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Database: PDB
Entry: 4FAM
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HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 22-MAY-12   4FAM              
TITLE     CRYSTAL STRUCTURE OF HUMAN 17BETA-HYDROXYSTEROID DEHYDROGENASE TYPE 5 
TITLE    2 IN COMPLEX WITH 3-((3,4-DIHYDROISOQUINOLIN-2(1H)-YL)SULFONYL)BENZOIC 
TITLE    3 ACID (17)                                                            
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, 
COMPND   5 3-ALPHA-HSD TYPE II, BRAIN, 3-ALPHA-HYDROXYSTEROID DEHYDROGENASE TYPE
COMPND   6 2, 3-ALPHA-HSD TYPE 2, CHLORDECONE REDUCTASE HOMOLOG HAKRB,          
COMPND   7 DIHYDRODIOL DEHYDROGENASE 3, DD-3, DD3, DIHYDRODIOL DEHYDROGENASE    
COMPND   8 TYPE I, HA1753, INDANOL DEHYDROGENASE, PROSTAGLANDIN F SYNTHASE,     
COMPND   9 PGFS, TESTOSTERONE 17-BETA-DEHYDROGENASE 5, TRANS-1,2-DIHYDROBENZENE-
COMPND  10 1,2-DIOL DEHYDROGENASE;                                              
COMPND  11 EC: 1.-.-.-, 1.1.1.213, 1.1.1.112, 1.1.1.188, 1.1.1.63, 1.1.1.64,    
COMPND  12 1.3.1.20;                                                            
COMPND  13 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_STRAIN: BL21 DE3;                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21A                                    
KEYWDS    ALDO-KETO REDUCTASE, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.P.TURNBULL,S.M.F.JAMIESON,D.G.BROOKE,D.HEINRICH,G.J.ATWELL,S.SILVA, 
AUTHOR   2 E.J.HAMILTON,L.J.M.RIGOREAU,E.TRIVIER,C.SOUDY,S.S.SAMLAL,P.J.OWEN,   
AUTHOR   3 E.SCHROEDER,T.RAYNHAM,J.U.FLANAGAN,W.A.DENNY                         
REVDAT   1   10-OCT-12 4FAM    0                                                
JRNL        AUTH   S.M.JAMIESON,D.G.BROOKE,D.HEINRICH,G.J.ATWELL,S.SILVA,       
JRNL        AUTH 2 E.J.HAMILTON,A.P.TURNBULL,L.J.RIGOREAU,E.TRIVIER,C.SOUDY,    
JRNL        AUTH 3 S.S.SAMLAL,P.J.OWEN,E.SCHROEDER,T.RAYNHAM,J.U.FLANAGAN,      
JRNL        AUTH 4 W.A.DENNY                                                    
JRNL        TITL   3-(3,4-DIHYDROISOQUINOLIN-2(1H)-YLSULFONYL)BENZOIC ACIDS; A  
JRNL        TITL 2 NEW CLASS OF HIGHLY POTENT AND SELECTIVE INHIBITORS OF THE   
JRNL        TITL 3 TYPE 5 17-BETA-HYDROXYSTEROID DEHYDROGENASE AKR1C3           
JRNL        REF    J.MED.CHEM.                   V.  55  7746 2012              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   22877157                                                     
JRNL        DOI    10.1021/JM3007867                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 20.03                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 47140                          
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) : 0.170                           
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
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      : 2524                            
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) : 3194                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.71                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2510                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 169                          
REMARK   3   BIN FREE R VALUE                    : 0.2940                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4972                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 176                                     
REMARK   3   SOLVENT ATOMS            : 571                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.52                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.60000                                             
REMARK   3    B22 (A**2) : 1.32000                                              
