GenomeNet

Database: PDB
Entry: 4XOZ
LinkDB: 4XOZ
Original site: 4XOZ 
HEADER    TRANSFERASE                             16-JAN-15   4XOZ              
TITLE     CRYSTAL STRUCTURE OF ERK2 IN COMPLEX WITH AN INHIBITOR                
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: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: MAPK1, ERK2, MAPK, PRKM1;                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.GELIN,F.ALLEMAND,G.LABESSE,J.F.GUICHOU                              
REVDAT   3   06-SEP-17 4XOZ    1       REMARK SITE   ATOM                       
REVDAT   2   19-AUG-15 4XOZ    1       JRNL                                     
REVDAT   1   12-AUG-15 4XOZ    0                                                
JRNL        AUTH   M.GELIN,V.DELFOSSE,F.ALLEMAND,F.HOH,Y.SALLAZ-DAMAZ,          
JRNL        AUTH 2 M.PIROCCHI,W.BOURGUET,J.L.FERRER,G.LABESSE,J.F.GUICHOU       
JRNL        TITL   COMBINING `DRY' CO-CRYSTALLIZATION AND IN SITU DIFFRACTION   
JRNL        TITL 2 TO FACILITATE LIGAND SCREENING BY X-RAY CRYSTALLOGRAPHY.     
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  71  1777 2015              
JRNL        REFN                   ESSN 1399-0047                               
JRNL        PMID   26249358                                                     
JRNL        DOI    10.1107/S1399004715010342                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.95                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.260                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 85.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 27176                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.147                           
REMARK   3   R VALUE            (WORKING SET) : 0.145                           
REMARK   3   FREE R VALUE                     : 0.188                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.110                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2515                            
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 28.9521 -  5.1017    0.85     2566   122  0.1350 0.1538        
REMARK   3     2  5.1017 -  4.0530    0.87     2625   158  0.1141 0.1587        
REMARK   3     3  4.0530 -  3.5417    0.89     2708   126  0.1158 0.1763        
REMARK   3     4  3.5417 -  3.2183    0.89     2666   133  0.1402 0.1832        
REMARK   3     5  3.2183 -  2.9879    0.89     2725   139  0.1434 0.1706        
REMARK   3     6  2.9879 -  2.8119    0.90     2702   142  0.1555 0.2005        
REMARK   3     7  2.8119 -  2.6712    0.90     2726   151  0.1522 0.2224        
REMARK   3     8  2.6712 -  2.5550    0.91     2709   173  0.1569 0.1934        
REMARK   3     9  2.5550 -  2.4567    0.90     2725   162  0.1565 0.2081        
REMARK   3    10  2.4567 -  2.3719    0.90     2743   148  0.1664 0.2362        
REMARK   3    11  2.3719 -  2.2978    0.91     2726   161  0.1646 0.2189        
REMARK   3    12  2.2978 -  2.2321    0.92     2731   149  0.1677 0.1940        
REMARK   3    13  2.2321 -  2.1734    0.91     2728   178  0.1637 0.2064        
REMARK   3    14  2.1734 -  2.1204    0.91     2723   176  0.1721 0.1970        
REMARK   3    15  2.1204 -  2.0722    0.88     2680   136  0.1803 0.2164        
REMARK   3    16  2.0722 -  2.0281    0.79     2403    94  0.1937 0.2428        
REMARK   3    17  2.0281 -  1.9875    0.66     2023    87  0.2265 0.2810        
REMARK   3    18  1.9875 -  1.9500    0.58     1754    80  0.2414 0.2682        
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)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.420           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.44                          
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      :  0.012           2927                                  
REMARK   3   ANGLE     :  1.424           3967                                  
REMARK   3   CHIRALITY :  0.062            438                                  
REMARK   3   PLANARITY :  0.007            504                                  
REMARK   3   DIHEDRAL  : 14.354           1114                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 9:118)                              
REMARK   3    ORIGIN FOR THE GROUP (A): -13.5128  12.7231  34.5441              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3268 T22:   0.3337                                     
REMARK   3      T33:   0.2574 T12:   0.0110                                     
REMARK   3      T13:  -0.0354 T23:   0.0553                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5619 L22:   0.0615                                     
REMARK   3      L33:   3.1190 L12:   0.0274                                     
REMARK   3      L13:  -0.9726 L23:  -0.0767                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0265 S12:   0.2616 S13:   0.2481                       
REMARK   3      S21:  -0.1210 S22:   0.0708 S23:   0.0783                       
REMARK   3      S31:  -0.4224 S32:  -0.4985 S33:  -0.0920                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 119:312)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   1.6291   7.9980  58.3074              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1267 T22:   0.0976                                     
REMARK   3      T33:   0.1510 T12:   0.0162                                     
REMARK   3      T13:   0.0192 T23:   0.0008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1773 L22:   0.7683                                     
REMARK   3      L33:   1.3591 L12:   0.9797                                     
REMARK   3      L13:   1.0372 L23:   0.2412                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0134 S12:   0.0572 S13:   0.1375                       
