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Database: PDB
Entry: 4WRH
LinkDB: 4WRH
Original site: 4WRH 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 24-OCT-14   4WRH              
TITLE     AKR1C3 COMPLEXED WITH BREAKDOWN PRODUCT OF N-(TERT-BUTYL)-2-(2-CHLORO-
TITLE    2 4-(((3-MERCAPTO-5-METHYL-4H-1,2,4-TRIAZOL-4-YL)AMINO)METHYL)-6-      
TITLE    3 METHOXYPHENOXY)ACETAMIDE                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALDO-KETO REDUCTASE FAMILY 1 MEMBER C3;                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: 17-BETA-HYDROXYSTEROID DEHYDROGENASE TYPE 5,17-BETA-HSD 5,3-
COMPND   5 ALPHA-HSD TYPE II,BRAIN,3-ALPHA-HYDROXYSTEROID DEHYDROGENASE TYPE 2, 
COMPND   6 3-ALPHA-HSD TYPE 2,CHLORDECONE REDUCTASE HOMOLOG HAKRB,DIHYDRODIOL   
COMPND   7 DEHYDROGENASE 3,DD3,DIHYDRODIOL DEHYDROGENASE TYPE I,HA1753,INDANOL  
COMPND   8 DEHYDROGENASE,PROSTAGLANDIN F SYNTHASE,PGFS,TESTOSTERONE 17-BETA-    
COMPND   9 DEHYDROGENASE 5,TRANS-1,2-DIHYDROBENZENE-1,2-DIOL DEHYDROGENASE;     
COMPND  10 EC: 1.-.-.-,1.1.1.357,1.1.1.112,1.1.1.188,1.1.1.239,1.1.1.64,        
COMPND  11 1.3.1.20;                                                            
COMPND  12 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: AKR1C3, DDH1, HSD17B5, KIAA0119, PGFS;                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: BL21(DE3);                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET22B                                    
KEYWDS    OXIDOREDUCTASE, INHIBITOR, COMPLEX, OXIDOREDUCTASE-OXIDOREDUCTASE     
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.J.SQUIRE,J.U.FLANAGAN,Y.YOSAATMADJA                                 
REVDAT   1   05-NOV-14 4WRH    0                                                
JRNL        AUTH   Y.YOSAATMADJA,R.-W.KO,J.U.FLANAGAN,C.J.SQUIRE                
JRNL        TITL   BREAKDOWN PRODUCT OF                                         
JRNL        TITL 2 N-(TERT-BUTYL)-2-(2-CHLORO-4-(((3-MERCAPTO-5-METHYL-4H-1,2,  
JRNL        TITL 3 4-TRIAZOL-4-YL)AMINO)METHYL)-6-METHOXYPHENOXY)ACETAMIDE      
JRNL        TITL 4 TRAPPED IN ACTIVE SITE OF AKR1C3                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 52.89                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 43428                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.187                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2306                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.65                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3124                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.68                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2300                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 168                          
REMARK   3   BIN FREE R VALUE                    : 0.2600                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2487                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 83                                      
REMARK   3   SOLVENT ATOMS            : 204                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.03000                                              
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : -0.02000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.082         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.078         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.049         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.731         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2675 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2531 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3642 ; 1.352 ; 1.999       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5824 ; 0.827 ; 3.006       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   327 ; 5.813 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   117 ;35.685 ;23.846       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   446 ;10.940 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;13.252 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   402 ; 0.079 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2990 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   610 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1281 ; 0.444 ; 1.059       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1280 ; 0.444 ; 1.057       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1605 ; 0.751 ; 1.585       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1606 ; 0.751 ; 1.587       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1394 ; 0.652 ; 1.144       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1394 ; 0.651 ; 1.144       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2034 ; 1.029 ; 1.687       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3251 ; 3.765 ; 9.477       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3252 ; 3.765 ; 9.483       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     6        A   700                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.1569  -4.9153 -10.8776              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0047 T22:   0.0038                                     
REMARK   3      T33:   0.0231 T12:   0.0021                                     
REMARK   3      T13:  -0.0046 T23:   0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8570 L22:   0.5819                                     
REMARK   3      L33:   1.5580 L12:   0.0024                                     
REMARK   3      L13:  -0.1167 L23:  -0.4196                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0032 S12:   0.0417 S13:   0.1222                       
REMARK   3      S21:  -0.0231 S22:  -0.0313 S23:   0.0334                       
REMARK   3      S31:  -0.0524 S32:   0.0051 S33:   0.0280                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4WRH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000204384.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.826534                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45804                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 95.570                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.68200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3UWE                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM SODIUM ACETATE, 20% PEG 3350      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   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       28.25450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       47.78350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.75150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       47.78350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.25450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       31.75150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     GLU A   322                                                      
REMARK 465     TYR A   323                                                      
REMARK 465     LEU A   324                                                      
REMARK 465     GLU A   325                                                      
REMARK 465     HIS A   326                                                      
REMARK 465     HIS A   327                                                      
REMARK 465     HIS A   328                                                      
REMARK 465     HIS A   329                                                      
REMARK 465     HIS A   330                                                      
REMARK 465     HIS A   331                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  31    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  33    CE   NZ                                             
REMARK 470     GLU A  36    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  75    CE   NZ                                             
REMARK 470     ASN A 101    CG   OD1  ND2                                       
REMARK 470     LYS A 104    CG   CD   CE   NZ                                   
REMARK 470     GLU A 126    CD   OE1  OE2                                       
REMARK 470     SER A 129    OG                                                  
REMARK 470     GLU A 133    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 171    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 201    CD   CE   NZ                                        
REMARK 470     LYS A 225    CG   CD   CE   NZ                                   
REMARK 470     GLN A 275    OE1  NE2                                            
REMARK 470     ASN A 302    OD1  ND2                                            
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   OH   TYR A    55     NAC  YY1 A   403              2.15            