REMARK   3    B33 (A**2) : -0.67000                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.12000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.167         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.155         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.095         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.400         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.931                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5283 ; 0.020 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  3623 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7175 ; 2.030 ; 2.004       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8761 ; 1.048 ; 3.006       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   632 ; 6.573 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   232 ;37.716 ;23.966       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   874 ;13.475 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    32 ;14.812 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   793 ; 0.271 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5763 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1057 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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 4FAM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAY-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB072663.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54182                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : VARIMAX HF OPTICS                  
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944+                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : STRUCTURESTUDIO                    
REMARK 200  DATA SCALING SOFTWARE          : STRUCTURESTUDIO                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49665                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.030                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 2.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2FGB                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M POTASSIUM THIOCYANATE, 20 % (W/    
REMARK 280  V) PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       53.38200            
REMARK 290   SMTRY3   2  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 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     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 465     MET B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     LYS B     4                                                      
REMARK 465     HIS B     5                                                      
REMARK 465     SER B   320                                                      
REMARK 465     ASP B   321                                                      
REMARK 465     GLU B   322                                                      
REMARK 465     TYR B   323                                                      
REMARK 465     LEU B   324                                                      
REMARK 465     GLU B   325                                                      
REMARK 465     HIS B   326                                                      
REMARK 465     HIS B   327                                                      
REMARK 465     HIS B   328                                                      
REMARK 465     HIS B   329                                                      
REMARK 465     HIS B   330                                                      
REMARK 465     HIS B   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     GLU A  59    CD   OE1  OE2                                       
REMARK 470     LYS A 104    CE   NZ                                             
REMARK 470     GLU A 127    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 133    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 134    CG   OD1  ND2                                       
REMARK 470     LYS A 136    CG   CD   CE   NZ                                   
REMARK 470     ARG A 171    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 201    CD   CE   NZ                                        
REMARK 470     LYS A 246    CD   CE   NZ                                        
REMARK 470     LYS A 294    CD   CE   NZ                                        
REMARK 470     LYS B 104    CE   NZ                                             
REMARK 470     LYS B 123    CE   NZ                                             
REMARK 470     GLU B 126    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 127    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 133    CD   OE1  OE2                                       
REMARK 470     LYS B 136    CG   CD   CE   NZ                                   
REMARK 470     ARG B 171    CZ   NH1  NH2                                       
