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Database: PDB
Entry: 4G3E
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Original site: 4G3E 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       13-JUL-12   4G3E              
TITLE     CRYSTAL STRUCTURE OF MURINE NF-KAPPAB INDUCING KINASE (NIK) BOUND TO A
TITLE    2 6-ALKYNYLINDOLINE (CMP1)                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NF-KAPPA-BETA-INDUCING KINASE;                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: SERINE/THREONINE-PROTEIN KINASE NIK;                        
COMPND   5 EC: 2.7.11.25;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: MAP3K14, NF-KAPPAB INDUCING KINASE, NIK;                       
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS TRANSFER VECTOR;          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PACGP67                                   
KEYWDS    NON-RD KINASE, PROTEIN SERINE/THREONINE KINASE, NF-KAPPAB, STRUCTURE- 
KEYWDS   2 BASED DRUG DESIGN, MAP3K14, TRANSFERASE, TRANSFERASE-TRANSFERASE     
KEYWDS   3 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.G.HYMOWITZ,G.DE LEON-BOENIG                                         
REVDAT   3   24-JAN-18 4G3E    1       AUTHOR REMARK                            
REVDAT   2   23-JAN-13 4G3E    1       JRNL                                     
REVDAT   1   15-AUG-12 4G3E    0                                                
JRNL        AUTH   G.DE LEON-BOENIG,K.K.BOWMAN,J.A.FENG,T.CRAWFORD,C.EVERETT,   
JRNL        AUTH 2 Y.FRANKE,A.OH,M.STANLEY,S.T.STABEN,M.A.STAROVASNIK,          
JRNL        AUTH 3 H.J.WALLWEBER,J.WU,L.C.WU,A.R.JOHNSON,S.G.HYMOWITZ           
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF THE         
JRNL        TITL 2 NF-KAPPAB INDUCING KINASE REVEALS A NARROW BUT FLEXIBLE      
JRNL        TITL 3 ACTIVE SITE.                                                 
JRNL        REF    STRUCTURE                     V.  20  1704 2012              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   22921830                                                     
JRNL        DOI    10.1016/J.STR.2012.07.013                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.73                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 32110                          
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) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 3259                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 25                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1574                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.14                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2950                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 163                          
REMARK   3   BIN FREE R VALUE                    : 0.3650                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4956                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 69                                      
REMARK   3   SOLVENT ATOMS            : 61                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.28000                                             
REMARK   3    B22 (A**2) : -0.28000                                             
REMARK   3    B33 (A**2) : 0.57000                                              
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): 0.381         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.262         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.190         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.602        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.913                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5150 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6969 ; 1.224 ; 1.992       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   634 ; 5.697 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   212 ;38.370 ;23.443       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   892 ;16.331 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    37 ;18.466 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   748 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3858 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   334        A   472                          
REMARK   3    ORIGIN FOR THE GROUP (A):  46.3999  40.0639  -3.0370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0576 T22:   0.0915                                     
REMARK   3      T33:   0.2102 T12:   0.0679                                     
REMARK   3      T13:   0.0136 T23:   0.0208                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0346 L22:   5.4137                                     
REMARK   3      L33:   1.6367 L12:  -0.7101                                     
REMARK   3      L13:  -1.6015 L23:   0.1059                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0670 S12:   0.0915 S13:   0.2536                       
