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Database: PDB
Entry: 5CEI
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Original site: 5CEI 
HEADER    TRANSCRIPTION/TRANSFERASE/INHIBITOR     06-JUL-15   5CEI              
TITLE     CRYSTAL STRUCTURE OF CDK8:CYCLIN C COMPLEX WITH COMPOUND 22           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 8;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-403;                                        
COMPND   5 SYNONYM: CELL DIVISION PROTEIN KINASE 8,MEDIATOR COMPLEX SUBUNIT     
COMPND   6 CDK8,MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT CDK8,PROTEIN
COMPND   7 KINASE K35;                                                          
COMPND   8 EC: 2.7.11.22,2.7.11.23;                                             
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: CYCLIN-C;                                                  
COMPND  12 CHAIN: B;                                                            
COMPND  13 SYNONYM: SRB11 HOMOLOG,HSRB11;                                       
COMPND  14 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: CDK8;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: CCNC;                                                          
SOURCE  13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    KINASE, INHIBITOR, CDK8, CYCLIN DEPENDENT KINASE, CYCLIN,             
KEYWDS   2 TRANSCRIPTION-TRANSFERASE-INHIBITOR COMPLEX                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.KIEFER,E.V.SCHNEIDER,K.MASKOS,M.F.T.KOEHLER                       
REVDAT   3   06-MAR-24 5CEI    1       REMARK                                   
REVDAT   2   11-MAY-16 5CEI    1       JRNL                                     
REVDAT   1   10-FEB-16 5CEI    0                                                
JRNL        AUTH   M.F.KOEHLER,P.BERGERON,E.M.BLACKWOOD,K.BOWMAN,K.R.CLARK,     
JRNL        AUTH 2 R.FIRESTEIN,J.R.KIEFER,K.MASKOS,M.L.MCCLELAND,L.ORREN,       
JRNL        AUTH 3 L.SALPHATI,S.SCHMIDT,E.V.SCHNEIDER,J.WU,M.H.BERESINI         
JRNL        TITL   DEVELOPMENT OF A POTENT, SPECIFIC CDK8 KINASE INHIBITOR      
JRNL        TITL 2 WHICH PHENOCOPIES CDK8/19 KNOCKOUT CELLS.                    
JRNL        REF    ACS MED.CHEM.LETT.            V.   7   223 2016              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   26985305                                                     
JRNL        DOI    10.1021/ACSMEDCHEMLETT.5B00278                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.24 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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) : 2.24                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.84                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 40213                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.490                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1402                            
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 47.8538 -  4.8245    0.95     3980   146  0.1744 0.2224        
REMARK   3     2  4.8245 -  3.8299    0.97     3892   157  0.1392 0.1932        
REMARK   3     3  3.8299 -  3.3459    0.97     3832   157  0.1544 0.1997        
REMARK   3     4  3.3459 -  3.0401    0.98     3898   126  0.1676 0.2265        
REMARK   3     5  3.0401 -  2.8222    0.99     3917   137  0.1748 0.2821        
REMARK   3     6  2.8222 -  2.6558    0.98     3847   145  0.1889 0.2416        
REMARK   3     7  2.6558 -  2.5228    0.99     3857   122  0.1924 0.2640        
REMARK   3     8  2.5228 -  2.4130    0.99     3902   145  0.2038 0.2624        
REMARK   3     9  2.4130 -  2.3201    1.00     3874   142  0.2275 0.2643        
REMARK   3    10  2.3201 -  2.2400    0.97     3812   125  0.2877 0.3143        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.290           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.84                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.42                          
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      :  0.007           5319                                  
REMARK   3   ANGLE     :  0.975           7161                                  
REMARK   3   CHIRALITY :  0.038            757                                  
REMARK   3   PLANARITY :  0.005            903                                  
