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Database: PDB
Entry: 4KFJ
LinkDB: 4KFJ
Original site: 4KFJ 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 26-APR-13   4KFJ              
TITLE     HUMAN DIHYDROFOLATE REDUCTASE COMPLEXED WITH NADPH AND 5-{3-[3-       
TITLE    2 METHOXY-5-(ISOQUIN-5-YL)PHENYL]PROP-1-YN-1-YL}6-ETHYLPRIMIDINE-2,4-  
TITLE    3 DIAMINE                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROFOLATE REDUCTASE;                                   
COMPND   3 CHAIN: A, B;                                                         
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, HUDHFR;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET41A(+)                                 
KEYWDS    OXIDOREDUCTASE, 5,6,7,8-TETRAHYDROFOLATE; NADP+, HYDRIDE SHIFT,       
KEYWDS   2 CYTOSOL, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.M.LAMB,A.C.ANDERSON                                                 
REVDAT   4   17-DEC-14 4KFJ    1       REMARK                                   
REVDAT   3   20-NOV-13 4KFJ    1       HET    HETATM HETNAM REMARK              
REVDAT   2   30-OCT-13 4KFJ    1       JRNL                                     
REVDAT   1   09-OCT-13 4KFJ    0                                                
JRNL        AUTH   K.M.LAMB,N.G-DAYANANDAN,D.L.WRIGHT,A.C.ANDERSON              
JRNL        TITL   ELUCIDATING FEATURES THAT DRIVE THE DESIGN OF SELECTIVE      
JRNL        TITL 2 ANTIFOLATES USING CRYSTAL STRUCTURES OF HUMAN DIHYDROFOLATE  
JRNL        TITL 3 REDUCTASE.                                                   
JRNL        REF    BIOCHEMISTRY                  V.  52  7318 2013              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   24053334                                                     
JRNL        DOI    10.1021/BI400852H                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.76 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT 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) : 1.76                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.89                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 39299                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1970                            
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 19.8942 -  4.2280    0.91     2590   129  0.1709 0.1738        
REMARK   3     2  4.2280 -  3.3612    0.96     2659   126  0.1551 0.2265        
REMARK   3     3  3.3612 -  2.9378    0.99     2712   135  0.1857 0.2263        
REMARK   3     4  2.9378 -  2.6699    1.00     2695   148  0.2093 0.2553        
REMARK   3     5  2.6699 -  2.4789    1.00     2664   163  0.2170 0.2523        
REMARK   3     6  2.4789 -  2.3330    1.00     2690   155  0.2183 0.2991        
REMARK   3     7  2.3330 -  2.2163    1.00     2685   130  0.2167 0.2768        
REMARK   3     8  2.2163 -  2.1200    1.00     2677   150  0.2111 0.2739        
REMARK   3     9  2.1200 -  2.0384    1.00     2700   113  0.2137 0.2415        
REMARK   3    10  2.0384 -  1.9681    1.00     2660   141  0.2230 0.2925        
REMARK   3    11  1.9681 -  1.9067    1.00     2683   133  0.2317 0.2820        
REMARK   3    12  1.9067 -  1.8522    0.99     2669   129  0.2295 0.2886        
REMARK   3    13  1.8522 -  1.8035    1.00     2632   169  0.2420 0.3169        
REMARK   3    14  1.8035 -  1.7600    0.99     2613   149  0.2678 0.3465        
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)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.360           
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      :  0.012           3409                                  
REMARK   3   ANGLE     :  1.600           4652                                  
REMARK   3   CHIRALITY :  0.103            490                                  
REMARK   3   PLANARITY :  0.007            586                                  
REMARK   3   DIHEDRAL  : 17.102           1360                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 4KFJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB079274.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JUN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97916                            
REMARK 200  MONOCHROMATOR                  : ADSC QUANTUM 4R                    
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39426                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.760                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER FOR MR                                         
REMARK 200 STARTING MODEL: PDB ENTRY 2C2S                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, 0.2-0.3M LITHIUM          
REMARK 280  SULFATE, 25-30% (W/V) PEG 4000, 1% (V/V) TRIFLUOROETHANOL, 11MM     
REMARK 280  MGCL2, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.14700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       48.14700            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       43.90550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       47.03750            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       43.90550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       47.03750            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       48.14700            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       43.90550            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       47.03750            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       48.14700            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       43.90550            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       47.03750            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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 326  LIES ON A SPECIAL POSITION.                          
