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Database: PDB
Entry: 5T8O
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Original site: 5T8O 
HEADER    TRANSFERASE                             08-SEP-16   5T8O              
TITLE     CRYSTAL STRUCTURE OF MURINE NF-KAPPAB INDUCING KINASE (NIK) BOUND TO  
TITLE    2 IMIDAZOBENZOXEPIN COMPOUND 3                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 14;         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: NF-KAPPA-BETA-INDUCING KINASE,SERINE/THREONINE-PROTEIN      
COMPND   5 KINASE NIK;                                                          
COMPND   6 EC: 2.7.11.25;                                                       
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE 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.MCEWAN,S.G.HYMOWITZ                                       
REVDAT   3   08-FEB-17 5T8O    1       JRNL                                     
REVDAT   2   25-JAN-17 5T8O    1       JRNL                                     
REVDAT   1   11-JAN-17 5T8O    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.    2.41 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
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) : 2.41                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 143.95                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 31025                          
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) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.300                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 3549                            
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) : 2.41                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.47                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2259                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.65                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2920                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 271                          
REMARK   3   BIN FREE R VALUE                    : 0.3350                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5067                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 81                                      
REMARK   3   SOLVENT ATOMS            : 286                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.08000                                              
REMARK   3    B22 (A**2) : 0.08000                                              
REMARK   3    B33 (A**2) : -0.17000                                             
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): 0.396         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.273         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.199         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.556        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.890                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5291 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5059 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7165 ; 1.373 ; 1.990       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11684 ; 0.937 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   653 ; 6.284 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   220 ;35.963 ;23.318       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   912 ;15.209 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    38 ;17.682 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   768 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5854 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1166 ; 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):  2609 ; 0.430 ; 1.670       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2610 ; 0.430 ; 1.670       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3256 ; 0.784 ; 2.501       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3256 ; 0.784 ; 2.502       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2682 ; 0.393 ; 1.761       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2683 ; 0.393 ; 1.761       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3907 ; 0.650 ; 2.623       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5948 ; 3.484 ;13.683       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5923 ; 3.410 ;13.606       
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):  28.3640  28.1400   2.8020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0075 T22:   0.0188                                     
REMARK   3      T33:   0.0862 T12:  -0.0033                                     
REMARK   3      T13:   0.0010 T23:   0.0360                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2268 L22:   4.0744                                     
REMARK   3      L33:   4.3331 L12:  -1.9214                                     
REMARK   3      L13:   1.0599 L23:  -0.6144                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0708 S12:   0.0153 S13:  -0.1183                       
REMARK   3      S21:   0.1149 S22:  -0.0952 S23:   0.0411                       