REMARK   3      S21:  -0.0639 S22:  -0.0858 S23:  -0.2112                       
REMARK   3      S31:   0.0415 S32:  -0.0361 S33:   0.0188                       
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   473        A   671                          
REMARK   3    ORIGIN FOR THE GROUP (A):  53.0599  12.4309  -4.2842              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1887 T22:   0.0426                                     
REMARK   3      T33:   0.0170 T12:   0.0560                                     
REMARK   3      T13:   0.0378 T23:   0.0031                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7396 L22:   4.3899                                     
REMARK   3      L33:   3.9335 L12:   0.4319                                     
REMARK   3      L13:  -0.1751 L23:  -0.3596                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0918 S12:   0.1618 S13:  -0.1261                       
REMARK   3      S21:  -0.2607 S22:   0.0187 S23:  -0.2023                       
REMARK   3      S31:   0.1244 S32:   0.2347 S33:   0.0731                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   334        B   472                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.3036  67.0408   2.6789              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0089 T22:   0.0927                                     
REMARK   3      T33:   0.1800 T12:   0.0202                                     
REMARK   3      T13:  -0.0229 T23:  -0.0300                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5853 L22:   5.4904                                     
REMARK   3      L33:   2.3037 L12:   1.3026                                     
REMARK   3      L13:  -1.1479 L23:   0.6700                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1000 S12:   0.0162 S13:   0.0281                       
REMARK   3      S21:   0.0406 S22:  -0.0803 S23:  -0.2389                       
REMARK   3      S31:  -0.0432 S32:   0.0091 S33:  -0.0197                       
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   473        B   674                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.3244  42.9371   1.0622              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0810 T22:   0.1124                                     
REMARK   3      T33:   0.0546 T12:  -0.0391                                     
REMARK   3      T13:  -0.0290 T23:   0.0435                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4109 L22:   4.1307                                     
REMARK   3      L33:   4.7559 L12:   0.1693                                     
REMARK   3      L13:   0.5093 L23:   0.4486                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2121 S12:   0.0146 S13:  -0.1720                       
REMARK   3      S21:   0.0469 S22:  -0.0633 S23:  -0.0196                       
REMARK   3      S31:   0.4816 S32:   0.0103 S33:  -0.1488                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4G3E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000073687.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAY-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97946                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32116                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.59800                            
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: APO MURINE NIK KINASE DOMAIN                         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2UL PROTEIN WITH 2UL WELL SOLUTION OF    
REMARK 280  0.5 M AMMONIUM SULFATE, 0.9 M LITHIUM SULFATE,0.1M SODIUM           
REMARK 280  CITRATE TRIBASIC DIHYDRATE THEN SOAKED IN WELL SOLUTION WITH 1      
REMARK 280  MM CMP1, PH 6.2, VAPOR 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       22.57550            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       33.86325            
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       11.28775            
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 A   549                                                      
REMARK 465     LYS A   550                                                      
REMARK 465     SER A   551                                                      
REMARK 465     LEU A   552                                                      
REMARK 465     LEU A   553                                                      
REMARK 465     THR A   554                                                      
REMARK 465     GLY A   555                                                      
REMARK 465     ASP A   556                                                      
REMARK 465     TYR A   557                                                      
REMARK 465     ARG A   603                                                      
