GenomeNet

Database: PDB
Entry: 4XP3
LinkDB: 4XP3
Original site: 4XP3 
HEADER    TRANSFERASE                             16-JAN-15   4XP3              
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: 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 4XP3    1       REMARK SITE   ATOM                       
REVDAT   2   19-AUG-15 4XP3    1       JRNL                                     
REVDAT   1   12-AUG-15 4XP3    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.    1.78 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) : 1.78                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.20                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.280                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 77.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 55296                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.150                           
REMARK   3   R VALUE            (WORKING SET) : 0.149                           
REMARK   3   FREE R VALUE                     : 0.179                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2800                            
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 23.2000 -  4.8223    0.86     2906   148  0.1708 0.1800        
REMARK   3     2  4.8223 -  3.8332    0.87     2915   163  0.1238 0.1459        
REMARK   3     3  3.8332 -  3.3503    0.86     2916   134  0.1287 0.1437        
REMARK   3     4  3.3503 -  3.0447    0.85     2820   149  0.1405 0.1578        
REMARK   3     5  3.0447 -  2.8269    0.84     2853   142  0.1470 0.1829        
REMARK   3     6  2.8269 -  2.6605    0.83     2787   166  0.1516 0.1990        
REMARK   3     7  2.6605 -  2.5274    0.82     2718   175  0.1450 0.1806        
REMARK   3     8  2.5274 -  2.4175    0.81     2681   166  0.1435 0.1843        
REMARK   3     9  2.4175 -  2.3245    0.80     2732   154  0.1471 0.1884        
REMARK   3    10  2.3245 -  2.2444    0.80     2670   150  0.1457 0.1940        
REMARK   3    11  2.2444 -  2.1742    0.79     2670   152  0.1507 0.1987        
REMARK   3    12  2.1742 -  2.1121    0.78     2580   177  0.1569 0.1808        
REMARK   3    13  2.1121 -  2.0566    0.78     2592   165  0.1597 0.1913        
REMARK   3    14  2.0566 -  2.0064    0.78     2650   105  0.1553 0.1752        
REMARK   3    15  2.0064 -  1.9608    0.76     2595   112  0.1591 0.1999        
REMARK   3    16  1.9608 -  1.9191    0.76     2512   143  0.1625 0.2577        
REMARK   3    17  1.9191 -  1.8808    0.75     2547   108  0.1717 0.1886        
REMARK   3    18  1.8808 -  1.8453    0.71     2419   118  0.1887 0.2644        
REMARK   3    19  1.8453 -  1.8123    0.67     2284    98  0.1964 0.2205        
REMARK   3    20  1.8123 -  1.7816    0.48     1649    75  0.2220 0.2637        
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)     : 0.140            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.070           
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      :  0.009           3041                                  
REMARK   3   ANGLE     :  1.021           4116                                  
REMARK   3   CHIRALITY :  0.043            441                                  
REMARK   3   PLANARITY :  0.005            523                                  
REMARK   3   DIHEDRAL  : 13.273           1188                                  
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): -13.8823  12.5481  34.2231              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2043 T22:   0.2186                                     
REMARK   3      T33:   0.1672 T12:   0.0072                                     
REMARK   3      T13:  -0.0176 T23:   0.0575                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2661 L22:   0.4480                                     
REMARK   3      L33:   1.9889 L12:   0.1481                                     
REMARK   3      L13:  -0.2688 L23:   0.1884                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0027 S12:   0.1319 S13:   0.1581                       
REMARK   3      S21:  -0.1752 S22:   0.1315 S23:   0.1313                       
REMARK   3      S31:  -0.3206 S32:  -0.3812 S33:  -0.0995                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 119:312)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   0.9305   7.8341  57.2330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0770 T22:   0.0570                                     
REMARK   3      T33:   0.1014 T12:   0.0091                                     
REMARK   3      T13:   0.0102 T23:   0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2638 L22:   0.6266                                     
REMARK   3      L33:   0.9856 L12:   0.6351                                     
REMARK   3      L13:   0.6321 L23:   0.2379                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0066 S12:  -0.0053 S13:   0.0621                       
REMARK   3      S21:   0.0111 S22:   0.0044 S23:  -0.0085                       
REMARK   3      S31:  -0.0403 S32:   0.0339 S33:  -0.0166                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 313:354)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.2932  -0.7527  35.2749              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1913 T22:   0.1662                                     
REMARK   3      T33:   0.1711 T12:  -0.0269                                     
REMARK   3      T13:   0.0101 T23:  -0.0422                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3726 L22:   1.6091                                     
REMARK   3      L33:   2.9805 L12:   0.2405                                     