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A   91   NE   CZ   NH1  NH2                                  
REMARK 480     ARG B   91   NE   CZ   NH1  NH2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B 149   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
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 110      -90.27    -93.25                                   
REMARK 500    MET A 139       47.28    -90.35                                   
REMARK 500    ASP B 110      -89.35    -88.38                                   
REMARK 500    MET B 139       48.80    -89.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 206  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 143   O                                                      
REMARK 620 2 PRO A  23   O   115.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 203  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  21   OD1                                                    
REMARK 620 2 SER B  59   O   121.1                                              
REMARK 620 3 HOH B 412   O   114.7  94.7                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1R0 A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOH A 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FOL B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 205                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 206                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4KAK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4KBN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4KD7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4KEB   RELATED DB: PDB                                   
DBREF  4KFJ A    1   186  UNP    P00374   DYR_HUMAN        2    187             
DBREF  4KFJ B    1   186  UNP    P00374   DYR_HUMAN        2    187             
SEQRES   1 A  186  VAL GLY SER LEU ASN CYS ILE VAL ALA VAL SER GLN ASN          
SEQRES   2 A  186  MET GLY ILE GLY LYS ASN GLY ASP LEU PRO TRP PRO PRO          
SEQRES   3 A  186  LEU ARG ASN GLU PHE ARG TYR PHE GLN ARG MET THR THR          
SEQRES   4 A  186  THR SER SER VAL GLU GLY LYS GLN ASN LEU VAL ILE MET          
SEQRES   5 A  186  GLY LYS LYS THR TRP PHE SER ILE PRO GLU LYS ASN ARG          
SEQRES   6 A  186  PRO LEU LYS GLY ARG ILE ASN LEU VAL LEU SER ARG GLU          
SEQRES   7 A  186  LEU LYS GLU PRO PRO GLN GLY ALA HIS PHE LEU SER ARG          
SEQRES   8 A  186  SER LEU ASP ASP ALA LEU LYS LEU THR GLU GLN PRO GLU          
SEQRES   9 A  186  LEU ALA ASN LYS VAL ASP MET VAL TRP ILE VAL GLY GLY          
SEQRES  10 A  186  SER SER VAL TYR LYS GLU ALA MET ASN HIS PRO GLY HIS          
SEQRES  11 A  186  LEU LYS LEU PHE VAL THR ARG ILE MET GLN ASP PHE GLU          
SEQRES  12 A  186  SER ASP THR PHE PHE PRO GLU ILE ASP LEU GLU LYS TYR          
SEQRES  13 A  186  LYS LEU LEU PRO GLU TYR PRO GLY VAL LEU SER ASP VAL          
SEQRES  14 A  186  GLN GLU GLU LYS GLY ILE LYS TYR LYS PHE GLU VAL TYR          
SEQRES  15 A  186  GLU LYS ASN ASP                                              
SEQRES   1 B  186  VAL GLY SER LEU ASN CYS ILE VAL ALA VAL SER GLN ASN          
SEQRES   2 B  186  MET GLY ILE GLY LYS ASN GLY ASP LEU PRO TRP PRO PRO          
SEQRES   3 B  186  LEU ARG ASN GLU PHE ARG TYR PHE GLN ARG MET THR THR          
SEQRES   4 B  186  THR SER SER VAL GLU GLY LYS GLN ASN LEU VAL ILE MET          
SEQRES   5 B  186  GLY LYS LYS THR TRP PHE SER ILE PRO GLU LYS ASN ARG          
SEQRES   6 B  186  PRO LEU LYS GLY ARG ILE ASN LEU VAL LEU SER ARG GLU          
SEQRES   7 B  186  LEU LYS GLU PRO PRO GLN GLY ALA HIS PHE LEU SER ARG          
SEQRES   8 B  186  SER LEU ASP ASP ALA LEU LYS LEU THR GLU GLN PRO GLU          
SEQRES   9 B  186  LEU ALA ASN LYS VAL ASP MET VAL TRP ILE VAL GLY GLY          
SEQRES  10 B  186  SER SER VAL TYR LYS GLU ALA MET ASN HIS PRO GLY HIS          
SEQRES  11 B  186  LEU LYS LEU PHE VAL THR ARG ILE MET GLN ASP PHE GLU          
SEQRES  12 B  186  SER ASP THR PHE PHE PRO GLU ILE ASP LEU GLU LYS TYR          
SEQRES  13 B  186  LYS LEU LEU PRO GLU TYR PRO GLY VAL LEU SER ASP VAL          
SEQRES  14 B  186  GLN GLU GLU LYS GLY ILE LYS TYR LYS PHE GLU VAL TYR          
SEQRES  15 B  186  GLU LYS ASN ASP                                              
HET    NDP  A 201      48                                                       
