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Database: PDB
Entry: 4G3F
LinkDB: 4G3F
Original site: 4G3F 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       13-JUL-12   4G3F              
TITLE     CRYSTAL STRUCTURE OF MURINE NF-KAPPAB INDUCING KINASE (NIK) BOUND TO A
TITLE    2 2-(AMINOTHIAZOLY)PHENOL (CMP2)                                       
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, STRUCTURE- 
KEYWDS   2 BASED DRUG DESIGN, MAP3K14, TRANSFERASE, TRANSFERASE-TRANSFERASE     
KEYWDS   3 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.G.HYMOWITZ,G.DE LEON-BOENIG                                         
REVDAT   3   24-JAN-18 4G3F    1       AUTHOR                                   
REVDAT   2   23-JAN-13 4G3F    1       JRNL                                     
REVDAT   1   08-AUG-12 4G3F    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.    1.64 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.3_928)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.64                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.23                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 39407                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.208                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.010                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 3946                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 33.2324 -  4.9821    0.98     1404   141  0.2127 0.2381        
REMARK   3     2  4.9821 -  3.9565    0.99     1358   131  0.1531 0.1742        
REMARK   3     3  3.9565 -  3.4570    0.99     1335   146  0.1719 0.1828        
REMARK   3     4  3.4570 -  3.1412    0.99     1297   144  0.1801 0.2000        
REMARK   3     5  3.1412 -  2.9162    0.98     1266   175  0.1852 0.2302        
REMARK   3     6  2.9162 -  2.7443    0.99     1304   135  0.1934 0.2003        
REMARK   3     7  2.7443 -  2.6069    0.99     1285   146  0.1812 0.2206        
REMARK   3     8  2.6069 -  2.4935    0.98     1268   150  0.1752 0.1970        
REMARK   3     9  2.4935 -  2.3975    0.98     1291   130  0.1765 0.2154        
REMARK   3    10  2.3975 -  2.3148    0.98     1301   137  0.1719 0.2152        
REMARK   3    11  2.3148 -  2.2425    0.98     1260   136  0.1622 0.2071        
REMARK   3    12  2.2425 -  2.1784    0.98     1272   150  0.1655 0.1909        
REMARK   3    13  2.1784 -  2.1210    0.98     1256   145  0.1633 0.1827        
REMARK   3    14  2.1210 -  2.0693    0.97     1278   130  0.1641 0.2230        
REMARK   3    15  2.0693 -  2.0223    0.97     1245   143  0.1570 0.2031        
REMARK   3    16  2.0223 -  1.9792    0.97     1259   138  0.1572 0.2168        
REMARK   3    17  1.9792 -  1.9396    0.98     1264   146  0.1621 0.2081        
REMARK   3    18  1.9396 -  1.9030    0.97     1242   137  0.1657 0.2048        
REMARK   3    19  1.9030 -  1.8691    0.97     1235   149  0.1729 0.1969        
REMARK   3    20  1.8691 -  1.8374    0.97     1278   137  0.1669 0.2268        
REMARK   3    21  1.8374 -  1.8077    0.97     1233   135  0.1784 0.2179        
REMARK   3    22  1.8077 -  1.7799    0.97     1247   163  0.1777 0.2293        
REMARK   3    23  1.7799 -  1.7538    0.96     1244   119  0.1971 0.2648        
REMARK   3    24  1.7538 -  1.7290    0.95     1230   148  0.1924 0.2423        
REMARK   3    25  1.7290 -  1.7057    0.95     1242   114  0.1909 0.2261        
REMARK   3    26  1.7057 -  1.6835    0.95     1205   138  0.2115 0.2143        
REMARK   3    27  1.6835 -  1.6625    0.95     1209   151  0.2233 0.2522        
REMARK   3    28  1.6625 -  1.6425    0.89     1153   132  0.2481 0.2611        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.86                                          
REMARK   3   K_SOL              : 0.38                                          
REMARK   3   B_SOL              : 39.73                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.520           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.05510                                              
REMARK   3    B22 (A**2) : -0.13350                                             
REMARK   3    B33 (A**2) : 0.07840                                              
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           2555                                  
REMARK   3   ANGLE     :  1.123           3462                                  