REMARK 470     LYS B 201    CD   CE   NZ                                        
REMARK 470     LYS B 225    CD   CE   NZ                                        
REMARK 470     LYS B 246    CD   CE   NZ                                        
REMARK 470     LYS B 249    CE   NZ                                             
REMARK 470     GLU B 291    CG   CD   OE1  OE2                                  
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 A   736     O    HOH A   740              1.51            
REMARK 500   O    HOH B  1027     O    HOH B  1063              1.71            
REMARK 500   O    HOH B   895     O    HOH B  1058              1.76            
REMARK 500   NE2  GLN B   275     O    HOH B  1027              1.85            
REMARK 500   O    HOH B   817     O    HOH B   963              1.96            
REMARK 500   O    HOH B  1015     O    HOH B  1077              1.98            
REMARK 500   O    HOH B   911     O    HOH B  1055              2.02            
REMARK 500   O    HOH A   532     O    HOH A   752              2.07            
REMARK 500   O    HOH B   819     O    HOH B   951              2.09            
REMARK 500   CB   ASN A   134     O    HOH A   699              2.13            
REMARK 500   O    HOH A   514     O    HOH A   744              2.19            
REMARK 500   O    HOH B   801     O    HOH B   966              2.19            
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   O    HOH B   974     O    HOH B  1062     1455     1.65            
REMARK 500   O    HOH B   931     O    HOH B  1063     1455     1.80            
REMARK 500   O    HOH B   967     O    HOH B  1058     1655     1.84            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A  90   CG    HIS A  90   CD2     0.060                       
REMARK 500    HIS A 304   CG    HIS A 304   CD2     0.065                       
REMARK 500    HIS B  53   CG    HIS B  53   CD2     0.064                       
REMARK 500    HIS B 314   CG    HIS B 314   CD2     0.062                       
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    LEU A  63   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    ARG A 199   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG A 301   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG B 263   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG B 263   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 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       14.20   -140.30                                   
REMARK 500    GLU A 133      -72.30    -26.02                                   
REMARK 500    ASN A 134     -165.34    -64.76                                   
REMARK 500    PHE A 197       73.71   -152.33                                   
REMARK 500    SER A 221      165.98     80.07                                   
REMARK 500    ARG A 250     -152.97   -126.12                                   
REMARK 500    ARG A 301       28.08   -148.99                                   
REMARK 500    PHE B 197       68.31   -155.92                                   
REMARK 500    SER B 221      169.98     82.74                                   
REMARK 500    ARG B 250     -144.36   -120.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 TYR A  319     SER A  320                  146.23                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN B 198        24.1      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 844        DISTANCE =  5.89 ANGSTROMS                       
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 0SZ A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO 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                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0SZ B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 705                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4FA3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FAL   RELATED DB: PDB                                   
DBREF  4FAM A    1   323  UNP    P42330   AK1C3_HUMAN      1    323             
DBREF  4FAM B    1   323  UNP    P42330   AK1C3_HUMAN      1    323             
SEQADV 4FAM LEU A  324  UNP  P42330              EXPRESSION TAG                 
SEQADV 4FAM GLU A  325  UNP  P42330              EXPRESSION TAG                 
