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Database: PDB
Entry: 5BVD
LinkDB: 5BVD
Original site: 5BVD 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       05-JUN-15   5BVD              
TITLE     TETRAHYDROPYRROLO-DIAZEPENONES AS INHIBITORS OF ERK2 KINASE           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MAPK 1,ERT1,EXTRACELLULAR SIGNAL-REGULATED KINASE 2,ERK-2,  
COMPND   5 MAP KINASE ISOFORM P42,P42-MAPK,MITOGEN-ACTIVATED PROTEIN KINASE 2,  
COMPND   6 MAPK 2;                                                              
COMPND   7 EC: 2.7.11.24;                                                       
COMPND   8 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: MAPK1, ERK2, PRKM1, PRKM2;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    INHIBITOR, KINASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.MA,S.STEVEN                                                         
REVDAT   1   09-SEP-15 5BVD    0                                                
JRNL        AUTH   J.T.BAGDANOFF,R.JAIN,W.HAN,S.ZHU,A.M.MADIERA,P.S.LEE,X.MA,   
JRNL        AUTH 2 D.POON                                                       
JRNL        TITL   TETRAHYDROPYRROLO-DIAZEPENONES AS INHIBITORS OF ERK2 KINASE. 
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  25  3788 2015              
JRNL        REFN                   ESSN 1464-3405                               
JRNL        PMID   26259804                                                     
JRNL        DOI    10.1016/J.BMCL.2015.07.091                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 61.35                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 30837                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.207                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1550                            
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 61.3768 -  4.2252    1.00     2834   165  0.1678 0.1936        
REMARK   3     2  4.2252 -  3.3537    1.00     2700   152  0.1476 0.1925        
REMARK   3     3  3.3537 -  2.9298    1.00     2670   138  0.1734 0.2001        
REMARK   3     4  2.9298 -  2.6619    1.00     2675   140  0.1791 0.1965        
REMARK   3     5  2.6619 -  2.4711    1.00     2631   132  0.1761 0.2080        
REMARK   3     6  2.4711 -  2.3254    1.00     2664   118  0.1735 0.2630        
REMARK   3     7  2.3254 -  2.2090    1.00     2633   143  0.1785 0.2363        
REMARK   3     8  2.2090 -  2.1128    1.00     2619   142  0.1700 0.2072        
REMARK   3     9  2.1128 -  2.0315    1.00     2621   147  0.1773 0.2052        
REMARK   3    10  2.0315 -  1.9614    1.00     2622   139  0.1986 0.2457        
REMARK   3    11  1.9614 -  1.9000    1.00     2618   134  0.2070 0.2495        
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)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.790           
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      :  0.008           2821                                  
REMARK   3   ANGLE     :  1.058           3824                                  
REMARK   3   CHIRALITY :  0.045            413                                  
REMARK   3   PLANARITY :  0.005            506                                  
REMARK   3   DIHEDRAL  : 14.410           1058                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   6.9024   2.9630  20.1529              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0753 T22:   0.0669                                     
REMARK   3      T33:   0.0890 T12:   0.0059                                     
REMARK   3      T13:   0.0025 T23:  -0.0104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2971 L22:   0.1180                                     
REMARK   3      L33:   0.9244 L12:   0.0055                                     
REMARK   3      L13:  -0.1399 L23:   0.2285                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0026 S12:   0.0444 S13:  -0.0246                       
REMARK   3      S21:   0.0178 S22:  -0.0239 S23:  -0.0112                       
REMARK   3      S31:  -0.0200 S32:  -0.0651 S33:  -0.0000                       
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 5BVD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000210592.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-JUN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : PROCESS                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30901                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 71.280                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: 1ERK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20MM MG SULFATE, 20% PEG 3350, VAPOR     
REMARK 280  DIFFUSION, SITTING 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       22.13550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.22550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.64100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.22550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.13550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.64100            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -2                                                      