REMARK   3   DIHEDRAL  : 13.623           2005                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 126 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   4.0553  65.6282  54.9007              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4133 T22:   0.2929                                     
REMARK   3      T33:   0.3488 T12:   0.0046                                     
REMARK   3      T13:  -0.0329 T23:   0.0584                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4773 L22:   2.1091                                     
REMARK   3      L33:   0.8962 L12:  -0.5999                                     
REMARK   3      L13:  -0.2346 L23:   0.9574                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1553 S12:   0.2329 S13:   0.1097                       
REMARK   3      S21:  -0.3338 S22:  -0.1691 S23:   0.1572                       
REMARK   3      S31:  -0.1700 S32:  -0.1127 S33:   0.0035                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 127 THROUGH 362 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   9.7158  39.6219  57.5180              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2476 T22:   0.2607                                     
REMARK   3      T33:   0.2476 T12:   0.0159                                     
REMARK   3      T13:  -0.0285 T23:   0.0100                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8388 L22:   2.1767                                     
REMARK   3      L33:   1.3483 L12:   0.3439                                     
REMARK   3      L13:  -0.2458 L23:  -0.0550                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0060 S12:   0.1758 S13:  -0.0566                       
REMARK   3      S21:  -0.0603 S22:   0.0536 S23:   0.1284                       
REMARK   3      S31:   0.0384 S32:  -0.0708 S33:  -0.0547                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID -3 THROUGH 17 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   9.7048  64.2591  78.3370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2613 T22:   0.3498                                     
REMARK   3      T33:   0.2803 T12:  -0.0541                                     
REMARK   3      T13:   0.0724 T23:  -0.0112                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6788 L22:   8.3020                                     
REMARK   3      L33:   4.3964 L12:  -2.3883                                     
REMARK   3      L13:  -0.2761 L23:   1.2535                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1232 S12:   0.0052 S13:   0.2004                       
REMARK   3      S21:  -0.3629 S22:   0.0649 S23:  -0.0535                       
REMARK   3      S31:   0.1735 S32:   0.5206 S33:  -0.1684                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 18 THROUGH 54 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.3998  78.5175  87.7440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2945 T22:   0.2683                                     
REMARK   3      T33:   0.3322 T12:  -0.0292                                     
REMARK   3      T13:   0.0665 T23:   0.0143                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7990 L22:   3.4194                                     
REMARK   3      L33:   2.1121 L12:   0.1609                                     
REMARK   3      L13:   0.0692 L23:   0.5767                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1604 S12:  -0.0456 S13:   0.3715                       
REMARK   3      S21:  -0.1443 S22:   0.2281 S23:  -0.1676                       
REMARK   3      S31:  -0.3339 S32:   0.1604 S33:  -0.0669                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 55 THROUGH 75 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.7123  66.7069  80.7870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2460 T22:   0.2393                                     
REMARK   3      T33:   0.2074 T12:   0.0072                                     
REMARK   3      T13:   0.0393 T23:  -0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3582 L22:   4.5776                                     
REMARK   3      L33:   3.1368 L12:   0.8689                                     
REMARK   3      L13:   0.1960 L23:   0.5871                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0450 S12:   0.0693 S13:  -0.2789                       
REMARK   3      S21:  -0.2192 S22:   0.1019 S23:  -0.1935                       
REMARK   3      S31:   0.2288 S32:   0.1965 S33:  -0.0485                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 76 THROUGH 264 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.0563  67.2481  87.3844              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2405 T22:   0.2419                                     