SEQADV 4FAM HIS A  326  UNP  P42330              EXPRESSION TAG                 
SEQADV 4FAM HIS A  327  UNP  P42330              EXPRESSION TAG                 
SEQADV 4FAM HIS A  328  UNP  P42330              EXPRESSION TAG                 
SEQADV 4FAM HIS A  329  UNP  P42330              EXPRESSION TAG                 
SEQADV 4FAM HIS A  330  UNP  P42330              EXPRESSION TAG                 
SEQADV 4FAM HIS A  331  UNP  P42330              EXPRESSION TAG                 
SEQADV 4FAM LEU B  324  UNP  P42330              EXPRESSION TAG                 
SEQADV 4FAM GLU B  325  UNP  P42330              EXPRESSION TAG                 
SEQADV 4FAM HIS B  326  UNP  P42330              EXPRESSION TAG                 
SEQADV 4FAM HIS B  327  UNP  P42330              EXPRESSION TAG                 
SEQADV 4FAM HIS B  328  UNP  P42330              EXPRESSION TAG                 
SEQADV 4FAM HIS B  329  UNP  P42330              EXPRESSION TAG                 
SEQADV 4FAM HIS B  330  UNP  P42330              EXPRESSION TAG                 
SEQADV 4FAM HIS B  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                                      
SEQRES   1 B  331  MET ASP SER LYS HIS GLN CYS VAL LYS LEU ASN ASP GLY          
SEQRES   2 B  331  HIS PHE MET PRO VAL LEU GLY PHE GLY THR TYR ALA PRO          
SEQRES   3 B  331  PRO GLU VAL PRO ARG SER LYS ALA LEU GLU VAL THR LYS          
SEQRES   4 B  331  LEU ALA ILE GLU ALA GLY PHE ARG HIS ILE ASP SER ALA          
SEQRES   5 B  331  HIS LEU TYR ASN ASN GLU GLU GLN VAL GLY LEU ALA ILE          
SEQRES   6 B  331  ARG SER LYS ILE ALA ASP GLY SER VAL LYS ARG GLU ASP          
SEQRES   7 B  331  ILE PHE TYR THR SER LYS LEU TRP SER THR PHE HIS ARG          
SEQRES   8 B  331  PRO GLU LEU VAL ARG PRO ALA LEU GLU ASN SER LEU LYS          
SEQRES   9 B  331  LYS ALA GLN LEU ASP TYR VAL ASP LEU TYR LEU ILE HIS          
SEQRES  10 B  331  SER PRO MET SER LEU LYS PRO GLY GLU GLU LEU SER PRO          
SEQRES  11 B  331  THR ASP GLU ASN GLY LYS VAL ILE PHE ASP ILE VAL ASP          
SEQRES  12 B  331  LEU CYS THR THR TRP GLU ALA MET GLU LYS CYS LYS ASP          
SEQRES  13 B  331  ALA GLY LEU ALA LYS SER ILE GLY VAL SER ASN PHE ASN          
SEQRES  14 B  331  ARG ARG GLN LEU GLU MET ILE LEU ASN LYS PRO GLY LEU          
SEQRES  15 B  331  LYS TYR LYS PRO VAL CYS ASN GLN VAL GLU CYS HIS PRO          
SEQRES  16 B  331  TYR PHE ASN ARG SER LYS LEU LEU ASP PHE CYS LYS SER          
SEQRES  17 B  331  LYS ASP ILE VAL LEU VAL ALA TYR SER ALA LEU GLY SER          
SEQRES  18 B  331  GLN ARG ASP LYS ARG TRP VAL ASP PRO ASN SER PRO VAL          
SEQRES  19 B  331  LEU LEU GLU ASP PRO VAL LEU CYS ALA LEU ALA LYS LYS          
SEQRES  20 B  331  HIS LYS ARG THR PRO ALA LEU ILE ALA LEU ARG TYR GLN          
SEQRES  21 B  331  LEU GLN ARG GLY VAL VAL VAL LEU ALA LYS SER TYR ASN          
SEQRES  22 B  331  GLU GLN ARG ILE ARG GLN ASN VAL GLN VAL PHE GLU PHE          
SEQRES  23 B  331  GLN LEU THR ALA GLU ASP MET LYS ALA ILE ASP GLY LEU          
SEQRES  24 B  331  ASP ARG ASN LEU HIS TYR PHE ASN SER ASP SER PHE ALA          
SEQRES  25 B  331  SER HIS PRO ASN TYR PRO TYR SER ASP GLU TYR LEU GLU          
SEQRES  26 B  331  HIS HIS HIS HIS HIS HIS                                      
HET    NAP  A 401      48                                                       
HET    0SZ  A 402      22                                                       
HET    EDO  A 403       4                                                       
HET    EDO  A 404       4                                                       
HET    EDO  A 405       4                                                       
HET    EDO  A 406       4                                                       
HET    EDO  A 407       4                                                       
HET    EDO  A 408       4                                                       
HET    NAP  B 701      48                                                       
HET    0SZ  B 702      22                                                       
HET    EDO  B 703       4                                                       
HET    EDO  B 704       4                                                       
HET    EDO  B 705       4                                                       