REMARK   3      S21:  -0.0017 S22:   0.0134 S23:  -0.0365                       
REMARK   3      S31:  -0.0826 S32:   0.0917 S33:  -0.0032                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 313:354)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.4147   0.2926  35.1931              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2589 T22:   0.2757                                     
REMARK   3      T33:   0.2503 T12:  -0.0135                                     
REMARK   3      T13:   0.0123 T23:  -0.0133                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7780 L22:   1.5051                                     
REMARK   3      L33:   3.2735 L12:  -0.1020                                     
REMARK   3      L13:  -0.0238 L23:  -1.8052                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0049 S12:   0.2078 S13:  -0.0269                       
REMARK   3      S21:  -0.2692 S22:  -0.2581 S23:  -0.1036                       
REMARK   3      S31:   0.3056 S32:   0.4419 S33:   0.1347                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN S                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.2080   6.1452  51.6357              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2351 T22:   0.2102                                     
REMARK   3      T33:   0.2395 T12:  -0.0072                                     
REMARK   3      T13:   0.0038 T23:   0.0198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9122 L22:   0.5225                                     
REMARK   3      L33:   0.8725 L12:   0.0893                                     
REMARK   3      L13:  -0.1217 L23:   0.0580                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0303 S12:  -0.0410 S13:   0.0135                       
REMARK   3      S21:  -0.0450 S22:   0.0308 S23:  -0.0205                       
REMARK   3      S31:   0.0595 S32:   0.0080 S33:  -0.0027                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -12.5385  11.9959  38.5255              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6844 T22:   0.3098                                     
REMARK   3      T33:   0.2629 T12:  -0.0488                                     
REMARK   3      T13:   0.1057 T23:  -0.0126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0165 L22:   3.5175                                     
REMARK   3      L33:   1.5307 L12:   0.4765                                     
REMARK   3      L13:   0.9809 L23:  -0.9299                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4275 S12:   0.0766 S13:   0.2365                       
REMARK   3      S21:   0.0707 S22:   0.2537 S23:   0.0026                       
REMARK   3      S31:  -0.1958 S32:   0.0726 S33:  -0.6088                       
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 4XOZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-JAN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000206000.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933000                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27177                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.025                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.1                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : 0.02300                            
REMARK 200  R SYM                      (I) : 0.02300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.20900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.20900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: 3QYW                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG MME 2000, 0.1M MES PH 6.5,       
REMARK 280  0.1M AMMONIUM SULFATE, 0.02M BETA-MERCAPTOETHANOL, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       35.77500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.                         
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 180 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 16720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A   330                                                      
REMARK 465     MET A   331                                                      
REMARK 465     GLU A   332                                                      
REMARK 465     LEU A   333                                                      
REMARK 465     ASP A   334                                                      
REMARK 465     GLY A   355                                                      
REMARK 465     TYR A   356                                                      
REMARK 465     ARG A   357                                                      
REMARK 465     SER A   358                                                      
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     ARG A  77    CZ   NH1  NH2                                       
REMARK 470     LYS A 115    CE   NZ                                             
REMARK 470     ARG A 223    CZ   NH1  NH2                                       
REMARK 470     LYS A 229    CE   NZ                                             
REMARK 470     GLU A 324    CD   OE1  OE2                                       
REMARK 470     ASP A 335    CG   OD1  OD2                                       
REMARK 470     GLU A 347    CD   OE1  OE2                                       
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       -1.02     72.29                                   
REMARK 500    ASP A 147       40.83   -142.32                                   
REMARK 500    ASP A 165       75.89     64.03                                   
REMARK 500    ASN A 199       15.04   -160.75                                   
