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Database: PDB
Entry: 4KD7
LinkDB: 4KD7
Original site: 4KD7 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 24-APR-13   4KD7              
TITLE     HUMAN DIHYDROFOLATE REDUCTASE COMPLEXED WITH NADPH AND 5-{3-[3-       
TITLE    2 METHOXY-5(PYRIDINE-4-YL)PHENYL]PROP-1-YN-1-YL}-6-ETHYL-PYRIMIDINE-2, 
TITLE    3 4-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 4KD7    1       REMARK                                   
REVDAT   3   20-NOV-13 4KD7    1       HET    HETATM HETNAM REMARK              
REVDAT   2   30-OCT-13 4KD7    1       JRNL                                     
REVDAT   1   09-OCT-13 4KD7    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.    2.71 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) : 2.71                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.28                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 21899                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.120                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1122                            
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 33.2877 -  5.4238    0.98     2690   139  0.2050 0.2073        
REMARK   3     2  5.4238 -  4.3080    1.00     2652   144  0.1467 0.1880        
REMARK   3     3  4.3080 -  3.7642    1.00     2572   154  0.1492 0.1809        
REMARK   3     4  3.7642 -  3.4205    1.00     2610   148  0.1528 0.2284        
REMARK   3     5  3.4205 -  3.1755    1.00     2611   123  0.1847 0.2367        
REMARK   3     6  3.1755 -  2.9884    1.00     2561   132  0.1981 0.2742        
REMARK   3     7  2.9884 -  2.8388    1.00     2563   149  0.2049 0.2734        
REMARK   3     8  2.8388 -  2.7153    0.98     2518   133  0.2107 0.3005        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.130           
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      :  0.005           3338                                  
REMARK   3   ANGLE     :  0.901           4544                                  
REMARK   3   CHIRALITY :  0.066            469                                  
REMARK   3   PLANARITY :  0.003            576                                  
REMARK   3   DIHEDRAL  : 14.991           1292                                  
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 4KD7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB079190.                                      
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   : 21954                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.715                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.280                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
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) : 2.71                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
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                                                
REMARK 200 STARTING MODEL: 2W3A                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.69                     
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       72.34200            
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       72.34200            
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       52.62900            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       52.62450            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       52.62900            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       52.62450            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       72.34200            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       52.62900            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       52.62450            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       72.34200            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       52.62900            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       52.62450            
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 323  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 320  LIES ON A SPECIAL POSITION.                          
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      -89.04    -95.98                                   
REMARK 500    ASP B 110      -89.18    -96.86                                   
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 9DR A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 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 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9DR B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 204                 
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: 4KEB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4KFJ   RELATED DB: PDB                                   
DBREF  4KD7 A    1   186  UNP    P00374   DYR_HUMAN        2    187             
DBREF  4KD7 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    9DR  A 202      27                                                       
HET    SO4  A 203       5                                                       
HET    SO4  A 204       5                                                       
HET    NDP  B 201      48                                                       
HET    9DR  B 202      27                                                       
HET    SO4  B 203       5                                                       
HET    SO4  B 204       5                                                       
HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