REMARK   3      T33:   0.3038 T12:  -0.0385                                     
REMARK   3      T13:   0.0299 T23:  -0.0126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3834 L22:   1.3419                                     
REMARK   3      L33:   2.3201 L12:  -0.4417                                     
REMARK   3      L13:  -0.2862 L23:  -0.3424                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0651 S12:  -0.0617 S13:   0.0435                       
REMARK   3      S21:  -0.0651 S22:   0.0098 S23:   0.0289                       
REMARK   3      S31:  -0.0125 S32:   0.0579 S33:  -0.0821                       
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 5CEI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUL-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000211481.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-FEB-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.999996                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.16                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40329                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.240                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.843                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.24                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.44900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
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   (%): 52.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350 AND 0.20 M SODIUM           
REMARK 280  FORMATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   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       35.56400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       83.72400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.04500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       83.72400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.56400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.04500            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A    -2                                                      
REMARK 465     ASP A    -1                                                      
REMARK 465     ASN A   117                                                      
REMARK 465     LYS A   118                                                      
REMARK 465     LYS A   119                                                      
REMARK 465     PRO A   120                                                      
REMARK 465     VAL A   121                                                      
REMARK 465     LEU A   187                                                      
REMARK 465     ALA A   188                                                      
REMARK 465     ASP A   189                                                      
REMARK 465     LEU A   190                                                      
REMARK 465     ASP A   191                                                      
REMARK 465     PRO A   192                                                      
REMARK 465     VAL A   193                                                      
REMARK 465     VAL A   194                                                      
REMARK 465     VAL A   195                                                      
REMARK 465     ASP A   240                                                      
REMARK 465     ILE A   241                                                      
REMARK 465     LYS A   242                                                      
REMARK 465     THR A   243                                                      
REMARK 465     GLU A   363                                                      
REMARK 465     PRO A   364                                                      
REMARK 465     ASP A   365                                                      
REMARK 465     ASP A   366                                                      
REMARK 465     LYS A   367                                                      
REMARK 465     GLY A   368                                                      
REMARK 465     ASP A   369                                                      
REMARK 465     LYS A   370                                                      
REMARK 465     LYS A   371                                                      