REMARK 465     GLY A   676                                                      
REMARK 465     ASN A   677                                                      
REMARK 465     SER A   678                                                      
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 465     TYR B   601                                                      
REMARK 465     PHE B   602                                                      
REMARK 465     ARG B   603                                                      
REMARK 465     GLY B   676                                                      
REMARK 465     ASN B   677                                                      
REMARK 465     SER B   678                                                      
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    TRP A 362       31.68    -82.69                                   
REMARK 500    VAL A 399      -50.10   -125.00                                   
REMARK 500    GLN A 405      -76.73    -45.85                                   
REMARK 500    ARG A 407       95.31    -64.99                                   
REMARK 500    CYS A 428     -155.23   -144.04                                   
REMARK 500    CYS A 446      -49.34    178.15                                   
REMARK 500    ASP A 517       50.26   -150.78                                   
REMARK 500    ASP A 536       82.98     63.15                                   
REMARK 500    ASP A 576     -168.44   -129.94                                   
REMARK 500    TRP A 598      -19.75     73.53                                   
REMARK 500    PRO A 616       35.58    -73.86                                   
REMARK 500    LYS A 668       76.68   -119.85                                   
REMARK 500    GLN B 405     -132.19     25.31                                   
REMARK 500    CYS B 428     -157.25   -143.92                                   
REMARK 500    ASP B 517       52.08   -150.72                                   
REMARK 500    ASP B 536       90.15     70.18                                   
REMARK 500    PRO B 545       27.95    -70.29                                   
REMARK 500    ASP B 546      -10.96   -146.77                                   
REMARK 500    ASP B 576     -166.40   -128.99                                   
REMARK 500    PRO B 616       37.85    -70.55                                   
REMARK 500    LYS B 668     -119.47   -122.83                                   
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 GLN B  405     PRO B  406                  149.04                    
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 0WC A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0WC B 702                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4G3C   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4G3D   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4G3F   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4G3G   RELATED DB: PDB                                   
DBREF  4G3E A  329   675  UNP    Q9WUL6   M3K14_MOUSE    329    675             
DBREF  4G3E B  329   675  UNP    Q9WUL6   M3K14_MOUSE    329    675             
SEQADV 4G3E GLY A  327  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3E SER A  328  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3E GLY A  676  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3E ASN A  677  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3E SER A  678  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3E GLY B  327  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3E SER B  328  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3E GLY B  676  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3E ASN B  677  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3E SER B  678  UNP  Q9WUL6              EXPRESSION TAG                 
SEQRES   1 A  352  GLY SER ALA LEU GLU LYS VAL PRO VAL GLU GLU TYR LEU          
SEQRES   2 A  352  VAL HIS ALA LEU GLN GLY SER VAL SER SER GLY GLN ALA          
SEQRES   3 A  352  HIS SER LEU ALA SER LEU ALA LYS THR TRP SER SER GLY          
SEQRES   4 A  352  SER ALA LYS LEU GLN ARG LEU GLY PRO GLU THR GLU ASP          
SEQRES   5 A  352  ASN GLU GLY VAL LEU LEU THR GLU LYS LEU LYS PRO VAL          
SEQRES   6 A  352  ASP TYR GLU TYR ARG GLU GLU VAL HIS TRP MET THR HIS          
SEQRES   7 A  352  GLN PRO ARG VAL GLY ARG GLY SER PHE GLY GLU VAL HIS          
SEQRES   8 A  352  ARG MET LYS ASP LYS GLN THR GLY PHE GLN CYS ALA VAL          
SEQRES   9 A  352  LYS LYS VAL ARG LEU GLU VAL PHE ARG VAL GLU GLU LEU          
SEQRES  10 A  352  VAL ALA CYS ALA GLY LEU SER SER PRO ARG ILE VAL PRO          
SEQRES  11 A  352  LEU TYR GLY ALA VAL ARG GLU GLY PRO TRP VAL ASN ILE          
SEQRES  12 A  352  PHE MET GLU LEU LEU GLU GLY GLY SER LEU GLY GLN LEU          
SEQRES  13 A  352  ILE LYS GLN MET GLY CYS LEU PRO GLU ASP ARG ALA LEU          
