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Database: PDB
Entry: 4YKF
LinkDB: 4YKF
Original site: 4YKF 
HEADER    OXIDOREDUCTASE                          04-MAR-15   4YKF              
TITLE     CRYSTAL STRUCTURE OF THE ALKYLHYDROPEROXIDE REDUCTASE SUBUNIT F (AHPF)
TITLE    2 WITH NADH FROM ESCHERICHIA COLI                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALKYL HYDROPEROXIDE REDUCTASE SUBUNIT F;                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ALKYL HYDROPEROXIDE REDUCTASE F52A PROTEIN;                 
COMPND   5 EC: 1.8.1.-;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K12;                           
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: AHPF, B0606, JW0599;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA GAMI 2;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.KAMARIAH,M.S.S.MANIMEKALAI,G.GRUBER,F.EISENHABER,B.EISENHABER       
REVDAT   1   15-JUL-15 4YKF    0                                                
JRNL        AUTH   N.KAMARIAH,M.S.S.MANIMEKALAI,W.NARTEY,F.EISENHABER,          
JRNL        AUTH 2 B.EISENHABER,G.GRUBER                                        
JRNL        TITL   CRYSTALLOGRAPHIC AND SOLUTION STUDIES OF NAD(+)- AND         
JRNL        TITL 2 NADH-BOUND ALKYLHYDROPEROXIDE REDUCTASE SUBUNIT F (AHPF)     
JRNL        TITL 3 FROM ESCHERICHIA COLI PROVIDE INSIGHT INTO SEQUENTIAL        
JRNL        TITL 4 ENZYMATIC STEPS                                              
JRNL        REF    BIOCHIM.BIOPHYS.ACTA          V.1847  1139 2015              
JRNL        REFN                   ISSN 0006-3002                               
JRNL        PMID   26092085                                                     
JRNL        DOI    10.1016/J.BBABIO.2015.06.011                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   P.V.DIP,N.KAMARIAH,M.S.S.MANIMEKALAI,W.NARTEY,               
REMARK   1  AUTH 2 A.M.BALAKRISHNA,F.EISENHABER,B.EISENHABER,G.GRUBER           
REMARK   1  TITL   STRUCTURE, MECHANISM AND ENSEMBLE FORMATION OF THE           
REMARK   1  TITL 2 ALKYLHYDROPEROXIDE REDUCTASE SUBUNITS AHPC AND AHPF FROM     
REMARK   1  TITL 3 ESCHERICHIA COLI                                             
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  70  2848 2014              
REMARK   1  REFN                   ESSN 1399-0047                               
REMARK   1  PMID   25372677                                                     
REMARK   1  DOI    10.1107/S1399004714019233                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 21672                          
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) : 0.228                           
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.288                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1168                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.57                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1463                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.42                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2760                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 60                           
REMARK   3   BIN FREE R VALUE                    : 0.3320                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3947                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 187                                     
REMARK   3   SOLVENT ATOMS            : 142                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.56                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.46000                                             
REMARK   3    B22 (A**2) : -2.93000                                             
REMARK   3    B33 (A**2) : 2.49000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.37000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.571         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.335         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.211         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.838        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.892                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.833                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4189 ; 0.015 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4022 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5680 ; 1.676 ; 1.984       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9268 ; 0.818 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   520 ; 7.247 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   168 ;36.565 ;25.119       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   707 ;17.700 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;15.741 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   658 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4854 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   863 ; 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):  2083 ; 2.084 ; 3.092       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2082 ; 2.081 ; 3.091       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2602 ; 3.345 ; 4.632       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER 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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   521                          
REMARK   3    ORIGIN FOR THE GROUP (A): -25.5586  59.3634 142.0154              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0565 T22:   0.0735                                     
REMARK   3      T33:   0.1027 T12:  -0.0012                                     
REMARK   3      T13:  -0.0423 T23:   0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0039 L22:   0.0851                                     
REMARK   3      L33:   0.3041 L12:  -0.0122                                     
REMARK   3      L13:  -0.0109 L23:   0.0299                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0113 S12:  -0.0126 S13:  -0.0075                       
REMARK   3      S21:  -0.0675 S22:   0.0194 S23:   0.0522                       
REMARK   3      S31:  -0.0437 S32:  -0.0245 S33:  -0.0307                       
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   4                                                                      
REMARK   4 4YKF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000207598.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSRRC                              
REMARK 200  BEAMLINE                       : BL13B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9789                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA 0.1.26                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22917                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.870                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.3                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.500                              
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: 4O5Q                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NA-HEPES, 2.5 % (V/V) PEG 400, 2   
REMARK 280  M AMMONIUM SULFATE, 10 MM CADMIUM CHLORIDE, PH 7.5, VAPOR           
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       53.54500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.69500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       53.54500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       29.69500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15100 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 46500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -266.0 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   BIOMT1   2 -1.000000  0.000000  0.000000      -25.38837            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      339.08979            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 716  LIES ON A SPECIAL POSITION.                          
