GenomeNet

Database: PDB
Entry: 4G3G
LinkDB: 4G3G
Original site: 4G3G 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       13-JUL-12   4G3G              
TITLE     CRYSTAL STRUCTURE OF MURINE NF-KAPPAB INDUCING KINASE (NIK) V408L     
TITLE    2 BOUND TO A 2-(AMINOTHIAZOLYL)PHENOL (CMP3)                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NF-KAPPA-BETA-INDUCING KINASE;                             
COMPND   3 CHAIN: A;                                                            
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), 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 STRUCTURE-BASED DRUG DESIGN, TRANSFERASE, TRANSFERASE-TRANSFERASE    
KEYWDS   3 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.HYMOWITZ                                                            
REVDAT   2   23-JAN-13 4G3G    1       JRNL                                     
REVDAT   1   08-AUG-12 4G3G    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) : 46.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 10329                          
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) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1143                            
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) : 478                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.96                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2830                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 62                           
REMARK   3   BIN FREE R VALUE                    : 0.3570                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2421                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 38                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.35                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.58000                                              
REMARK   3    B22 (A**2) : -1.06000                                             
REMARK   3    B33 (A**2) : -0.51000                                             
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): 1.690         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.323         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.209         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.010        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.936                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.905                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2554 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3460 ; 1.195 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   321 ; 5.426 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   109 ;31.578 ;23.028       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   445 ;14.918 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;15.772 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   364 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1948 ; 0.004 ; 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   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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  : 1                                          
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   345        A   676                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.7916  17.6438   2.4961              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0143 T22:   0.0617                                     
REMARK   3      T33:   0.0461 T12:  -0.0029                                     
REMARK   3      T13:   0.0083 T23:  -0.0133                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6051 L22:   2.2126                                     
REMARK   3      L33:   1.5469 L12:   0.2004                                     
REMARK   3      L13:   0.0736 L23:  -0.4455                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0358 S12:  -0.0242 S13:  -0.0041                       
REMARK   3      S21:  -0.0030 S22:   0.0129 S23:   0.1264                       
REMARK   3      S31:   0.1250 S32:  -0.0392 S33:   0.0229                       
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 4G3G 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 RCSB ID CODE IS RCSB073689.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-JAN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 7.0                                
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   : 11486                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.570                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6000                            
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     (%) : 93.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.61900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 UL PROTEIN PLUS 0.2 UL OF 0.5 MM     
REMARK 280  CMP3, 100 MM HEPES PH 7.0, 0.01 M ZINC CHLORIDE, 20% PEG 6000,      
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
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   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
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       32.12500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       32.12500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       37.21150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       67.66000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       37.21150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       67.66000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       32.12500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       37.21150            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       67.66000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       32.12500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       37.21150            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       67.66000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 822  LIES ON A SPECIAL POSITION.                          
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     MET A   329                                                      
REMARK 465     HIS A   330                                                      
REMARK 465     HIS A   331                                                      
REMARK 465     HIS A   332                                                      
REMARK 465     HIS A   333                                                      
REMARK 465     HIS A   334                                                      
REMARK 465     HIS A   335                                                      
REMARK 465     GLY A   336                                                      
REMARK 465     GLU A   337                                                      
REMARK 465     ASN A   338                                                      
REMARK 465     LEU A   339                                                      
REMARK 465     TYR A   340                                                      
REMARK 465     PHE A   341                                                      
REMARK 465     GLN A   342                                                      
REMARK 465     GLY A   343                                                      
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     GLN A   544                                                      
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     ASN A   677                                                      