REMARK 465     ASN A   372                                                      
REMARK 465     GLN A   373                                                      
REMARK 465     GLN A   374                                                      
REMARK 465     GLN A   375                                                      
REMARK 465     GLN A   376                                                      
REMARK 465     GLN A   377                                                      
REMARK 465     GLY A   378                                                      
REMARK 465     ASN A   379                                                      
REMARK 465     ASN A   380                                                      
REMARK 465     HIS A   381                                                      
REMARK 465     THR A   382                                                      
REMARK 465     ASN A   383                                                      
REMARK 465     GLY A   384                                                      
REMARK 465     THR A   385                                                      
REMARK 465     GLY A   386                                                      
REMARK 465     HIS A   387                                                      
REMARK 465     PRO A   388                                                      
REMARK 465     GLY A   389                                                      
REMARK 465     ASN A   390                                                      
REMARK 465     GLN A   391                                                      
REMARK 465     ASP A   392                                                      
REMARK 465     SER A   393                                                      
REMARK 465     SER A   394                                                      
REMARK 465     HIS A   395                                                      
REMARK 465     THR A   396                                                      
REMARK 465     GLN A   397                                                      
REMARK 465     GLY A   398                                                      
REMARK 465     PRO A   399                                                      
REMARK 465     PRO A   400                                                      
REMARK 465     LEU A   401                                                      
REMARK 465     LYS A   402                                                      
REMARK 465     LYS A   403                                                      
REMARK 465     ASN B   265                                                      
REMARK 465     SER B   266                                                      
REMARK 465     GLU B   267                                                      
REMARK 465     GLY B   268                                                      
REMARK 465     GLU B   269                                                      
REMARK 465     GLN B   270                                                      
REMARK 465     GLY B   271                                                      
REMARK 465     PRO B   272                                                      
REMARK 465     ASN B   273                                                      
REMARK 465     GLY B   274                                                      
REMARK 465     SER B   275                                                      
REMARK 465     GLN B   276                                                      
REMARK 465     ASN B   277                                                      
REMARK 465     SER B   278                                                      
REMARK 465     SER B   279                                                      
REMARK 465     TYR B   280                                                      
REMARK 465     SER B   281                                                      
REMARK 465     GLN B   282                                                      
REMARK 465     SER B   283                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 115    CG   CD   CE   NZ                                   
REMARK 470     GLU A 357    CG   CD   OE1  OE2                                  
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A    6   CD   CE   NZ                                        
REMARK 480     ARG A   15   NE   CZ   NH1  NH2                                  
REMARK 480     GLU A   23   CG   CD   OE1  OE2                                  
