GenomeNet

Database: PDB
Entry: 4G3C
LinkDB: 4G3C
Original site: 4G3C 
HEADER    TRANSFERASE                             13-JUL-12   4G3C              
TITLE     CRYSTAL STRUCTURE OF APO MURINE NF-KAPPAB INDUCING KINASE (NIK)       
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-KABBAB 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, MAP3K14,   
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.G.HYMOWITZ,G.DE LEON-BOENIG                                         
REVDAT   3   24-JAN-18 4G3C    1       AUTHOR                                   
REVDAT   2   23-JAN-13 4G3C    1       JRNL                                     
REVDAT   1   08-AUG-12 4G3C    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.    2.15 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) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.40                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 44453                          
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) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 5003                            
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) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.20                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2470                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.78                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2550                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 280                          
REMARK   3   BIN FREE R VALUE                    : 0.2850                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4990                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 192                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.43                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.24000                                             
REMARK   3    B22 (A**2) : -0.24000                                             
REMARK   3    B33 (A**2) : 0.49000                                              
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): 0.196         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.173         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.113         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.892         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
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):  6972 ; 1.102 ; 1.982       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   645 ; 5.378 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   215 ;32.774 ;23.442       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   899 ;13.995 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    37 ;19.666 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   755 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3857 ; 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):  45.6611  39.8679  -3.2365              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0492 T22:   0.0517                                     
REMARK   3      T33:   0.1295 T12:   0.0468                                     
REMARK   3      T13:   0.0523 T23:   0.0371                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8312 L22:   2.5824                                     
REMARK   3      L33:   0.8857 L12:  -0.1817                                     
REMARK   3      L13:   0.1128 L23:   0.4378                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0609 S12:   0.0242 S13:   0.2484                       
REMARK   3      S21:   0.0209 S22:  -0.0711 S23:  -0.0842                       
REMARK   3      S31:   0.0201 S32:  -0.0113 S33:   0.0102                       
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):  52.6668  12.6661  -4.2930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1261 T22:   0.0335                                     
REMARK   3      T33:   0.0094 T12:   0.0466                                     
REMARK   3      T13:   0.0202 T23:   0.0030                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1725 L22:   2.0695                                     
REMARK   3      L33:   1.4715 L12:  -0.1094                                     
REMARK   3      L13:  -0.4203 L23:  -0.8527                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0207 S12:   0.0980 S13:  -0.0630                       
REMARK   3      S21:  -0.0918 S22:  -0.0829 S23:  -0.0738                       
REMARK   3      S31:   0.1698 S32:   0.0461 S33:   0.0622                       
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):  30.8999  66.9831   2.5281              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0160 T22:   0.0141                                     
REMARK   3      T33:   0.1124 T12:   0.0007                                     
REMARK   3      T13:   0.0098 T23:  -0.0277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0351 L22:   2.5433                                     
REMARK   3      L33:   1.5748 L12:   0.5796                                     
REMARK   3      L13:   0.0906 L23:   0.2812                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0073 S12:  -0.0448 S13:   0.0323                       
REMARK   3      S21:   0.0192 S22:  -0.0085 S23:  -0.2448                       
REMARK   3      S31:  -0.0211 S32:   0.0478 S33:   0.0158                       
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):  17.4444  42.7844   1.0765              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0459 T22:   0.0792                                     
REMARK   3      T33:   0.0127 T12:  -0.0220                                     
REMARK   3      T13:  -0.0061 T23:   0.0126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4675 L22:   2.0214                                     
REMARK   3      L33:   2.4482 L12:   0.0014                                     
REMARK   3      L13:   0.1007 L23:   0.0261                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1088 S12:  -0.0490 S13:  -0.0518                       
REMARK   3      S21:   0.0152 S22:  -0.0585 S23:   0.0195                       
REMARK   3      S31:   0.2715 S32:   0.0106 S33:  -0.0503                       
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 4G3C 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_1000073685.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-DEC-08                          
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               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97740                            
REMARK 200  MONOCHROMATOR                  : SI(220) ASYMMETRIC CUT SINGLE      
REMARK 200                                   CRYSTAL                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49462                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
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                : 3.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.58400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
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: HOMOLOGY MODEL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
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 , PH 6.2, VAPOR DIFFUSION, HANGING       
REMARK 280  DROP, TEMPERATURE 276K                                              
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       22.54150            
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       33.81225            