REMARK   3      L13:  -0.3157 L23:  -1.6813                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0225 S12:   0.0769 S13:  -0.0000                       
REMARK   3      S21:  -0.3064 S22:   0.0401 S23:  -0.0261                       
REMARK   3      S31:   0.2490 S32:   0.2559 S33:  -0.0782                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN S                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.5610   6.9561  49.7472              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1267 T22:   0.1155                                     
REMARK   3      T33:   0.1408 T12:   0.0094                                     
REMARK   3      T13:   0.0140 T23:  -0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6867 L22:   0.7833                                     
REMARK   3      L33:   0.7477 L12:   0.2663                                     
REMARK   3      L13:   0.1758 L23:  -0.1243                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0156 S12:  -0.0001 S13:   0.0214                       
REMARK   3      S21:  -0.0283 S22:   0.0405 S23:   0.0092                       
REMARK   3      S31:  -0.0246 S32:  -0.0156 S33:  -0.0265                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -16.6100  12.8294  41.5138              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2964 T22:   0.3467                                     
REMARK   3      T33:   0.2827 T12:  -0.0774                                     
REMARK   3      T13:  -0.0659 T23:   0.1601                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0000 L22:   4.3897                                     
REMARK   3      L33:   4.1977 L12:  -0.7070                                     
REMARK   3      L13:  -2.5049 L23:   0.8660                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0825 S12:  -0.1685 S13:   0.2631                       
REMARK   3      S21:  -0.0014 S22:   0.0416 S23:  -0.0673                       
REMARK   3      S31:  -0.1633 S32:   0.0941 S33:  -0.0859                       
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 4XP3 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_1000206005.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-DEC-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.542                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55297                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.780                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 56.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.03700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.87                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.14900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.600                              
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   (%): 47.47                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
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       34.84150            
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: 1100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 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     ASP A   335                                                      
REMARK 465     GLY A   355                                                      
REMARK 465     TYR A   356                                                      
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   846     O    HOH A   866              1.96            
REMARK 500   O    HOH A   808     O    HOH A   878              2.04            
REMARK 500   O    HOH A   862     O    HOH A   936              2.07            
REMARK 500   O    HOH A   832     O    HOH A   845              2.11            
REMARK 500   OE1  GLU A    10     O    HOH A   501              2.11            
REMARK 500   O    HOH A   958     O    HOH A   960              2.14            
REMARK 500   O    HOH A   713     O    HOH A   919              2.15            
REMARK 500   O    HOH A   890     O    HOH A   894              2.15            
REMARK 500   O    HOH A   695     O    HOH A   704              2.15            
REMARK 500   O    HOH A   771     O    HOH A   835              2.16            
REMARK 500   O    HOH A   774     O    HOH A   835              2.17            
REMARK 500   O    HOH A   517     O    HOH A   526              2.18            
REMARK 500   O    HOH A   803     O    HOH A   918              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    ASP A 147       43.42   -147.16                                   
REMARK 500    ASP A 165       94.31     60.88                                   
REMARK 500    ALA A 187      179.47     65.58                                   
REMARK 500    ASN A 199       19.12   -163.58                                   
REMARK 500    LEU A 292       49.68    -95.45                                   
REMARK 500    ASP A 316       91.85   -162.69                                   
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 956        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH A 957        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH A 958        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH A 959        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH A 960        DISTANCE =  7.23 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                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 413                 
DBREF  4XP3 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 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 4XP3 CME A  159  CYS  MODIFIED RESIDUE                                   