REMARK 500    LEU A 292       56.76    -94.00                                   
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 620 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                 
DBREF  4XOZ A    8   358  UNP    P63086   MK01_RAT         8    358             
SEQRES   1 A  351  GLY PRO GLU MET VAL ARG GLY GLN VAL PHE ASP VAL GLY          
SEQRES   2 A  351  PRO ARG TYR THR ASN LEU SER TYR ILE GLY GLU GLY ALA          
SEQRES   3 A  351  TYR GLY MET VAL CYS SER ALA TYR ASP ASN LEU ASN LYS          
SEQRES   4 A  351  VAL ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU HIS          
SEQRES   5 A  351  GLN THR TYR CYS GLN ARG THR LEU ARG GLU ILE LYS ILE          
SEQRES   6 A  351  LEU LEU ARG PHE ARG HIS GLU ASN ILE ILE GLY ILE ASN          
SEQRES   7 A  351  ASP ILE ILE ARG ALA PRO THR ILE GLU GLN MET LYS ASP          
SEQRES   8 A  351  VAL TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU TYR          
SEQRES   9 A  351  LYS LEU LEU LYS THR GLN HIS LEU SER ASN ASP HIS ILE          
SEQRES  10 A  351  CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS TYR          
SEQRES  11 A  351  ILE HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  12 A  351  SER ASN LEU LEU LEU ASN THR THR CME ASP LEU LYS ILE          
SEQRES  13 A  351  CYS ASP PHE GLY LEU ALA ARG VAL ALA ASP PRO ASP HIS          
SEQRES  14 A  351  ASP HIS THR GLY PHE LEU THR GLU TYR VAL ALA THR ARG          
SEQRES  15 A  351  TRP TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS GLY          
SEQRES  16 A  351  TYR THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS ILE          
SEQRES  17 A  351  LEU ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO GLY          
SEQRES  18 A  351  LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY ILE          
SEQRES  19 A  351  LEU GLY SER PRO SER GLN GLU ASP LEU ASN CYS ILE ILE          
SEQRES  20 A  351  ASN LEU LYS ALA ARG ASN TYR LEU LEU SER LEU PRO HIS          
SEQRES  21 A  351  LYS ASN LYS VAL PRO TRP ASN ARG LEU PHE PRO ASN ALA          
SEQRES  22 A  351  ASP SER LYS ALA LEU ASP LEU LEU ASP LYS MET LEU THR          
SEQRES  23 A  351  PHE ASN PRO HIS LYS ARG ILE GLU VAL GLU GLN ALA LEU          
SEQRES  24 A  351  ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO SER ASP          
SEQRES  25 A  351  GLU PRO ILE ALA GLU ALA PRO PHE LYS PHE ASP MET GLU          
SEQRES  26 A  351  LEU ASP ASP LEU PRO LYS GLU LYS LEU LYS GLU LEU ILE          
SEQRES  27 A  351  PHE GLU GLU THR ALA ARG PHE GLN PRO GLY TYR ARG SER          
MODRES 4XOZ CME A  159  CYS  MODIFIED RESIDUE                                   
HET    CME  A 159      10                                                       
HET    620  A 401      22                                                       
HET    SO4  A 402       5                                                       
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     620 N~1~-[3-(BENZYLOXY)BENZYL]-1H-TETRAZOLE-1,5-DIAMINE              
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  CME    C5 H11 N O3 S2                                               
FORMUL   2  620    C15 H16 N6 O                                                 
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  HOH   *141(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 ASP A  173  ASP A  177  5                                   5    
HELIX    6 AA6 THR A  188  ARG A  192  5                                   5    
HELIX    7 AA7 ALA A  193  ASN A  199  1                                   7    
HELIX    8 AA8 LYS A  205  ASN A  222  1                                  18    
HELIX    9 AA9 HIS A  230  GLY A  243  1                                  14    
HELIX   10 AB1 SER A  246  ASN A  251  1                                   6    
HELIX   11 AB2 ASN A  255  LEU A  265  1                                  11    
HELIX   12 AB3 PRO A  272  PHE A  277  1                                   6    
HELIX   13 AB4 ASP A  281  LEU A  292  1                                  12    
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 PRO A  337  ALA A  350  1                                  14    
HELIX   18 AB9 ARG A  351  GLN A  353  5                                   3    
SHEET    1 AA1 2 MET A  11  VAL A  12  0                                        
SHEET    2 AA1 2 GLN A  15  VAL A  16 -1  O  GLN A  15   N  VAL A  12           
SHEET    1 AA2 5 TYR A  23  GLY A  30  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  GLN A 103   N  ALA A  50           
SHEET    5 AA2 5 ASP A  86  ILE A  88 -1  N  ILE A  88   O  TYR A 100           
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           
SHEET    1 AA4 2 VAL A 143  LEU A 144  0                                        
SHEET    2 AA4 2 ARG A 170  VAL A 171 -1  O  ARG A 170   N  LEU A 144           
LINK         C   THR A 158                 N   CME A 159     1555   1555  1.33  
LINK         C   CME A 159                 N   ASP A 160     1555   1555  1.33  
CISPEP   1 GLY A   20    PRO A   21          0         3.35                     
CISPEP   2 GLN A  353    PRO A  354          0        -1.17                     
SITE     1 AC1  9 LYS A  52  ILE A  54  GLU A  69  ILE A 101                    
SITE     2 AC1  9 GLN A 103  ASP A 104  MET A 106  HOH A 625                    
SITE     3 AC1  9 HOH A 568                                                     
SITE     1 AC2  3 ARG A 189  ARG A 192  TYR A 231                               
CRYST1   49.170   71.550   60.890  90.00 108.60  90.00 P 1 21 1      2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020338  0.000000  0.006844        0.00000                         
SCALE2      0.000000  0.013976  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017328        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system