SEQRES  14 A  352  TYR TYR LEU GLY GLN ALA LEU GLU GLY LEU GLU TYR LEU          
SEQRES  15 A  352  HIS THR ARG ARG ILE LEU HIS GLY ASP VAL LYS ALA ASP          
SEQRES  16 A  352  ASN VAL LEU LEU SER SER ASP GLY SER ARG ALA ALA LEU          
SEQRES  17 A  352  CYS ASP PHE GLY HIS ALA LEU CYS LEU GLN PRO ASP GLY          
SEQRES  18 A  352  LEU GLY LYS SER LEU LEU THR GLY ASP TYR ILE PRO GLY          
SEQRES  19 A  352  THR GLU THR HIS MET ALA PRO GLU VAL VAL MET GLY LYS          
SEQRES  20 A  352  PRO CYS ASP ALA LYS VAL ASP ILE TRP SER SER CYS CYS          
SEQRES  21 A  352  MET MET LEU HIS MET LEU ASN GLY CYS HIS PRO TRP THR          
SEQRES  22 A  352  GLN TYR PHE ARG GLY PRO LEU CYS LEU LYS ILE ALA SER          
SEQRES  23 A  352  GLU PRO PRO PRO ILE ARG GLU ILE PRO PRO SER CYS ALA          
SEQRES  24 A  352  PRO LEU THR ALA GLN ALA ILE GLN GLU GLY LEU ARG LYS          
SEQRES  25 A  352  GLU PRO VAL HIS ARG ALA SER ALA MET GLU LEU ARG ARG          
SEQRES  26 A  352  LYS VAL GLY LYS ALA LEU GLN GLU VAL GLY GLY LEU LYS          
SEQRES  27 A  352  SER PRO TRP LYS GLY GLU TYR LYS GLU PRO ARG GLY ASN          
SEQRES  28 A  352  SER                                                          
SEQRES   1 B  352  GLY SER ALA LEU GLU LYS VAL PRO VAL GLU GLU TYR LEU          
SEQRES   2 B  352  VAL HIS ALA LEU GLN GLY SER VAL SER SER GLY GLN ALA          
SEQRES   3 B  352  HIS SER LEU ALA SER LEU ALA LYS THR TRP SER SER GLY          
SEQRES   4 B  352  SER ALA LYS LEU GLN ARG LEU GLY PRO GLU THR GLU ASP          
SEQRES   5 B  352  ASN GLU GLY VAL LEU LEU THR GLU LYS LEU LYS PRO VAL          
SEQRES   6 B  352  ASP TYR GLU TYR ARG GLU GLU VAL HIS TRP MET THR HIS          
SEQRES   7 B  352  GLN PRO ARG VAL GLY ARG GLY SER PHE GLY GLU VAL HIS          
SEQRES   8 B  352  ARG MET LYS ASP LYS GLN THR GLY PHE GLN CYS ALA VAL          
SEQRES   9 B  352  LYS LYS VAL ARG LEU GLU VAL PHE ARG VAL GLU GLU LEU          
SEQRES  10 B  352  VAL ALA CYS ALA GLY LEU SER SER PRO ARG ILE VAL PRO          
SEQRES  11 B  352  LEU TYR GLY ALA VAL ARG GLU GLY PRO TRP VAL ASN ILE          
SEQRES  12 B  352  PHE MET GLU LEU LEU GLU GLY GLY SER LEU GLY GLN LEU          
SEQRES  13 B  352  ILE LYS GLN MET GLY CYS LEU PRO GLU ASP ARG ALA LEU          
SEQRES  14 B  352  TYR TYR LEU GLY GLN ALA LEU GLU GLY LEU GLU TYR LEU          
SEQRES  15 B  352  HIS THR ARG ARG ILE LEU HIS GLY ASP VAL LYS ALA ASP          
SEQRES  16 B  352  ASN VAL LEU LEU SER SER ASP GLY SER ARG ALA ALA LEU          
SEQRES  17 B  352  CYS ASP PHE GLY HIS ALA LEU CYS LEU GLN PRO ASP GLY          
SEQRES  18 B  352  LEU GLY LYS SER LEU LEU THR GLY ASP TYR ILE PRO GLY          
SEQRES  19 B  352  THR GLU THR HIS MET ALA PRO GLU VAL VAL MET GLY LYS          
SEQRES  20 B  352  PRO CYS ASP ALA LYS VAL ASP ILE TRP SER SER CYS CYS          
SEQRES  21 B  352  MET MET LEU HIS MET LEU ASN GLY CYS HIS PRO TRP THR          
SEQRES  22 B  352  GLN TYR PHE ARG GLY PRO LEU CYS LEU LYS ILE ALA SER          
SEQRES  23 B  352  GLU PRO PRO PRO ILE ARG GLU ILE PRO PRO SER CYS ALA          
SEQRES  24 B  352  PRO LEU THR ALA GLN ALA ILE GLN GLU GLY LEU ARG LYS          
SEQRES  25 B  352  GLU PRO VAL HIS ARG ALA SER ALA MET GLU LEU ARG ARG          
SEQRES  26 B  352  LYS VAL GLY LYS ALA LEU GLN GLU VAL GLY GLY LEU LYS          
SEQRES  27 B  352  SER PRO TRP LYS GLY GLU TYR LYS GLU PRO ARG GLY ASN          
SEQRES  28 B  352  SER                                                          
HET    SO4  A 701       5                                                       
HET    SO4  A 702       5                                                       
HET    0WC  A 703      27                                                       
HET    SO4  B 701       5                                                       
HET    0WC  B 702      27                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     0WC (2R)-4-[1-(2-AMINO-5-CHLOROPYRIMIDIN-4-YL)-2,3-DIHYDRO-          
HETNAM   2 0WC  1H-INDOL-6-YL]-2-(1,3-THIAZOL-2-YL)BUT-3-YN-2-OL                
FORMUL   3  SO4    3(O4 S 2-)                                                   
FORMUL   5  0WC    2(C19 H16 CL N5 O S)                                         
FORMUL   8  HOH   *61(H2 O)                                                     
HELIX    1   1 PRO A  334  GLN A  344  1                                  11    
HELIX    2   2 GLN A  351  LYS A  360  1                                  10    
HELIX    3   3 GLU A  436  PHE A  438  5                                   3    
HELIX    4   4 ARG A  439  ALA A  445  1                                   7    
HELIX    5   5 SER A  478  GLY A  487  1                                  10    
HELIX    6   6 PRO A  490  ARG A  511  1                                  22    
HELIX    7   7 LYS A  519  ASP A  521  5                                   3    
HELIX    8   8 THR A  561  MET A  565  5                                   5    
HELIX    9   9 ALA A  566  MET A  571  1                                   6    