REMARK 480     ARG A   29   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS A   39   CE   NZ                                             
REMARK 480     ASP A   42   CG   OD1  OD2                                       
REMARK 480     LYS A   44   CG   CD   CE   NZ                                   
REMARK 480     ASP A   46   CG   OD1  OD2                                       
REMARK 480     LYS A   47   NZ                                                  
REMARK 480     ILE A   59   CD1                                                 
REMARK 480     LYS A   74   CG   CD   CE   NZ                                   
REMARK 480     LYS A   83   CE   NZ                                             
REMARK 480     LYS A  109   CE   NZ                                             
REMARK 480     ARG A  112   CZ   NH1  NH2                                       
REMARK 480     GLN A  122   CD   OE1  NE2                                       
REMARK 480     LEU A  123   CG   CD1  CD2                                       
REMARK 480     ARG A  125   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS A  185   NZ                                                  
REMARK 480     ARG A  237   CZ   NH1  NH2                                       
REMARK 480     GLN A  238   CG   CD   OE1  NE2                                  
REMARK 480     SER A  244   OG                                                  
REMARK 480     LYS A  265   CD   CE   NZ                                        
REMARK 480     LYS A  271   CG   CD   CE   NZ                                   
REMARK 480     LYS A  272   CE   NZ                                             
REMARK 480     LYS A  281   CD   CE   NZ                                        
REMARK 480     ARG A  284   CZ   NH1  NH2                                       
REMARK 480     LYS A  295   CE   NZ                                             
REMARK 480     LYS A  301   CD   CE   NZ                                        
REMARK 480     LYS A  303   CE   NZ                                             
REMARK 480     GLN A  350   CG   CD   OE1  NE2                                  
REMARK 480     LYS A  355   CD   CE   NZ                                        
REMARK 480     ASP B   -3   CG   OD1  OD2                                       
REMARK 480     LYS B   -1   CG   CD   CE   NZ                                   
REMARK 480     LYS B   18   NZ                                                  
REMARK 480     LEU B   22   CD1  CD2                                            
REMARK 480     LYS B   23   CG   CD   CE   NZ                                   
REMARK 480     LYS B   27   CE   NZ                                             
REMARK 480     LYS B   30   CD   CE   NZ                                        
REMARK 480     LYS B   56   CD   CE   NZ                                        
REMARK 480     GLN B   60   CD   OE1  NE2                                       
REMARK 480     LYS B   79   CE   NZ                                             
REMARK 480     VAL B  102   CG1  CG2                                            
REMARK 480     LYS B  117   CD   CE   NZ                                        
REMARK 480     LYS B  126   CD   CE   NZ                                        
REMARK 480     GLU B  127   CG   CD   OE1  OE2                                  
REMARK 480     ARG B  131   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLU B  137   CD   OE1  OE2                                       
REMARK 480     GLN B  164   CD   OE1  NE2                                       
REMARK 480     GLU B  169   CD   OE1  OE2                                       
REMARK 480     MET B  171   CE                                                  
REMARK 480     GLN B  210   CD   OE1  NE2                                       
REMARK 480     LYS B  211   CD   CE   NZ                                        
REMARK 480     GLN B  215   CD   OE1  NE2                                       
REMARK 480     SER B  221   OG                                                  
REMARK 480     GLU B  225   CG   CD   OE1  OE2                                  
REMARK 480     LYS B  226   CE   NZ                                             
REMARK 480     LYS B  236   CD   CE   NZ                                        
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   O2   EDO B   307     O    HOH B   401              2.13            
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    TYR A  22        7.10   -152.09                                   
