZ,A.JOHNSON,N.KAYAGAKI,P.B.KOHLI,K.KNUPPEL, 
JRNL        AUTH 4 J.KRAEMER,S.KRUGER,P.LOKE,P.MCEWAN,C.MONTALBETTI,            
JRNL        AUTH 5 D.A.ROBERTS,M.SMITH,S.STEINBACHER,S.SUJATHA-BHASKAR,         
JRNL        AUTH 6 R.TAKAHASHI,X.WANG,L.C.WU,Y.ZHANG,S.T.STABEN                 
JRNL        TITL   STRUCTURE-BASED DESIGN OF TRICYCLIC NF-KAPPA B INDUCING      
JRNL        TITL 2 KINASE (NIK) INHIBITORS THAT HAVE HIGH SELECTIVITY OVER      
JRNL        TITL 3 PHOSPHOINOSITIDE-3-KINASE (PI3K).                            
JRNL        REF    J. MED. CHEM.                 V.  60   627 2017              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   28005357                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.6B01363                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.32 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.32                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 71.43                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 38277                          
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) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1920                            
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) : 2.32                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.38                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2836                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2470                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 161                          
REMARK   3   BIN FREE R VALUE                    : 0.3040                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5086                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 54                                      
REMARK   3   SOLVENT ATOMS            : 130                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.95                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.19000                                             
REMARK   3    B22 (A**2) : -0.19000                                             
REMARK   3    B33 (A**2) : 0.38000                                              
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): 0.237         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.203         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.145         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.383        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5269 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5150 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7132 ; 1.519 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11763 ; 0.974 ; 3.004       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   652 ; 6.488 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   219 ;35.588 ;23.379       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   909 ;16.417 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    38 ;18.305 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   765 ; 0.082 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5913 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1161 ; 0.002 ; 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):  2617 ; 1.336 ; 3.347       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2616 ; 1.336 ; 3.345       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3263 ; 2.233 ; 5.010       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3264 ; 2.233 ; 5.012       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2652 ; 1.706 ; 3.658       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2653 ; 1.705 ; 3.658       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3869 ; 2.785 ; 5.393       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5781 ; 5.025 ;26.926       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5782 ; 5.025 ;26.930       
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  : 6                                          
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   334        A   410                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.9123  43.0840   2.4654              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0428 T22:   0.0753                                     
REMARK   3      T33:   0.1582 T12:   0.0536                                     
REMARK   3      T13:  -0.0403 T23:  -0.0730                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2961 L22:   4.9512                                     
