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Database: PDB
Entry: 6DE4
LinkDB: 6DE4
Original site: 6DE4 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 11-MAY-18   6DE4              
TITLE     HOMO SAPIENS DIHYDROFOLATE REDUCTASE COMPLEXED WITH BETA-NADPH AND 3'-
TITLE    2 [(2R)-4-(2,4-DIAMINO-6-ETHYLPHENYL)BUT-3-YN-2-YL]-5'-METHOXY-[1,1'-  
TITLE    3 BIPHENYL]-4-CARBOXYLIC ACID                                          
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;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    DHFR, ANTIFOLATES, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.HAJIAN,D.WRIGHT                                                     
REVDAT   3   18-DEC-19 6DE4    1       REMARK                                   
REVDAT   2   10-JUL-19 6DE4    1       JRNL                                     
REVDAT   1   23-MAY-18 6DE4    0                                                
JRNL        AUTH   B.HAJIAN,E.SCOCCHERA,C.SHOEN,J.KRUCINSKA,K.VISWANATHAN,      
JRNL        AUTH 2 N.G-DAYANANDAN,H.ERLANDSEN,A.ESTRADA,K.MIKUSOVA,             
JRNL        AUTH 3 J.KORDULAKOVA,M.CYNAMON,D.WRIGHT                             
JRNL        TITL   DRUGGING THE FOLATE PATHWAY IN MYCOBACTERIUM TUBERCULOSIS:   
JRNL        TITL 2 THE ROLE OF MULTI-TARGETING AGENTS.                          
JRNL        REF    CELL CHEM BIOL                V.  26   781 2019              
JRNL        REFN                   ESSN 2451-9456                               
JRNL        PMID   30930162                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2019.02.013                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.41 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.41                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.36                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.370                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 30735                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.460                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1987                            
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 42.3708 -  5.8055    0.99     2171   153  0.1997 0.2476        
REMARK   3     2  5.8055 -  4.6098    1.00     2102   145  0.1634 0.1638        
REMARK   3     3  4.6098 -  4.0276    1.00     2082   142  0.1426 0.1935        
REMARK   3     4  4.0276 -  3.6596    1.00     2070   143  0.1685 0.2123        
REMARK   3     5  3.6596 -  3.3974    1.00     2072   143  0.1713 0.2378        
REMARK   3     6  3.3974 -  3.1972    1.00     2047   136  0.2012 0.2468        
REMARK   3     7  3.1972 -  3.0371    1.00     2075   138  0.2199 0.2186        
REMARK   3     8  3.0371 -  2.9049    1.00     2030   139  0.1992 0.2598        
REMARK   3     9  2.9049 -  2.7931    1.00     2044   146  0.1888 0.2176        
REMARK   3    10  2.7931 -  2.6968    1.00     2040   144  0.1921 0.2465        
REMARK   3    11  2.6968 -  2.6124    1.00     2038   141  0.1985 0.2457        
REMARK   3    12  2.6124 -  2.5378    1.00     2023   143  0.2136 0.2588        
REMARK   3    13  2.5378 -  2.4710    1.00     2027   140  0.2163 0.2573        
REMARK   3    14  2.4710 -  2.4107    0.95     1927   134  0.2154 0.2522        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.990           
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      :  0.008           3395                                  
REMARK   3   ANGLE     :  1.057           4620                                  
REMARK   3   CHIRALITY :  0.041            477                                  
REMARK   3   PLANARITY :  0.004            593                                  
REMARK   3   DIHEDRAL  : 16.352           1310                                  
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 6DE4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000234469.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-MAY-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30735                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.411                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.364                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 7.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.41                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.77900                            
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: NULL                                                  
