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Database: PDB
Entry: 5N9L
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HEADER    TRANSFERASE                             25-FEB-17   5N9L              
TITLE     CRYSTAL STRUCTURE OF HUMAN PROTEIN KINASE CK2 CATALYTIC SUBUNIT IN    
TITLE    2 COMPLEX WITH THE ATP-COMPETITIVE DIBENZOFURAN INHIBITOR TF (4B)      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CK II ALPHA;                                                
COMPND   5 EC: 2.7.11.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CSNK2A1, CK2A1;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEIN KINASE, CK2, CASEIN KINASE 2, PROTEIN PHOSPHORYLATION, ATP-   
KEYWDS   2 COMPETITIVE INHITITORS, DIBENZOFURAN DERIVATIVES, TRANSFERASE,       
KEYWDS   3 TIGHT-BINDING INHIBITORS                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.SCHNITZLER,A.GRATZ,A.BOLLACKE,M.WEYRICH,U.KUCKLAENDER,B.WUENSCH,    
AUTHOR   2 C.GOETZ,K.NIEFIND,J.JOSE                                             
REVDAT   4   25-APR-18 5N9L    1       JRNL                                     
REVDAT   3   18-APR-18 5N9L    1       JRNL                                     
REVDAT   2   07-MAR-18 5N9L    1       JRNL                                     
REVDAT   1   28-FEB-18 5N9L    0                                                
JRNL        AUTH   A.SCHNITZLER,A.GRATZ,A.BOLLACKE,M.WEYRICH,U.KUCKLANDER,      
JRNL        AUTH 2 B.WUNSCH,C.GOTZ,K.NIEFIND,J.JOSE                             
JRNL        TITL   A PI-HALOGEN BOND OF DIBENZOFURANONES WITH THE GATEKEEPER    
JRNL        TITL 2 PHE113 IN HUMAN PROTEIN KINASE CK2 LEADS TO POTENT TIGHT     
JRNL        TITL 3 BINDING INHIBITORS.                                          
JRNL        REF    PHARMACEUTICALS               V.  11       2018              
JRNL        REFN                   ESSN 1424-8247                               
JRNL        PMID   29462988                                                     
JRNL        DOI    10.3390/PH11010023                                           
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   I.ERMAKOVA,B.BOLDYREFF,O.G.ISSINGER,K.NIEFIND                
REMARK   1  TITL   CRYSTAL STRUCTURE OF A C-TERMINAL DELETION MUTANT OF HUMAN   
REMARK   1  TITL 2 PROTEIN KINASE CK2 CATALYTIC SUBUNIT.                        
REMARK   1  REF    J. MOL. BIOL.                 V. 330   925 2003              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   12860116                                                     
REMARK   1  DOI    10.1016/S0022-2836(03)00638-7                                
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   C.W.YDE,I.ERMAKOVA,O.G.ISSINGER,K.NIEFIND                    
REMARK   1  TITL   INCLINING THE PURINE BASE BINDING PLANE IN PROTEIN KINASE    
REMARK   1  TITL 2 CK2 BY EXCHANGING THE FLANKING SIDE-CHAINS GENERATES A       
REMARK   1  TITL 3 PREFERENCE FOR ATP AS A COSUBSTRATE.                         
REMARK   1  REF    J. MOL. BIOL.                 V. 347   399 2005              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   15740749                                                     
REMARK   1  DOI    10.1016/J.JMB.2005.01.003                                    
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   K.NIEFIND,N.BISCHOFF,A.G.GOLUB,V.G.BDZHOLA,A.O.BALANDA,      
REMARK   1  AUTH 2 A.O.PRYKHOD'KO,S.M.YARMOLUK                                  
REMARK   1  TITL   STRUCTURAL HYPERVARIABILITY OF THE TWO HUMAN PROTEIN KINASE  
REMARK   1  TITL 2 CK2 CATALYTIC SUBUNIT PARALOGS REVEALED BY COMPLEX           
REMARK   1  TITL 3 STRUCTURES WITH A FLAVONOL- AND A                            
REMARK   1  TITL 4 THIENO[2,3-D]PYRIMIDINE-BASED INHIBITOR.                     