REMARK   3      L33:   4.9429 L12:   0.7435                                     
REMARK   3      L13:  -0.7863 L23:  -0.4981                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0555 S12:  -0.1116 S13:  -0.0123                       
REMARK   3      S21:   0.1019 S22:   0.0385 S23:  -0.2763                       
REMARK   3      S31:  -0.0855 S32:  -0.0444 S33:   0.0169                       
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   411        A   543                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.1008  49.2208  -0.1274              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0788 T22:   0.0812                                     
REMARK   3      T33:   0.1012 T12:   0.0307                                     
REMARK   3      T13:   0.0041 T23:  -0.0332                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1639 L22:   0.9129                                     
REMARK   3      L33:   0.8413 L12:  -0.6086                                     
REMARK   3      L13:   0.3887 L23:   0.4893                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0071 S12:   0.1091 S13:   0.0991                       
REMARK   3      S21:   0.0033 S22:   0.0462 S23:  -0.2563                       
REMARK   3      S31:   0.0427 S32:  -0.0280 S33:  -0.0391                       
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 :   A   544        A   675                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.9000  54.7894   6.6368              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0617 T22:   0.2138                                     
REMARK   3      T33:   0.0112 T12:   0.0520                                     
REMARK   3      T13:  -0.0068 T23:  -0.0311                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6770 L22:   3.6846                                     
REMARK   3      L33:   5.5029 L12:   0.8839                                     
REMARK   3      L13:   1.2607 L23:   1.4479                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0553 S12:  -0.3787 S13:   0.1825                       
REMARK   3      S21:   0.2853 S22:  -0.0858 S23:   0.0844                       
REMARK   3      S31:  -0.2665 S32:  -0.1951 S33:   0.1411                       
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   334        B   410                          
REMARK   3    ORIGIN FOR THE GROUP (A):  71.9115  31.6462  -3.1898              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0254 T22:   0.0221                                     
REMARK   3      T33:   0.1116 T12:  -0.0171                                     
REMARK   3      T13:   0.0446 T23:  -0.0407                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9120 L22:   6.0121                                     
REMARK   3      L33:   4.3653 L12:   0.3376                                     
REMARK   3      L13:   0.0831 L23:  -0.3125                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0630 S12:  -0.0383 S13:   0.1003                       
REMARK   3      S21:   0.0500 S22:   0.0158 S23:  -0.1958                       
REMARK   3      S31:  -0.0804 S32:   0.0358 S33:   0.0471                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   411        B   554                          
REMARK   3    ORIGIN FOR THE GROUP (A):  55.4106  23.7780  -4.7349              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0966 T22:   0.0415                                     
REMARK   3      T33:   0.0402 T12:   0.0109                                     
REMARK   3      T13:   0.0123 T23:  -0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6368 L22:   2.5181                                     
REMARK   3      L33:   0.7534 L12:   1.5956                                     
REMARK   3      L13:   0.1086 L23:   0.4412                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0179 S12:   0.0089 S13:   0.1874                       
REMARK   3      S21:  -0.0616 S22:   0.0538 S23:  -0.1513                       
REMARK   3      S31:   0.1059 S32:  -0.0515 S33:  -0.0359                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   555        B   674                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.2288  16.5450  -0.4928              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0441 T22:   0.1275                                     
REMARK   3      T33:   0.0343 T12:  -0.0525                                     