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    SER A  51     -165.62   -128.62                                   
REMARK 500    GLU A 126     -131.60   -133.48                                   
REMARK 500    PHE A 197       75.61   -156.71                                   
REMARK 500    SER A 221      168.58     75.64                                   
REMARK 500    ARG A 250     -149.27   -126.88                                   
REMARK 500    ARG A 301       29.87   -148.12                                   
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 NAP A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue YY2 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue YY1 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405                 
DBREF  4WRH A    1   323  UNP    P42330   AK1C3_HUMAN      1    323             
SEQADV 4WRH LEU A  324  UNP  P42330              EXPRESSION TAG                 
SEQADV 4WRH GLU A  325  UNP  P42330              EXPRESSION TAG                 
SEQADV 4WRH HIS A  326  UNP  P42330              EXPRESSION TAG                 
SEQADV 4WRH HIS A  327  UNP  P42330              EXPRESSION TAG                 
SEQADV 4WRH HIS A  328  UNP  P42330              EXPRESSION TAG                 
SEQADV 4WRH HIS A  329  UNP  P42330              EXPRESSION TAG                 
SEQADV 4WRH HIS A  330  UNP  P42330              EXPRESSION TAG                 
SEQADV 4WRH HIS A  331  UNP  P42330              EXPRESSION TAG                 
SEQRES   1 A  331  MET ASP SER LYS HIS GLN CYS VAL LYS LEU ASN ASP GLY          
SEQRES   2 A  331  HIS PHE MET PRO VAL LEU GLY PHE GLY THR TYR ALA PRO          
SEQRES   3 A  331  PRO GLU VAL PRO ARG SER LYS ALA LEU GLU VAL THR LYS          
SEQRES   4 A  331  LEU ALA ILE GLU ALA GLY PHE ARG HIS ILE ASP SER ALA          
SEQRES   5 A  331  HIS LEU TYR ASN ASN GLU GLU GLN VAL GLY LEU ALA ILE          
SEQRES   6 A  331  ARG SER LYS ILE ALA ASP GLY SER VAL LYS ARG GLU ASP          
SEQRES   7 A  331  ILE PHE TYR THR SER LYS LEU TRP SER THR PHE HIS ARG          
SEQRES   8 A  331  PRO GLU LEU VAL ARG PRO ALA LEU GLU ASN SER LEU LYS          
SEQRES   9 A  331  LYS ALA GLN LEU ASP TYR VAL ASP LEU TYR LEU ILE HIS          
SEQRES  10 A  331  SER PRO MET SER LEU LYS PRO GLY GLU GLU LEU SER PRO          
SEQRES  11 A  331  THR ASP GLU ASN GLY LYS VAL ILE PHE ASP ILE VAL ASP          
SEQRES  12 A  331  LEU CYS THR THR TRP GLU ALA MET GLU LYS CYS LYS ASP          
SEQRES  13 A  331  ALA GLY LEU ALA LYS SER ILE GLY VAL SER ASN PHE ASN          
SEQRES  14 A  331  ARG ARG GLN LEU GLU MET ILE LEU ASN LYS PRO GLY LEU          
SEQRES  15 A  331  LYS TYR LYS PRO VAL CYS ASN GLN VAL GLU CYS HIS PRO          
SEQRES  16 A  331  TYR PHE ASN ARG SER LYS LEU LEU ASP PHE CYS LYS SER          
SEQRES  17 A  331  LYS ASP ILE VAL LEU VAL ALA TYR SER ALA LEU GLY SER          
SEQRES  18 A  331  GLN ARG ASP LYS ARG TRP VAL ASP PRO ASN SER PRO VAL          
SEQRES  19 A  331  LEU LEU GLU ASP PRO VAL LEU CYS ALA LEU ALA LYS LYS          
SEQRES  20 A  331  HIS LYS ARG THR PRO ALA LEU ILE ALA LEU ARG TYR GLN          
SEQRES  21 A  331  LEU GLN ARG GLY VAL VAL VAL LEU ALA LYS SER TYR ASN          
SEQRES  22 A  331  GLU GLN ARG ILE ARG GLN ASN VAL GLN VAL PHE GLU PHE          
SEQRES  23 A  331  GLN LEU THR ALA GLU ASP MET LYS ALA ILE ASP GLY LEU          
SEQRES  24 A  331  ASP ARG ASN LEU HIS TYR PHE ASN SER ASP SER PHE ALA          
SEQRES  25 A  331  SER HIS PRO ASN TYR PRO TYR SER ASP GLU TYR LEU GLU          
SEQRES  26 A  331  HIS HIS HIS HIS HIS HIS                                      
HET    NAP  A 401      48                                                       
HET    YY2  A 402      20                                                       
HET    YY1  A 403       7                                                       
HET    EDO  A 404       4                                                       
HET    EDO  A 405       4                                                       
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETNAM     YY2 2-[4-(AMINOMETHYL)-2-CHLORO-6-METHOXYPHENOXY]-N-TERT-            
HETNAM   2 YY2  BUTYLACETAMIDE                                                  
HETNAM     YY1 5-METHYL-4H-1,2,4-TRIAZOLE-3-THIOL                               
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  NAP    C21 H28 N7 O17 P3                                            
FORMUL   3  YY2    C14 H21 CL N2 O3                                             