REMARK   3   CHIRALITY :  0.076            364                                  
REMARK   3   PLANARITY :  0.006            449                                  
REMARK   3   DIHEDRAL  : 12.345            970                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESSEQ 345:676)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  18.7599  17.8369   2.4650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0698 T22:   0.0968                                     
REMARK   3      T33:   0.0827 T12:   0.0021                                     
REMARK   3      T13:   0.0097 T23:  -0.0073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1815 L22:   1.0653                                     
REMARK   3      L33:   0.9699 L12:  -0.1773                                     
REMARK   3      L13:   0.1619 L23:  -0.5144                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0125 S12:  -0.0054 S13:  -0.0145                       
REMARK   3      S21:   0.0111 S22:   0.0021 S23:   0.0508                       
REMARK   3      S31:   0.1007 S32:  -0.0081 S33:   0.0002                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4G3F 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_1000073688.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JUL-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 6.5                                
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   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.640                              
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     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 36.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.34000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.300                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 UL PLUS 2 UL WELL SOLUTION             
REMARK 280  CONTAINING 1 MM CMP2, 100 MM BIS-TRIS PH 6.5, 100 MM SODIUM         
REMARK 280  CHLORIDE, 20% PEG 400, VAPOR DIFFUSION, SITTING DROP,               
REMARK 280  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       32.42850            
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       32.42850            
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       37.39450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       67.80950            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       37.39450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       67.80950            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       32.42850            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       37.39450            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       67.80950            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       32.42850            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       37.39450            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       67.80950            
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 910  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     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   OE2  GLU A   506     O    HOH A   932              2.06            
REMARK 500   O    TRP A   667     O    HOH A   875              2.07            
REMARK 500   O    HOH A   867     O    HOH A  1023              2.09            
REMARK 500   O    PRO A   406     O    HOH A  1034              2.12            
REMARK 500   OE1  GLN A   630     O    HOH A  1024              2.12            
REMARK 500   OG   SER A   583     O    HOH A   822              2.14            
REMARK 500   O    SER A   346     O    HOH A  1001              2.16            
REMARK 500   O    HOH A   825     O    HOH A  1028              2.18            
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    GLU A 398      -15.53     75.95                                   
REMARK 500    GLN A 405      173.02     72.87                                   
REMARK 500    ASP A 517       62.23   -155.70                                   
REMARK 500    ASP A 536       93.96     68.62                                   
REMARK 500    TRP A 598      -40.48     76.04                                   
REMARK 500    ARG A 603      -68.06   -107.10                                   
REMARK 500    PRO A 616       42.82    -79.43                                   