REMARK   1  REF    PHARMACEUTICALS (BASEL)       V.  10       2017              
REMARK   1  REFN                   ESSN 1424-8247                               
REMARK   1  PMID   28085026                                                     
REMARK   1  DOI    10.3390/PH10010009                                           
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   C.GOETZ,A.GRATZ,U.KUCKLAENDER,J.JOSE                         
REMARK   1  TITL   TF--A NOVEL CELL-PERMEABLE AND SELECTIVE INHIBITOR OF HUMAN  
REMARK   1  TITL 2 PROTEIN KINASE CK2 INDUCES APOPTOSIS IN THE PROSTATE CANCER  
REMARK   1  TITL 3 CELL LINE LNCAP.                                             
REMARK   1  REF    BIOCHIM. BIOPHYS. ACTA        V.1820   970 2012              
REMARK   1  REFN                   ISSN 0006-3002                               
REMARK   1  PMID   22387500                                                     
REMARK   1  DOI    10.1016/J.BBAGEN.2012.02.009                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.79 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.14                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.390                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 27726                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.164                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1389                            
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 36.1427 -  3.8552    0.98     2770   170  0.1481 0.1667        
REMARK   3     2  3.8552 -  3.0605    0.98     2738   137  0.1444 0.1838        
REMARK   3     3  3.0605 -  2.6738    0.98     2741   130  0.1707 0.2119        
REMARK   3     4  2.6738 -  2.4294    0.97     2658   145  0.1715 0.2189        
REMARK   3     5  2.4294 -  2.2553    0.97     2681   146  0.1733 0.2151        
REMARK   3     6  2.2553 -  2.1223    0.96     2653   117  0.1737 0.2357        
REMARK   3     7  2.1223 -  2.0161    0.96     2620   159  0.1751 0.2335        
REMARK   3     8  2.0161 -  1.9283    0.97     2660   131  0.1936 0.1978        
REMARK   3     9  1.9283 -  1.8541    0.96     2642   140  0.2049 0.2682        
REMARK   3    10  1.8541 -  1.7901    0.79     2174   114  0.2392 0.2826        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.340           
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) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.003           2954                                  
REMARK   3   ANGLE     :  0.664           3998                                  
REMARK   3   CHIRALITY :  0.045            406                                  
REMARK   3   PLANARITY :  0.005            515                                  
REMARK   3   DIHEDRAL  : 12.671           1754                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 88 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -18.3945   3.0423  46.0867              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2301 T22:   0.3382                                     
REMARK   3      T33:   0.3428 T12:  -0.0494                                     
REMARK   3      T13:   0.0074 T23:   0.0445                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4446 L22:   2.0929                                     
REMARK   3      L33:   0.5566 L12:  -1.8595                                     
REMARK   3      L13:   0.2616 L23:  -0.3389                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0008 S12:  -0.1983 S13:  -0.4108                       
REMARK   3      S21:  -0.0139 S22:   0.1052 S23:   0.4420                       
REMARK   3      S31:   0.1112 S32:  -0.2015 S33:  -0.1008                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 89 THROUGH 249 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.0760  10.6099  43.8001              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1547 T22:   0.1480                                     
REMARK   3      T33:   0.1682 T12:   0.0148                                     
REMARK   3      T13:  -0.0105 T23:   0.0175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1458 L22:   0.8376                                     
REMARK   3      L33:   1.2202 L12:  -0.1187                                     
REMARK   3      L13:  -0.0609 L23:  -0.0047                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0142 S12:  -0.1131 S13:   0.0766                       
REMARK   3      S21:  -0.0594 S22:   0.0039 S23:   0.2159                       
REMARK   3      S31:  -0.0980 S32:  -0.1454 S33:  -0.0195                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 250 THROUGH 330 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  11.5942   9.7354  41.2006              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1573 T22:   0.2008                                     
REMARK   3      T33:   0.2061 T12:   0.0072                                     
REMARK   3      T13:  -0.0083 T23:   0.0108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2146 L22:   2.2117                                     
REMARK   3      L33:   2.4436 L12:   0.1974                                     
REMARK   3      L13:   0.1249 L23:   1.0343                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0056 S12:   0.0315 S13:  -0.0159                       
REMARK   3      S21:  -0.1244 S22:   0.0724 S23:  -0.0916                       
REMARK   3      S31:  -0.0349 S32:   0.2024 S33:  -0.0685                       