HET    1R0  A 202      31                                                       
HET     MG  A 203       1                                                       
HET     CL  A 204       1                                                       
HET    EOH  A 205       3                                                       
HET     MG  A 206       1                                                       
HET    NDP  B 201      48                                                       
HET    FOL  B 202      32                                                       
HET     MG  B 203       1                                                       
HET     CL  B 204       1                                                       
HET     MG  B 205       1                                                       
HET     MG  B 206       1                                                       
HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
HETNAM   2 NDP  PHOSPHATE                                                       
HETNAM     1R0 6-ETHYL-5-{3-[3-(ISOQUINOLIN-5-YL)-5-                            
HETNAM   2 1R0  METHOXYPHENYL]PROP-1-YN-1-YL}PYRIMIDINE-2,4-DIAMINE             
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     EOH ETHANOL                                                          
HETNAM     FOL FOLIC ACID                                                       
FORMUL   3  NDP    2(C21 H30 N7 O17 P3)                                         
FORMUL   4  1R0    C25 H23 N5 O                                                 
FORMUL   5   MG    5(MG 2+)                                                     
FORMUL   6   CL    2(CL 1-)                                                     
FORMUL   7  EOH    C2 H6 O                                                      
FORMUL  10  FOL    C19 H19 N7 O6                                                
FORMUL  15  HOH   *386(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  THR A  100  1                                   9    
HELIX    5   5 GLY A  117  HIS A  127  1                                  11    
HELIX    6   6 LEU B   27  THR B   40  1                                  14    
HELIX    7   7 LYS B   54  ILE B   60  1                                   7    
HELIX    8   8 PRO B   61  ARG B   65  5                                   5    
HELIX    9   9 SER B   92  GLU B  101  1                                  10    
HELIX   10  10 GLN B  102  ASN B  107  1                                   6    
HELIX   11  11 GLY B  117  ASN B  126  1                                  10    
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 SER A   3  VAL A  10  1  N  ASN A   5   O  ILE A 114           
SHEET    6   A 8 HIS A 130  ILE A 138  1  O  PHE A 134   N  CYS A   6           
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 SER A   3  VAL A  10  1  N  ASN A   5   O  ILE A 114           
SHEET    6   B 8 HIS A 130  ILE A 138  1  O  PHE A 134   N  CYS A   6           
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           
SHEET    1   D 8 PHE B  88  SER B  90  0                                        
SHEET    2   D 8 ARG B  70  LEU B  75  1  N  VAL B  74   O  PHE B  88           
SHEET    3   D 8 GLN B  47  GLY B  53  1  N  ASN B  48   O  ILE B  71           
SHEET    4   D 8 VAL B 109  ILE B 114  1  O  TRP B 113   N  LEU B  49           
SHEET    5   D 8 SER B   3  VAL B  10  1  N  ASN B   5   O  ILE B 114           
SHEET    6   D 8 HIS B 130  ILE B 138  1  O  PHE B 134   N  CYS B   6           
SHEET    7   D 8 ILE B 175  LYS B 184 -1  O  LYS B 178   N  ARG B 137           
SHEET    8   D 8 LYS B 157  LEU B 158 -1  N  LYS B 157   O  GLU B 183           
SHEET    1   E 8 PHE B  88  SER B  90  0                                        
SHEET    2   E 8 ARG B  70  LEU B  75  1  N  VAL B  74   O  PHE B  88           
SHEET    3   E 8 GLN B  47  GLY B  53  1  N  ASN B  48   O  ILE B  71           
SHEET    4   E 8 VAL B 109  ILE B 114  1  O  TRP B 113   N  LEU B  49           
SHEET    5   E 8 SER B   3  VAL B  10  1  N  ASN B   5   O  ILE B 114           
SHEET    6   E 8 HIS B 130  ILE B 138  1  O  PHE B 134   N  CYS B   6           
SHEET    7   E 8 ILE B 175  LYS B 184 -1  O  LYS B 178   N  ARG B 137           
SHEET    8   E 8 GLN B 170  GLU B 172 -1  N  GLN B 170   O  TYR B 177           