REMARK 500    TRP A 667       82.15    -65.36                                   
REMARK 500    LYS A 668     -151.42   -147.16                                   
REMARK 500    LYS A 668     -151.42    115.24                                   
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 0WB 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: 4G3G   RELATED DB: PDB                                   
DBREF  4G3F A  345   675  UNP    Q9WUL6   M3K14_MOUSE    345    675             
SEQADV 4G3F GLY A  343  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3F SER A  344  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3F GLY A  676  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3F ASN A  677  UNP  Q9WUL6              EXPRESSION TAG                 
SEQADV 4G3F SER A  678  UNP  Q9WUL6              EXPRESSION TAG                 
SEQRES   1 A  336  GLY SER GLY SER VAL SER SER GLY GLN ALA HIS SER LEU          
SEQRES   2 A  336  ALA SER LEU ALA LYS THR TRP SER SER GLY SER ALA LYS          
SEQRES   3 A  336  LEU GLN ARG LEU GLY PRO GLU THR GLU ASP ASN GLU GLY          
SEQRES   4 A  336  VAL LEU LEU THR GLU LYS LEU LYS PRO VAL ASP TYR GLU          
SEQRES   5 A  336  TYR ARG GLU GLU VAL HIS TRP MET THR HIS GLN PRO ARG          
SEQRES   6 A  336  VAL GLY ARG GLY SER PHE GLY GLU VAL HIS ARG MET LYS          
SEQRES   7 A  336  ASP LYS GLN THR GLY PHE GLN CYS ALA VAL LYS LYS VAL          
SEQRES   8 A  336  ARG LEU GLU VAL PHE ARG VAL GLU GLU LEU VAL ALA CYS          
SEQRES   9 A  336  ALA GLY LEU SER SER PRO ARG ILE VAL PRO LEU TYR GLY          
SEQRES  10 A  336  ALA VAL ARG GLU GLY PRO TRP VAL ASN ILE PHE MET GLU          
SEQRES  11 A  336  LEU LEU GLU GLY GLY SER LEU GLY GLN LEU ILE LYS GLN          
SEQRES  12 A  336  MET GLY CYS LEU PRO GLU ASP ARG ALA LEU TYR TYR LEU          
SEQRES  13 A  336  GLY GLN ALA LEU GLU GLY LEU GLU TYR LEU HIS THR ARG          
SEQRES  14 A  336  ARG ILE LEU HIS GLY ASP VAL LYS ALA ASP ASN VAL LEU          
SEQRES  15 A  336  LEU SER SER ASP GLY SER ARG ALA ALA LEU CYS ASP PHE          
SEQRES  16 A  336  GLY HIS ALA LEU CYS LEU GLN PRO ASP GLY LEU GLY LYS          
SEQRES  17 A  336  SER LEU LEU THR GLY ASP TYR ILE PRO GLY THR GLU THR          
SEQRES  18 A  336  HIS MET ALA PRO GLU VAL VAL MET GLY LYS PRO CYS ASP          
SEQRES  19 A  336  ALA LYS VAL ASP ILE TRP SER SER CYS CYS MET MET LEU          
SEQRES  20 A  336  HIS MET LEU ASN GLY CYS HIS PRO TRP THR GLN TYR PHE          
SEQRES  21 A  336  ARG GLY PRO LEU CYS LEU LYS ILE ALA SER GLU PRO PRO          
SEQRES  22 A  336  PRO ILE ARG GLU ILE PRO PRO SER CYS ALA PRO LEU THR          
SEQRES  23 A  336  ALA GLN ALA ILE GLN GLU GLY LEU ARG LYS GLU PRO VAL          
SEQRES  24 A  336  HIS ARG ALA SER ALA MET GLU LEU ARG ARG LYS VAL GLY          
SEQRES  25 A  336  LYS ALA LEU GLN GLU VAL GLY GLY LEU LYS SER PRO TRP          
SEQRES  26 A  336  LYS GLY GLU TYR LYS GLU PRO ARG GLY ASN SER                  
HET    0WB  A 701      22                                                       
HETNAM     0WB 3-{2-[(5-FLUORO-2-HYDROXYPHENYL)AMINO]-1,3-THIAZOL-4-            
HETNAM   2 0WB  YL}BENZONITRILE                                                 
FORMUL   2  0WB    C16 H10 F N3 O S                                             
FORMUL   3  HOH   *244(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  MET A  571  1                                   6    
HELIX    8   8 ALA A  577  GLY A  594  1                                  18    
HELIX    9   9 LEU A  606  GLU A  613  1                                   8    
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  PHE A 470   N  TYR A 458           
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  GLY A 409   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 15 VAL A 408  GLY A 411  VAL A 416  ALA A 429                    
SITE     2 AC1 15 VAL A 430  LYS A 431  GLU A 442  ILE A 469                    
SITE     3 AC1 15 MET A 471  LEU A 473  LEU A 474  ASP A 521                    
SITE     4 AC1 15 ASN A 522  LEU A 524  ASP A 536                               
CRYST1   74.789  135.619   64.857  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      0.013371  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007374  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015419        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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