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Database: PDB
Entry: 4XOY
LinkDB: 4XOY
Original site: 4XOY 
HEADER    TRANSFERASE                             16-JAN-15   4XOY              
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 FRAGMENT: UNP RESIDUES 8-358;                                        
COMPND   5 SYNONYM: MAPK 1,ERT1,EXTRACELLULAR SIGNAL-REGULATED KINASE 2,ERK-2,  
COMPND   6 MAP KINASE ISOFORM P42,P42-MAPK,MITOGEN-ACTIVATED PROTEIN KINASE 2,  
COMPND   7 MAPK 2;                                                              
COMPND   8 EC: 2.7.11.24;                                                       
COMPND   9 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 4XOY    1       REMARK SITE   ATOM                       
REVDAT   2   19-AUG-15 4XOY    1       JRNL                                     
REVDAT   1   12-AUG-15 4XOY    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.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.29                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.880                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 78.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 36039                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.460                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3411                            
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 29.2897 -  6.0405    0.75     1292   137  0.1939 0.2364        
REMARK   3     2  6.0405 -  4.8014    0.79     1376   146  0.1752 0.1956        
REMARK   3     3  4.8014 -  4.1964    0.80     1414   134  0.1471 0.1772        
REMARK   3     4  4.1964 -  3.8136    0.81     1391   141  0.1467 0.1508        
REMARK   3     5  3.8136 -  3.5408    0.80     1395   156  0.1572 0.1954        
REMARK   3     6  3.5408 -  3.3323    0.81     1402   134  0.1677 0.2218        
REMARK   3     7  3.3323 -  3.1657    0.82     1457   148  0.1764 0.2317        
REMARK   3     8  3.1657 -  3.0280    0.82     1369   155  0.1792 0.2164        
REMARK   3     9  3.0280 -  2.9115    0.82     1415   147  0.1866 0.2413        
REMARK   3    10  2.9115 -  2.8112    0.82     1414   162  0.1824 0.2170        
REMARK   3    11  2.8112 -  2.7233    0.82     1432   142  0.1869 0.2154        
REMARK   3    12  2.7233 -  2.6455    0.83     1442   133  0.1845 0.2453        
REMARK   3    13  2.6455 -  2.5759    0.83     1431   159  0.1797 0.2606        
REMARK   3    14  2.5759 -  2.5131    0.83     1434   165  0.1829 0.2321        
REMARK   3    15  2.5131 -  2.4560    0.84     1386   162  0.1804 0.2191        
REMARK   3    16  2.4560 -  2.4038    0.83     1454   145  0.1881 0.2271        
REMARK   3    17  2.4038 -  2.3557    0.85     1433   168  0.1906 0.2410        
REMARK   3    18  2.3557 -  2.3113    0.83     1475   136  0.1908 0.2518        
REMARK   3    19  2.3113 -  2.2700    0.85     1457   152  0.1993 0.2639        
REMARK   3    20  2.2700 -  2.2315    0.83     1397   160  0.2059 0.2877        
REMARK   3    21  2.2315 -  2.1956    0.83     1504   145  0.2104 0.2785        
REMARK   3    22  2.1956 -  2.1618    0.55      942    93  0.2412 0.2746        
REMARK   3    23  2.1618 -  2.1300    0.56      970    85  0.2558 0.2872        
REMARK   3    24  2.1300 -  2.1000    0.55      946   106  0.2794 0.2962        
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)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.670           
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           2785                                  
REMARK   3   ANGLE     :  1.124           3767                                  
REMARK   3   CHIRALITY :  0.043            415                                  
REMARK   3   PLANARITY :  0.006            477                                  
REMARK   3   DIHEDRAL  : 14.976           1048                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 9 THROUGH 120 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -15.0987  12.4248  35.7518              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0814 T22:   0.1244                                     
REMARK   3      T33:  -0.1000 T12:   0.0148                                     
REMARK   3      T13:  -0.0352 T23:   0.0773                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0019 L22:  -0.0003                                     
REMARK   3      L33:   0.0033 L12:  -0.0074                                     
REMARK   3      L13:   0.0028 L23:  -0.0005                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0079 S12:  -0.0394 S13:   0.0458                       
REMARK   3      S21:  -0.0151 S22:   0.0541 S23:   0.0780                       
REMARK   3      S31:  -0.0222 S32:  -0.0580 S33:  -0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 121 THROUGH 353 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.2576   6.5204  55.2666              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0501 T22:   0.0490                                     
REMARK   3      T33:   0.0675 T12:  -0.0024                                     
REMARK   3      T13:   0.0021 T23:   0.0075                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0313 L22:   0.0503                                     
REMARK   3      L33:   0.0263 L12:   0.0108                                     
REMARK   3      L13:   0.0123 L23:  -0.0128                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0036 S12:   0.0026 S13:   0.0441                       
REMARK   3      S21:   0.0022 S22:   0.0015 S23:   0.0088                       
REMARK   3      S31:   0.0220 S32:   0.0094 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 4XOY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JAN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000206048.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUL-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
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                       : BM30A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97922                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28103                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.305                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.8                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 67.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.950                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: ISOMORPHOUS REPLACEMENT WITH A SIMPLE RIGID BODY     
REMARK 200  WITH REFMAC5, USING ANOTHER STRUCTURE OF THE SAME PROTEINE (3QYW)   
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
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       35.70850            
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: 16120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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     GLY A     8                                                      
