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Database: PDB
Entry: 5T8Q
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Original site: 5T8Q 
HEADER    TRANSFERASE                             08-SEP-16   5T8Q              
TITLE     CRYSTAL STRUCTURE OF MURINE NF-KAPPAB INDUCING KINASE (NIK) BOUND TO  
TITLE    2 ARYL PYRROLE FRAGMENT 17                                             
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.A.MCEWAN,S.G.HYMOWITZ                                     
REVDAT   3   08-FEB-17 5T8Q    1       JRNL                                     
REVDAT   2   25-JAN-17 5T8Q    1       JRNL                                     
REVDAT   1   11-JAN-17 5T8Q    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.    2.63 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) : 2.63                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.79                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 25565                          
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.400                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 2953                            
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) : 2.63                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.70                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1606                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.04                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 190                          
REMARK   3   BIN FREE R VALUE                    : 0.3920                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5060                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 87                                      
REMARK   3   SOLVENT ATOMS            : 71                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.94                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.07000                                             
REMARK   3    B22 (A**2) : -0.07000                                             
REMARK   3    B33 (A**2) : 0.14000                                              
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): 0.576         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.310         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.212         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.781        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5273 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5134 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7138 ; 1.601 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11723 ; 0.999 ; 3.004       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   650 ; 6.831 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   219 ;36.644 ;23.379       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   907 ;16.946 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    38 ;15.353 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   769 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5834 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1160 ; 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):  2603 ; 1.334 ; 3.545       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2602 ; 1.328 ; 3.543       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3246 ; 2.240 ; 5.311       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3247 ; 2.240 ; 5.313       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2670 ; 1.510 ; 3.784       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2671 ; 1.510 ; 3.784       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3891 ; 2.389 ; 5.615       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5678 ; 5.002 ;28.077       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5679 ; 5.001 ;28.080       
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):  28.4033  27.7455  -0.7572              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0558 T22:   0.0883                                     
REMARK   3      T33:   0.1074 T12:  -0.0047                                     
REMARK   3      T13:   0.0521 T23:  -0.0699                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3247 L22:   5.5868                                     
REMARK   3      L33:   2.9261 L12:  -0.4944                                     
REMARK   3      L13:   0.1759 L23:  -0.8515                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0018 S12:   0.0512 S13:  -0.0528                       
REMARK   3      S21:  -0.0446 S22:  -0.0530 S23:   0.1247                       
REMARK   3      S31:   0.1312 S32:  -0.1197 S33:   0.0548                       
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):  21.9084  44.7762   1.6083              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1369 T22:   0.1136                                     
REMARK   3      T33:   0.0751 T12:  -0.0362                                     
REMARK   3      T13:   0.0878 T23:  -0.0351                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0790 L22:   5.7196                                     
REMARK   3      L33:   0.5248 L12:  -0.5798                                     
REMARK   3      L13:   0.5281 L23:   0.0459                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0584 S12:  -0.0105 S13:   0.0158                       
REMARK   3      S21:  -0.0669 S22:   0.0946 S23:  -0.0648                       
REMARK   3      S31:  -0.1189 S32:   0.1455 S33:  -0.0362                       
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):  16.3476  62.3654  -5.1852              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2095 T22:   0.0357                                     
REMARK   3      T33:   0.1866 T12:  -0.0265                                     
REMARK   3      T13:   0.0719 T23:   0.0117                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8202 L22:   4.8633                                     