REMARK 200 STARTING MODEL: 4KAK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH 7.6,0.2M LISO4, 15MM        
REMARK 280  CACL2, 6% ETOH, 15% ETHYLENE GLYCOL, VAPOR DIFFUSION,               
REMARK 280  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       72.16650            
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       72.16650            
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       52.30550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       52.33000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       52.30550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       52.33000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       72.16650            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       52.30550            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       52.33000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       72.16650            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       52.30550            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       52.33000            
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 322  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 328  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 316  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 323  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU A   123     N6A  NDP A   201              1.99            
REMARK 500   NH1  ARG A    91     O    HOH A   301              2.01            
REMARK 500   O2   SO4 B   207     O    HOH B   301              2.04            
REMARK 500   NZ   LYS A   157     O    HOH A   302              2.05            
REMARK 500  CL     CL A   203     O    HOH A   337              2.05            
REMARK 500   O2   SO4 B   206     O    HOH B   302              2.06            
REMARK 500   NZ   LYS B   157     O    HOH B   303              2.10            
REMARK 500   OE1  GLU B   123     O    HOH B   304              2.14            
REMARK 500   O1X  NDP A   201     O    HOH A   303              2.14            
REMARK 500   O    EOH A   206     O    HOH A   304              2.15            
REMARK 500   NZ   LYS A    68     O    HOH A   305              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500  CL     CL B   205     O    HOH B   333     3657     1.93            
REMARK 500   O    EOH A   207     O    EOH B   209     7557     2.00            
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    LYS A  18      116.91   -161.73                                   
REMARK 500    ASN A 107      -45.77     72.13                                   
REMARK 500    ASP A 110      -88.09    -95.32                                   
REMARK 500    ASP A 110      -88.95    -95.32                                   
REMARK 500    SER B   3      113.51     64.72                                   
REMARK 500    LYS B  18      116.79   -160.17                                   
REMARK 500    ASN B 107      -40.72     73.51                                   
REMARK 500    ASP B 110      -89.05    -97.26                                   
REMARK 500    ASP B 110      -90.06    -97.26                                   
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 G6Y A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EOH A 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EOH A 207                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue G6Y B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 205                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 207                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EOH B 208                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EOH B 209                 
DBREF  6DE4 A    1   186  UNP    P00374   DYR_HUMAN        2    187             
DBREF  6DE4 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    G6Y  A 202      31                                                       
HET     CL  A 203       1                                                       
HET    GOL  A 204      14                                                       
HET    GOL  A 205      14                                                       
HET    EOH  A 206       9                                                       
HET    EOH  A 207       9                                                       
HET    NDP  B 201      48                                                       
HET    G6Y  B 202      31                                                       
HET     CA  B 203       1                                                       
