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Database: PDB
Entry: 4M6L
LinkDB: 4M6L
Original site: 4M6L 
HEADER    OXIDOREDUCTASE                          09-AUG-13   4M6L              
TITLE     CRYSTAL STRUCTURE OF HUMAN DIHYDROFOLATE REDUCTASE (DHFR) BOUND TO    
TITLE    2 NADP+ AND 5,10-DIDEAZATETRAHYDROFOLIC ACID                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROFOLATE REDUCTASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 1.5.1.3;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DHFR;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/PDNAY;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21A                                    
KEYWDS    ROSSMANN FOLD, NADPH BINDING, FOLATE BINDING, OXIDOREDUCTASE          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.BHABHA,D.C.EKIERT,P.E.WRIGHT,I.A.WILSON                             
REVDAT   3   20-NOV-13 4M6L    1       JRNL                                     
REVDAT   2   16-OCT-13 4M6L    1       JRNL                                     
REVDAT   1   25-SEP-13 4M6L    0                                                
JRNL        AUTH   G.BHABHA,D.C.EKIERT,M.JENNEWEIN,C.M.ZMASEK,L.M.TUTTLE,       
JRNL        AUTH 2 G.KROON,H.J.DYSON,A.GODZIK,I.A.WILSON,P.E.WRIGHT             
JRNL        TITL   DIVERGENT EVOLUTION OF PROTEIN CONFORMATIONAL DYNAMICS IN    
JRNL        TITL 2 DIHYDROFOLATE REDUCTASE.                                     
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  20  1243 2013              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   24077226                                                     
JRNL        DOI    10.1038/NSMB.2676                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.37                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 24628                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1256                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 47.3871 -  3.5357    1.00     2887   135  0.1718 0.2167        
REMARK   3     2  3.5357 -  2.8065    1.00     2674   137  0.1701 0.2279        
REMARK   3     3  2.8065 -  2.4518    1.00     2621   150  0.1862 0.2413        
REMARK   3     4  2.4518 -  2.2276    1.00     2587   149  0.1878 0.2434        
REMARK   3     5  2.2276 -  2.0679    1.00     2557   149  0.1918 0.2111        
REMARK   3     6  2.0679 -  1.9460    0.99     2581   119  0.1998 0.2585        
REMARK   3     7  1.9460 -  1.8486    0.98     2501   150  0.2518 0.3027        
REMARK   3     8  1.8486 -  1.7681    0.98     2492   143  0.3124 0.3103        
REMARK   3     9  1.7681 -  1.7000    0.97     2472   124  0.3546 0.3693        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.60                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.030           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           1680                                  
REMARK   3   ANGLE     :  1.248           2286                                  
REMARK   3   CHIRALITY :  0.075            242                                  
REMARK   3   PLANARITY :  0.005            288                                  
REMARK   3   DIHEDRAL  : 15.309            659                                  
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 1 through 27 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  26.8745   5.1534 -29.0339              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3003 T22:   0.1200                                     
REMARK   3      T33:   0.1775 T12:   0.0453                                     
REMARK   3      T13:   0.0224 T23:  -0.0055                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6482 L22:   0.3133                                     
REMARK   3      L33:   0.6748 L12:  -0.2537                                     
REMARK   3      L13:  -0.1278 L23:   0.6070                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0865 S12:  -0.0963 S13:   0.0939                       
REMARK   3      S21:  -0.0586 S22:  -0.0107 S23:  -0.1027                       
REMARK   3      S31:  -0.2291 S32:  -0.0416 S33:   0.0370                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 28 through 101 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  23.7203   2.6120 -14.7877              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2902 T22:   0.1617                                     
REMARK   3      T33:   0.1831 T12:   0.0511                                     
REMARK   3      T13:   0.0372 T23:  -0.0129                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2113 L22:   0.2740                                     
REMARK   3      L33:   1.9262 L12:   0.2368                                     
REMARK   3      L13:   0.3177 L23:   0.0447                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0952 S12:  -0.1669 S13:   0.0421                       
REMARK   3      S21:   0.1345 S22:  -0.0574 S23:   0.1635                       
REMARK   3      S31:  -0.3093 S32:  -0.1523 S33:   0.0341                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 102 through 111 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  26.4376  -7.7054  -5.8318              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4234 T22:   0.3672                                     
REMARK   3      T33:   0.2431 T12:  -0.0186                                     
REMARK   3      T13:  -0.0276 T23:  -0.0101                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0412 L22:   0.0123                                     