REMARK   3      S31:  -0.0043 S32:   0.0460 S33:   0.1660                       
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):  45.2000  21.4910   0.5100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0641 T22:   0.0261                                     
REMARK   3      T33:   0.0599 T12:   0.0113                                     
REMARK   3      T13:  -0.0105 T23:   0.0236                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5094 L22:   0.6018                                     
REMARK   3      L33:   0.8829 L12:  -0.2684                                     
REMARK   3      L13:  -0.7782 L23:  -0.1245                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0409 S12:   0.1696 S13:   0.1690                       
REMARK   3      S21:  -0.0360 S22:  -0.0434 S23:   0.0871                       
REMARK   3      S31:  -0.1388 S32:   0.0386 S33:   0.0842                       
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):  62.9660  15.9490   7.5900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0677 T22:   0.1612                                     
REMARK   3      T33:   0.0806 T12:   0.0054                                     
REMARK   3      T13:  -0.0284 T23:   0.0820                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0717 L22:   3.4259                                     
REMARK   3      L33:   7.5004 L12:   1.1022                                     
REMARK   3      L13:  -3.3336 L23:  -0.8197                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0227 S12:  -0.6313 S13:  -0.4236                       
REMARK   3      S21:   0.3025 S22:  -0.1436 S23:  -0.2633                       
REMARK   3      S31:   0.4494 S32:   0.4365 S33:   0.1662                       
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):   0.1290  40.2190  -2.8910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0271 T22:   0.0054                                     
REMARK   3      T33:   0.0787 T12:   0.0020                                     
REMARK   3      T13:  -0.0385 T23:  -0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8228 L22:   3.6321                                     
REMARK   3      L33:   4.5380 L12:  -0.2225                                     
REMARK   3      L13:  -0.1983 L23:   0.5224                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0281 S12:   0.0629 S13:  -0.1005                       
REMARK   3      S21:  -0.0217 S22:   0.0969 S23:  -0.1273                       
REMARK   3      S31:  -0.0287 S32:  -0.0575 S33:  -0.0688                       
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):  17.0940  47.6610  -3.9330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1069 T22:   0.0143                                     
REMARK   3      T33:   0.0254 T12:   0.0199                                     
REMARK   3      T13:  -0.0416 T23:  -0.0013                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1098 L22:   4.5601                                     
REMARK   3      L33:   0.7697 L12:   2.5091                                     
REMARK   3      L13:  -0.1117 L23:  -0.4421                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1259 S12:   0.1510 S13:   0.1301                       
REMARK   3      S21:  -0.1272 S22:   0.0340 S23:   0.1935                       
REMARK   3      S31:  -0.2405 S32:  -0.0330 S33:   0.0918                       
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):  34.2510  55.4200   0.8650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0912 T22:   0.0967                                     
REMARK   3      T33:   0.1207 T12:  -0.0315                                     
REMARK   3      T13:  -0.0197 T23:  -0.0222                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2773 L22:   5.9641                                     
REMARK   3      L33:   6.5103 L12:  -1.0178                                     
REMARK   3      L13:  -1.1250 L23:   0.7914                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0143 S12:  -0.1782 S13:   0.1418                       
REMARK   3      S21:   0.1083 S22:   0.1139 S23:  -0.7742                       
REMARK   3      S31:   0.0104 S32:   0.7300 S33:  -0.1282                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5T8O 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_1000213322.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-MAR-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               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
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 : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34595                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.410                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.890                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.41                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06                     
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       22.73500            
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       34.10250            