HET     CA  B 204       1                                                       
HET     CL  B 205       1                                                       
HET    SO4  B 206       5                                                       
HET    SO4  B 207       5                                                       
HET    EOH  B 208       9                                                       
HET    EOH  B 209       9                                                       
HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
HETNAM   2 NDP  PHOSPHATE                                                       
HETNAM     G6Y 3'-[(2R)-4-(2,4-DIAMINO-6-ETHYLPYRIMIDIN-5-YL)BUT-3-YN-          
HETNAM   2 G6Y  2-YL]-5'-METHOXY[1,1'-BIPHENYL]-4-CARBOXYLIC ACID               
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETNAM     EOH ETHANOL                                                          
HETNAM      CA CALCIUM ION                                                      
HETNAM     SO4 SULFATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  NDP    2(C21 H30 N7 O17 P3)                                         
FORMUL   4  G6Y    2(C24 H24 N4 O3)                                             
FORMUL   5   CL    2(CL 1-)                                                     
FORMUL   6  GOL    2(C3 H8 O3)                                                  
FORMUL   8  EOH    4(C2 H6 O)                                                   
FORMUL  12   CA    2(CA 2+)                                                     
FORMUL  15  SO4    2(O4 S 2-)                                                   
FORMUL  19  HOH   *70(H2 O)                                                     
HELIX    1 AA1 LEU A   27  THR A   40  1                                  14    
HELIX    2 AA2 LYS A   54  ILE A   60  1                                   7    
HELIX    3 AA3 PRO A   61  ARG A   65  5                                   5    
HELIX    4 AA4 SER A   92  THR A  100  1                                   9    
HELIX    5 AA5 GLY A  117  HIS A  127  1                                  11    
HELIX    6 AA6 LEU B   27  THR B   40  1                                  14    
HELIX    7 AA7 LYS B   54  ILE B   60  1                                   7    
HELIX    8 AA8 PRO B   61  ARG B   65  5                                   5    
HELIX    9 AA9 SER B   92  THR B  100  1                                   9    
HELIX   10 AB1 GLY B  117  HIS B  127  1                                  11    
SHEET    1 AA1 8 PHE A  88  SER A  90  0                                        
SHEET    2 AA1 8 ARG A  70  LEU A  75  1  N  VAL A  74   O  SER A  90           
SHEET    3 AA1 8 GLN A  47  GLY A  53  1  N  VAL A  50   O  ILE A  71           
SHEET    4 AA1 8 VAL A 109  ILE A 114  1  O  TRP A 113   N  ILE A  51           
SHEET    5 AA1 8 LEU A   4  VAL A  10  1  N  ASN A   5   O  ILE A 114           
SHEET    6 AA1 8 LEU A 131  ILE A 138  1  O  THR A 136   N  VAL A  10           
SHEET    7 AA1 8 ILE A 175  LYS A 184 -1  O  GLU A 180   N  VAL A 135           
SHEET    8 AA1 8 LYS A 157  LEU A 158 -1  N  LYS A 157   O  GLU A 183           
SHEET    1 AA2 8 PHE A  88  SER A  90  0                                        
SHEET    2 AA2 8 ARG A  70  LEU A  75  1  N  VAL A  74   O  SER A  90           
SHEET    3 AA2 8 GLN A  47  GLY A  53  1  N  VAL A  50   O  ILE A  71           
SHEET    4 AA2 8 VAL A 109  ILE A 114  1  O  TRP A 113   N  ILE A  51           
SHEET    5 AA2 8 LEU A   4  VAL A  10  1  N  ASN A   5   O  ILE A 114           
SHEET    6 AA2 8 LEU A 131  ILE A 138  1  O  THR A 136   N  VAL A  10           
SHEET    7 AA2 8 ILE A 175  LYS A 184 -1  O  GLU A 180   N  VAL A 135           
SHEET    8 AA2 8 GLN A 170  GLU A 172 -1  N  GLN A 170   O  TYR A 177           
SHEET    1 AA3 2 GLY A  15  GLY A  17  0                                        
SHEET    2 AA3 2 THR A 146  PHE A 147 -1  O  THR A 146   N  ILE A  16           
SHEET    1 AA4 8 PHE B  88  SER B  90  0                                        
SHEET    2 AA4 8 ILE B  71  LEU B  75  1  N  VAL B  74   O  SER B  90           
SHEET    3 AA4 8 GLN B  47  GLY B  53  1  N  VAL B  50   O  ILE B  71           
SHEET    4 AA4 8 VAL B 109  ILE B 114  1  O  TRP B 113   N  LEU B  49           
SHEET    5 AA4 8 LEU B   4  VAL B  10  1  N  ASN B   5   O  ILE B 114           
SHEET    6 AA4 8 LEU B 131  ILE B 138  1  O  PHE B 134   N  CYS B   6           
SHEET    7 AA4 8 ILE B 175  LYS B 184 -1  O  GLU B 180   N  VAL B 135           