REMARK 500    ASP A  46       29.59     44.46                                   
REMARK 500    ASP A 151       39.68   -153.63                                   
REMARK 500    LEU A 316       55.54    -90.76                                   
REMARK 500    SER B 221       76.08   -106.34                                   
REMARK 500    ASP B 223       97.82    -64.52                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLN A  238     GLU A  239                  145.19                    
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 EDO A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 50R A 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 307                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4G6L   RELATED DB: PDB                                   
DBREF  5CEI A    1   403  UNP    P49336   CDK8_HUMAN       1    403             
DBREF  5CEI B    1   283  UNP    P24863   CCNC_HUMAN       1    283             
SEQADV 5CEI ASP A   -2  UNP  P49336              EXPRESSION TAG                 
SEQADV 5CEI ASP A   -1  UNP  P49336              EXPRESSION TAG                 
SEQADV 5CEI LYS A    0  UNP  P49336              EXPRESSION TAG                 
SEQADV 5CEI ASP B   -3  UNP  P24863              EXPRESSION TAG                 
SEQADV 5CEI ASP B   -2  UNP  P24863              EXPRESSION TAG                 
SEQADV 5CEI LYS B   -1  UNP  P24863              EXPRESSION TAG                 
SEQADV 5CEI ALA B    0  UNP  P24863              EXPRESSION TAG                 
SEQRES   1 A  406  ASP ASP LYS MET ASP TYR ASP PHE LYS VAL LYS LEU SER          
SEQRES   2 A  406  SER GLU ARG GLU ARG VAL GLU ASP LEU PHE GLU TYR GLU          
SEQRES   3 A  406  GLY CYS LYS VAL GLY ARG GLY THR TYR GLY HIS VAL TYR          
SEQRES   4 A  406  LYS ALA LYS ARG LYS ASP GLY LYS ASP ASP LYS ASP TYR          
SEQRES   5 A  406  ALA LEU LYS GLN ILE GLU GLY THR GLY ILE SER MET SER          
SEQRES   6 A  406  ALA CYS ARG GLU ILE ALA LEU LEU ARG GLU LEU LYS HIS          
SEQRES   7 A  406  PRO ASN VAL ILE SER LEU GLN LYS VAL PHE LEU SER HIS          
SEQRES   8 A  406  ALA ASP ARG LYS VAL TRP LEU LEU PHE ASP TYR ALA GLU          
SEQRES   9 A  406  HIS ASP LEU TRP HIS ILE ILE LYS PHE HIS ARG ALA SER          
SEQRES  10 A  406  LYS ALA ASN LYS LYS PRO VAL GLN LEU PRO ARG GLY MET          
SEQRES  11 A  406  VAL LYS SER LEU LEU TYR GLN ILE LEU ASP GLY ILE HIS          
SEQRES  12 A  406  TYR LEU HIS ALA ASN TRP VAL LEU HIS ARG ASP LEU LYS          
SEQRES  13 A  406  PRO ALA ASN ILE LEU VAL MET GLY GLU GLY PRO GLU ARG          
SEQRES  14 A  406  GLY ARG VAL LYS ILE ALA ASP MET GLY PHE ALA ARG LEU          
SEQRES  15 A  406  PHE ASN SER PRO LEU LYS PRO LEU ALA ASP LEU ASP PRO          
SEQRES  16 A  406  VAL VAL VAL THR PHE TRP TYR ARG ALA PRO GLU LEU LEU          
SEQRES  17 A  406  LEU GLY ALA ARG HIS TYR THR LYS ALA ILE ASP ILE TRP          
SEQRES  18 A  406  ALA ILE GLY CYS ILE PHE ALA GLU LEU LEU THR SER GLU          
SEQRES  19 A  406  PRO ILE PHE HIS CYS ARG GLN GLU ASP ILE LYS THR SER          
SEQRES  20 A  406  ASN PRO TYR HIS HIS ASP GLN LEU ASP ARG ILE PHE ASN          
SEQRES  21 A  406  VAL MET GLY PHE PRO ALA ASP LYS ASP TRP GLU ASP ILE          
SEQRES  22 A  406  LYS LYS MET PRO GLU HIS SER THR LEU MET LYS ASP PHE          
SEQRES  23 A  406  ARG ARG ASN THR TYR THR ASN CYS SER LEU ILE LYS TYR          
SEQRES  24 A  406  MET GLU LYS HIS LYS VAL LYS PRO ASP SER LYS ALA PHE          
SEQRES  25 A  406  HIS LEU LEU GLN LYS LEU LEU THR MET ASP PRO ILE LYS          
SEQRES  26 A  406  ARG ILE THR SER GLU GLN ALA MET GLN ASP PRO TYR PHE          
SEQRES  27 A  406  LEU GLU ASP PRO LEU PRO THR SER ASP VAL PHE ALA GLY          
SEQRES  28 A  406  CYS GLN ILE PRO TYR PRO LYS ARG GLU PHE LEU THR GLU          
SEQRES  29 A  406  GLU GLU PRO ASP ASP LYS GLY ASP LYS LYS ASN GLN GLN          
SEQRES  30 A  406  GLN GLN GLN GLY ASN ASN HIS THR ASN GLY THR GLY HIS          
SEQRES  31 A  406  PRO GLY ASN GLN ASP SER SER HIS THR GLN GLY PRO PRO          
SEQRES  32 A  406  LEU LYS LYS                                                  
SEQRES   1 B  287  ASP ASP LYS ALA MET ALA GLY ASN PHE TRP GLN SER SER          
SEQRES   2 B  287  HIS TYR LEU GLN TRP ILE LEU ASP LYS GLN ASP LEU LEU          
SEQRES   3 B  287  LYS GLU ARG GLN LYS ASP LEU LYS PHE LEU SER GLU GLU          
SEQRES   4 B  287  GLU TYR TRP LYS LEU GLN ILE PHE PHE THR ASN VAL ILE          
SEQRES   5 B  287  GLN ALA LEU GLY GLU HIS LEU LYS LEU ARG GLN GLN VAL          
SEQRES   6 B  287  ILE ALA THR ALA THR VAL TYR PHE LYS ARG PHE TYR ALA          