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETNAM     0SZ 3-(3,4-DIHYDROISOQUINOLIN-2(1H)-YLSULFONYL)BENZOIC ACID          
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  NAP    2(C21 H28 N7 O17 P3)                                         
FORMUL   4  0SZ    2(C16 H15 N O4 S)                                            
FORMUL   5  EDO    9(C2 H6 O2)                                                  
FORMUL  16  HOH   *571(H2 O)                                                    
HELIX    1   1 ARG A   31  GLY A   45  1                                  15    
HELIX    2   2 ALA A   52  ASN A   56  5                                   5    
HELIX    3   3 ASN A   57  ASP A   71  1                                  15    
HELIX    4   4 LYS A   75  ILE A   79  5                                   5    
HELIX    5   5 TRP A   86  HIS A   90  5                                   5    
HELIX    6   6 ARG A   91  GLU A   93  5                                   3    
HELIX    7   7 LEU A   94  GLN A  107  1                                  14    
HELIX    8   8 ASP A  143  ALA A  157  1                                  15    
HELIX    9   9 ASN A  169  ASN A  178  1                                  10    
HELIX   10  10 ARG A  199  LYS A  209  1                                  11    
HELIX   11  11 VAL A  234  GLU A  237  5                                   4    
HELIX   12  12 ASP A  238  LYS A  249  1                                  12    
HELIX   13  13 THR A  251  ARG A  263  1                                  13    
HELIX   14  14 ASN A  273  VAL A  281  1                                   9    
HELIX   15  15 GLN A  282  PHE A  286  5                                   5    
HELIX   16  16 THR A  289  GLY A  298  1                                  10    
HELIX   17  17 SER A  308  SER A  313  1                                   6    
HELIX   18  18 ARG B   31  GLY B   45  1                                  15    
HELIX   19  19 ALA B   52  ASN B   56  5                                   5    
HELIX   20  20 ASN B   57  ASP B   71  1                                  15    
HELIX   21  21 LYS B   75  ILE B   79  5                                   5    
HELIX   22  22 TRP B   86  HIS B   90  5                                   5    
HELIX   23  23 ARG B   91  GLU B   93  5                                   3    
HELIX   24  24 LEU B   94  ALA B  106  1                                  13    
HELIX   25  25 ASP B  143  ALA B  157  1                                  15    
HELIX   26  26 ASN B  169  ASN B  178  1                                  10    
HELIX   27  27 ARG B  199  LYS B  209  1                                  11    
HELIX   28  28 VAL B  234  GLU B  237  5                                   4    
HELIX   29  29 ASP B  238  LYS B  249  1                                  12    
HELIX   30  30 THR B  251  ARG B  263  1                                  13    
HELIX   31  31 ASN B  273  VAL B  281  1                                   9    
HELIX   32  32 GLN B  282  PHE B  286  5                                   5    
HELIX   33  33 THR B  289  GLY B  298  1                                  10    
HELIX   34  34 SER B  308  SER B  313  1                                   6    
SHEET    1   A 2 CYS A   7  LYS A   9  0                                        
SHEET    2   A 2 PHE A  15  PRO A  17 -1  O  MET A  16   N  VAL A   8           
SHEET    1   B 9 LEU A  19  GLY A  22  0                                        
SHEET    2   B 9 HIS A  48  ASP A  50  1  O  HIS A  48   N  PHE A  21           
SHEET    3   B 9 PHE A  80  LEU A  85  1  O  PHE A  80   N  ILE A  49           
SHEET    4   B 9 VAL A 111  ILE A 116  1  O  LEU A 115   N  LEU A  85           
SHEET    5   B 9 ALA A 160  SER A 166  1  O  LYS A 161   N  VAL A 111           
SHEET    6   B 9 CYS A 188  GLU A 192  1  O  GLN A 190   N  VAL A 165           
SHEET    7   B 9 VAL A 212  TYR A 216  1  O  VAL A 214   N  VAL A 191           
SHEET    8   B 9 VAL A 266  LYS A 270  1  O  VAL A 266   N  ALA A 215           
SHEET    9   B 9 LEU A  19  GLY A  22  1  N  GLY A  20   O  VAL A 267           
SHEET    1   C 2 CYS B   7  LYS B   9  0                                        
SHEET    2   C 2 PHE B  15  PRO B  17 -1  O  MET B  16   N  VAL B   8           
SHEET    1   D 9 LEU B  19  GLY B  22  0                                        