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 210   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A 432   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 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    ASP A  28     -167.36   -102.02                                   
REMARK 500    SER A  57       74.40   -109.81                                   
REMARK 500    ARG A  61      141.34    -38.62                                   
REMARK 500    LEU A  83     -148.25   -103.82                                   
REMARK 500    CYS A 129       97.75    -66.38                                   
REMARK 500    PHE A 159       64.42   -100.49                                   
REMARK 500    ASN A 167       40.61     37.76                                   
REMARK 500    ASN A 177       49.25     32.57                                   
REMARK 500    ALA A 204      -71.66    -36.00                                   
REMARK 500    ARG A 244      107.16   -160.04                                   
REMARK 500    VAL A 253      -88.90   -104.80                                   
REMARK 500    SER A 260      -19.87     85.68                                   
REMARK 500    ASP A 283       96.61    -64.82                                   
REMARK 500    GLU A 299      -18.59    -46.40                                   
REMARK 500    THR A 339       -0.49     68.42                                   
REMARK 500    LYS A 519      -66.07   -151.07                                   
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 ARG A  202     ALA A  203                  125.87                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 603  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  85   NE2                                                    
REMARK 620 2 HIS A 130   ND1  85.9                                              
REMARK 620 3 GLU A 110   OE1  66.7  35.4                                        
REMARK 620 4 GLU A 110   OE2  65.0  34.1   3.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAI A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 619                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4YKG   RELATED DB: PDB                                   
DBREF  4YKF A    1   521  UNP    P35340   AHPF_ECOLI       1    521             
SEQRES   1 A  521  MET LEU ASP THR ASN MET LYS THR GLN LEU LYS ALA TYR          
SEQRES   2 A  521  LEU GLU LYS LEU THR LYS PRO VAL GLU LEU ILE ALA THR          
SEQRES   3 A  521  LEU ASP ASP SER ALA LYS SER ALA GLU ILE LYS GLU LEU          
SEQRES   4 A  521  LEU ALA GLU ILE ALA GLU LEU SER ASP LYS VAL THR PHE          
SEQRES   5 A  521  LYS GLU ASP ASN SER LEU PRO VAL ARG LYS PRO SER PHE          
SEQRES   6 A  521  LEU ILE THR ASN PRO GLY SER ASN GLN GLY PRO ARG PHE          
SEQRES   7 A  521  ALA GLY SER PRO LEU GLY HIS GLU PHE THR SER LEU VAL          
SEQRES   8 A  521  LEU ALA LEU LEU TRP THR GLY GLY HIS PRO SER LYS GLU          
SEQRES   9 A  521  ALA GLN SER LEU LEU GLU GLN ILE ARG HIS ILE ASP GLY          
SEQRES  10 A  521  ASP PHE GLU PHE GLU THR TYR TYR SER LEU SER CYS HIS          
SEQRES  11 A  521  ASN CYS PRO ASP VAL VAL GLN ALA LEU ASN LEU MET SER          
SEQRES  12 A  521  VAL LEU ASN PRO ARG ILE LYS HIS THR ALA ILE ASP GLY          
SEQRES  13 A  521  GLY THR PHE GLN ASN GLU ILE THR ASP ARG ASN VAL MET          
SEQRES  14 A  521  GLY VAL PRO ALA VAL PHE VAL ASN GLY LYS GLU PHE GLY          
SEQRES  15 A  521  GLN GLY ARG MET THR LEU THR GLU ILE VAL ALA LYS ILE          
SEQRES  16 A  521  ASP THR GLY ALA GLU LYS ARG ALA ALA GLU GLU LEU ASN          
SEQRES  17 A  521  LYS ARG ASP ALA TYR ASP VAL LEU ILE VAL GLY SER GLY          
SEQRES  18 A  521  PRO ALA GLY ALA ALA ALA ALA ILE TYR SER ALA ARG LYS          
SEQRES  19 A  521  GLY ILE ARG THR GLY LEU MET GLY GLU ARG PHE GLY GLY          