SEQRES   7 B  287  ARG TYR SER LEU LYS SER ILE ASP PRO VAL LEU MET ALA          
SEQRES   8 B  287  PRO THR CYS VAL PHE LEU ALA SER LYS VAL GLU GLU PHE          
SEQRES   9 B  287  GLY VAL VAL SER ASN THR ARG LEU ILE ALA ALA ALA THR          
SEQRES  10 B  287  SER VAL LEU LYS THR ARG PHE SER TYR ALA PHE PRO LYS          
SEQRES  11 B  287  GLU PHE PRO TYR ARG MET ASN HIS ILE LEU GLU CYS GLU          
SEQRES  12 B  287  PHE TYR LEU LEU GLU LEU MET ASP CYS CYS LEU ILE VAL          
SEQRES  13 B  287  TYR HIS PRO TYR ARG PRO LEU LEU GLN TYR VAL GLN ASP          
SEQRES  14 B  287  MET GLY GLN GLU ASP MET LEU LEU PRO LEU ALA TRP ARG          
SEQRES  15 B  287  ILE VAL ASN ASP THR TYR ARG THR ASP LEU CYS LEU LEU          
SEQRES  16 B  287  TYR PRO PRO PHE MET ILE ALA LEU ALA CYS LEU HIS VAL          
SEQRES  17 B  287  ALA CYS VAL VAL GLN GLN LYS ASP ALA ARG GLN TRP PHE          
SEQRES  18 B  287  ALA GLU LEU SER VAL ASP MET GLU LYS ILE LEU GLU ILE          
SEQRES  19 B  287  ILE ARG VAL ILE LEU LYS LEU TYR GLU GLN TRP LYS ASN          
SEQRES  20 B  287  PHE ASP GLU ARG LYS GLU MET ALA THR ILE LEU SER LYS          
SEQRES  21 B  287  MET PRO LYS PRO LYS PRO PRO PRO ASN SER GLU GLY GLU          
SEQRES  22 B  287  GLN GLY PRO ASN GLY SER GLN ASN SER SER TYR SER GLN          
SEQRES  23 B  287  SER                                                          
HET    EDO  A 501       4                                                       
HET    EDO  A 502       4                                                       
HET    EDO  A 503       4                                                       
HET    EDO  A 504       4                                                       
HET    FMT  A 505       3                                                       
HET    FMT  A 506       3                                                       
HET    FMT  A 507       3                                                       
HET    50R  A 508      21                                                       
HET    EDO  A 509       4                                                       
HET    EDO  B 301       4                                                       
HET    EDO  B 302       4                                                       
HET    FMT  B 303       3                                                       
HET    FMT  B 304       3                                                       
HET    FMT  B 305       3                                                       
HET    FMT  B 306       3                                                       
HET    EDO  B 307       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     FMT FORMIC ACID                                                      
HETNAM     50R 4-(4-IODOPHENOXY)-N-METHYLTHIENO[2,3-C]PYRIDINE-2-               
HETNAM   2 50R  CARBOXAMIDE                                                     
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  EDO    8(C2 H6 O2)                                                  
FORMUL   7  FMT    7(C H2 O2)                                                   
FORMUL  10  50R    C15 H11 I N2 O2 S                                            
FORMUL  19  HOH   *180(H2 O)                                                    
HELIX    1 AA1 ASP A    2  ARG A   13  1                                  12    
HELIX    2 AA2 ARG A   15  LEU A   19  1                                   5    
HELIX    3 AA3 SER A   60  ARG A   71  1                                  12    
HELIX    4 AA4 LEU A  104  SER A  114  1                                  11    
HELIX    5 AA5 GLY A  126  ASN A  145  1                                  20    
HELIX    6 AA6 LYS A  153  ALA A  155  5                                   3    
HELIX    7 AA7 ARG A  178  SER A  182  5                                   5    
HELIX    8 AA8 ALA A  201  LEU A  206  1                                   6    
HELIX    9 AA9 THR A  212  SER A  230  1                                  19    
HELIX   10 AB1 HIS A  248  GLY A  260  1                                  13    
HELIX   11 AB2 TRP A  267  MET A  273  5                                   7    
HELIX   12 AB3 GLU A  275  PHE A  283  1                                   9    
HELIX   13 AB4 ARG A  284  THR A  289  5                                   6    
HELIX   14 AB5 SER A  292  HIS A  300  1                                   9    
HELIX   15 AB6 SER A  306  LEU A  316  1                                  11    
HELIX   16 AB7 ASP A  319  ARG A  323  5                                   5    