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 5N9L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003734.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-OCT-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06DA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99987                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27738                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.790                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 36.140                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.05600                            
REMARK 200  R SYM                      (I) : 0.05600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 65.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.54500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
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: 2PVR                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PRIOR TO THE CRYSTALLIZATION TF WAS      
REMARK 280  SOLUBILIZED IN 100 % DMSO IN A CONCENTRATION OF 10 MM. TF WAS       
REMARK 280  MIXED WITH HUMAN CK2ALPHA (CONSTRUCT 1-335; 8-10 MG/ML IN 500 MM    
REMARK 280  SODIUM CHLORIDE, 25 MM TRIS/HCL PH 8.5) IN A RATIO OF 1:5. AFTER    
REMARK 280  A SHORT TIME OF INCUBATION THIS MIXTURE WAS MIXED WITH RESERVOIR    
REMARK 280  SOLUTION [32 % (W/V) PEG4000, 0.2 M AMMONIUM ACETATE, 0.1 M         
REMARK 280  CITRATE PH 5.6] IN A RATIO OF 5:2. 3.5 MICROLITER OF THE            
REMARK 280  RESULTING MIXTURE WAS THEN EQUILIBRATED AGAINST THE RESERVOIR       
REMARK 280  SOLUTION. THE CRYSTAL GROWTH WAS INDUCED BY SEEDING WITH 150        
REMARK 280  NANOLITER SEED SUSPENSION AFTER AN EQUILIBRATION TIME OF TWO        
REMARK 280  DAYS., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       22.85300            
REMARK 290   SMTRY3   2  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL                          
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 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     1                                                      
REMARK 465     GLN A   331                                                      
REMARK 465     ALA A   332                                                      
REMARK 465     ARG A   333                                                      
REMARK 465     MET A   334                                                      
REMARK 465     GLY A   335                                                      
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   O    HOH A   627     O    HOH A   686              2.16            
REMARK 500   O    HOH A   654     O    HOH A   712              2.19            
REMARK 500   O    HOH A   648     O    HOH A   680              2.19            
REMARK 500   O    HOH A   676     O    HOH A   713              2.19            
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    ASN A  61       10.40   -145.37                                   
REMARK 500    VAL A  73      -63.20   -141.82                                   
REMARK 500    LYS A  74      128.60   -175.63                                   
REMARK 500    ASP A 156       42.59   -147.84                                   
REMARK 500    ASP A 175       79.63     43.77                                   
REMARK 500    ALA A 193      159.69     64.07                                   
REMARK 500    MET A 208       58.65    -91.64                                   
REMARK 500    HIS A 234       73.43   -106.62                                   
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 8QH A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 407                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5N9N   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5N9K   RELATED DB: PDB                                   
DBREF  5N9L A    1   335  UNP    P68400   CSK21_HUMAN      1    335             
SEQRES   1 A  335  MET SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR          
SEQRES   2 A  335  ASP VAL ASN THR HIS ARG PRO ARG GLU TYR TRP ASP TYR          
SEQRES   3 A  335  GLU SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR          
SEQRES   4 A  335  GLN LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU          
SEQRES   5 A  335  VAL PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL          
SEQRES   6 A  335  VAL VAL LYS ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE          
SEQRES   7 A  335  LYS ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY          
SEQRES   8 A  335  PRO ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO          
SEQRES   9 A  335  VAL SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN          
SEQRES  10 A  335  ASN THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP          
SEQRES  11 A  335  TYR ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA          
SEQRES  12 A  335  LEU ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP          
SEQRES  13 A  335  VAL LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG          
SEQRES  14 A  335  LYS LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR          
SEQRES  15 A  335  HIS PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG          
SEQRES  16 A  335  TYR PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET          
SEQRES  17 A  335  TYR ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET          
SEQRES  18 A  335  LEU ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS          
SEQRES  19 A  335  GLY HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS          