SHEET    1   F 2 GLY B  15  GLY B  17  0                                        
SHEET    2   F 2 THR B 146  PHE B 147 -1  O  THR B 146   N  ILE B  16           
LINK         O   GLU A 143                MG    MG A 206     1555   1555  2.71  
LINK         O   PRO A  23                MG    MG A 206     1555   1555  2.91  
LINK         O   ASN A  64                MG    MG A 203     1555   1555  2.92  
LINK         OD1 ASP B  21                MG    MG B 203     1555   1555  2.93  
LINK         O   SER B  41                MG    MG B 205     1555   1555  2.96  
LINK         O   SER B  59                MG    MG B 203     1555   1555  2.99  
LINK        MG    MG B 203                 O   HOH B 412     1555   1555  2.63  
LINK        MG    MG B 206                 O   HOH B 383     1555   1555  2.81  
CISPEP   1 ARG A   65    PRO A   66          0        -6.89                     
CISPEP   2 GLY A  116    GLY A  117          0         4.59                     
CISPEP   3 ARG B   65    PRO B   66          0        -7.37                     
CISPEP   4 GLY B  116    GLY B  117          0         4.14                     
SITE     1 AC1 32 VAL A   8  ALA A   9  ILE A  16  GLY A  17                    
SITE     2 AC1 32 GLY A  20  ASP A  21  LEU A  22  GLY A  53                    
SITE     3 AC1 32 LYS A  54  LYS A  55  THR A  56  SER A  59                    
SITE     4 AC1 32 LEU A  75  SER A  76  ARG A  77  GLU A  78                    
SITE     5 AC1 32 ARG A  91  VAL A 115  GLY A 117  SER A 118                    
SITE     6 AC1 32 SER A 119  VAL A 120  TYR A 121  GLU A 123                    
SITE     7 AC1 32 THR A 146  1R0 A 202  HOH A 315  HOH A 320                    
SITE     8 AC1 32 HOH A 329  HOH A 361  HOH A 398  HOH A 486                    
SITE     1 AC2 17 ILE A   7  VAL A   8  ALA A   9  GLU A  30                    
SITE     2 AC2 17 PHE A  31  PHE A  34  GLN A  35  SER A  59                    
SITE     3 AC2 17 PRO A  61  ASN A  64  LEU A  67  ARG A  70                    
SITE     4 AC2 17 TYR A 121  THR A 136  NDP A 201  HOH A 329                    
SITE     5 AC2 17 HOH A 339                                                     
SITE     1 AC3  4 ASN A  64  PRO A  66  LEU A  67  LYS A  68                    
SITE     1 AC4  3 SER A 167  LYS A 178  PHE A 179                               
SITE     1 AC5  1 HOH A 484                                                     
SITE     1 AC6  2 PRO A  23  GLU A 143                                          
SITE     1 AC7 35 VAL B   8  ALA B   9  ILE B  16  GLY B  17                    
SITE     2 AC7 35 GLY B  20  ASP B  21  LEU B  22  GLY B  53                    
SITE     3 AC7 35 LYS B  54  LYS B  55  THR B  56  SER B  59                    
SITE     4 AC7 35 LEU B  75  SER B  76  ARG B  77  GLU B  78                    
SITE     5 AC7 35 ARG B  91  SER B  92  VAL B 115  GLY B 117                    
SITE     6 AC7 35 SER B 118  SER B 119  TYR B 121  THR B 146                    
SITE     7 AC7 35 FOL B 202  HOH B 313  HOH B 324  HOH B 363                    
SITE     8 AC7 35 HOH B 378  HOH B 387  HOH B 399  HOH B 412                    
SITE     9 AC7 35 HOH B 416  HOH B 432  HOH B 482                               
SITE     1 AC8 18 ILE B   7  VAL B   8  ALA B   9  LEU B  22                    
SITE     2 AC8 18 GLU B  30  PHE B  31  PHE B  34  GLN B  35                    
SITE     3 AC8 18 ASN B  64  LEU B  67  ARG B  70  VAL B 115                    
SITE     4 AC8 18 THR B 136  NDP B 201   MG B 203  HOH B 306                    
SITE     5 AC8 18 HOH B 412  HOH B 491                                          
SITE     1 AC9  4 ASP B  21  SER B  59  FOL B 202  HOH B 412                    
SITE     1 BC1  1 ARG B  28                                                     
SITE     1 BC2  1 SER B  41                                                     
SITE     1 BC3  4 HOH A 477  LEU B 153  TYR B 156  HOH B 383                    
CRYST1   87.811   94.075   96.294  90.00  90.00  90.00 C 2 2 21     16          
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      0.011388  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010630  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010385        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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