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Database: PDB
Entry: 4KEB
LinkDB: 4KEB
Original site: 4KEB 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 25-APR-13   4KEB              
TITLE     HUMAN DIHYDROFOLATE REDUCTASE COMPLEXED WITH NADPH AND 5-{3-[3-       
TITLE    2 METHOXY-5-(ISOQUIN-5-YL)PHENYL]BUT-1-YN-1-YL}6-ETHYLPYRIMIDINE-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 4KEB    1       REMARK                                   
REVDAT   3   20-NOV-13 4KEB    1       HET    HETATM HETNAM REMARK              
REVDAT   2   30-OCT-13 4KEB    1       JRNL                                     
REVDAT   1   09-OCT-13 4KEB    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.    1.45 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) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 16.10                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 69735                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.206                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3471                            
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 16.0967 -  4.2153    0.96     2674   170  0.1798 0.1909        
REMARK   3     2  4.2153 -  3.3557    0.98     2679   128  0.1538 0.1851        
REMARK   3     3  3.3557 -  2.9345    1.00     2725   122  0.1790 0.2005        
REMARK   3     4  2.9345 -  2.6675    0.99     2680   128  0.1905 0.2166        
REMARK   3     5  2.6675 -  2.4770    0.99     2672   137  0.1771 0.2475        
REMARK   3     6  2.4770 -  2.3314    0.99     2678   135  0.1699 0.2057        
REMARK   3     7  2.3314 -  2.2150    0.99     2622   156  0.1663 0.1883        
REMARK   3     8  2.2150 -  2.1188    1.00     2676   136  0.1553 0.2187        
REMARK   3     9  2.1188 -  2.0374    1.00     2640   147  0.1532 0.2020        
REMARK   3    10  2.0374 -  1.9672    1.00     2660   134  0.1523 0.2069        
REMARK   3    11  1.9672 -  1.9058    0.99     2647   126  0.1568 0.2101        
REMARK   3    12  1.9058 -  1.8514    0.99     2631   142  0.1603 0.2135        
REMARK   3    13  1.8514 -  1.8027    0.99     2627   139  0.1594 0.2222        
REMARK   3    14  1.8027 -  1.7588    0.99     2657   122  0.1533 0.1987        
REMARK   3    15  1.7588 -  1.7189    1.00     2647   135  0.1552 0.1991        
REMARK   3    16  1.7189 -  1.6823    1.00     2631   141  0.1570 0.2187        
REMARK   3    17  1.6823 -  1.6487    1.00     2618   138  0.1594 0.2210        
REMARK   3    18  1.6487 -  1.6176    1.00     2651   142  0.1495 0.2317        
REMARK   3    19  1.6176 -  1.5888    1.00     2661   133  0.1495 0.2197        
REMARK   3    20  1.5888 -  1.5618    1.00     2608   136  0.1562 0.2597        
REMARK   3    21  1.5618 -  1.5367    1.00     2635   164  0.1699 0.2403        
REMARK   3    22  1.5367 -  1.5130    1.00     2624   131  0.1744 0.2574        
REMARK   3    23  1.5130 -  1.4908    1.00     2640   142  0.1787 0.2621        
REMARK   3    24  1.4908 -  1.4698    1.00     2643   153  0.1842 0.2179        
REMARK   3    25  1.4698 -  1.4500    1.00     2638   134  0.1790 0.1998        
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)     : 0.130            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.620           
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           3480                                  
REMARK   3   ANGLE     :  1.589           4749                                  
REMARK   3   CHIRALITY :  0.099            501                                  
REMARK   3   PLANARITY :  0.008            602                                  
REMARK   3   DIHEDRAL  : 14.693           1374                                  
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 4KEB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAY-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB079230.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-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) : 0.97016                            
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   : 92033                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450                              
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     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 8.000                              
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) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
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: 2C2S                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, 0.2-0.3M LITHIUM          
REMARK 280  SULFATE, 25-32%(W/V) PEG 4000, PH 7.5, VAPOR DIFFUSION, HANGING     
REMARK 280  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       48.07750            
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       48.07750            
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       43.85450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       46.82950            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       43.85450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       46.82950            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       48.07750            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       43.85450            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       46.82950            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       48.07750            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       43.85450            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       46.82950            
