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Database: PDB
Entry: 4YKG
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Original site: 4YKG 
HEADER    OXIDOREDUCTASE                          04-MAR-15   4YKG              
TITLE     CRYSTAL STRUCTURE OF THE ALKYLHYDROPEROXIDE REDUCTASE SUBUNIT F (AHPF)
TITLE    2 WITH NAD+ 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 4YKG    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.    2.40 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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 24472                          
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) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.285                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1317                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1774                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.75                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2600                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 82                           
REMARK   3   BIN FREE R VALUE                    : 0.3050                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3949                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 193                                     
REMARK   3   SOLVENT ATOMS            : 158                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.03                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.35000                                             
REMARK   3    B22 (A**2) : -2.48000                                             
REMARK   3    B33 (A**2) : 2.13000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.11000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.428         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.301         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.198         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.976        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.905                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.870                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4201 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4031 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5695 ; 1.518 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9293 ; 0.784 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   522 ; 7.122 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   168 ;39.465 ;25.119       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   706 ;17.496 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;13.512 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   663 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4884 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   865 ; 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):  2085 ; 2.386 ; 4.070       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2084 ; 2.386 ; 4.069       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2605 ; 3.848 ; 6.098       
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):   44.140   -6.286   84.205              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0933 T22:   0.0100                                     
REMARK   3      T33:   0.1020 T12:   0.0121                                     
REMARK   3      T13:  -0.0263 T23:   0.0077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0166 L22:   0.0960                                     
REMARK   3      L33:   0.1947 L12:  -0.0125                                     
REMARK   3      L13:  -0.0521 L23:   0.0666                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0218 S12:   0.0011 S13:   0.0111                       
REMARK   3      S21:  -0.0636 S22:   0.0002 S23:   0.0249                       
REMARK   3      S31:  -0.0549 S32:  -0.0069 S33:  -0.0219                       
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 4YKG 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_1000207600.                                   
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) : 1.00                               
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 : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26052                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.9                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.10800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.64800                            
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: 4O5Q                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.57                                     
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       53.44100            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.78800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       53.44100            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       29.78800            
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: 15710 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 46780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -244.0 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       62.54655            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      113.13073            
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   O2A  NAD A   602     O    HOH A   701              2.16            
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  29      -20.15     69.98                                   