SEQRES  20 A  521  GLN ILE LEU ASP THR VAL ASP ILE GLU ASN TYR ILE SER          
SEQRES  21 A  521  VAL PRO LYS THR GLU GLY GLN LYS LEU ALA GLY ALA LEU          
SEQRES  22 A  521  LYS VAL HIS VAL ASP GLU TYR ASP VAL ASP VAL ILE ASP          
SEQRES  23 A  521  SER GLN SER ALA SER LYS LEU ILE PRO ALA ALA VAL GLU          
SEQRES  24 A  521  GLY GLY LEU HIS GLN ILE GLU THR ALA SER GLY ALA VAL          
SEQRES  25 A  521  LEU LYS ALA ARG SER ILE ILE VAL ALA THR GLY ALA LYS          
SEQRES  26 A  521  TRP ARG ASN MET ASN VAL PRO GLY GLU ASP GLN TYR ARG          
SEQRES  27 A  521  THR LYS GLY VAL THR TYR CYS PRO HIS CYS ASP GLY PRO          
SEQRES  28 A  521  LEU PHE LYS GLY LYS ARG VAL ALA VAL ILE GLY GLY GLY          
SEQRES  29 A  521  ASN SER GLY VAL GLU ALA ALA ILE ASP LEU ALA GLY ILE          
SEQRES  30 A  521  VAL GLU HIS VAL THR LEU LEU GLU PHE ALA PRO GLU MET          
SEQRES  31 A  521  LYS ALA ASP GLN VAL LEU GLN ASP LYS LEU ARG SER LEU          
SEQRES  32 A  521  LYS ASN VAL ASP ILE ILE LEU ASN ALA GLN THR THR GLU          
SEQRES  33 A  521  VAL LYS GLY ASP GLY SER LYS VAL VAL GLY LEU GLU TYR          
SEQRES  34 A  521  ARG ASP ARG VAL SER GLY ASP ILE HIS ASN ILE GLU LEU          
SEQRES  35 A  521  ALA GLY ILE PHE VAL GLN ILE GLY LEU LEU PRO ASN THR          
SEQRES  36 A  521  ASN TRP LEU GLU GLY ALA VAL GLU ARG ASN ARG MET GLY          
SEQRES  37 A  521  GLU ILE ILE ILE ASP ALA LYS CYS GLU THR ASN VAL LYS          
SEQRES  38 A  521  GLY VAL PHE ALA ALA GLY ASP CYS THR THR VAL PRO TYR          
SEQRES  39 A  521  LYS GLN ILE ILE ILE ALA THR GLY GLU GLY ALA LYS ALA          
SEQRES  40 A  521  SER LEU SER ALA PHE ASP TYR LEU ILE ARG THR LYS THR          
SEQRES  41 A  521  ALA                                                          
HET    FAD  A 601      53                                                       
HET    NAI  A 602      44                                                       
HET     CD  A 603       1                                                       
HET    SO4  A 604       5                                                       
HET    SO4  A 605       5                                                       
HET    SO4  A 606       5                                                       
HET    SO4  A 607       5                                                       
HET    SO4  A 608       5                                                       
HET    SO4  A 609       5                                                       
HET    SO4  A 610       5                                                       
HET    SO4  A 611       5                                                       
HET    SO4  A 612       5                                                       
HET    SO4  A 613       5                                                       
HET    GOL  A 614       6                                                       
HET    GOL  A 615       6                                                       
HET    GOL  A 616       6                                                       
HET    PEG  A 617       7                                                       
HET    PEG  A 618       7                                                       
HET    PEG  A 619       7                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE                     
HETNAM      CD CADMIUM ION                                                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     NAI NADH                                                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  FAD    C27 H33 N9 O15 P2                                            
FORMUL   3  NAI    C21 H29 N7 O14 P2                                            
FORMUL   4   CD    CD 2+                                                        