REMARK 465     PRO A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     ALA A   172                                                      
REMARK 465     ASP A   173                                                      
REMARK 465     PRO A   174                                                      
REMARK 465     ASP A   175                                                      
REMARK 465     HIS A   176                                                      
REMARK 465     ASP A   177                                                      
REMARK 465     HIS A   178                                                      
REMARK 465     THR A   179                                                      
REMARK 465     GLY A   180                                                      
REMARK 465     PHE A   181                                                      
REMARK 465     LEU A   182                                                      
REMARK 465     THR A   183                                                      
REMARK 465     GLU A   184                                                      
REMARK 465     TYR A   185                                                      
REMARK 465     VAL A   186                                                      
REMARK 465     ALA A   187                                                      
REMARK 465     SER A   200                                                      
REMARK 465     LYS A   201                                                      
REMARK 465     GLY A   202                                                      
REMARK 465     TYR A   203                                                      
REMARK 465     ARG A   357                                                      
REMARK 465     SER A   358                                                      
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   734     O    HOH A   755              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD1  ASN A   251     O    HOH A   606     1455     2.17            
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    ARG A 146       -6.37     78.16                                   
REMARK 500    ASP A 147       49.83   -141.79                                   
REMARK 500    ASP A 165       83.25     58.49                                   
REMARK 500    LEU A 292       51.80    -94.59                                   
REMARK 500    ASP A 316       83.71   -153.46                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 788        DISTANCE =  6.78 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 4VF A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 406                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5BVE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5BVF   RELATED DB: PDB                                   
DBREF  5BVD A    0   358  UNP    P28482   MK01_HUMAN       2    360             
SEQADV 5BVD GLY A   -2  UNP  P28482              EXPRESSION TAG                 
SEQADV 5BVD PRO A   -1  UNP  P28482              EXPRESSION TAG                 
SEQRES   1 A  361  GLY PRO ALA ALA ALA ALA ALA ALA GLY ALA GLY PRO GLU          
SEQRES   2 A  361  MET VAL ARG GLY GLN VAL PHE ASP VAL GLY PRO ARG TYR          
SEQRES   3 A  361  THR ASN LEU SER TYR ILE GLY GLU GLY ALA TYR GLY MET          
SEQRES   4 A  361  VAL CYS SER ALA TYR ASP ASN VAL ASN LYS VAL ARG VAL          
SEQRES   5 A  361  ALA ILE LYS LYS ILE SER PRO PHE GLU HIS GLN THR TYR          
SEQRES   6 A  361  CYS GLN ARG THR LEU ARG GLU ILE LYS ILE LEU LEU ARG          
SEQRES   7 A  361  PHE ARG HIS GLU ASN ILE ILE GLY ILE ASN ASP ILE ILE          
SEQRES   8 A  361  ARG ALA PRO THR ILE GLU GLN MET LYS ASP VAL TYR ILE          
SEQRES   9 A  361  VAL GLN ASP LEU MET GLU THR ASP LEU TYR LYS LEU LEU          
SEQRES  10 A  361  LYS THR GLN HIS LEU SER ASN ASP HIS ILE CYS TYR PHE          
SEQRES  11 A  361  LEU TYR GLN ILE LEU ARG GLY LEU LYS TYR ILE HIS SER          
SEQRES  12 A  361  ALA ASN VAL LEU HIS ARG ASP LEU LYS PRO SER ASN LEU          
SEQRES  13 A  361  LEU LEU ASN THR THR CYS ASP LEU LYS ILE CYS ASP PHE          
SEQRES  14 A  361  GLY LEU ALA ARG VAL ALA ASP PRO ASP HIS ASP HIS THR          
SEQRES  15 A  361  GLY PHE LEU THR GLU TYR VAL ALA THR ARG TRP TYR ARG          
SEQRES  16 A  361  ALA PRO GLU ILE MET LEU ASN SER LYS GLY TYR THR LYS          
SEQRES  17 A  361  SER ILE ASP ILE TRP SER VAL GLY CYS ILE LEU ALA GLU          
SEQRES  18 A  361  MET LEU SER ASN ARG PRO ILE PHE PRO GLY LYS HIS TYR          
SEQRES  19 A  361  LEU ASP GLN LEU ASN HIS ILE LEU GLY ILE LEU GLY SER          
SEQRES  20 A  361  PRO SER GLN GLU ASP LEU ASN CYS ILE ILE ASN LEU LYS          
SEQRES  21 A  361  ALA ARG ASN TYR LEU LEU SER LEU PRO HIS LYS ASN LYS          
SEQRES  22 A  361  VAL PRO TRP ASN ARG LEU PHE PRO ASN ALA ASP SER LYS          
SEQRES  23 A  361  ALA LEU ASP LEU LEU ASP LYS MET LEU THR PHE ASN PRO          
