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Database: PDB
Entry: 4ZFC
LinkDB: 4ZFC
Original site: 4ZFC 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 21-APR-15   4ZFC              
TITLE     CRYSTAL STRUCTURE OF AKR1C3 COMPLEXED WITH GLICAZIDE                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALDO-KETO REDUCTASE FAMILY 1 MEMBER C3;                    
COMPND   3 CHAIN: A, B;                                                         
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: 1.1.1.357,1.1.1.112,1.1.1.188,1.1.1.239,1.1.1.64,1.3.1.20;       
COMPND  11 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;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    AKR1C3 INHIBITOR, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZHAO,X.ZHRNG,X.HU                                                   
REVDAT   1   25-NOV-15 4ZFC    0                                                
JRNL        AUTH   Y.ZHAO,X.ZHENG,H.ZHANG,J.ZHAI,L.ZHANG,C.LI,K.ZENG,Y.CHEN,    
JRNL        AUTH 2 Q.LI,X.HU                                                    
JRNL        TITL   IN VITRO INHIBITION OF AKR1CS BY SULPHONYLUREAS AND THE      
JRNL        TITL 2 STRUCTURAL BASIS                                             
JRNL        REF    CHEM.BIOL.INTERACT.           V. 240   310 2015              
JRNL        REFN                   ISSN 0009-2797                               
JRNL        PMID   26362498                                                     
JRNL        DOI    10.1016/J.CBI.2015.09.006                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 80.37                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 43707                          
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) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2326                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3244                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.94                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2490                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 185                          
REMARK   3   BIN FREE R VALUE                    : 0.2890                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5089                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 140                                     
REMARK   3   SOLVENT ATOMS            : 367                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.48000                                              
REMARK   3    B22 (A**2) : -0.69000                                             
REMARK   3    B33 (A**2) : -0.86000                                             
REMARK   3    B12 (A**2) : 0.12000                                              
REMARK   3    B13 (A**2) : -1.75000                                             
REMARK   3    B23 (A**2) : 0.49000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.180         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.158         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.118         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.401         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5358 ; 0.018 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5108 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7273 ; 1.938 ; 1.990       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11784 ; 0.899 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   633 ; 6.139 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   244 ;37.847 ;24.057       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   930 ;13.621 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    34 ;12.818 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   791 ; 0.107 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6015 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1231 ; 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):  2538 ; 1.874 ; 1.997       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2537 ; 1.872 ; 1.995       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3169 ; 2.831 ; 2.984       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3170 ; 2.831 ; 2.986       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2820 ; 2.753 ; 2.326       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2821 ; 2.753 ; 2.327       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4105 ; 4.386 ; 3.355       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  6335 ; 6.056 ;16.836       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  6245 ; 5.923 ;16.689       