FORMUL   5  SO4    10(O4 S 2-)                                                  
FORMUL  15  GOL    3(C3 H8 O3)                                                  
FORMUL  18  PEG    3(C4 H10 O3)                                                 
FORMUL  21  HOH   *142(H2 O)                                                    
HELIX    1 AA1 ASP A    3  GLU A   15  1                                  13    
HELIX    2 AA2 SER A   30  GLU A   45  1                                  16    
HELIX    3 AA3 LEU A   83  HIS A   85  5                                   3    
HELIX    4 AA4 GLU A   86  GLY A   98  1                                  13    
HELIX    5 AA5 ALA A  105  HIS A  114  1                                  10    
HELIX    6 AA6 ASN A  131  ASN A  146  1                                  16    
HELIX    7 AA7 PHE A  159  ARG A  166  1                                   8    
HELIX    8 AA8 THR A  187  ASP A  196  1                                  10    
HELIX    9 AA9 ALA A  203  ARG A  210  1                                   8    
HELIX   10 AB1 GLY A  221  LYS A  234  1                                  14    
HELIX   11 AB2 GLY A  246  THR A  252  5                                   7    
HELIX   12 AB3 GLY A  266  GLU A  279  1                                  14    
HELIX   13 AB4 GLY A  333  ARG A  338  1                                   6    
HELIX   14 AB5 CYS A  345  GLY A  350  1                                   6    
HELIX   15 AB6 PRO A  351  LYS A  354  5                                   4    
HELIX   16 AB7 GLY A  364  VAL A  378  1                                  15    
HELIX   17 AB8 ASP A  393  LEU A  403  1                                  11    
HELIX   18 AB9 THR A  455  GLU A  459  5                                   5    
HELIX   19 AC1 GLN A  496  THR A  518  1                                  23    
SHEET    1 AA1 8 VAL A  50  GLU A  54  0                                        
SHEET    2 AA1 8 VAL A  21  THR A  26  1  N  ALA A  25   O  LYS A  53           
SHEET    3 AA1 8 SER A  64  THR A  68 -1  O  LEU A  66   N  ILE A  24           
SHEET    4 AA1 8 ARG A  77  ALA A  79 -1  O  PHE A  78   N  PHE A  65           
SHEET    5 AA1 8 ILE A 149  ASP A 155  1  O  ALA A 153   N  ALA A  79           
SHEET    6 AA1 8 PHE A 119  TYR A 125  1  N  THR A 123   O  ILE A 154           
SHEET    7 AA1 8 ALA A 173  VAL A 176 -1  O  PHE A 175   N  GLU A 122           
SHEET    8 AA1 8 LYS A 179  GLN A 183 -1  O  LYS A 179   N  VAL A 176           
SHEET    1 AA2 5 VAL A 282  ILE A 285  0                                        
SHEET    2 AA2 5 THR A 238  MET A 241  1  N  LEU A 240   O  ASP A 283           
SHEET    3 AA2 5 VAL A 215  VAL A 218  1  N  ILE A 217   O  MET A 241           
SHEET    4 AA2 5 ILE A 318  VAL A 320  1  O  ILE A 319   N  VAL A 218           
SHEET    5 AA2 5 VAL A 483  ALA A 485  1  O  PHE A 484   N  ILE A 318           
SHEET    1 AA3 2 ASP A 254  ILE A 255  0                                        
SHEET    2 AA3 2 THR A 264  GLU A 265 -1  O  THR A 264   N  ILE A 255           
SHEET    1 AA4 3 ALA A 290  ILE A 294  0                                        
SHEET    2 AA4 3 HIS A 303  THR A 307 -1  O  GLU A 306   N  SER A 291           
SHEET    3 AA4 3 VAL A 312  ALA A 315 -1  O  ALA A 315   N  HIS A 303           
SHEET    1 AA5 2 ALA A 324  TRP A 326  0                                        
SHEET    2 AA5 2 LEU A 451  PRO A 453 -1  O  LEU A 452   N  LYS A 325           
SHEET    1 AA6 5 VAL A 342  THR A 343  0                                        
SHEET    2 AA6 5 GLY A 444  VAL A 447  1  O  VAL A 447   N  THR A 343           
SHEET    3 AA6 5 ARG A 357  ILE A 361  1  N  ALA A 359   O  PHE A 446           
SHEET    4 AA6 5 HIS A 380  LEU A 384  1  O  THR A 382   N  VAL A 360           