SEQRES  24 A  361  HIS LYS ARG ILE GLU VAL GLU GLN ALA LEU ALA HIS PRO          
SEQRES  25 A  361  TYR LEU GLU GLN TYR TYR ASP PRO SER ASP GLU PRO ILE          
SEQRES  26 A  361  ALA GLU ALA PRO PHE LYS PHE ASP MET GLU LEU ASP ASP          
SEQRES  27 A  361  LEU PRO LYS GLU LYS LEU LYS GLU LEU ILE PHE GLU GLU          
SEQRES  28 A  361  THR ALA ARG PHE GLN PRO GLY TYR ARG SER                      
HET    4VF  A 401      33                                                       
HET    SO4  A 402       5                                                       
HET    SO4  A 403      10                                                       
HET    SO4  A 404       5                                                       
HET    SO4  A 405       5                                                       
HET    SO4  A 406       5                                                       
HETNAM     4VF 2-[(1S)-1-(3-CHLOROPHENYL)-2-HYDROXYETHYL]-7-[2-                 
HETNAM   2 4VF  (TETRAHYDRO-2H-PYRAN-4-YLAMINO)PYRIMIDIN-4-YL]-3,4-             
HETNAM   3 4VF  DIHYDROPYRROLO[1,2-A]PYRAZIN-1(2H)-ONE                          
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  4VF    C24 H26 CL N5 O3                                             
FORMUL   3  SO4    5(O4 S 2-)                                                   
FORMUL   8  HOH   *288(H2 O)                                                    
HELIX    1 AA1 HIS A   59  PHE A   76  1                                  18    
HELIX    2 AA2 LEU A  110  GLN A  117  1                                   8    
HELIX    3 AA3 SER A  120  ALA A  141  1                                  22    
HELIX    4 AA4 LYS A  149  SER A  151  5                                   3    
HELIX    5 AA5 THR A  188  ARG A  192  5                                   5    
HELIX    6 AA6 ALA A  193  ASN A  199  1                                   7    
HELIX    7 AA7 LYS A  205  ASN A  222  1                                  18    
HELIX    8 AA8 HIS A  230  GLY A  243  1                                  14    
HELIX    9 AA9 SER A  246  ASN A  251  1                                   6    
HELIX   10 AB1 ASN A  255  SER A  264  1                                  10    
HELIX   11 AB2 PRO A  272  PHE A  277  1                                   6    
HELIX   12 AB3 ASP A  281  LEU A  292  1                                  12    
HELIX   13 AB4 ASN A  295  ARG A  299  5                                   5    
HELIX   14 AB5 GLU A  301  ALA A  307  1                                   7    
HELIX   15 AB6 HIS A  308  GLU A  312  5                                   5    
HELIX   16 AB7 ASP A  316  GLU A  320  5                                   5    
HELIX   17 AB8 GLU A  332  LEU A  336  5                                   5    
HELIX   18 AB9 PRO A  337  ALA A  350  1                                  14    
HELIX   19 AC1 ARG A  351  GLN A  353  5                                   3    
SHEET    1 AA1 2 GLU A  10  VAL A  12  0                                        
SHEET    2 AA1 2 GLN A  15  PHE A  17 -1  O  PHE A  17   N  GLU A  10           
SHEET    1 AA2 5 TYR A  23  GLY A  32  0                                        
SHEET    2 AA2 5 GLY A  35  ASP A  42 -1  O  TYR A  41   N  THR A  24           
SHEET    3 AA2 5 VAL A  47  ILE A  54 -1  O  ILE A  51   N  CYS A  38           
SHEET    4 AA2 5 VAL A  99  ASP A 104 -1  O  ILE A 101   N  LYS A  52           
SHEET    5 AA2 5 ASP A  86  ILE A  88 -1  N  ASP A  86   O  VAL A 102           
SHEET    1 AA3 3 THR A 108  ASP A 109  0                                        
SHEET    2 AA3 3 LEU A 153  LEU A 155 -1  O  LEU A 155   N  THR A 108           
SHEET    3 AA3 3 LEU A 161  ILE A 163 -1  O  LYS A 162   N  LEU A 154           
CISPEP   1 GLY A   20    PRO A   21          0         3.64                     
SITE     1 AC1 19 GLU A  31  GLY A  32  TYR A  34  GLY A  35                    
SITE     2 AC1 19 MET A  36  VAL A  37  ALA A  50  LYS A  52                    
SITE     3 AC1 19 ASP A 104  MET A 106  GLU A 107  THR A 108                    
SITE     4 AC1 19 ASP A 109  LYS A 112  ASN A 152  LEU A 154                    
SITE     5 AC1 19 ASP A 165  HOH A 537  HOH A 665                               
SITE     1 AC2  4 LYS A  46  HIS A 267  LYS A 340  HOH A 531                    
SITE     1 AC3  4 GLU A  58  HIS A  59  GLN A  60  THR A  61                    
SITE     1 AC4  4 ARG A  13  SER A  27  TYR A  28  HOH A 528                    
SITE     1 AC5  6 ARG A 189  ARG A 192  HIS A 230  TYR A 231                    
SITE     2 AC5  6 GLN A 304  HOH A 696                                          
SITE     1 AC6  5 THR A  61  ARG A  65  ARG A 146  ARG A 170                    
SITE     2 AC6  5 HOH A 506                                                     
CRYST1   44.271   71.282  120.451  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      0.022588  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014029  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008302        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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