REMARK   3      T13:  -0.0183 T23:   0.0315                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2902 L22:   3.2730                                     
REMARK   3      L33:   5.3754 L12:  -0.5312                                     
REMARK   3      L13:   0.1851 L23:  -0.1511                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0806 S12:  -0.0262 S13:   0.0787                       
REMARK   3      S21:   0.0040 S22:   0.1085 S23:   0.2746                       
REMARK   3      S31:   0.0176 S32:  -0.5627 S33:  -0.0279                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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 5T8P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-SEP-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000213315.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-FEB-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97626                            
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          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40214                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.320                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 71.430                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : 0.08700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.32                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.69200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.3-0.9M AMMONIUM SULPHATE, 0.05-0.1M    
REMARK 280  SODIUM CITRATE, 0.7-1.0M LITHIUM SULPHATE, PH 6.2, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       22.63000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       33.94500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       11.31500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   327                                                      
REMARK 465     SER A   328                                                      
REMARK 465     ALA A   329                                                      
REMARK 465     LEU A   330                                                      
REMARK 465     GLU A   331                                                      
REMARK 465     LYS A   332                                                      
REMARK 465     SER A   364                                                      
REMARK 465     GLY A   365                                                      
REMARK 465     SER A   366                                                      
REMARK 465     ALA A   367                                                      
REMARK 465     LYS A   368                                                      
REMARK 465     LEU A   369                                                      
REMARK 465     GLN A   370                                                      
REMARK 465     ARG A   371                                                      
REMARK 465     LEU A   372                                                      
REMARK 465     GLY A   373                                                      
REMARK 465     PRO A   374                                                      
REMARK 465     GLU A   375                                                      
REMARK 465     THR A   376                                                      
REMARK 465     GLU A   377                                                      
REMARK 465     GLY A   549                                                      
REMARK 465     LYS A   550                                                      
REMARK 465     GLY B   327                                                      
REMARK 465     SER B   328                                                      
REMARK 465     ALA B   329                                                      
REMARK 465     LEU B   330                                                      
REMARK 465     GLU B   331                                                      
REMARK 465     LYS B   332                                                      
REMARK 465     VAL B   333                                                      
REMARK 465     SER B   364                                                      
REMARK 465     GLY B   365                                                      
REMARK 465     SER B   366                                                      
REMARK 465     ALA B   367                                                      
REMARK 465     LYS B   368                                                      
REMARK 465     LEU B   369                                                      