SEQRES  20 A  335  VAL LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS          
SEQRES  21 A  335  TYR ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU          
SEQRES  22 A  335  GLY ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS          
SEQRES  23 A  335  SER GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP          
SEQRES  24 A  335  PHE LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG          
SEQRES  25 A  335  LEU THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR          
SEQRES  26 A  335  THR VAL VAL LYS ASP GLN ALA ARG MET GLY                      
HET    8QH  A 401      26                                                       
HET    ACT  A 402       4                                                       
HET    ACT  A 403       4                                                       
HET    GOL  A 404       6                                                       
HET    GOL  A 405       6                                                       
HET    GOL  A 406       6                                                       
HET    GOL  A 407       6                                                       
HETNAM     8QH (4~{Z})-6,7-BIS(CHLORANYL)-4-[[(4-METHYLPHENYL)                  
HETNAM   2 8QH  AMINO]METHYLIDENE]-8-OXIDANYL-1,2-DIHYDRODIBENZOFURAN-          
HETNAM   3 8QH  3-ONE                                                           
HETNAM     ACT ACETATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  8QH    C20 H15 CL2 N O3                                             
FORMUL   3  ACT    2(C2 H3 O2 1-)                                               
FORMUL   5  GOL    4(C3 H8 O3)                                                  
FORMUL   9  HOH   *218(H2 O)                                                    
HELIX    1 AA1 PRO A   20  ASP A   25  1                                   6    
HELIX    2 AA2 TYR A   26  HIS A   29  5                                   4    
HELIX    3 AA3 ASN A   35  ASP A   37  5                                   3    
HELIX    4 AA4 LYS A   74  ARG A   89  1                                  16    
HELIX    5 AA5 ASP A  120  GLN A  126  1                                   7    
HELIX    6 AA6 THR A  129  MET A  150  1                                  22    
HELIX    7 AA7 LYS A  158  HIS A  160  5                                   3    
HELIX    8 AA8 SER A  194  LYS A  198  5                                   5    
HELIX    9 AA9 GLY A  199  VAL A  204  1                                   6    
HELIX   10 AB1 TYR A  211  ARG A  228  1                                  18    
HELIX   11 AB2 ASP A  237  GLY A  250  1                                  14    
HELIX   12 AB3 GLY A  250  TYR A  261  1                                  12    
HELIX   13 AB4 ASP A  266  ILE A  272  5                                   7    
HELIX   14 AB5 ARG A  280  VAL A  285  5                                   6    
HELIX   15 AB6 ASN A  289  VAL A  293  5                                   5    
HELIX   16 AB7 SER A  294  LEU A  305  1                                  12    
HELIX   17 AB8 ASP A  308  ARG A  312  5                                   5    
HELIX   18 AB9 THR A  314  GLU A  320  1                                   7    
HELIX   19 AC1 HIS A  321  TYR A  325  5                                   5    
SHEET    1 AA1 5 TYR A  39  ARG A  47  0                                        
SHEET    2 AA1 5 SER A  51  ASN A  58 -1  O  GLU A  55   N  VAL A  42           
SHEET    3 AA1 5 LYS A  64  LEU A  70 -1  O  ILE A  69   N  GLU A  52           
SHEET    4 AA1 5 PRO A 109  GLU A 114 -1  O  PHE A 113   N  VAL A  66           
SHEET    5 AA1 5 LEU A  97  LYS A 102 -1  N  VAL A 101   O  ALA A 110           
SHEET    1 AA2 2 ILE A 152  MET A 153  0                                        
SHEET    2 AA2 2 GLU A 180  PHE A 181 -1  O  GLU A 180   N  MET A 153           
SHEET    1 AA3 2 VAL A 162  ASP A 165  0                                        
SHEET    2 AA3 2 LYS A 170  LEU A 173 -1  O  LYS A 170   N  ASP A 165           
CISPEP   1 GLU A  230    PRO A  231          0        -1.87                     
SITE     1 AC1 13 ARG A  47  GLY A  48  SER A  51  VAL A  53                    
SITE     2 AC1 13 VAL A  66  LYS A  68  PHE A 113  VAL A 116                    
SITE     3 AC1 13 MET A 163  ILE A 174  ASP A 175  HOH A 592                    
SITE     4 AC1 13 HOH A 669                                                     
SITE     1 AC2  3 ARG A  80  ARG A 155  LEU A 178                               
SITE     1 AC3  4 ASP A 156  LYS A 158  ALA A 193  SER A 194                    
SITE     1 AC4  7 GLY A  90  GLY A  91  PRO A  92  ASN A  93                    
SITE     2 AC4  7 ILE A  94  ARG A 172  HOH A 529                               
SITE     1 AC5  4 GLU A  32  GLU A  86  ARG A  89  ILE A 100                    
SITE     1 AC6  4 GLN A 310  SER A 311  ARG A 312  GLU A 317                    
SITE     1 AC7  8 GLN A  36  TYR A  39  ASP A 103  PRO A 104                    
SITE     2 AC7  8 ALA A 110  ARG A 280  HOH A 638  HOH A 651                    
CRYST1   57.437   45.706   63.187  90.00 110.94  90.00 P 1 21 1      2          
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      0.017410  0.000000  0.006663        0.00000                         
SCALE2      0.000000  0.021879  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016945        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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