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       11.27075            
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     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     ARG B   675                                                      
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: 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    VAL A 430   CB  -  CA  -  C   ANGL. DEV. = -11.7 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    GLN A 405     -135.86     35.97                                   
REMARK 500    ASP A 517       56.91   -149.07                                   
REMARK 500    ASP A 536       97.29     68.68                                   
REMARK 500    TYR A 601      -29.11     73.19                                   
REMARK 500    PRO A 616       36.27    -73.72                                   
REMARK 500    LYS A 668     -113.80     65.58                                   
REMARK 500    GLU B 398       -0.12     67.12                                   
REMARK 500    GLN B 405     -132.69     34.30                                   
REMARK 500    VAL B 408      -75.94   -103.01                                   
REMARK 500    ARG B 410     -169.21   -123.33                                   
REMARK 500    ASP B 517       55.42   -151.20                                   
REMARK 500    ASP B 536       96.03     66.80                                   
REMARK 500    PRO B 545      -18.25    -47.32                                   
REMARK 500    LEU B 553       48.59     76.41                                   
REMARK 500    ASP B 576     -164.67   -125.01                                   
REMARK 500    PRO B 616       41.24    -75.63                                   
REMARK 500    LYS B 668     -141.65     66.59                                   
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 B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 703                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4G3D   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4G3E   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4G3F   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4G3G   RELATED DB: PDB                                   
DBREF  4G3C A  329   675  UNP    Q9WUL6   M3K14_MOUSE    329    675             
DBREF  4G3C B  329   675  UNP    Q9WUL6   M3K14_MOUSE    329    675             
SEQADV 4G3C GLY A  327  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3C SER A  328  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3C GLY A  676  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3C ASN A  677  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3C SER A  678  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3C GLY B  327  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3C SER B  328  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3C GLY B  676  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3C ASN B  677  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3C 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    SO4  A 703       5                                                       
HET    SO4  B 701       5                                                       
HET    SO4  B 702       5                                                       
HET    SO4  B 703       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    6(O4 S 2-)                                                   
FORMUL   9  HOH   *192(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 THR A  361  SER A  363  5                                   3    
HELIX    4   4 GLU A  436  ARG A  439  5                                   4    
HELIX    5   5 VAL A  440  ALA A  445  1                                   6    
HELIX    6   6 LEU A  479  GLY A  487  1                                   9    
HELIX    7   7 PRO A  490  ARG A  511  1                                  22    
HELIX    8   8 LYS A  519  ASP A  521  5                                   3    
HELIX    9   9 THR A  561  MET A  565  5                                   5    
HELIX   10  10 ALA A  566  MET A  571  1                                   6    
HELIX   11  11 ALA A  577  GLY A  594  1                                  18    
HELIX   12  12 PRO A  605  GLU A  613  1                                   9    
HELIX   13  13 PRO A  615  ILE A  620  5                                   6    
HELIX   14  14 ALA A  625  LEU A  636  1                                  12    
HELIX   15  15 GLU A  639  ARG A  643  5                                   5    
HELIX   16  16 SER A  645  VAL A  660  1                                  16    
HELIX   17  17 VAL B  335  GLN B  344  1                                  10    
HELIX   18  18 GLN B  351  LYS B  360  1                                  10    
HELIX   19  19 THR B  361  SER B  363  5                                   3    
HELIX   20  20 GLU B  436  ARG B  439  5                                   4    
HELIX   21  21 VAL B  440  ALA B  445  1                                   6    
HELIX   22  22 SER B  478  GLY B  487  1                                  10    
HELIX   23  23 PRO B  490  ARG B  511  1                                  22    
HELIX   24  24 LYS B  519  ASP B  521  5                                   3    
HELIX   25  25 THR B  561  MET B  565  5                                   5    
HELIX   26  26 ALA B  566  MET B  571  1                                   6    
HELIX   27  27 ALA B  577  GLY B  594  1                                  18    
HELIX   28  28 PRO B  605  GLU B  613  1                                   9    
HELIX   29  29 PRO B  616  ILE B  620  5                                   5    
HELIX   30  30 ALA B  625  LEU B  636  1                                  12    
HELIX   31  31 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  VAL A 433   O  VAL A 467           
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 3 GLY A 477  SER A 478  0                                        
SHEET    2   B 3 VAL A 523  LEU A 525 -1  O  LEU A 525   N  GLY A 477           
SHEET    3   B 3 ALA A 532  LEU A 534 -1  O  ALA A 533   N  LEU A 524           
SHEET    1   C 2 ILE A 513  LEU A 514  0                                        
SHEET    2   C 2 LEU A 541  CYS A 542 -1  O  LEU A 541   N  LEU A 514           
SHEET    1   D 7 VAL B 347  SER B 349  0                                        
SHEET    2   D 7 ASN B 379  LEU B 383  1  O  LEU B 383   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  LYS B 431   O  ILE B 469           
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  8 CYS A 446  VAL A 455  MET A 471  LEU A 534                    
SITE     2 AC1  8 CYS A 535  ASP A 536  PHE A 537  HOH A 873                    
SITE     1 AC2  2 ARG A 650  ARG A 651                                          
SITE     1 AC3  4 ARG A 637  LYS A 638  GLU A 639  HIS A 642                    
SITE     1 AC4  8 CYS B 446  VAL B 455  MET B 471  LEU B 534                    
SITE     2 AC4  8 CYS B 535  ASP B 536  PHE B 537  HOH B 883                    
SITE     1 AC5  2 TYR B 507  ARG B 511                                          
SITE     1 AC6  4 ARG B 637  LYS B 638  GLU B 639  HIS B 642                    
CRYST1  142.211  142.211   45.083  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      0.007032  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007032  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022181        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system