SHEET    8 AA4 8 LYS B 157  LEU B 158 -1  N  LYS B 157   O  GLU B 183           
SHEET    1 AA5 8 PHE B  88  SER B  90  0                                        
SHEET    2 AA5 8 ILE B  71  LEU B  75  1  N  VAL B  74   O  SER B  90           
SHEET    3 AA5 8 GLN B  47  GLY B  53  1  N  VAL B  50   O  ILE B  71           
SHEET    4 AA5 8 VAL B 109  ILE B 114  1  O  TRP B 113   N  LEU B  49           
SHEET    5 AA5 8 LEU B   4  VAL B  10  1  N  ASN B   5   O  ILE B 114           
SHEET    6 AA5 8 LEU B 131  ILE B 138  1  O  PHE B 134   N  CYS B   6           
SHEET    7 AA5 8 ILE B 175  LYS B 184 -1  O  GLU B 180   N  VAL B 135           
SHEET    8 AA5 8 GLN B 170  GLU B 172 -1  N  GLN B 170   O  TYR B 177           
SHEET    1 AA6 2 GLY B  15  GLY B  17  0                                        
SHEET    2 AA6 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         1.49                     
CISPEP   2 GLY A  116    GLY A  117          0         2.97                     
CISPEP   3 ARG B   65    PRO B   66          0         0.12                     
CISPEP   4 GLY B  116    GLY B  117          0         4.82                     
SITE     1 AC1 29 VAL A   8  ALA A   9  ILE A  16  GLY A  17                    
SITE     2 AC1 29 GLY A  20  ASP A  21  LEU A  22  GLY A  53                    
SITE     3 AC1 29 LYS A  54  LYS A  55  THR A  56  SER A  59                    
SITE     4 AC1 29 LEU A  75  SER A  76  ARG A  77  GLU A  78                    
SITE     5 AC1 29 ARG A  91  VAL A 115  GLY A 116  GLY A 117                    
SITE     6 AC1 29 SER A 118  VAL A 120  TYR A 121  GLU A 123                    
SITE     7 AC1 29 THR A 146  G6Y A 202  HOH A 303  HOH A 306                    
SITE     8 AC1 29 HOH A 307                                                     
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  SER A  59  ASN A  64                    
SITE     3 AC2 13 VAL A 115  TYR A 121  THR A 136  NDP A 201                    
SITE     4 AC2 13 GOL A 204                                                     
SITE     1 AC3  3 ARG A  32  ARG A  36  HOH A 337                               
SITE     1 AC4  7 LEU A  22  TRP A  24  PRO A  26  LEU A  27                    
SITE     2 AC4  7 GLU A  30  PHE A  31  G6Y A 202                               
SITE     1 AC5  6 GLY A   2  SER A   3  SER A  42  ASP A 110                    
SITE     2 AC5  6 MET A 111  LYS A 132                                          
SITE     1 AC6  2 ARG A  28  HOH A 304                                          
SITE     1 AC7  4 PHE B  31  GLN B  35  EOH B 209  HOH B 306                    
SITE     1 AC8 28 VAL B   8  ALA B   9  ILE B  16  GLY B  17                    
SITE     2 AC8 28 GLY B  20  ASP B  21  GLY B  53  LYS B  54                    
SITE     3 AC8 28 LYS B  55  THR B  56  SER B  59  LEU B  75                    
SITE     4 AC8 28 SER B  76  ARG B  77  GLU B  78  ARG B  91                    
SITE     5 AC8 28 VAL B 115  GLY B 116  GLY B 117  SER B 118                    
SITE     6 AC8 28 SER B 119  VAL B 120  TYR B 121  GLU B 123                    
SITE     7 AC8 28 THR B 146  G6Y B 202  HOH B 304  HOH B 308                    
SITE     1 AC9 13 ILE B   7  VAL B   8  ALA B   9  ASP B  21                    
SITE     2 AC9 13 GLU B  30  PHE B  31  PHE B  34  SER B  59                    
SITE     3 AC9 13 ASN B  64  VAL B 115  TYR B 121  THR B 136                    
SITE     4 AC9 13 NDP B 201                                                     
SITE     1 AD1  2 ARG B  77  ARG B  91                                          
SITE     1 AD2  1 GLY B  85                                                     
SITE     1 AD3  3 ARG B  32  ARG B  36  HOH B 333                               
SITE     1 AD4  5 GLU A 172  LYS A 173  GLY A 174  LYS B  98                    
SITE     2 AD4  5 HOH B 302                                                     
SITE     1 AD5  5 LYS A  98  GLU B 172  LYS B 173  GLY B 174                    
SITE     2 AD5  5 HOH B 301                                                     
SITE     1 AD6  4 GLN A  84  GLY A  85  LYS B 157  HOH B 303                    
SITE     1 AD7  4 ARG A  91  EOH A 207  HOH A 308  HOH B 306                    
CRYST1  104.611  104.660  144.333  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      0.009559  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009555  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006928        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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