MODRES 4XP3 CME A  252  CYS  MODIFIED RESIDUE                                   
HET    CME  A 159      10                                                       
HET    CME  A 252      10                                                       
HET    DX4  A 401      11                                                       
HET    SO4  A 402       5                                                       
HET    DMS  A 403       4                                                       
HET    DMS  A 404       4                                                       
HET    DMS  A 405       4                                                       
HET    DMS  A 406       4                                                       
HET    DMS  A 407       4                                                       
HET    DMS  A 408       4                                                       
HET    DMS  A 409       4                                                       
HET    DMS  A 410       4                                                       
HET    DMS  A 411       4                                                       
HET    DMS  A 412       4                                                       
HET    DMS  A 413       4                                                       
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     DX4 2-AMINO-1,9-DIHYDRO-6H-PURINE-6-THIONE                           
HETNAM     SO4 SULFATE ION                                                      
HETNAM     DMS DIMETHYL SULFOXIDE                                               
FORMUL   1  CME    2(C5 H11 N O3 S2)                                            
FORMUL   2  DX4    C5 H5 N5 S                                                   
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  DMS    11(C2 H6 O S)                                                
FORMUL  15  HOH   *460(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  LEU A  232  5                                   3    
HELIX   10 AB1 ASP A  233  GLY A  243  1                                  11    
HELIX   11 AB2 SER A  246  CME A  252  1                                   7    
HELIX   12 AB3 ASN A  255  SER A  264  1                                  10    
HELIX   13 AB4 PRO A  272  PHE A  277  1                                   6    
HELIX   14 AB5 ASP A  281  LEU A  292  1                                  12    
HELIX   15 AB6 GLU A  301  ALA A  307  1                                   7    
HELIX   16 AB7 HIS A  308  GLU A  312  5                                   5    
HELIX   17 AB8 ASP A  316  GLU A  320  5                                   5    
HELIX   18 AB9 PRO A  337  THR A  349  1                                  13    
HELIX   19 AC1 ALA A  350  GLN A  353  5                                   4    
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  GLU A  31  0                                        
SHEET    2 AA2 5 MET A  36  ASP A  42 -1  O  TYR A  41   N  THR A  24           
SHEET    3 AA2 5 VAL A  47  ILE A  54 -1  O  VAL A  49   N  ALA A  40           
SHEET    4 AA2 5 VAL A  99  ASP A 104 -1  O  VAL A  99   N  ILE A  54           
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  
LINK         C   ASN A 251                 N   CME A 252     1555   1555  1.33  
LINK         C   CME A 252                 N   ILE A 253     1555   1555  1.33  
CISPEP   1 GLY A   20    PRO A   21          0         1.10                     
SITE     1 AC1 10 ALA A  50  LYS A  52  GLN A 103  ASP A 104                    
SITE     2 AC1 10 LEU A 105  MET A 106  LEU A 154  DMS A 404                    
SITE     3 AC1 10 HOH A 619  HOH A 680                                          
SITE     1 AC2  6 TYR A 185  ARG A 189  ARG A 192  TYR A 231                    
SITE     2 AC2  6 HOH A 734  HOH A 767                                          
SITE     1 AC3  3 HIS A 297  GLN A 304  HOH A 759                               
SITE     1 AC4  6 ASP A 109  SER A 151  CYS A 164  DX4 A 401                    
SITE     2 AC4  6 HOH A 600  HOH A 511                                          
SITE     1 AC5  3 THR A 188  TRP A 190  HOH A 788                               
SITE     1 AC6  2 LYS A 149  SER A 151                                          
SITE     1 AC7  3 SER A 221  PRO A 224  PHE A 277                               
SITE     1 AC8  1 ASN A 222                                                     
SITE     1 AC9  6 LYS A 270  TRP A 273  LEU A 285  ASP A 289                    
SITE     2 AC9  6 HOH A 764  HOH A 644                                          
SITE     1 AD1 10 HIS A 118  LEU A 119  ILE A 124  LEU A 220                    
SITE     2 AD1 10 ASN A 279  ALA A 280  HOH A 756  HOH A 622                    
SITE     3 AD1 10 HOH A 635  HOH A 530                                          
SITE     1 AD2  5 ARG A  77  TYR A 137  ALA A 323  GLU A 324                    
SITE     2 AD2  5 HOH A 775                                                     
SITE     1 AD3  5 LEU A 105  MET A 106  GLU A 107  ASN A 156                    
SITE     2 AD3  5 THR A 157                                                     
SITE     1 AD4  5 ARG A  75  PRO A 326  PHE A 327  LYS A 328                    
SITE     2 AD4  5 PHE A 329                                                     
CRYST1   48.600   69.683   59.819  90.00 108.91  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      0.020576  0.000000  0.007049        0.00000                         
SCALE2      0.000000  0.014351  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017671        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system