REMARK   3      L33:   0.0517 L12:  -0.0370                                     
REMARK   3      L13:   0.0566 L23:  -0.0446                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2062 S12:  -0.4178 S13:  -0.3127                       
REMARK   3      S21:   0.3179 S22:   0.2784 S23:  -0.1712                       
REMARK   3      S31:   0.0728 S32:  -0.3664 S33:  -0.0004                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid 112 through 158 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  34.1625   0.4776 -27.8213              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2366 T22:   0.1401                                     
REMARK   3      T33:   0.1765 T12:  -0.0078                                     
REMARK   3      T13:   0.0190 T23:  -0.0013                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7131 L22:   0.9269                                     
REMARK   3      L33:   0.8855 L12:  -0.1612                                     
REMARK   3      L13:  -0.6798 L23:   0.1637                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1135 S12:  -0.1495 S13:   0.0580                       
REMARK   3      S21:  -0.0714 S22:  -0.0428 S23:  -0.0585                       
REMARK   3      S31:  -0.2372 S32:   0.2448 S33:   0.0257                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'A' and (resid 159 through 186 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  26.0632  -6.7001 -34.1410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1784 T22:   0.1092                                     
REMARK   3      T33:   0.2174 T12:   0.0507                                     
REMARK   3      T13:  -0.0073 T23:   0.0126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5505 L22:  -0.0638                                     
REMARK   3      L33:   0.9349 L12:   0.0294                                     
REMARK   3      L13:  -0.7329 L23:   0.2744                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0544 S12:  -0.0011 S13:  -0.1820                       
REMARK   3      S21:  -0.0774 S22:   0.0374 S23:   0.0812                       
REMARK   3      S31:   0.0313 S32:  -0.0130 S33:   0.0506                       
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 4M6L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-AUG-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB081530.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL CRYO-COOLED         
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24905                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 18.300                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.13000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 18.30                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.85000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4M6J                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2 M AMMONIUM SULFATE, 100 MM SODIUM    
REMARK 280  CITRATE, PH 4.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z+1/2                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/2                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       80.20400            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       80.20400            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       80.20400            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       80.20400            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       80.20400            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       80.20400            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 343  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 360  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 341  LIES ON A SPECIAL POSITION.                          
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     MET A     0                                                      
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 110      -97.11    -99.86                                   
REMARK 500    MET A 139       56.49    -90.38                                   
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 21V A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 204                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4M6J   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4M6K   RELATED DB: PDB                                   
DBREF  4M6L A    0   186  UNP    P00374   DYR_HUMAN        1    187             
SEQRES   1 A  187  MET VAL GLY SER LEU ASN CYS ILE VAL ALA VAL SER GLN          
SEQRES   2 A  187  ASN MET GLY ILE GLY LYS ASN GLY ASP LEU PRO TRP PRO          
SEQRES   3 A  187  PRO LEU ARG ASN GLU PHE ARG TYR PHE GLN ARG MET THR          
SEQRES   4 A  187  THR THR SER SER VAL GLU GLY LYS GLN ASN LEU VAL ILE          
SEQRES   5 A  187  MET GLY LYS LYS THR TRP PHE SER ILE PRO GLU LYS ASN          
SEQRES   6 A  187  ARG PRO LEU LYS GLY ARG ILE ASN LEU VAL LEU SER ARG          
SEQRES   7 A  187  GLU LEU LYS GLU PRO PRO GLN GLY ALA HIS PHE LEU SER          
SEQRES   8 A  187  ARG SER LEU ASP ASP ALA LEU LYS LEU THR GLU GLN PRO          
SEQRES   9 A  187  GLU LEU ALA ASN LYS VAL ASP MET VAL TRP ILE VAL GLY          
SEQRES  10 A  187  GLY SER SER VAL TYR LYS GLU ALA MET ASN HIS PRO GLY          
SEQRES  11 A  187  HIS LEU LYS LEU PHE VAL THR ARG ILE MET GLN ASP PHE          