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 347  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     LYS A   80   CG   CD   CE   NZ                                   
REMARK 480     ARG A   91   NE   CZ   NH1  NH2                                  
REMARK 480     LYS A  108   CD   CE   NZ                                        
REMARK 480     ARG B   28   NE   CZ   NH1  NH2                                  
REMARK 480     LYS B   80   CG   CD   CE   NZ                                   
REMARK 480     ARG B   91   NE   CZ   NH1  NH2                                  
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      -90.88    -94.35                                   
REMARK 500    MET A 139       48.11    -87.98                                   
REMARK 500    ASP B 110      -88.60    -92.67                                   
REMARK 500    MET B 139       46.65    -87.93                                   
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 NDP A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1QZ A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FOL B 202                 
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: 4KFJ   RELATED DB: PDB                                   
DBREF  4KEB A    1   186  UNP    P00374   DYR_HUMAN        2    187             
DBREF  4KEB 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    1QZ  A 202      32                                                       
HET    NDP  B 201      48                                                       
HET    FOL  B 202      32                                                       
HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
HETNAM   2 NDP  PHOSPHATE                                                       
HETNAM     1QZ 6-ETHYL-5-{(3S)-3-[3-(ISOQUINOLIN-5-YL)-5-                       
HETNAM   2 1QZ  METHOXYPHENYL]BUT-1-YN-1-YL}PYRIMIDINE-2,4-DIAMINE              
HETNAM     FOL FOLIC ACID                                                       
FORMUL   3  NDP    2(C21 H30 N7 O17 P3)                                         
FORMUL   4  1QZ    C26 H25 N5 O                                                 
FORMUL   6  FOL    C19 H19 N7 O6                                                
FORMUL   7  HOH   *427(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  ASN A  126  1                                  10    
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  THR B  100  1                                   9    
HELIX   10  10 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 ILE B  71  LEU B  75  1  N  VAL B  74   O  PHE B  88           
SHEET    3   D 8 GLN B  47  GLY B  53  1  N  VAL B  50   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 ILE B  71  LEU B  75  1  N  VAL B  74   O  PHE B  88           
SHEET    3   E 8 GLN B  47  GLY B  53  1  N  VAL B  50   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           
CISPEP   1 ARG A   65    PRO A   66          0        -7.76                     
CISPEP   2 GLY A  116    GLY A  117          0         5.82                     
CISPEP   3 ARG B   65    PRO B   66          0        -7.29                     
CISPEP   4 GLY B  116    GLY B  117          0         5.17                     
SITE     1 AC1 33 VAL A   8  ALA A   9  ILE A  16  GLY A  17                    
SITE     2 AC1 33 GLY A  20  ASP A  21  LEU A  22  GLY A  53                    
SITE     3 AC1 33 LYS A  54  LYS A  55  THR A  56  LEU A  75                    
SITE     4 AC1 33 SER A  76  ARG A  77  GLU A  78  ARG A  91                    
SITE     5 AC1 33 VAL A 115  GLY A 117  SER A 118  SER A 119                    
SITE     6 AC1 33 VAL A 120  TYR A 121  GLU A 123  THR A 146                    
SITE     7 AC1 33 1QZ A 202  HOH A 329  HOH A 336  HOH A 423                    
SITE     8 AC1 33 HOH A 433  HOH A 442  HOH A 445  HOH A 466                    
SITE     9 AC1 33 HOH A 509                                                     
SITE     1 AC2 16 ILE A   7  VAL A   8  ALA A   9  LEU A  22                    
SITE     2 AC2 16 GLU A  30  PHE A  31  PHE A  34  PRO A  61                    
SITE     3 AC2 16 ASN A  64  LEU A  67  ARG A  70  TYR A 121                    
SITE     4 AC2 16 THR A 136  NDP A 201  HOH A 325  HOH A 509                    
SITE     1 AC3 36 VAL B   8  ALA B   9  ILE B  16  GLY B  17                    
SITE     2 AC3 36 GLY B  20  ASP B  21  LEU B  22  GLY B  53                    
SITE     3 AC3 36 LYS B  54  LYS B  55  THR B  56  SER B  59                    
SITE     4 AC3 36 LEU B  75  SER B  76  ARG B  77  GLU B  78                    
SITE     5 AC3 36 ARG B  91  VAL B 115  GLY B 117  SER B 118                    
SITE     6 AC3 36 SER B 119  VAL B 120  TYR B 121  GLU B 123                    
SITE     7 AC3 36 THR B 146  FOL B 202  HOH B 314  HOH B 319                    
SITE     8 AC3 36 HOH B 343  HOH B 361  HOH B 373  HOH B 374                    
SITE     9 AC3 36 HOH B 438  HOH B 464  HOH B 481  HOH B 508                    
SITE     1 AC4 17 ILE B   7  VAL B   8  ALA B   9  GLU B  30                    
SITE     2 AC4 17 PHE B  31  PHE B  34  GLN B  35  ASN B  64                    
SITE     3 AC4 17 LEU B  67  ARG B  70  VAL B 115  TYR B 121                    
SITE     4 AC4 17 THR B 136  NDP B 201  HOH B 448  HOH B 493                    
SITE     5 AC4 17 HOH B 508                                                     
CRYST1   87.709   93.659   96.155  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      0.011401  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010677  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010400        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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