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  : NULL                                       
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 4ZFC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000209153.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-DEC-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : SEALED TUBE                        
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : OXFORD DIFFRACTION ENHANCE ULTRA   
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : OXFORD ONYX CCD                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.21                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46034                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 80.368                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.51600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15%-20% PEG8000, 100MM MES, 0.14M        
REMARK 280  NACL, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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 TOTAL BURIED SURFACE AREA: 1210 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL                         
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 TOTAL BURIED SURFACE AREA: 1200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
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 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     ASP A   321                                                      
REMARK 465     GLU A   322                                                      
REMARK 465     TYR A   323                                                      
REMARK 465     ASP B   321                                                      
REMARK 465     GLU B   322                                                      
REMARK 465     TYR B   323                                                      
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   O    HOH B   669     O    HOH B   680              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  66   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ASP A  71   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  57        1.26   -151.85                                   
REMARK 500    ALA A 157        1.69    -67.38                                   
REMARK 500    PHE A 197       73.74   -166.92                                   
REMARK 500    SER A 221      172.91     73.28                                   
REMARK 500    ARG A 250     -149.99   -136.39                                   
REMARK 500    GLN A 282        1.20    -67.47                                   
REMARK 500    ASN B  57       10.29   -143.92                                   
REMARK 500    LEU B 182      123.87    -38.12                                   
REMARK 500    PHE B 197       80.29   -157.18                                   
REMARK 500    SER B 221      166.79     81.97                                   
REMARK 500    ARG B 250     -151.29   -121.99                                   
REMARK 500    ARG B 301       27.03   -141.33                                   
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 GCZ A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAP B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GCZ B 402                 
DBREF  4ZFC A    1   323  UNP    P42330   AK1C3_HUMAN      1    323             
DBREF  4ZFC B    1   323  UNP    P42330   AK1C3_HUMAN      1    323             
SEQRES   1 A  323  MET ASP SER LYS HIS GLN CYS VAL LYS LEU ASN ASP GLY          
SEQRES   2 A  323  HIS PHE MET PRO VAL LEU GLY PHE GLY THR TYR ALA PRO          
SEQRES   3 A  323  PRO GLU VAL PRO ARG SER LYS ALA LEU GLU VAL THR LYS          
SEQRES   4 A  323  LEU ALA ILE GLU ALA GLY PHE ARG HIS ILE ASP SER ALA          
SEQRES   5 A  323  HIS LEU TYR ASN ASN GLU GLU GLN VAL GLY LEU ALA ILE          
SEQRES   6 A  323  ARG SER LYS ILE ALA ASP GLY SER VAL LYS ARG GLU ASP          
SEQRES   7 A  323  ILE PHE TYR THR SER LYS LEU TRP SER THR PHE HIS ARG          
SEQRES   8 A  323  PRO GLU LEU VAL ARG PRO ALA LEU GLU ASN SER LEU LYS          
SEQRES   9 A  323  LYS ALA GLN LEU ASP TYR VAL ASP LEU TYR LEU ILE HIS          
SEQRES  10 A  323  SER PRO MET SER LEU LYS PRO GLY GLU GLU LEU SER PRO          
SEQRES  11 A  323  THR ASP GLU ASN GLY LYS VAL ILE PHE ASP ILE VAL ASP          