REMARK 465     GLN B   370                                                      
REMARK 465     ARG B   371                                                      
REMARK 465     LEU B   372                                                      
REMARK 465     GLY B   373                                                      
REMARK 465     PRO B   374                                                      
REMARK 465     GLU B   375                                                      
REMARK 465     THR B   376                                                      
REMARK 465     GLU B   377                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL A 333    CG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 493   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG B 493   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A 337      -55.60    -28.54                                   
REMARK 500    VAL A 399      -57.02   -120.97                                   
REMARK 500    ASP A 517       57.71   -150.49                                   
REMARK 500    ASP A 536       94.01     69.52                                   
REMARK 500    LEU A 552      -77.05     46.26                                   
REMARK 500    GLN A 600      150.83    154.32                                   
REMARK 500    PRO A 616       38.82    -73.92                                   
REMARK 500    LYS A 668     -115.95     58.24                                   
REMARK 500    ASP B 392       57.27     37.69                                   
REMARK 500    TYR B 395       96.81   -160.40                                   
REMARK 500    GLU B 398       -6.82     75.48                                   
REMARK 500    ASP B 517       58.67   -154.71                                   
REMARK 500    ASP B 536       87.14     72.71                                   
REMARK 500    LEU B 553       49.80     81.13                                   
REMARK 500    PRO B 616       41.21    -79.87                                   
REMARK 500    LYS B 668     -115.35   -127.19                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 774 A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 774 B 703                 
DBREF  5T8P A  329   675  UNP    Q9WUL6   M3K14_MOUSE    329    675             
DBREF  5T8P B  329   675  UNP    Q9WUL6   M3K14_MOUSE    329    675             
SEQADV 5T8P GLY A  327  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 5T8P SER A  328  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 5T8P GLY B  327  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 5T8P SER B  328  UNP  Q9WUL6              EXPRESSION TAG                 
SEQRES   1 A  349  GLY SER ALA LEU GLU LYS VAL PRO VAL GLU GLU TYR LEU          
SEQRES   2 A  349  VAL HIS ALA LEU GLN GLY SER VAL SER SER GLY GLN ALA          
SEQRES   3 A  349  HIS SER LEU ALA SER LEU ALA LYS THR TRP SER SER GLY          
SEQRES   4 A  349  SER ALA LYS LEU GLN ARG LEU GLY PRO GLU THR GLU ASP          
SEQRES   5 A  349  ASN GLU GLY VAL LEU LEU THR GLU LYS LEU LYS PRO VAL          
SEQRES   6 A  349  ASP TYR GLU TYR ARG GLU GLU VAL HIS TRP MET THR HIS          
SEQRES   7 A  349  GLN PRO ARG VAL GLY ARG GLY SER PHE GLY GLU VAL HIS          
SEQRES   8 A  349  ARG MET LYS ASP LYS GLN THR GLY PHE GLN CYS ALA VAL          
SEQRES   9 A  349  LYS LYS VAL ARG LEU GLU VAL PHE ARG VAL GLU GLU LEU          
SEQRES  10 A  349  VAL ALA CYS ALA GLY LEU SER SER PRO ARG ILE VAL PRO          
SEQRES  11 A  349  LEU TYR GLY ALA VAL ARG GLU GLY PRO TRP VAL ASN ILE          
SEQRES  12 A  349  PHE MET GLU LEU LEU GLU GLY GLY SER LEU GLY GLN LEU          
SEQRES  13 A  349  ILE LYS GLN MET GLY CYS LEU PRO GLU ASP ARG ALA LEU          
SEQRES  14 A  349  TYR TYR LEU GLY GLN ALA LEU GLU GLY LEU GLU TYR LEU          
SEQRES  15 A  349  HIS THR ARG ARG ILE LEU HIS GLY ASP VAL LYS ALA ASP          
SEQRES  16 A  349  ASN VAL LEU LEU SER SER ASP GLY SER ARG ALA ALA LEU          
SEQRES  17 A  349  CYS ASP PHE GLY HIS ALA LEU CYS LEU GLN PRO ASP GLY          
SEQRES  18 A  349  LEU GLY LYS SER LEU LEU THR GLY ASP TYR ILE PRO GLY          
SEQRES  19 A  349  THR GLU THR HIS MET ALA PRO GLU VAL VAL MET GLY LYS          
SEQRES  20 A  349  PRO CYS ASP ALA LYS VAL ASP ILE TRP SER SER CYS CYS          
SEQRES  21 A  349  MET MET LEU HIS MET LEU ASN GLY CYS HIS PRO TRP THR          
SEQRES  22 A  349  GLN TYR PHE ARG GLY PRO LEU CYS LEU LYS ILE ALA SER          
SEQRES  23 A  349  GLU PRO PRO PRO ILE ARG GLU ILE PRO PRO SER CYS ALA          
SEQRES  24 A  349  PRO LEU THR ALA GLN ALA ILE GLN GLU GLY LEU ARG LYS          