FORMUL   4  YY1    C3 H5 N3 S                                                   
FORMUL   5  EDO    2(C2 H6 O2)                                                  
FORMUL   7  HOH   *204(H2 O)                                                    
HELIX    1 AA1 ARG A   31  GLY A   45  1                                  15    
HELIX    2 AA2 ALA A   52  ASN A   56  5                                   5    
HELIX    3 AA3 ASN A   57  ASP A   71  1                                  15    
HELIX    4 AA4 LYS A   75  ILE A   79  5                                   5    
HELIX    5 AA5 TRP A   86  HIS A   90  5                                   5    
HELIX    6 AA6 ARG A   91  GLU A   93  5                                   3    
HELIX    7 AA7 LEU A   94  GLN A  107  1                                  14    
HELIX    8 AA8 ASP A  143  ALA A  157  1                                  15    
HELIX    9 AA9 ASN A  169  ASN A  178  1                                  10    
HELIX   10 AB1 ARG A  199  LYS A  209  1                                  11    
HELIX   11 AB2 VAL A  234  GLU A  237  5                                   4    
HELIX   12 AB3 ASP A  238  LYS A  249  1                                  12    
HELIX   13 AB4 THR A  251  ARG A  263  1                                  13    
HELIX   14 AB5 ASN A  273  VAL A  281  1                                   9    
HELIX   15 AB6 GLN A  282  PHE A  286  5                                   5    
HELIX   16 AB7 THR A  289  GLY A  298  1                                  10    
HELIX   17 AB8 SER A  308  SER A  313  1                                   6    
HELIX   18 AB9 TYR A  317  ASP A  321  5                                   5    
SHEET    1 AA1 2 CYS A   7  LYS A   9  0                                        
SHEET    2 AA1 2 PHE A  15  PRO A  17 -1  O  MET A  16   N  VAL A   8           
SHEET    1 AA2 9 LEU A  19  GLY A  22  0                                        
SHEET    2 AA2 9 HIS A  48  ASP A  50  1  O  HIS A  48   N  PHE A  21           
SHEET    3 AA2 9 PHE A  80  LEU A  85  1  O  PHE A  80   N  ILE A  49           
SHEET    4 AA2 9 VAL A 111  ILE A 116  1  O  LEU A 115   N  LEU A  85           
SHEET    5 AA2 9 ALA A 160  SER A 166  1  O  LYS A 161   N  VAL A 111           
SHEET    6 AA2 9 CYS A 188  GLU A 192  1  O  CYS A 188   N  VAL A 165           
SHEET    7 AA2 9 VAL A 212  TYR A 216  1  O  VAL A 214   N  VAL A 191           
SHEET    8 AA2 9 VAL A 266  LYS A 270  1  O  VAL A 266   N  ALA A 215           
SHEET    9 AA2 9 LEU A  19  GLY A  22  1  N  GLY A  20   O  VAL A 267           
SITE     1 AC1 34 GLY A  22  THR A  23  TYR A  24  ASP A  50                    
SITE     2 AC1 34 TYR A  55  HIS A 117  SER A 166  ASN A 167                    
SITE     3 AC1 34 GLN A 190  TYR A 216  SER A 217  ALA A 218                    
SITE     4 AC1 34 LEU A 219  GLY A 220  SER A 221  GLN A 222                    
SITE     5 AC1 34 LEU A 236  ALA A 253  LEU A 268  ALA A 269                    
SITE     6 AC1 34 LYS A 270  SER A 271  TYR A 272  ARG A 276                    
SITE     7 AC1 34 GLN A 279  ASN A 280  YY1 A 403  HOH A 563                    
SITE     8 AC1 34 HOH A 569  HOH A 597  HOH A 625  HOH A 631                    
SITE     9 AC1 34 HOH A 668  HOH A 678                                          
SITE     1 AC2 10 TRP A  86  SER A 118  SER A 129  ASN A 167                    
SITE     2 AC2 10 TYR A 216  PHE A 306  PHE A 311  PRO A 318                    
SITE     3 AC2 10 YY1 A 403  HOH A 627                                          
SITE     1 AC3  7 TYR A  24  LEU A  54  TYR A  55  HIS A 117                    
SITE     2 AC3  7 NAP A 401  YY2 A 402  HOH A 597                               
SITE     1 AC4  9 GLN A   6  PRO A  17  VAL A  18  LEU A  19                    
SITE     2 AC4  9 GLY A  45  PHE A  46  ARG A  47  HIS A  48                    
SITE     3 AC4  9 PHE A 284                                                     
SITE     1 AC5  5 PHE A 197  ARG A 199  HOH A 576  HOH A 580                    
SITE     2 AC5  5 HOH A 671                                                     
CRYST1   56.509   63.503   95.567  90.00  90.00  90.00 P 21 21 21    4          
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      0.017696  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015747  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010464        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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