SEQRES  12 A  187  GLU SER ASP THR PHE PHE PRO GLU ILE ASP LEU GLU LYS          
SEQRES  13 A  187  TYR LYS LEU LEU PRO GLU TYR PRO GLY VAL LEU SER ASP          
SEQRES  14 A  187  VAL GLN GLU GLU LYS GLY ILE LYS TYR LYS PHE GLU VAL          
SEQRES  15 A  187  TYR GLU LYS ASN ASP                                          
HET    21V  A 201      32                                                       
HET    NAP  A 202      48                                                       
HET    DTT  A 203       8                                                       
HET    SO4  A 204       5                                                       
HETNAM     21V N-(4-{2-[(6S)-2-AMINO-4-OXO-1,4,5,6,7,8-                         
HETNAM   2 21V  HEXAHYDROPYRIDO[2,3-D]PYRIMIDIN-6-YL]ETHYL}BENZOYL)-L-          
HETNAM   3 21V  GLUTAMIC ACID                                                   
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETNAM     DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE                                   
HETNAM     SO4 SULFATE ION                                                      
HETSYN     21V 5,10-DIDEAZATETRAHYDROFOLIC ACID                                 
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
HETSYN     DTT 1,4-DITHIOTHREITOL                                               
FORMUL   2  21V    C21 H25 N5 O6                                                
FORMUL   3  NAP    C21 H28 N7 O17 P3                                            
FORMUL   4  DTT    C4 H10 O2 S2                                                 
FORMUL   5  SO4    O4 S 2-                                                      
FORMUL   6  HOH   *143(H2 O)                                                    
HELIX    1   1 LEU A   27  THR A   40  1                                  14    
HELIX    2   2 LYS A   54  ILE A   60  1                                   7    
HELIX    3   3 PRO A   61  ARG A   65  5                                   5    
HELIX    4   4 SER A   92  GLN A  102  1                                  11    
HELIX    5   5 GLN A  102  ASN A  107  1                                   6    
HELIX    6   6 GLY A  117  HIS A  127  1                                  11    
SHEET    1   A 8 PHE A  88  SER A  90  0                                        
SHEET    2   A 8 ILE A  71  LEU A  75  1  N  VAL A  74   O  PHE A  88           
SHEET    3   A 8 GLN A  47  GLY A  53  1  N  VAL A  50   O  ILE A  71           
SHEET    4   A 8 VAL A 109  ILE A 114  1  O  TRP A 113   N  LEU A  49           
SHEET    5   A 8 LEU A   4  VAL A  10  1  N  ASN A   5   O  ILE A 114           
SHEET    6   A 8 LEU A 131  ILE A 138  1  O  ILE A 138   N  VAL A  10           
SHEET    7   A 8 ILE A 175  LYS A 184 -1  O  LYS A 178   N  ARG A 137           
SHEET    8   A 8 LYS A 157  LEU A 158 -1  N  LYS A 157   O  GLU A 183           
SHEET    1   B 8 PHE A  88  SER A  90  0                                        
SHEET    2   B 8 ILE A  71  LEU A  75  1  N  VAL A  74   O  PHE A  88           
SHEET    3   B 8 GLN A  47  GLY A  53  1  N  VAL A  50   O  ILE A  71           
SHEET    4   B 8 VAL A 109  ILE A 114  1  O  TRP A 113   N  LEU A  49           
SHEET    5   B 8 LEU A   4  VAL A  10  1  N  ASN A   5   O  ILE A 114           
SHEET    6   B 8 LEU A 131  ILE A 138  1  O  ILE A 138   N  VAL A  10           
SHEET    7   B 8 ILE A 175  LYS A 184 -1  O  LYS A 178   N  ARG A 137           
SHEET    8   B 8 GLN A 170  GLU A 172 -1  N  GLN A 170   O  TYR A 177           
SHEET    1   C 2 GLY A  15  GLY A  17  0                                        
SHEET    2   C 2 THR A 146  PHE A 147 -1  O  THR A 146   N  ILE A  16           
CISPEP   1 ARG A   65    PRO A   66          0        -5.31                     
CISPEP   2 GLY A  116    GLY A  117          0         1.51                     
SITE     1 AC1 19 ILE A   7  VAL A   8  ALA A   9  LEU A  22                    
SITE     2 AC1 19 GLU A  30  PHE A  31  PHE A  34  GLN A  35                    
SITE     3 AC1 19 THR A  56  ASN A  64  LEU A  67  ARG A  70                    
SITE     4 AC1 19 VAL A 115  TYR A 121  THR A 136  NAP A 202                    
SITE     5 AC1 19 HOH A 311  HOH A 415  HOH A 442                               
SITE     1 AC2 28 VAL A   8  ALA A   9  ILE A  16  GLY A  17                    
SITE     2 AC2 28 GLY A  20  ASP A  21  LEU A  22  GLY A  53                    
SITE     3 AC2 28 LYS A  54  LYS A  55  THR A  56  LEU A  75                    
SITE     4 AC2 28 SER A  76  ARG A  77  GLU A  78  ARG A  91                    
SITE     5 AC2 28 VAL A 115  GLY A 116  GLY A 117  SER A 118                    
SITE     6 AC2 28 SER A 119  VAL A 120  TYR A 121  GLU A 123                    
SITE     7 AC2 28 THR A 146  21V A 201  HOH A 356  HOH A 412                    
SITE     1 AC3  5 PHE A  58  ARG A  77  PRO A  83  GLN A  84                    
SITE     2 AC3  5 ARG A  91                                                     
SITE     1 AC4  6 ARG A  77  LEU A  79  LYS A  80  GLU A  81                    
SITE     2 AC4  6 ARG A  91  HOH A 405                                          
CRYST1   67.781   67.781  160.408  90.00  90.00 120.00 P 63 2 2     12          
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      0.014753  0.008518  0.000000        0.00000                         
SCALE2      0.000000  0.017036  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006234        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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