SHEET    2   D 9 HIS B  48  ASP B  50  1  O  ASP B  50   N  PHE B  21           
SHEET    3   D 9 PHE B  80  LEU B  85  1  O  PHE B  80   N  ILE B  49           
SHEET    4   D 9 VAL B 111  ILE B 116  1  O  LEU B 115   N  LEU B  85           
SHEET    5   D 9 ALA B 160  SER B 166  1  O  LYS B 161   N  VAL B 111           
SHEET    6   D 9 CYS B 188  GLU B 192  1  O  CYS B 188   N  VAL B 165           
SHEET    7   D 9 VAL B 212  TYR B 216  1  O  VAL B 214   N  VAL B 191           
SHEET    8   D 9 VAL B 266  LYS B 270  1  O  VAL B 266   N  ALA B 215           
SHEET    9   D 9 LEU B  19  GLY B  22  1  N  GLY B  20   O  VAL B 267           
SITE     1 AC1 35 GLY A  22  THR A  23  TYR A  24  ASP A  50                    
SITE     2 AC1 35 TYR A  55  HIS A 117  SER A 166  ASN A 167                    
SITE     3 AC1 35 GLN A 190  TYR A 216  SER A 217  ALA A 218                    
SITE     4 AC1 35 LEU A 219  GLY A 220  SER A 221  GLN A 222                    
SITE     5 AC1 35 LEU A 236  ALA A 253  LEU A 268  ALA A 269                    
SITE     6 AC1 35 LYS A 270  SER A 271  TYR A 272  ARG A 276                    
SITE     7 AC1 35 GLN A 279  ASN A 280  0SZ A 402  HOH A 506                    
SITE     8 AC1 35 HOH A 515  HOH A 521  HOH A 539  HOH A 559                    
SITE     9 AC1 35 HOH A 629  HOH A 719  HOH A 759                               
SITE     1 AC2  9 TYR A  24  TYR A  55  TRP A  86  HIS A 117                    
SITE     2 AC2  9 PHE A 311  NAP A 401  EDO A 403  HOH A 515                    
SITE     3 AC2  9 HOH A 745                                                     
SITE     1 AC3  5 TRP A  86  SER A  87  SER A 118  MET A 120                    
SITE     2 AC3  5 0SZ A 402                                                     
SITE     1 AC4  5 ALA A  44  ASP A 143  ARG A 278  VAL A 281                    
SITE     2 AC4  5 HOH A 750                                                     
SITE     1 AC5  5 LEU A 122  SER A 129  VAL A 137  PHE A 311                    
SITE     2 AC5  5 HOH A 745                                                     
SITE     1 AC6  6 TYR A  24  ARG A 226  TRP A 227  HOH A 574                    
SITE     2 AC6  6 HOH A 664  HOH A 774                                          
SITE     1 AC7  8 LYS A 225  TRP A 227  VAL A 228  HOH A 546                    
SITE     2 AC7  8 HOH A 600  HOH A 691  HOH A 771  HIS B  14                    
SITE     1 AC8  9 GLN A   6  PRO A  17  VAL A  18  LEU A  19                    
SITE     2 AC8  9 GLY A  45  PHE A  46  ARG A  47  HIS A  48                    
SITE     3 AC8  9 PHE A 284                                                     
SITE     1 AC9 34 GLY B  22  THR B  23  TYR B  24  ASP B  50                    
SITE     2 AC9 34 TYR B  55  HIS B 117  SER B 166  ASN B 167                    
SITE     3 AC9 34 GLN B 190  TYR B 216  SER B 217  ALA B 218                    
SITE     4 AC9 34 LEU B 219  GLY B 220  SER B 221  GLN B 222                    
SITE     5 AC9 34 ALA B 253  LEU B 268  ALA B 269  LYS B 270                    
SITE     6 AC9 34 SER B 271  TYR B 272  ARG B 276  GLN B 279                    
SITE     7 AC9 34 ASN B 280  0SZ B 702  HOH B 802  HOH B 809                    
SITE     8 AC9 34 HOH B 831  HOH B 837  HOH B 853  HOH B 964                    
SITE     9 AC9 34 HOH B 979  HOH B 985                                          
SITE     1 BC1 12 TYR B  24  LEU B  54  TYR B  55  HIS B 117                    
SITE     2 BC1 12 ASN B 167  TYR B 216  TRP B 227  PHE B 311                    
SITE     3 BC1 12 NAP B 701  EDO B 703  HOH B 853  HOH B1031                    
SITE     1 BC2  5 TRP B  86  SER B  87  SER B 118  MET B 120                    
SITE     2 BC2  5 0SZ B 702                                                     
SITE     1 BC3  5 TYR B 319  HOH B 817  HOH B 963  HOH B1047                    
SITE     2 BC3  5 HOH B1072                                                     
SITE     1 BC4  4 ALA B  44  ARG B 278  HOH B 967  HOH B1065                    
CRYST1   48.717  106.764   74.882  90.00 103.11  90.00 P 1 21 1      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      0.020527  0.000000  0.004780        0.00000                         
SCALE2      0.000000  0.009366  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013712        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system