SHEET    5 AA6 5 VAL A 406  ILE A 409  1  O  ASP A 407   N  LEU A 383           
SHEET    1 AA7 3 ALA A 412  GLY A 419  0                                        
SHEET    2 AA7 3 VAL A 424  ASP A 431 -1  O  GLU A 428   N  THR A 415           
SHEET    3 AA7 3 ILE A 437  GLU A 441 -1  O  HIS A 438   N  TYR A 429           
SSBOND   1 CYS A  129    CYS A  132                          1555   1555  2.07  
SSBOND   2 CYS A  345    CYS A  348                          1555   1555  2.06  
LINK         NE2 HIS A  85                CD    CD A 603     1555   1555  2.58  
LINK         ND1 HIS A 130                CD    CD A 603     1555   1555  2.54  
LINK         OE1 GLU A 110                CD    CD A 603     1555   4547  2.38  
LINK         OE2 GLU A 110                CD    CD A 603     1555   4547  2.27  
CISPEP   1 LYS A   62    PRO A   63          0         2.81                     
CISPEP   2 VAL A  171    PRO A  172          0         3.48                     
SITE     1 AC1 30 GLY A 219  GLY A 221  PRO A 222  ALA A 223                    
SITE     2 AC1 30 GLY A 242  GLU A 243  ARG A 244  GLY A 247                    
SITE     3 AC1 30 GLN A 248  ASN A 257  GLN A 288  ALA A 290                    
SITE     4 AC1 30 ALA A 321  THR A 322  GLY A 323  CYS A 348                    
SITE     5 AC1 30 ASN A 454  GLY A 487  ASP A 488  LYS A 495                    
SITE     6 AC1 30 GLN A 496  ILE A 497  ALA A 500  HOH A 707                    
SITE     7 AC1 30 HOH A 722  HOH A 723  HOH A 732  HOH A 737                    
SITE     8 AC1 30 HOH A 742  HOH A 760                                          
SITE     1 AC2 17 ILE A 361  GLY A 362  GLY A 363  GLY A 364                    
SITE     2 AC2 17 ASN A 365  SER A 366  GLU A 369  LEU A 384                    
SITE     3 AC2 17 GLU A 385  PHE A 386  LYS A 391  ILE A 449                    
SITE     4 AC2 17 MET A 467  HOH A 706  HOH A 733  HOH A 745                    
SITE     5 AC2 17 HOH A 748                                                     
SITE     1 AC3  4 HIS A  85  GLU A 110  HIS A 114  HIS A 130                    
SITE     1 AC4  5 PRO A 453  ASN A 454  THR A 455  ASN A 456                    
SITE     2 AC4  5 TRP A 457                                                     
SITE     1 AC5  4 HIS A 438  ASN A 439  HOH A 754  HOH A 785                    
SITE     1 AC6  4 GLY A 333  GLU A 334  ASP A 335  GLN A 336                    
SITE     1 AC7  3 ASP A 393  GLN A 394  HOH A 774                               
SITE     1 AC8  3 ASP A 473  ALA A 474  HOH A 716                               
SITE     1 AC9  2 ARG A 357  HIS A 380                                          
SITE     1 AD1  3 ILE A 440  GLU A 441  HOH A 758                               
SITE     1 AD2  3 ARG A 210  ASP A 211  ARG A 237                               
SITE     1 AD3  2 ARG A 517  HOH A 777                                          
SITE     1 AD4  4 GLN A 413  ARG A 432  HOH A 729  HOH A 767                    
SITE     1 AD5  3 LYS A 340  LEU A 352  PHE A 353                               
SITE     1 AD6  2 SER A  30  ALA A  31                                          
SITE     1 AD7  2 ARG A 466  PEG A 617                                          
SITE     1 AD8  3 ASN A 465  THR A 491  GOL A 616                               
SITE     1 AD9  2 LYS A 354  GLY A 355                                          
SITE     1 AE1  1 ASP A 281                                                     
CRYST1  107.090   59.390  121.350  90.00 111.34  90.00 C 1 2 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      0.009338  0.000000  0.003648        0.00000                         
SCALE2      0.000000  0.016838  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008847        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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