REMARK   3      L33:   5.5018 L12:   1.1747                                     
REMARK   3      L13:   0.8831 L23:   0.5602                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3528 S12:   0.2782 S13:   0.2585                       
REMARK   3      S21:  -0.4827 S22:   0.1549 S23:   0.2251                       
REMARK   3      S31:  -0.2138 S32:  -0.2062 S33:   0.1980                       
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):  40.0311  -0.3996   5.0915              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0049 T22:   0.0943                                     
REMARK   3      T33:   0.0626 T12:   0.0085                                     
REMARK   3      T13:  -0.0058 T23:  -0.0700                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5520 L22:   5.5754                                     
REMARK   3      L33:   4.5827 L12:  -0.5588                                     
REMARK   3      L13:  -0.6300 L23:  -0.1520                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0777 S12:   0.1369 S13:   0.0615                       
REMARK   3      S21:  -0.1178 S22:  -0.0296 S23:   0.1098                       
REMARK   3      S31:   0.0542 S32:  -0.0293 S33:  -0.0482                       
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):  47.8813  16.3927   5.9395              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0792 T22:   0.2051                                     
REMARK   3      T33:   0.0871 T12:   0.0026                                     
REMARK   3      T13:   0.0445 T23:  -0.0627                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5197 L22:   3.7325                                     
REMARK   3      L33:   0.8861 L12:   1.9404                                     
REMARK   3      L13:   0.0849 L23:  -0.4619                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0736 S12:   0.0376 S13:   0.1333                       
REMARK   3      S21:  -0.0703 S22:  -0.0436 S23:  -0.1032                       
REMARK   3      S31:  -0.0722 S32:   0.3202 S33:  -0.0301                       
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):  55.1887  33.3636   1.1019              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1430 T22:   0.1279                                     
REMARK   3      T33:   0.3270 T12:  -0.0546                                     
REMARK   3      T13:   0.1292 T23:  -0.0774                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3313 L22:   3.7110                                     
REMARK   3      L33:   6.1008 L12:  -0.2687                                     
REMARK   3      L13:  -0.5227 L23:   0.2444                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0973 S12:   0.0329 S13:   0.6892                       
REMARK   3      S21:   0.0340 S22:  -0.1801 S23:   0.0329                       
REMARK   3      S31:  -0.6178 S32:   0.0515 S33:   0.0828                       
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 5T8Q 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_1000213323.                                   
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                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9173                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28412                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.630                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.790                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.63                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.66000                            
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: 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   (%): 63.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33                     
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       23.22750            
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       34.84125            
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       11.61375            
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     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     ASP A   546                                                      
REMARK 465     GLY A   547                                                      
REMARK 465     LEU A   548                                                      
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     SER A 551    OG                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP A   392     NH2  ARG B   407              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 418   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG B 407   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    CYS B 446   CA  -  CB  -  SG  ANGL. DEV. =   6.9 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    VAL A 399      -58.45   -123.32                                   
REMARK 500    ASP A 517       58.99   -164.25                                   
REMARK 500    SER A 526      170.25    -59.60                                   
REMARK 500    ASP A 536       94.38     73.75                                   
REMARK 500    LEU A 552      -46.58     79.86                                   
REMARK 500    TRP A 598      -31.24     76.56                                   
REMARK 500    PRO A 605      103.22    -45.40                                   
REMARK 500    LYS A 668       72.28   -113.16                                   
REMARK 500    VAL B 440      -39.51    -34.05                                   
REMARK 500    ALA B 445      -70.31    -62.56                                   
REMARK 500    ASP B 517       60.91   -157.43                                   
REMARK 500    ASP B 536       96.91     64.87                                   
REMARK 500    GLN B 544      161.65    -44.93                                   