REMARK 465     PRO A    56                                                      
REMARK 465     PHE A    57                                                      
REMARK 465     GLU A    58                                                      
REMARK 465     HIS A    59                                                      
REMARK 465     GLN A    60                                                      
REMARK 465     GLU A   184                                                      
REMARK 465     TYR A   185                                                      
REMARK 465     VAL A   186                                                      
REMARK 465     LYS A   328                                                      
REMARK 465     PHE A   329                                                      
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     PRO A   354                                                      
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     THR A  61    OG1  CG2                                            
REMARK 470     LYS A 229    CG   CD   CE   NZ                                   
REMARK 470     ASP A 335    CB   CG   OD1  OD2                                  
REMARK 470     LYS A 340    CG   CD   CE   NZ                                   
REMARK 470     GLU A 347    CG   CD   OE1  OE2                                  
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   OE1  GLU A   303     O    HOH A   501              2.00            
REMARK 500   OG1  THR A   183     O    HOH A   502              2.07            
REMARK 500   OH   TYR A   315     O    HOH A   503              2.13            
REMARK 500   O    ALA A    33     O    HOH A   504              2.14            
REMARK 500   NH1  ARG A    65     O    HOH A   505              2.17            
REMARK 500   OD2  ASP A   249     O    HOH A   506              2.17            
REMARK 500   O    HOH A   507     O    HOH A   631              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  17       75.49   -118.36                                   
REMARK 500    TYR A  34      -42.55     84.80                                   
REMARK 500    ASN A  45       39.27   -143.93                                   
REMARK 500    LYS A  97      -70.91   -119.31                                   
REMARK 500    ARG A 146       -1.71     76.38                                   
REMARK 500    ASP A 147       41.50   -141.90                                   
REMARK 500    ASP A 165       87.56     67.24                                   
REMARK 500    ASP A 173       73.51   -153.86                                   
REMARK 500    ASN A 199       20.76   -154.56                                   
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 642        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH A 643        DISTANCE =  6.61 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DX4 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  4XOY 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  CME 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  CME 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 CME 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 4XOY CME A  125  CYS  MODIFIED RESIDUE                                   
MODRES 4XOY CME A  159  CYS  MODIFIED RESIDUE                                   
MODRES 4XOY CME A  164  CYS  MODIFIED RESIDUE                                   
MODRES 4XOY CME A  252  CYS  MODIFIED RESIDUE                                   
HET    CME  A 125      10                                                       
HET    CME  A 159      10                                                       
HET    CME  A 164      10                                                       
HET    CME  A 252      10                                                       
HET    DX4  A 401      11                                                       
HET    SO4  A 402       5                                                       
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     DX4 2-AMINO-1,9-DIHYDRO-6H-PURINE-6-THIONE                           
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  CME    4(C5 H11 N O3 S2)                                            
FORMUL   2  DX4    C5 H5 N5 S                                                   
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  HOH   *143(H2 O)                                                    
HELIX    1 AA1 TYR A   62  PHE A   76  1                                  15    
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  CME A  252  1                                   7    
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  THR A  349  1                                  13    
HELIX   18 AB9 ALA A  350  GLN A  353  5                                   4    
SHEET    1 AA1 5 TYR A  23  GLU A  31  0                                        
SHEET    2 AA1 5 MET A  36  ASP A  42 -1  O  VAL A  37   N  GLY A  30           
SHEET    3 AA1 5 VAL A  47  ILE A  54 -1  O  ILE A  51   N  CYS A  38           
SHEET    4 AA1 5 VAL A  99  ASP A 104 -1  O  GLN A 103   N  ALA A  50           
SHEET    5 AA1 5 ASP A  86  ILE A  88 -1  N  ASP A  86   O  VAL A 102           
SHEET    1 AA2 3 THR A 108  ASP A 109  0                                        
SHEET    2 AA2 3 LEU A 153  LEU A 155 -1  O  LEU A 155   N  THR A 108           
SHEET    3 AA2 3 LEU A 161  ILE A 163 -1  O  LYS A 162   N  LEU A 154           
SHEET    1 AA3 2 VAL A 143  LEU A 144  0                                        
SHEET    2 AA3 2 ARG A 170  VAL A 171 -1  O  ARG A 170   N  LEU A 144           
LINK         C   ILE A 124                 N   CME A 125     1555   1555  1.33  
LINK         C   CME A 125                 N   TYR A 126     1555   1555  1.34  
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  
LINK         C   ILE A 163                 N   CME A 164     1555   1555  1.33  
LINK         C   CME A 164                 N   ASP A 165     1555   1555  1.33  
LINK         C   ASN A 251                 N   CME A 252     1555   1555  1.33  
LINK         C   CME A 252                 N   ILE A 253     1555   1555  1.32  
SITE     1 AC1  6 ALA A  50  LYS A  52  GLN A 103  ASP A 104                    
SITE     2 AC1  6 MET A 106  CME A 164                                          
SITE     1 AC2  4 ARG A 189  ARG A 192  TYR A 231  HOH A 518                    
CRYST1   49.178   71.417   61.263  90.00 109.51  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      0.020334  0.000000  0.007205        0.00000                         
SCALE2      0.000000  0.014002  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017317        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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