SEQRES  12 A  323  LEU CYS THR THR TRP GLU ALA MET GLU LYS CYS LYS ASP          
SEQRES  13 A  323  ALA GLY LEU ALA LYS SER ILE GLY VAL SER ASN PHE ASN          
SEQRES  14 A  323  ARG ARG GLN LEU GLU MET ILE LEU ASN LYS PRO GLY LEU          
SEQRES  15 A  323  LYS TYR LYS PRO VAL CYS ASN GLN VAL GLU CYS HIS PRO          
SEQRES  16 A  323  TYR PHE ASN ARG SER LYS LEU LEU ASP PHE CYS LYS SER          
SEQRES  17 A  323  LYS ASP ILE VAL LEU VAL ALA TYR SER ALA LEU GLY SER          
SEQRES  18 A  323  GLN ARG ASP LYS ARG TRP VAL ASP PRO ASN SER PRO VAL          
SEQRES  19 A  323  LEU LEU GLU ASP PRO VAL LEU CYS ALA LEU ALA LYS LYS          
SEQRES  20 A  323  HIS LYS ARG THR PRO ALA LEU ILE ALA LEU ARG TYR GLN          
SEQRES  21 A  323  LEU GLN ARG GLY VAL VAL VAL LEU ALA LYS SER TYR ASN          
SEQRES  22 A  323  GLU GLN ARG ILE ARG GLN ASN VAL GLN VAL PHE GLU PHE          
SEQRES  23 A  323  GLN LEU THR ALA GLU ASP MET LYS ALA ILE ASP GLY LEU          
SEQRES  24 A  323  ASP ARG ASN LEU HIS TYR PHE ASN SER ASP SER PHE ALA          
SEQRES  25 A  323  SER HIS PRO ASN TYR PRO TYR SER ASP GLU TYR                  
SEQRES   1 B  323  MET ASP SER LYS HIS GLN CYS VAL LYS LEU ASN ASP GLY          
SEQRES   2 B  323  HIS PHE MET PRO VAL LEU GLY PHE GLY THR TYR ALA PRO          
SEQRES   3 B  323  PRO GLU VAL PRO ARG SER LYS ALA LEU GLU VAL THR LYS          
SEQRES   4 B  323  LEU ALA ILE GLU ALA GLY PHE ARG HIS ILE ASP SER ALA          
SEQRES   5 B  323  HIS LEU TYR ASN ASN GLU GLU GLN VAL GLY LEU ALA ILE          
SEQRES   6 B  323  ARG SER LYS ILE ALA ASP GLY SER VAL LYS ARG GLU ASP          
SEQRES   7 B  323  ILE PHE TYR THR SER LYS LEU TRP SER THR PHE HIS ARG          
SEQRES   8 B  323  PRO GLU LEU VAL ARG PRO ALA LEU GLU ASN SER LEU LYS          
SEQRES   9 B  323  LYS ALA GLN LEU ASP TYR VAL ASP LEU TYR LEU ILE HIS          
SEQRES  10 B  323  SER PRO MET SER LEU LYS PRO GLY GLU GLU LEU SER PRO          
SEQRES  11 B  323  THR ASP GLU ASN GLY LYS VAL ILE PHE ASP ILE VAL ASP          
SEQRES  12 B  323  LEU CYS THR THR TRP GLU ALA MET GLU LYS CYS LYS ASP          
SEQRES  13 B  323  ALA GLY LEU ALA LYS SER ILE GLY VAL SER ASN PHE ASN          
SEQRES  14 B  323  ARG ARG GLN LEU GLU MET ILE LEU ASN LYS PRO GLY LEU          
SEQRES  15 B  323  LYS TYR LYS PRO VAL CYS ASN GLN VAL GLU CYS HIS PRO          
SEQRES  16 B  323  TYR PHE ASN ARG SER LYS LEU LEU ASP PHE CYS LYS SER          
SEQRES  17 B  323  LYS ASP ILE VAL LEU VAL ALA TYR SER ALA LEU GLY SER          
SEQRES  18 B  323  GLN ARG ASP LYS ARG TRP VAL ASP PRO ASN SER PRO VAL          
SEQRES  19 B  323  LEU LEU GLU ASP PRO VAL LEU CYS ALA LEU ALA LYS LYS          
SEQRES  20 B  323  HIS LYS ARG THR PRO ALA LEU ILE ALA LEU ARG TYR GLN          
SEQRES  21 B  323  LEU GLN ARG GLY VAL VAL VAL LEU ALA LYS SER TYR ASN          
SEQRES  22 B  323  GLU GLN ARG ILE ARG GLN ASN VAL GLN VAL PHE GLU PHE          
SEQRES  23 B  323  GLN LEU THR ALA GLU ASP MET LYS ALA ILE ASP GLY LEU          
SEQRES  24 B  323  ASP ARG ASN LEU HIS TYR PHE ASN SER ASP SER PHE ALA          
SEQRES  25 B  323  SER HIS PRO ASN TYR PRO TYR SER ASP GLU TYR                  
HET    NAP  A 401      48                                                       
HET    GCZ  A 402      22                                                       
HET    NAP  B 401      48                                                       
HET    GCZ  B 402      22                                                       
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETNAM     GCZ N-[(3AR,6AS)-HEXAHYDROCYCLOPENTA[C]PYRROL-2(1H)-                 
HETNAM   2 GCZ  YLCARBAMOYL]-4-METHYLBENZENESULFONAMIDE                         
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
HETSYN     GCZ GLICLAZIDE                                                       
FORMUL   3  NAP    2(C21 H28 N7 O17 P3)                                         
FORMUL   4  GCZ    2(C15 H21 N3 O3 S)                                           
FORMUL   7  HOH   *367(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  GLN A  282  1                                  10    
HELIX   15 AB6 VAL A  283  PHE A  286  5                                   4    
HELIX   16 AB7 THR A  289  GLY A  298  1                                  10    
HELIX   17 AB8 SER A  308  HIS A  314  1                                   7    
HELIX   18 AB9 ARG B   31  GLY B   45  1                                  15    
HELIX   19 AC1 ALA B   52  ASN B   56  5                                   5    