HETNAM   2 NDP  PHOSPHATE                                                       
HETNAM     9DR 6-ETHYL-5-{3-[3-METHOXY-5-(PYRIDIN-4-YL)PHENYL]PROP-1-           
HETNAM   2 9DR  YN-1-YL}PYRIMIDINE-2,4-DIAMINE                                  
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  NDP    2(C21 H30 N7 O17 P3)                                         
FORMUL   4  9DR    2(C21 H21 N5 O)                                              
FORMUL   5  SO4    4(O4 S 2-)                                                   
FORMUL  11  HOH   *136(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 GLN A  102  ASN A  107  1                                   6    
HELIX    6   6 GLY A  117  HIS A  127  1                                  11    
HELIX    7   7 LEU B   27  THR B   40  1                                  14    
HELIX    8   8 LYS B   54  ILE B   60  1                                   7    
HELIX    9   9 PRO B   61  ARG B   65  5                                   5    
HELIX   10  10 SER B   92  THR B  100  1                                   9    
HELIX   11  11 GLN B  102  ASN B  107  1                                   6    
HELIX   12  12 GLY B  117  HIS B  127  1                                  11    
SHEET    1   A 8 PHE A  88  SER A  90  0                                        
SHEET    2   A 8 ARG A  70  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  VAL A 112           
SHEET    6   A 8 LEU A 131  ILE A 138  1  O  THR A 136   N  VAL A  10           
SHEET    7   A 8 ILE A 175  LYS A 184 -1  O  TYR A 182   N  LEU A 133           
SHEET    8   A 8 LYS A 157  LEU A 159 -1  N  LEU A 159   O  VAL A 181           
SHEET    1   B 8 PHE A  88  SER A  90  0                                        
SHEET    2   B 8 ARG A  70  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  VAL A 112           
SHEET    6   B 8 LEU A 131  ILE A 138  1  O  THR A 136   N  VAL A  10           
SHEET    7   B 8 ILE A 175  LYS A 184 -1  O  TYR A 182   N  LEU A 133           
SHEET    8   B 8 GLN A 170  GLU A 172 -1  N  GLU A 172   O  ILE A 175           
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  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 LEU B   4  VAL B  10  1  N  ASN B   5   O  VAL B 112           
SHEET    6   D 8 HIS B 130  ILE B 138  1  O  THR B 136   N  VAL B  10           
SHEET    7   D 8 ILE B 175  ASN B 185 -1  O  TYR B 182   N  LEU B 133           
SHEET    8   D 8 LYS B 157  LEU B 159 -1  N  LEU B 159   O  VAL B 181           
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  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 LEU B   4  VAL B  10  1  N  ASN B   5   O  VAL B 112           
SHEET    6   E 8 HIS B 130  ILE B 138  1  O  THR B 136   N  VAL B  10           
SHEET    7   E 8 ILE B 175  ASN B 185 -1  O  TYR B 182   N  LEU B 133           
SHEET    8   E 8 VAL B 169  GLU B 172 -1  N  GLU B 172   O  ILE B 175           
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        -2.02                     
CISPEP   2 GLY A  116    GLY A  117          0         2.51                     
CISPEP   3 ARG B   65    PRO B   66          0        -2.30                     
CISPEP   4 GLY B  116    GLY B  117          0         2.47                     
SITE     1 AC1 28 VAL A   8  ALA A   9  ILE A  16  GLY A  20                    
SITE     2 AC1 28 ASP A  21  LEU A  22  TRP A  24  GLY A  53                    
SITE     3 AC1 28 LYS A  54  LYS A  55  THR A  56  LEU A  75                    
SITE     4 AC1 28 SER A  76  ARG A  77  GLU A  78  ARG A  91                    
SITE     5 AC1 28 VAL A 115  GLY A 116  GLY A 117  SER A 118                    
SITE     6 AC1 28 SER A 119  VAL A 120  TYR A 121  GLU A 123                    
SITE     7 AC1 28 THR A 146  9DR A 202  HOH A 311  HOH A 343                    
SITE     1 AC2 13 ILE A   7  VAL A   8  ALA A   9  GLU A  30                    
SITE     2 AC2 13 PHE A  31  PHE A  34  GLN A  35  SER A  59                    
SITE     3 AC2 13 LEU A  67  VAL A 115  TYR A 121  THR A 136                    
SITE     4 AC2 13 NDP A 201                                                     
SITE     1 AC3  3 ARG A  77  ARG A  91  ARG B  28                               
SITE     1 AC4  2 ARG A  28  LYS A  68                                          
SITE     1 AC5 27 VAL B   8  ALA B   9  ILE B  16  GLY B  20                    
SITE     2 AC5 27 ASP B  21  LEU B  22  TRP B  24  GLY B  53                    
SITE     3 AC5 27 LYS B  54  LYS B  55  THR B  56  LEU B  75                    
SITE     4 AC5 27 SER B  76  ARG B  77  GLU B  78  ARG B  91                    
SITE     5 AC5 27 VAL B 115  GLY B 116  GLY B 117  SER B 118                    
SITE     6 AC5 27 SER B 119  VAL B 120  TYR B 121  GLU B 123                    
SITE     7 AC5 27 THR B 146  9DR B 202  HOH B 307                               
SITE     1 AC6 14 ILE B   7  VAL B   8  ALA B   9  GLU B  30                    
SITE     2 AC6 14 PHE B  31  PHE B  34  GLN B  35  SER B  59                    
SITE     3 AC6 14 LEU B  67  VAL B 115  TYR B 121  THR B 136                    
SITE     4 AC6 14 NDP B 201  HOH B 312                                          
SITE     1 AC7  3 ARG B  28  GLN B  35  LYS B  68                               
SITE     1 AC8  4 ARG A  28  HOH A 356  ARG B  77  ARG B  91                    
CRYST1  105.258  105.249  144.684  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      0.009500  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009501  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006912        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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