HELIX   17 AB8 THR A  325  GLN A  331  1                                   7    
HELIX   18 AB9 ASP A  332  GLU A  337  5                                   6    
HELIX   19 AC1 ASN B    4  GLN B    7  5                                   4    
HELIX   20 AC2 SER B    8  ILE B   15  1                                   8    
HELIX   21 AC3 ASP B   17  GLN B   26  1                                  10    
HELIX   22 AC4 LYS B   27  PHE B   31  5                                   5    
HELIX   23 AC5 SER B   33  LEU B   55  1                                  23    
HELIX   24 AC6 ARG B   58  TYR B   76  1                                  19    
HELIX   25 AC7 ASP B   82  GLU B   98  1                                  17    
HELIX   26 AC8 SER B  104  PHE B  120  1                                  17    
HELIX   27 AC9 ARG B  131  MET B  146  1                                  16    
HELIX   28 AD1 PRO B  155  GLY B  167  1                                  13    
HELIX   29 AD2 GLN B  168  TYR B  184  1                                  17    
HELIX   30 AD3 ASP B  187  TYR B  192  1                                   6    
HELIX   31 AD4 PRO B  193  GLN B  209  1                                  17    
HELIX   32 AD5 ALA B  213  GLU B  219  1                                   7    
HELIX   33 AD6 ASP B  223  PHE B  244  1                                  22    
HELIX   34 AD7 ASP B  245  MET B  257  1                                  13    
SHEET    1 AA1 3 PHE A  20  GLU A  21  0                                        
SHEET    2 AA1 3 GLY A  33  ARG A  40 -1  O  LYS A  39   N  GLU A  21           
SHEET    3 AA1 3 LYS A  26  ARG A  29 -1  N  GLY A  28   O  VAL A  35           
SHEET    1 AA2 5 PHE A  20  GLU A  21  0                                        
SHEET    2 AA2 5 GLY A  33  ARG A  40 -1  O  LYS A  39   N  GLU A  21           
SHEET    3 AA2 5 ASP A  48  ILE A  54 -1  O  LEU A  51   N  TYR A  36           
SHEET    4 AA2 5 LYS A  92  ASP A  98 -1  O  LEU A  95   N  LYS A  52           
SHEET    5 AA2 5 LEU A  81  SER A  87 -1  N  PHE A  85   O  TRP A  94           
SHEET    1 AA3 3 HIS A 102  ASP A 103  0                                        
SHEET    2 AA3 3 ILE A 157  VAL A 159 -1  O  VAL A 159   N  HIS A 102           
SHEET    3 AA3 3 VAL A 169  ILE A 171 -1  O  LYS A 170   N  LEU A 158           
CISPEP   1 ASP A  338    PRO A  339          0        -1.62                     
SITE     1 AC1  4 ARG A  71  GLU A  72  SER B   9  GLN B  13                    
SITE     1 AC2  1 TYR A 141                                                     
SITE     1 AC3  6 GLU A  17  PHE A  20  GLU A  21  TYR A  22                    
SITE     2 AC3  6 GLU A  23  LYS A  41                                          
SITE     1 AC4  3 LYS A 301  VAL A 302  LYS A 303                               
SITE     1 AC5  5 LYS A  52  GLU A  66  ALA A 172  ASP A 173                    
SITE     2 AC5  5 50R A 508                                                     
SITE     1 AC6  3 GLU A 165  ARG A 166  ARG A 168                               
SITE     1 AC7  2 ARG A 168  SER A 343                                          
SITE     1 AC8 15 VAL A  27  TYR A  32  VAL A  35  ALA A  50                    
SITE     2 AC8 15 LYS A  52  ILE A  79  TYR A  99  ALA A 100                    
SITE     3 AC8 15 ASP A 103  ALA A 155  LEU A 158  ASP A 173                    
SITE     4 AC8 15 ARG A 356  FMT A 505  HOH A 668                               
SITE     1 AC9  4 ASP A 305  HIS A 310  LYS B 242  ASN B 243                    
SITE     1 AD1  1 HOH B 414                                                     
SITE     1 AD2  4 GLU B  35  GLU B 239  GLN B 240  ASN B 243                    
SITE     1 AD3  4 ALA B   0  ALA B   2  VAL B 152  ARG B 157                    
SITE     1 AD4  4 PHE B  31  SER B 255  LYS B 256  MET B 257                    
SITE     1 AD5  2 ARG B  58  GLN B  59                                          
SITE     1 AD6  2 LEU B  57  GLN B  59                                          
SITE     1 AD7  6 ILE B  42  ASN B  46  TRP B 241  PHE B 244                    
SITE     2 AD7  6 GLU B 246  HOH B 401                                          
CRYST1   71.128   70.090  167.448  90.00  90.00  90.00 P 21 21 21    4          
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      0.014059  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014267  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005972        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system