REMARK 500    PRO A  59       32.83    -74.67                                   
REMARK 500    ASN A  73       59.46   -119.22                                   
REMARK 500    PRO A  82       31.74    -91.67                                   
REMARK 500    LEU A  83     -158.06   -112.55                                   
REMARK 500    ALA A 105      107.54    -51.55                                   
REMARK 500    GLU A 180      127.33    -35.48                                   
REMARK 500    ASP A 196       61.79   -104.43                                   
REMARK 500    ALA A 199     -172.61    -67.07                                   
REMARK 500    LYS A 201       81.87    -66.55                                   
REMARK 500    ARG A 202       82.94    -65.52                                   
REMARK 500    VAL A 253      -82.66   -113.99                                   
REMARK 500    SER A 260       -9.29     90.58                                   
REMARK 500    ARG A 338      108.29    -59.80                                   
REMARK 500    THR A 339        4.32     92.42                                   
REMARK 500    VAL A 433      -61.38    -90.21                                   
REMARK 500    LYS A 519     -163.15    -78.25                                   
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 LYS A  519     THR A  520                 -112.04                    
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 612  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  85   NE2                                                    
REMARK 620 2 HOH A 825   O   128.8                                              
REMARK 620 3 GLU A 110   OE1  37.6 105.2                                        
REMARK 620 4 GLU A 110   OE2  37.2 107.8   3.2                                  
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 NAD A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 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 CD A 612                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL 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 GOL A 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL 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 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 620                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4YKF   RELATED DB: PDB                                   
DBREF  4YKG 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 CSD 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                                                          
MODRES 4YKG CSD A  345  CYS  MODIFIED RESIDUE                                   
HET    CSD  A 345      13                                                       
HET    FAD  A 601      53                                                       
HET    NAD  A 602      44                                                       
HET    SO4  A 603       5                                                       
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     CD  A 612       1                                                       
HET    GOL  A 613       6                                                       
HET    GOL  A 614       6                                                       
HET    GOL  A 615       6                                                       
HET    GOL  A 616       6                                                       
HET    GOL  A 617       6                                                       
HET    GOL  A 618       6                                                       
HET    PEG  A 619       7                                                       
HET    PEG  A 620       7                                                       
HETNAM     CSD 3-SULFINOALANINE                                                 
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CD CADMIUM ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE                       
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  CSD    C3 H7 N O4 S                                                 
FORMUL   2  FAD    C27 H33 N9 O15 P2                                            
FORMUL   3  NAD    C21 H27 N7 O14 P2                                            
FORMUL   4  SO4    9(O4 S 2-)                                                   
FORMUL  13   CD    CD 2+                                                        
FORMUL  14  GOL    6(C3 H8 O3)                                                  
FORMUL  20  PEG    2(C4 H10 O3)                                                 
FORMUL  22  HOH   *158(H2 O)                                                    
HELIX    1 AA1 ASP A    3  GLU A   15  1                                  13    
HELIX    2 AA2 SER A   30  SER A   47  1                                  18    
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 ARG A  202  ARG A  210  1                                   9    
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 CSD A  345  GLY A  350  1                                   6    
HELIX   14 AB5 PRO A  351  LYS A  354  5                                   4    
HELIX   15 AB6 GLY A  364  VAL A  378  1                                  15    
HELIX   16 AB7 ASP A  393  LEU A  403  1                                  11    
HELIX   17 AB8 THR A  455  GLU A  459  5                                   5    
HELIX   18 AB9 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  LEU A  23   O  THR A  51           