REMARK 500    ASP B 576     -168.72   -128.53                                   
REMARK 500    THR B 599       71.32   -108.08                                   
REMARK 500    GLN B 600     -167.29   -102.09                                   
REMARK 500    PHE B 602       61.66   -111.57                                   
REMARK 500    PRO B 616       34.80    -81.60                                   
REMARK 500    PRO B 674     -170.77    -67.44                                   
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 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 SO4 A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 76Y A 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 76Y B 707                 
DBREF  5T8Q A  329   675  UNP    Q9WUL6   M3K14_MOUSE    329    675             
DBREF  5T8Q B  329   675  UNP    Q9WUL6   M3K14_MOUSE    329    675             
SEQADV 5T8Q GLY A  327  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 5T8Q SER A  328  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 5T8Q GLY B  327  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 5T8Q 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    SO4  A 705       5                                                       
HET    76Y  A 706      16                                                       
HET    SO4  B 701       5                                                       
HET    SO4  B 702       5                                                       
HET    SO4  B 703       5                                                       
HET    SO4  B 704       5                                                       
HET    SO4  B 705       5                                                       
HET    SO4  B 706       5                                                       
HET    76Y  B 707      16                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     76Y 1-[(2-CHLOROPHENYL)METHYL]PYRROLE-2-CARBOXAMIDE                  
FORMUL   3  SO4    11(O4 S 2-)                                                  
FORMUL   8  76Y    2(C12 H11 CL N2 O)                                           
FORMUL  16  HOH   *71(H2 O)                                                     
HELIX    1 AA1 VAL A  335  GLN A  344  1                                  10    
HELIX    2 AA2 GLN A  351  THR A  361  1                                  11    
HELIX    3 AA3 GLU A  436  ARG A  439  5                                   4    
HELIX    4 AA4 VAL A  440  ALA A  447  1                                   8    
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 ALA A  577  GLY A  594  1                                  18    
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 LEU B  479  GLY B  487  1                                   9    
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  GLY B  572  1                                   7    
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  615  ILE B  620  5                                   6    
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 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  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 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  PHE B 470   N  TYR B 458           
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  HIS B 417   O  VAL B 430           
SHEET    7 AA4 7 TRP B 401  THR B 403 -1  N  MET B 402   O  LYS B 420           
SHEET    1 AA5 3 GLY B 477  SER B 478  0                                        
SHEET    2 AA5 3 VAL B 523  LEU B 525 -1  O  LEU B 525   N  GLY B 477           
SHEET    3 AA5 3 ALA B 532  LEU B 534 -1  O  ALA B 533   N  LEU B 524           
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 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           
CISPEP   1 GLN A  405    PRO A  406          0        -0.59                     
CISPEP   2 GLN B  405    PRO B  406          0        -9.78                     
SITE     1 AC1  3 ARG A 637  LYS A 638  GLU A 639                               
SITE     1 AC2  5 HIS A 404  VAL A 408  ARG A 410  ARG A 418                    
SITE     2 AC2  5 76Y A 706                                                     
SITE     1 AC3  7 CYS A 446  VAL A 455  PRO A 456  MET A 471                    
SITE     2 AC3  7 CYS A 535  ASP A 536  PHE A 537                               
SITE     1 AC4  3 THR A 385  GLU A 386  LYS B 484                               
SITE     1 AC5  2 ARG A 650  ARG A 651                                          
SITE     1 AC6  9 ARG A 410  VAL A 416  ARG A 418  MET A 471                    
SITE     2 AC6  9 GLU A 472  LEU A 473  LEU A 474  LEU A 524                    
SITE     3 AC6  9 SO4 A 702                                                     
SITE     1 AC7  4 ARG B 637  LYS B 638  GLU B 639  HIS B 642                    
SITE     1 AC8  6 CYS B 446  VAL B 455  MET B 471  CYS B 535                    
SITE     2 AC8  6 ASP B 536  PHE B 537                                          
SITE     1 AC9  4 LYS A 519  HIS A 596  GLY B 350  GLN B 351                    
SITE     1 AD1  6 GLY A 350  GLN A 351  HOH A 820  LYS B 519                    
SITE     2 AD1  6 THR B 561  HIS B 596                                          
SITE     1 AD2  2 ARG B 410  ARG B 418                                          
SITE     1 AD3  5 LYS A 484  THR B 385  GLU B 386  LYS B 387                    
SITE     2 AD3  5 HOH B 820                                                     
SITE     1 AD4  8 ARG B 410  VAL B 416  MET B 471  GLU B 472                    
SITE     2 AD4  8 LEU B 473  LEU B 474  GLU B 475  LEU B 524                    
CRYST1  143.969  143.969   46.455  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      0.006946  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006946  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021526        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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