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       11.36750            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     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     VAL A   333                                                      
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     PRO A   545                                                      
REMARK 465     ASP A   546                                                      
REMARK 465     GLY A   547                                                      
REMARK 465     LEU A   548                                                      
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 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    ASP A 517       54.81   -164.31                                   
REMARK 500    ASP A 536       70.22     59.89                                   
REMARK 500    TRP A 598      -24.95     71.25                                   
REMARK 500    ARG A 603      -51.81   -138.35                                   
REMARK 500    PRO A 605      119.92    -32.68                                   
REMARK 500    PRO A 616       43.86    -81.42                                   
REMARK 500    ASP B 392       61.25     37.98                                   
REMARK 500    ASP B 517       52.17   -168.86                                   
REMARK 500    ASP B 536       69.96     60.16                                   
REMARK 500    PRO B 545      -63.90     -7.19                                   
REMARK 500    ASP B 546       36.98    -92.90                                   
REMARK 500    ASP B 576     -161.79   -129.71                                   
REMARK 500    TRP B 598      -24.88     79.35                                   
REMARK 500    PRO B 616       47.36    -80.13                                   
REMARK 500    LYS B 668      -73.25   -107.50                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU A  543     GLN A  544                  149.41                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 942        DISTANCE =  6.65 ANGSTROMS                       
REMARK 525    HOH A 943        DISTANCE =  7.24 ANGSTROMS                       
REMARK 525    HOH B 939        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH B 940        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH B 941        DISTANCE =  6.19 ANGSTROMS                       
REMARK 525    HOH B 942        DISTANCE =  7.10 ANGSTROMS                       
REMARK 525    HOH B 943        DISTANCE =  9.35 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 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 A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 76Z A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 76Z B 704                 
DBREF  5T8O A  329   675  UNP    Q9WUL6   M3K14_MOUSE    329    675             
DBREF  5T8O B  329   675  UNP    Q9WUL6   M3K14_MOUSE    329    675             
SEQADV 5T8O GLY A  327  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 5T8O SER A  328  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 5T8O GLY B  327  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 5T8O 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    SO4  A 701       5                                                       
HET    SO4  A 702       5                                                       
HET    SO4  A 703       5                                                       
HET    SO4  A 704       5                                                       
HET    76Z  A 705      23                                                       
HET    SO4  B 701       5                                                       
HET    SO4  B 702       5                                                       
HET    SO4  B 703       5                                                       
HET    76Z  B 704      23                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     76Z 10-(3-METHYL-3-OXIDANYL-BUT-1-YNYL)-5,6-                         
HETNAM   2 76Z  DIHYDROIMIDAZO[1,2-D][1,4]BENZOXAZEPINE-2-CARBOXAMIDE           
FORMUL   3  SO4    7(O4 S 2-)                                                   
FORMUL   7  76Z    2(C17 H17 N3 O3)                                             
FORMUL  12  HOH   *286(H2 O)                                                    
HELIX    1 AA1 PRO A  334  GLN A  344  1                                  11    
HELIX    2 AA2 GLN A  351  SER A  363  1                                  13    
HELIX    3 AA3 GLU A  436  ARG A  439  5                                   4    
HELIX    4 AA4 VAL A  440  ALA A  445  1                                   6    
HELIX    5 AA5 SER A  478  GLY A  487  1                                  10    
HELIX    6 AA6 PRO A  490  ARG A  511  1                                  22    
HELIX    7 AA7 LYS A  519  ASP A  521  5                                   3    
HELIX    8 AA8 THR A  561  MET A  565  5                                   5    
HELIX    9 AA9 ALA A  566  MET A  571  1                                   6    
HELIX   10 AB1 LYS A  578  GLY A  594  1                                  17    
HELIX   11 AB2 PRO A  605  GLU A  613  1                                   9    
HELIX   12 AB3 PRO A  616  ILE A  620  5                                   5    