REMARK 465     SER A   678                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH2  ARG A   650     O    HOH A   837              1.82            
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    SER A 346       56.04   -142.37                                   
REMARK 500    TYR A 393       16.89     59.08                                   
REMARK 500    GLU A 398      -15.99     76.31                                   
REMARK 500    GLN A 405     -173.02     67.26                                   
REMARK 500    ASP A 517       61.22   -154.85                                   
REMARK 500    ASP A 536       98.13     59.70                                   
REMARK 500    TRP A 598      -45.25     79.66                                   
REMARK 500    PRO A 616       41.07    -76.71                                   
REMARK 500    PRO A 674     -175.51    -64.63                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    TRP A 667        24.1      L          L   OUTSIDE RANGE           
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 0WA A 701                 
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: 4G3E   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4G3F   RELATED DB: PDB                                   
DBREF  4G3G A  345   675  UNP    Q9WUL6   M3K14_MOUSE    345    675             
SEQADV 4G3G MET A  329  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3G HIS A  330  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3G HIS A  331  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3G HIS A  332  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3G HIS A  333  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3G HIS A  334  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3G HIS A  335  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3G GLY A  336  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3G GLU A  337  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3G ASN A  338  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3G LEU A  339  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3G TYR A  340  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3G PHE A  341  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3G GLN A  342  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3G GLY A  343  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3G SER A  344  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3G LEU A  408  UNP  Q9WUL6    VAL   408 ENGINEERED MUTATION            
SEQADV 4G3G GLY A  676  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3G ASN A  677  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3G SER A  678  UNP  Q9WUL6              EXPRESSION TAG                 
SEQRES   1 A  350  MET HIS HIS HIS HIS HIS HIS GLY GLU ASN LEU TYR PHE          
SEQRES   2 A  350  GLN GLY SER GLY SER VAL SER SER GLY GLN ALA HIS SER          
SEQRES   3 A  350  LEU ALA SER LEU ALA LYS THR TRP SER SER GLY SER ALA          
SEQRES   4 A  350  LYS LEU GLN ARG LEU GLY PRO GLU THR GLU ASP ASN GLU          
SEQRES   5 A  350  GLY VAL LEU LEU THR GLU LYS LEU LYS PRO VAL ASP TYR          
SEQRES   6 A  350  GLU TYR ARG GLU GLU VAL HIS TRP MET THR HIS GLN PRO          
SEQRES   7 A  350  ARG LEU GLY ARG GLY SER PHE GLY GLU VAL HIS ARG MET          
SEQRES   8 A  350  LYS ASP LYS GLN THR GLY PHE GLN CYS ALA VAL LYS LYS          
SEQRES   9 A  350  VAL ARG LEU GLU VAL PHE ARG VAL GLU GLU LEU VAL ALA          
SEQRES  10 A  350  CYS ALA GLY LEU SER SER PRO ARG ILE VAL PRO LEU TYR          
SEQRES  11 A  350  GLY ALA VAL ARG GLU GLY PRO TRP VAL ASN ILE PHE MET          
SEQRES  12 A  350  GLU LEU LEU GLU GLY GLY SER LEU GLY GLN LEU ILE LYS          
SEQRES  13 A  350  GLN MET GLY CYS LEU PRO GLU ASP ARG ALA LEU TYR TYR          
SEQRES  14 A  350  LEU GLY GLN ALA LEU GLU GLY LEU GLU TYR LEU HIS THR          
SEQRES  15 A  350  ARG ARG ILE LEU HIS GLY ASP VAL LYS ALA ASP ASN VAL          
SEQRES  16 A  350  LEU LEU SER SER ASP GLY SER ARG ALA ALA LEU CYS ASP          
SEQRES  17 A  350  PHE GLY HIS ALA LEU CYS LEU GLN PRO ASP GLY LEU GLY          
SEQRES  18 A  350  LYS SER LEU LEU THR GLY ASP TYR ILE PRO GLY THR GLU          
SEQRES  19 A  350  THR HIS MET ALA PRO GLU VAL VAL MET GLY LYS PRO CYS          
SEQRES  20 A  350  ASP ALA LYS VAL ASP ILE TRP SER SER CYS CYS MET MET          
SEQRES  21 A  350  LEU HIS MET LEU ASN GLY CYS HIS PRO TRP THR GLN TYR          
SEQRES  22 A  350  PHE ARG GLY PRO LEU CYS LEU LYS ILE ALA SER GLU PRO          
SEQRES  23 A  350  PRO PRO ILE ARG GLU ILE PRO PRO SER CYS ALA PRO LEU          
SEQRES  24 A  350  THR ALA GLN ALA ILE GLN GLU GLY LEU ARG LYS GLU PRO          
SEQRES  25 A  350  VAL HIS ARG ALA SER ALA MET GLU LEU ARG ARG LYS VAL          
SEQRES  26 A  350  GLY LYS ALA LEU GLN GLU VAL GLY GLY LEU LYS SER PRO          
SEQRES  27 A  350  TRP LYS GLY GLU TYR LYS GLU PRO ARG GLY ASN SER              
HET    0WA  A 701      20                                                       
HETNAM     0WA 4-FLUORO-2-{[4-(PYRIDIN-4-YL)-1,3-THIAZOL-2-                     
HETNAM   2 0WA  YL]AMINO}PHENOL                                                 
FORMUL   2  0WA    C14 H10 F N3 O S                                             
FORMUL   3  HOH   *38(H2 O)                                                     
HELIX    1   1 GLN A  351  LYS A  360  1                                  10    
HELIX    2   2 VAL A  440  ALA A  445  1                                   6    
HELIX    3   3 SER A  478  GLY A  487  1                                  10    
HELIX    4   4 PRO A  490  THR A  510  1                                  21    
HELIX    5   5 LYS A  519  ASP A  521  5                                   3    
HELIX    6   6 THR A  561  MET A  565  5                                   5    
HELIX    7   7 ALA A  566  GLY A  572  1                                   7    
HELIX    8   8 ALA A  577  GLY A  594  1                                  18    
HELIX    9   9 PRO A  605  GLU A  613  1                                   9    
HELIX   10  10 PRO A  615  ILE A  620  5                                   6    
HELIX   11  11 ALA A  625  LEU A  636  1                                  12    
HELIX   12  12 GLU A  639  ARG A  643  5                                   5    
HELIX   13  13 SER A  645  VAL A  660  1                                  16    
SHEET    1   A 7 SER A 346  SER A 349  0                                        
SHEET    2   A 7 ASN A 379  LEU A 383  1  O  ASN A 379   N  SER A 346           
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  TRP A 466   N  GLU A 463           
SHEET    5   A 7 GLN A 427  ARG A 434 -1  N  VAL A 433   O  VAL A 467           
SHEET    6   A 7 GLY A 414  ASP A 421 -1  N  HIS A 417   O  VAL A 430           
SHEET    7   A 7 TRP A 401  GLY A 411 -1  N  LEU A 408   O  VAL A 416           
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           
SITE     1 AC1 14 LEU A 408  ARG A 410  GLY A 411  VAL A 416                    
SITE     2 AC1 14 ALA A 429  VAL A 430  LYS A 431  GLU A 442                    
SITE     3 AC1 14 ILE A 469  MET A 471  ASP A 521  ASN A 522                    
SITE     4 AC1 14 LEU A 524  ASP A 536                                          
CRYST1   74.423  135.320   64.250  90.00  90.00  90.00 C 2 2 21      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      0.013437  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007390  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015564        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system