SEQRES  25 A  349  GLU PRO VAL HIS ARG ALA SER ALA MET GLU LEU ARG ARG          
SEQRES  26 A  349  LYS VAL GLY LYS ALA LEU GLN GLU VAL GLY GLY LEU LYS          
SEQRES  27 A  349  SER PRO TRP LYS GLY GLU TYR LYS GLU PRO ARG                  
SEQRES   1 B  349  GLY SER ALA LEU GLU LYS VAL PRO VAL GLU GLU TYR LEU          
SEQRES   2 B  349  VAL HIS ALA LEU GLN GLY SER VAL SER SER GLY GLN ALA          
SEQRES   3 B  349  HIS SER LEU ALA SER LEU ALA LYS THR TRP SER SER GLY          
SEQRES   4 B  349  SER ALA LYS LEU GLN ARG LEU GLY PRO GLU THR GLU ASP          
SEQRES   5 B  349  ASN GLU GLY VAL LEU LEU THR GLU LYS LEU LYS PRO VAL          
SEQRES   6 B  349  ASP TYR GLU TYR ARG GLU GLU VAL HIS TRP MET THR HIS          
SEQRES   7 B  349  GLN PRO ARG VAL GLY ARG GLY SER PHE GLY GLU VAL HIS          
SEQRES   8 B  349  ARG MET LYS ASP LYS GLN THR GLY PHE GLN CYS ALA VAL          
SEQRES   9 B  349  LYS LYS VAL ARG LEU GLU VAL PHE ARG VAL GLU GLU LEU          
SEQRES  10 B  349  VAL ALA CYS ALA GLY LEU SER SER PRO ARG ILE VAL PRO          
SEQRES  11 B  349  LEU TYR GLY ALA VAL ARG GLU GLY PRO TRP VAL ASN ILE          
SEQRES  12 B  349  PHE MET GLU LEU LEU GLU GLY GLY SER LEU GLY GLN LEU          
SEQRES  13 B  349  ILE LYS GLN MET GLY CYS LEU PRO GLU ASP ARG ALA LEU          
SEQRES  14 B  349  TYR TYR LEU GLY GLN ALA LEU GLU GLY LEU GLU TYR LEU          
SEQRES  15 B  349  HIS THR ARG ARG ILE LEU HIS GLY ASP VAL LYS ALA ASP          
SEQRES  16 B  349  ASN VAL LEU LEU SER SER ASP GLY SER ARG ALA ALA LEU          
SEQRES  17 B  349  CYS ASP PHE GLY HIS ALA LEU CYS LEU GLN PRO ASP GLY          
SEQRES  18 B  349  LEU GLY LYS SER LEU LEU THR GLY ASP TYR ILE PRO GLY          
SEQRES  19 B  349  THR GLU THR HIS MET ALA PRO GLU VAL VAL MET GLY LYS          
SEQRES  20 B  349  PRO CYS ASP ALA LYS VAL ASP ILE TRP SER SER CYS CYS          
SEQRES  21 B  349  MET MET LEU HIS MET LEU ASN GLY CYS HIS PRO TRP THR          
SEQRES  22 B  349  GLN TYR PHE ARG GLY PRO LEU CYS LEU LYS ILE ALA SER          
SEQRES  23 B  349  GLU PRO PRO PRO ILE ARG GLU ILE PRO PRO SER CYS ALA          
SEQRES  24 B  349  PRO LEU THR ALA GLN ALA ILE GLN GLU GLY LEU ARG LYS          
SEQRES  25 B  349  GLU PRO VAL HIS ARG ALA SER ALA MET GLU LEU ARG ARG          
SEQRES  26 B  349  LYS VAL GLY LYS ALA LEU GLN GLU VAL GLY GLY LEU LYS          
SEQRES  27 B  349  SER PRO TRP LYS GLY GLU TYR LYS GLU PRO ARG                  
HET    774  A 701      17                                                       
HET    SO4  A 702       5                                                       
HET    SO4  A 703       5                                                       
HET    SO4  B 701       5                                                       
HET    SO4  B 702       5                                                       
HET    774  B 703      17                                                       
HETNAM     774 6,7-DIHYDROTHIENO[4,5]OXEPINO[1,2-~{C}]PYRIDINE-2-               
HETNAM   2 774  CARBOXAMIDE                                                     
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  774    2(C12 H10 N2 O2 S)                                           
FORMUL   4  SO4    4(O4 S 2-)                                                   
FORMUL   9  HOH   *130(H2 O)                                                    
HELIX    1 AA1 VAL A  335  GLN A  344  1                                  10    
HELIX    2 AA2 GLN A  351  LYS A  360  1                                  10    
HELIX    3 AA3 THR A  361  SER A  363  5                                   3    
HELIX    4 AA4 GLU A  436  ARG A  439  5                                   4    
HELIX    5 AA5 VAL A  440  ALA A  445  1                                   6    
HELIX    6 AA6 LEU A  479  GLY A  487  1                                   9    
HELIX    7 AA7 PRO A  490  ARG A  511  1                                  22    
HELIX    8 AA8 LYS A  519  ASP A  521  5                                   3    
HELIX    9 AA9 THR A  561  MET A  565  5                                   5    
HELIX   10 AB1 ALA A  566  MET A  571  1                                   6    
HELIX   11 AB2 ALA A  577  GLY A  594  1                                  18    
HELIX   12 AB3 PRO A  605  GLU A  613  1                                   9    
HELIX   13 AB4 PRO A  616  ILE A  620  5                                   5    
HELIX   14 AB5 ALA A  625  LEU A  636  1                                  12    
HELIX   15 AB6 GLU A  639  ARG A  643  5                                   5    