HELIX   10  10 ALA A  577  GLY A  594  1                                  18    
HELIX   11  11 PRO A  605  GLU A  613  1                                   9    
HELIX   12  12 PRO A  615  ILE A  620  5                                   6    
HELIX   13  13 ALA A  625  LEU A  636  1                                  12    
HELIX   14  14 GLU A  639  ARG A  643  5                                   5    
HELIX   15  15 SER A  645  VAL A  660  1                                  16    
HELIX   16  16 VAL B  335  GLN B  344  1                                  10    
HELIX   17  17 GLN B  351  LYS B  360  1                                  10    
HELIX   18  18 THR B  361  SER B  363  5                                   3    
HELIX   19  19 GLU B  436  ARG B  439  5                                   4    
HELIX   20  20 VAL B  440  ALA B  445  1                                   6    
HELIX   21  21 SER B  478  GLY B  487  1                                  10    
HELIX   22  22 PRO B  490  ARG B  511  1                                  22    
HELIX   23  23 LYS B  519  ASP B  521  5                                   3    
HELIX   24  24 THR B  561  MET B  565  5                                   5    
HELIX   25  25 ALA B  566  MET B  571  1                                   6    
HELIX   26  26 ALA B  577  GLY B  594  1                                  18    
HELIX   27  27 PRO B  605  GLU B  613  1                                   9    
HELIX   28  28 PRO B  615  ILE B  620  5                                   6    
HELIX   29  29 ALA B  625  LEU B  636  1                                  12    
HELIX   30  30 SER B  645  VAL B  660  1                                  16    
SHEET    1   A 7 VAL A 347  SER A 349  0                                        
SHEET    2   A 7 ASN A 379  LEU A 383  1  O  LEU A 383   N  SER A 348           
SHEET    3   A 7 LEU A 457  GLU A 463 -1  O  ARG A 462   N  GLU A 380           
SHEET    4   A 7 TRP A 466  MET A 471 -1  O  ASN A 468   N  VAL A 461           
SHEET    5   A 7 GLN A 427  ARG A 434 -1  N  LYS A 431   O  ILE A 469           
SHEET    6   A 7 VAL A 416  ASP A 421 -1  N  MET A 419   O  CYS A 428           
SHEET    7   A 7 TRP A 401  THR A 403 -1  N  MET A 402   O  LYS A 420           
SHEET    1   B 2 ILE A 513  LEU A 514  0                                        
SHEET    2   B 2 LEU A 541  CYS A 542 -1  O  LEU A 541   N  LEU A 514           
SHEET    1   C 2 VAL A 523  LEU A 525  0                                        
SHEET    2   C 2 ALA A 532  LEU A 534 -1  O  ALA A 533   N  LEU A 524           
SHEET    1   D 7 VAL B 347  SER B 349  0                                        
SHEET    2   D 7 ASN B 379  LEU B 383  1  O  GLY B 381   N  SER B 348           
SHEET    3   D 7 LEU B 457  GLU B 463 -1  O  ARG B 462   N  GLU B 380           
SHEET    4   D 7 TRP B 466  MET B 471 -1  O  PHE B 470   N  TYR B 458           
SHEET    5   D 7 GLN B 427  ARG B 434 -1  N  VAL B 433   O  VAL B 467           
SHEET    6   D 7 VAL B 416  ASP B 421 -1  N  MET B 419   O  CYS B 428           
SHEET    7   D 7 TRP B 401  THR B 403 -1  N  MET B 402   O  LYS B 420           
SHEET    1   E 2 ILE B 513  LEU B 514  0                                        
SHEET    2   E 2 LEU B 541  CYS B 542 -1  O  LEU B 541   N  LEU B 514           
SHEET    1   F 2 VAL B 523  LEU B 525  0                                        
SHEET    2   F 2 ALA B 532  LEU B 534 -1  O  ALA B 533   N  LEU B 524           
SITE     1 AC1  3 MET A 647  ARG A 650  ARG A 651                               
SITE     1 AC2  4 ARG A 637  LYS A 638  GLU A 639  HIS A 642                    
SITE     1 AC3 14 ARG A 410  VAL A 416  ALA A 429  GLU A 442                    
SITE     2 AC3 14 VAL A 455  ILE A 469  MET A 471  GLU A 472                    
SITE     3 AC3 14 LEU A 474  GLN A 481  LEU A 524  CYS A 535                    
SITE     4 AC3 14 ASP A 536  PHE A 537                                          
SITE     1 AC4  4 ARG B 637  LYS B 638  GLU B 639  HIS B 642                    
SITE     1 AC5 16 ARG B 410  GLY B 411  VAL B 416  ALA B 429                    
SITE     2 AC5 16 LYS B 431  GLU B 442  VAL B 455  ILE B 469                    
SITE     3 AC5 16 MET B 471  GLU B 472  LEU B 474  GLN B 481                    
SITE     4 AC5 16 LEU B 524  CYS B 535  ASP B 536  PHE B 537                    
CRYST1  143.145  143.145   45.151  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      0.006986  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006986  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022148        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2  0.732896 -0.680151 -0.016050       69.10763    1                    
MTRIX2   2  0.680038  0.733070 -0.012527      -30.25893    1                    
MTRIX3   2  0.020286 -0.001733  0.999793       -6.31223    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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