HELIX   13 AB4 ALA A  625  LEU A  636  1                                  12    
HELIX   14 AB5 GLU A  639  ARG A  643  5                                   5    
HELIX   15 AB6 SER A  645  VAL A  660  1                                  16    
HELIX   16 AB7 VAL B  335  GLN B  344  1                                  10    
HELIX   17 AB8 GLN B  351  THR B  361  1                                  11    
HELIX   18 AB9 GLU B  436  ARG B  439  5                                   4    
HELIX   19 AC1 VAL B  440  ALA B  445  1                                   6    
HELIX   20 AC2 SER B  478  GLY B  487  1                                  10    
HELIX   21 AC3 PRO B  490  ARG B  511  1                                  22    
HELIX   22 AC4 LYS B  519  ASP B  521  5                                   3    
HELIX   23 AC5 THR B  561  MET B  565  5                                   5    
HELIX   24 AC6 ALA B  566  MET B  571  1                                   6    
HELIX   25 AC7 ALA B  577  GLY B  594  1                                  18    
HELIX   26 AC8 PRO B  605  GLU B  613  1                                   9    
HELIX   27 AC9 PRO B  616  ILE B  620  5                                   5    
HELIX   28 AD1 ALA B  625  LEU B  636  1                                  12    
HELIX   29 AD2 SER B  645  VAL B  660  1                                  16    
SHEET    1 AA1 7 VAL A 347  SER A 349  0                                        
SHEET    2 AA1 7 GLU A 380  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  PHE A 470   N  GLY A 459           
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  HIS A 417   O  VAL A 430           
SHEET    7 AA1 7 TRP A 401  THR A 403 -1  N  MET A 402   O  LYS A 420           
SHEET    1 AA2 2 ILE A 513  LEU A 514  0                                        
SHEET    2 AA2 2 LEU A 541  CYS A 542 -1  O  LEU A 541   N  LEU A 514           
SHEET    1 AA3 2 VAL A 523  LEU A 525  0                                        
SHEET    2 AA3 2 ALA A 532  LEU A 534 -1  O  ALA A 533   N  LEU A 524           
SHEET    1 AA4 2 LYS A 550  SER A 551  0                                        
SHEET    2 AA4 2 PRO A 574  CYS A 575 -1  O  CYS A 575   N  LYS A 550           
SHEET    1 AA5 7 VAL B 347  SER B 349  0                                        
SHEET    2 AA5 7 ASN B 379  LEU B 383  1  O  LEU B 383   N  SER B 348           
SHEET    3 AA5 7 LEU B 457  GLU B 463 -1  O  ARG B 462   N  GLU B 380           
SHEET    4 AA5 7 TRP B 466  MET B 471 -1  O  ASN B 468   N  VAL B 461           
SHEET    5 AA5 7 GLN B 427  ARG B 434 -1  N  ALA B 429   O  MET B 471           
SHEET    6 AA5 7 VAL B 416  ASP B 421 -1  N  HIS B 417   O  VAL B 430           
SHEET    7 AA5 7 TRP B 401  THR B 403 -1  N  MET B 402   O  LYS B 420           
SHEET    1 AA6 2 ILE B 513  LEU B 514  0                                        
SHEET    2 AA6 2 LEU B 541  CYS B 542 -1  O  LEU B 541   N  LEU B 514           
SHEET    1 AA7 2 VAL B 523  LEU B 525  0                                        
SHEET    2 AA7 2 ALA B 532  LEU B 534 -1  O  ALA B 533   N  LEU B 524           
SHEET    1 AA8 2 LYS B 550  SER B 551  0                                        
SHEET    2 AA8 2 PRO B 574  CYS B 575 -1  O  CYS B 575   N  LYS B 550           
CISPEP   1 GLN A  405    PRO A  406          0         0.28                     
CISPEP   2 GLN B  405    PRO B  406          0        -2.77                     
SITE     1 AC1  3 ARG A 637  LYS A 638  GLU A 639                               
SITE     1 AC2  7 ARG A 410  GLY A 411  SER A 478  GLN A 481                    
SITE     2 AC2  7 76Z A 705  HOH A 830  HOH B 861                               
SITE     1 AC3  2 ARG A 650  ARG A 651                                          
SITE     1 AC4  5 LYS A 519  HIS A 596  GLY B 350  GLN B 351                    
SITE     2 AC4  5 HOH B 816                                                     
SITE     1 AC5 14 GLY A 411  VAL A 416  ALA A 429  GLU A 442                    
SITE     2 AC5 14 VAL A 455  ILE A 469  MET A 471  GLU A 472                    
SITE     3 AC5 14 LEU A 473  LEU A 474  LEU A 524  ASP A 536                    
SITE     4 AC5 14 PHE A 537  SO4 A 702                                          
SITE     1 AC6  4 GLY A 350  GLN A 351  LYS B 519  HIS B 596                    
SITE     1 AC7  5 ARG B 637  LYS B 638  GLU B 639  HIS B 642                    
SITE     2 AC7  5 HOH B 860                                                     
SITE     1 AC8  4 ARG B 410  GLY B 411  GLN B 481  76Z B 704                    
SITE     1 AC9 14 ARG B 410  GLY B 411  VAL B 416  ALA B 429                    
SITE     2 AC9 14 GLU B 442  ILE B 469  MET B 471  GLU B 472                    
SITE     3 AC9 14 LEU B 473  LEU B 474  LEU B 524  ASP B 536                    
SITE     4 AC9 14 PHE B 537  SO4 B 703                                          
CRYST1  143.950  143.950   45.470  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      0.006947  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006947  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021993        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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