SHEET    3 AA1 8 SER A  64  THR A  68 -1  O  THR A  68   N  GLU A  22           
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  TYR A 125   O  ILE A 154           
SHEET    7 AA1 8 ALA A 173  VAL A 174 -1  O  ALA A 173   N  TYR A 124           
SHEET    8 AA1 8 GLY A 182  GLN A 183 -1  O  GLY A 182   N  VAL A 174           
SHEET    1 AA2 6 VAL A 282  ILE A 285  0                                        
SHEET    2 AA2 6 THR A 238  MET A 241  1  N  LEU A 240   O  ILE A 285           
SHEET    3 AA2 6 TYR A 213  VAL A 218  1  N  ILE A 217   O  MET A 241           
SHEET    4 AA2 6 VAL A 312  VAL A 320  1  O  LYS A 314   N  TYR A 213           
SHEET    5 AA2 6 HIS A 303  THR A 307 -1  N  ILE A 305   O  LEU A 313           
SHEET    6 AA2 6 ALA A 290  ILE A 294 -1  N  SER A 291   O  GLU A 306           
SHEET    1 AA3 5 VAL A 282  ILE A 285  0                                        
SHEET    2 AA3 5 THR A 238  MET A 241  1  N  LEU A 240   O  ILE A 285           
SHEET    3 AA3 5 TYR A 213  VAL A 218  1  N  ILE A 217   O  MET A 241           
SHEET    4 AA3 5 VAL A 312  VAL A 320  1  O  LYS A 314   N  TYR A 213           
SHEET    5 AA3 5 VAL A 483  ALA A 485  1  O  PHE A 484   N  VAL A 320           
SHEET    1 AA4 2 ASP A 254  ILE A 255  0                                        
SHEET    2 AA4 2 THR A 264  GLU A 265 -1  O  THR A 264   N  ILE A 255           
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  ILE A 445   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  LEU A 384   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  ILE A 440   N  LEU A 427           
SSBOND   1 CYS A  129    CYS A  132                          1555   1555  2.04  
LINK         NE2 HIS A  85                CD    CD A 612     1555   1555  2.32  
LINK         C   TYR A 344                 N   CSD A 345     1555   1555  1.32  
LINK         C   CSD A 345                 N   PRO A 346     1555   1555  1.35  
LINK        CD    CD A 612                 O   HOH A 825     1555   1555  2.25  
LINK         OE1 GLU A 110                CD    CD A 612     1555   4647  2.31  
LINK         OE2 GLU A 110                CD    CD A 612     1555   4647  2.69  
CISPEP   1 LYS A   62    PRO A   63          0         4.08                     
CISPEP   2 VAL A  171    PRO A  172          0         3.06                     
SITE     1 AC1 32 GLY A 219  GLY A 221  PRO A 222  ALA A 223                    
SITE     2 AC1 32 GLY A 242  GLU A 243  ARG A 244  GLY A 247                    
SITE     3 AC1 32 GLN A 248  THR A 252  ASN A 257  GLN A 288                    
SITE     4 AC1 32 SER A 289  ALA A 290  ALA A 321  THR A 322                    
SITE     5 AC1 32 GLY A 323  CYS A 348  TRP A 457  GLY A 487                    
SITE     6 AC1 32 ASP A 488  LYS A 495  GLN A 496  ILE A 497                    
SITE     7 AC1 32 HOH A 716  HOH A 723  HOH A 739  HOH A 740                    
SITE     8 AC1 32 HOH A 746  HOH A 755  HOH A 761  HOH A 776                    
SITE     1 AC2 19 GLN A 336  ILE A 361  GLY A 362  GLY A 364                    
SITE     2 AC2 19 ASN A 365  SER A 366  LEU A 384  GLU A 385                    
SITE     3 AC2 19 PHE A 386  LYS A 391  ILE A 449  MET A 467                    
SITE     4 AC2 19 PRO A 493  HOH A 701  HOH A 726  HOH A 731                    
SITE     5 AC2 19 HOH A 738  HOH A 745  HOH A 788                               
SITE     1 AC3  6 PRO A 453  ASN A 454  THR A 455  ASN A 456                    
SITE     2 AC3  6 TRP A 457  HOH A 711                                          
SITE     1 AC4  4 HIS A 438  ASN A 439  HOH A 762  HOH A 769                    
SITE     1 AC5  4 GLY A 333  GLU A 334  ASP A 335  GLN A 336                    
SITE     1 AC6  3 ASP A 393  GLN A 394  HOH A 771                               
SITE     1 AC7  2 ARG A 357  HIS A 380                                          
SITE     1 AC8  3 ASP A 473  ALA A 474  HOH A 757                               
SITE     1 AC9  2 ARG A 327  ASN A 328                                          
SITE     1 AD1  5 GLU A 279  LYS A 354  GOL A 615  HOH A 720                    
SITE     2 AD1  5 HOH A 790                                                     
SITE     1 AD2  2 GLU A 243  SER A 289                                          
SITE     1 AD3  4 HIS A  85  GLU A 110  HIS A 130  HOH A 825                    
SITE     1 AD4  4 LEU A 352  PHE A 353  GOL A 618  HOH A 781                    
SITE     1 AD5  2 ARG A 466  HOH A 753                                          
SITE     1 AD6  4 ASP A 281  SO4 A 610  HOH A 720  HOH A 742                    
SITE     1 AD7  3 GLU A 265  GLN A 413  ARG A 432                               
SITE     1 AD8  2 ASP A 278  TYR A 280                                          
SITE     1 AD9 10 THR A 339  LYS A 340  GLY A 341  VAL A 342                    
SITE     2 AD9 10 THR A 343  ASP A 349  LEU A 352  PHE A 353                    
SITE     3 AD9 10 GOL A 613  HOH A 749                                          
SITE     1 AE1  7 LEU A   2  ASP A   3  THR A   4  ILE A 294                    
SITE     2 AE1  7 GLN A 304  GLU A 306  HOH A 843                               
SITE     1 AE2  4 GLU A 206  ARG A 210  ASP A 211  ARG A 237                    
CRYST1  106.882   59.576  121.508  90.00 111.40  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      0.009356  0.000000  0.003667        0.00000                         
SCALE2      0.000000  0.016785  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008839        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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