HELIX   16 AB7 SER A  645  VAL A  660  1                                  16    
HELIX   17 AB8 VAL B  335  GLN B  344  1                                  10    
HELIX   18 AB9 GLN B  351  LYS B  360  1                                  10    
HELIX   19 AC1 THR B  361  SER B  363  5                                   3    
HELIX   20 AC2 GLU B  436  ARG B  439  5                                   4    
HELIX   21 AC3 VAL B  440  ALA B  445  1                                   6    
HELIX   22 AC4 SER B  478  GLY B  487  1                                  10    
HELIX   23 AC5 PRO B  490  ARG B  511  1                                  22    
HELIX   24 AC6 LYS B  519  ASP B  521  5                                   3    
HELIX   25 AC7 THR B  561  MET B  565  5                                   5    
HELIX   26 AC8 ALA B  566  MET B  571  1                                   6    
HELIX   27 AC9 ALA B  577  GLY B  594  1                                  18    
HELIX   28 AD1 PRO B  605  GLU B  613  1                                   9    
HELIX   29 AD2 PRO B  616  ILE B  620  5                                   5    
HELIX   30 AD3 ALA B  625  LEU B  636  1                                  12    
HELIX   31 AD4 SER B  645  VAL B  660  1                                  16    
SHEET    1 AA1 7 VAL A 347  SER A 349  0                                        
SHEET    2 AA1 7 ASN A 379  LEU A 383  1  O  LEU A 383   N  SER A 348           
SHEET    3 AA1 7 LEU A 457  GLU A 463 -1  O  ARG A 462   N  GLU A 380           
SHEET    4 AA1 7 TRP A 466  MET A 471 -1  O  ASN A 468   N  VAL A 461           
SHEET    5 AA1 7 GLN A 427  ARG A 434 -1  N  VAL A 433   O  VAL A 467           
SHEET    6 AA1 7 VAL A 416  ASP A 421 -1  N  MET A 419   O  CYS A 428           
SHEET    7 AA1 7 TRP A 401  THR A 403 -1  N  MET A 402   O  LYS A 420           
SHEET    1 AA2 3 GLY A 477  SER A 478  0                                        
SHEET    2 AA2 3 VAL A 523  LEU A 525 -1  O  LEU A 525   N  GLY A 477           
SHEET    3 AA2 3 ALA A 532  LEU A 534 -1  O  ALA A 533   N  LEU A 524           
SHEET    1 AA3 2 ILE A 513  LEU A 514  0                                        
SHEET    2 AA3 2 LEU A 541  CYS A 542 -1  O  LEU A 541   N  LEU A 514           
SHEET    1 AA4 7 VAL B 347  SER B 349  0                                        
SHEET    2 AA4 7 ASN B 379  LEU B 383  1  O  LEU B 383   N  SER B 348           
SHEET    3 AA4 7 LEU B 457  GLU B 463 -1  O  ARG B 462   N  GLU B 380           
SHEET    4 AA4 7 TRP B 466  MET B 471 -1  O  ASN B 468   N  VAL B 461           
SHEET    5 AA4 7 GLN B 427  ARG B 434 -1  N  LYS B 431   O  ILE B 469           
SHEET    6 AA4 7 VAL B 416  ASP B 421 -1  N  MET B 419   O  CYS B 428           
SHEET    7 AA4 7 TRP B 401  THR B 403 -1  N  MET B 402   O  LYS B 420           
SHEET    1 AA5 2 ILE B 513  LEU B 514  0                                        
SHEET    2 AA5 2 LEU B 541  CYS B 542 -1  O  LEU B 541   N  LEU B 514           
SHEET    1 AA6 2 VAL B 523  LEU B 525  0                                        
SHEET    2 AA6 2 ALA B 532  LEU B 534 -1  O  ALA B 533   N  LEU B 524           
SHEET    1 AA7 2 LYS B 550  SER B 551  0                                        
SHEET    2 AA7 2 PRO B 574  CYS B 575 -1  O  CYS B 575   N  LYS B 550           
SITE     1 AC1  9 VAL A 416  ALA A 429  MET A 471  GLU A 472                    
SITE     2 AC1  9 LEU A 473  LEU A 474  ASP A 521  LEU A 524                    
SITE     3 AC1  9 ASP A 536                                                     
SITE     1 AC2  6 PRO A 406  VAL A 408  GLY A 409  ARG A 410                    
SITE     2 AC2  6 HIS A 417  ARG A 418                                          
SITE     1 AC3  3 ARG A 637  LYS A 638  GLU A 639                               
SITE     1 AC4  4 ARG B 637  LYS B 638  GLU B 639  HIS B 642                    
SITE     1 AC5  8 HIS B 404  PRO B 406  VAL B 408  GLY B 409                    
SITE     2 AC5  8 VAL B 416  HIS B 417  ARG B 418  HOH B 846                    
SITE     1 AC6  9 VAL B 416  ALA B 429  MET B 471  GLU B 472                    
SITE     2 AC6  9 LEU B 473  LEU B 474  ASP B 521  LEU B 524                    
SITE     3 AC6  9 ASP B 536                                                     
CRYST1  142.850  142.850   45.260  90.00  90.00  90.00 P 43          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      0.007000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022095        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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