HELIX   20 AC2 ASN B   57  ASP B   71  1                                  15    
HELIX   21 AC3 LYS B   75  ILE B   79  5                                   5    
HELIX   22 AC4 TRP B   86  HIS B   90  5                                   5    
HELIX   23 AC5 ARG B   91  GLN B  107  1                                  17    
HELIX   24 AC6 ASP B  143  ALA B  157  1                                  15    
HELIX   25 AC7 ASN B  169  ASN B  178  1                                  10    
HELIX   26 AC8 ARG B  199  LYS B  209  1                                  11    
HELIX   27 AC9 VAL B  234  GLU B  237  5                                   4    
HELIX   28 AD1 ASP B  238  LYS B  249  1                                  12    
HELIX   29 AD2 THR B  251  ARG B  263  1                                  13    
HELIX   30 AD3 ASN B  273  VAL B  281  1                                   9    
HELIX   31 AD4 GLN B  282  PHE B  286  5                                   5    
HELIX   32 AD5 THR B  289  GLY B  298  1                                  10    
HELIX   33 AD6 SER B  308  SER B  313  1                                   6    
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  ASP A  50   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  TYR A 216   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           
SHEET    1 AA3 2 CYS B   7  LYS B   9  0                                        
SHEET    2 AA3 2 PHE B  15  PRO B  17 -1  O  MET B  16   N  VAL B   8           
SHEET    1 AA4 9 LEU B  19  GLY B  22  0                                        
SHEET    2 AA4 9 HIS B  48  ASP B  50  1  O  HIS B  48   N  PHE B  21           
SHEET    3 AA4 9 PHE B  80  LEU B  85  1  O  PHE B  80   N  ILE B  49           
SHEET    4 AA4 9 VAL B 111  ILE B 116  1  O  LEU B 115   N  LEU B  85           
SHEET    5 AA4 9 ALA B 160  SER B 166  1  O  GLY B 164   N  TYR B 114           
SHEET    6 AA4 9 CYS B 188  GLU B 192  1  O  CYS B 188   N  VAL B 165           
SHEET    7 AA4 9 VAL B 212  TYR B 216  1  O  VAL B 214   N  VAL B 191           
SHEET    8 AA4 9 VAL B 266  LYS B 270  1  O  VAL B 266   N  ALA B 215           
SHEET    9 AA4 9 LEU B  19  GLY B  22  1  N  GLY B  20   O  VAL B 267           
SITE     1 AC1 31 GLY A  22  THR A  23  TYR A  24  ASP A  50                    
SITE     2 AC1 31 TYR A  55  LYS A  84  HIS A 117  SER A 166                    
SITE     3 AC1 31 ASN A 167  GLN A 190  TYR A 216  SER A 217                    
SITE     4 AC1 31 ALA A 218  LEU A 219  GLY A 220  SER A 221                    
SITE     5 AC1 31 GLN A 222  ALA A 253  LEU A 268  ALA A 269                    
SITE     6 AC1 31 LYS A 270  SER A 271  TYR A 272  ARG A 276                    
SITE     7 AC1 31 GLN A 279  ASN A 280  GCZ A 402  HOH A 518                    
SITE     8 AC1 31 HOH A 542  HOH A 576  HOH A 620                               
SITE     1 AC2 10 TYR A  24  LEU A  54  TYR A  55  HIS A 117                    
SITE     2 AC2 10 MET A 120  ASN A 167  TRP A 227  PHE A 306                    
SITE     3 AC2 10 NAP A 401  HOH A 533                                          
SITE     1 AC3 33 GLY B  22  THR B  23  TYR B  24  ASP B  50                    
SITE     2 AC3 33 TYR B  55  LYS B  84  HIS B 117  SER B 166                    
SITE     3 AC3 33 ASN B 167  GLN B 190  TYR B 216  SER B 217                    
SITE     4 AC3 33 ALA B 218  LEU B 219  GLY B 220  SER B 221                    
SITE     5 AC3 33 GLN B 222  ALA B 253  LEU B 268  ALA B 269                    
SITE     6 AC3 33 LYS B 270  SER B 271  TYR B 272  ARG B 276                    
SITE     7 AC3 33 GLN B 279  ASN B 280  GCZ B 402  HOH B 513                    
SITE     8 AC3 33 HOH B 518  HOH B 532  HOH B 551  HOH B 581                    
SITE     9 AC3 33 HOH B 637                                                     
SITE     1 AC4  9 TYR B  24  LEU B  54  TYR B  55  HIS B 117                    
SITE     2 AC4  9 ASN B 167  TRP B 227  PHE B 306  NAP B 401                    
SITE     3 AC4  9 HOH B 526                                                     
CRYST1   47.652   49.156   83.476  74.52  86.84  69.09 P 1           2          
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      0.020986 -0.008018  0.001001        0.00000                         
SCALE2      0.000000  0.021778 -0.005986        0.00000                         
SCALE3      0.000000  0.000000  0.012443        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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