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Database: PDB
Entry: 3V92
LinkDB: 3V92
Original site: 3V92 
HEADER    OXIDOREDUCTASE                          23-DEC-11   3V92              
TITLE     S663A STABLE-5-LOX                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ARACHIDONATE 5-LIPOXYGENASE;                               
COMPND   3 CHAIN: B, A;                                                         
COMPND   4 SYNONYM: 5-LO, 5-LIPOXYGENASE;                                       
COMPND   5 EC: 1.13.11.34;                                                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ALOX5, LOG5;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2(DE3);                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET 14                                    
KEYWDS    LIPOXYGENASE, DIOXYGENASE, OXIDOREDUCTASE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.C.GILBERT,Z.RUI,D.B.NEAU,M.WAIGHT,S.G.BARTLETT,W.E.BOEGLIN,         
AUTHOR   2 A.R.BRASH,M.E.NEWCOMER                                               
REVDAT   2   15-AUG-12 3V92    1       JRNL                                     
REVDAT   1   02-MAY-12 3V92    0                                                
JRNL        AUTH   N.C.GILBERT,Z.RUI,D.B.NEAU,M.T.WAIGHT,S.G.BARTLETT,          
JRNL        AUTH 2 W.E.BOEGLIN,A.R.BRASH,M.E.NEWCOMER                           
JRNL        TITL   CONVERSION OF HUMAN 5-LIPOXYGENASE TO A 15-LIPOXYGENASE BY A 
JRNL        TITL 2 POINT MUTATION TO MIMIC PHOSPHORYLATION AT SERINE-663.       
JRNL        REF    FASEB J.                      V.  26  3222 2012              
JRNL        REFN                   ISSN 0892-6638                               
JRNL        PMID   22516296                                                     
JRNL        DOI    10.1096/FJ.12-205286                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.74 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.2_869)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.74                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.47                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.400                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 41034                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2061                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 41.4727 -  6.7484    0.99     2626   166  0.1774 0.2082        
REMARK   3     2  6.7484 -  5.3600    1.00     2656   130  0.1905 0.2305        
REMARK   3     3  5.3600 -  4.6835    1.00     2635   137  0.1498 0.2044        
REMARK   3     4  4.6835 -  4.2558    1.00     2614   130  0.1425 0.1807        
REMARK   3     5  4.2558 -  3.9510    1.00     2651   144  0.1445 0.1894        
REMARK   3     6  3.9510 -  3.7182    1.00     2618   141  0.1484 0.2066        
REMARK   3     7  3.7182 -  3.5321    1.00     2600   164  0.1538 0.2127        
REMARK   3     8  3.5321 -  3.3784    0.99     2620   129  0.1737 0.2503        
REMARK   3     9  3.3784 -  3.2484    0.99     2581   140  0.1927 0.2769        
REMARK   3    10  3.2484 -  3.1364    0.99     2647   145  0.2088 0.2733        
REMARK   3    11  3.1364 -  3.0383    0.98     2581   111  0.2262 0.3171        
REMARK   3    12  3.0383 -  2.9515    0.97     2567   126  0.2353 0.2839        
REMARK   3    13  2.9515 -  2.8738    0.98     2549   132  0.2638 0.3588        
REMARK   3    14  2.8738 -  2.8037    0.96     2560   112  0.2852 0.3920        
REMARK   3    15  2.8037 -  2.7400    0.96     2468   154  0.2923 0.3444        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.86                                          
REMARK   3   K_SOL              : 0.37                                          
REMARK   3   B_SOL              : 25.60                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.770            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.330           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.09230                                              
REMARK   3    B22 (A**2) : -1.43920                                             
REMARK   3    B33 (A**2) : 1.34680                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.97690                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003          11214                                  
REMARK   3   ANGLE     :  0.669          15226                                  
REMARK   3   CHIRALITY :  0.050           1643                                  
REMARK   3   PLANARITY :  0.002           1975                                  
REMARK   3   DIHEDRAL  : 12.503           4146                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: all                                                    
REMARK   3    ORIGIN FOR THE GROUP (A): -10.0883 -66.5464 -33.0150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2140 T22:  -0.3445                                     
REMARK   3      T33:  -0.1122 T12:   0.1721                                     
REMARK   3      T13:   0.0580 T23:  -0.1279                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1668 L22:   0.2096                                     
REMARK   3      L33:   0.1873 L12:   0.0732                                     
REMARK   3      L13:  -0.0536 L23:  -0.1356                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0120 S12:   0.0767 S13:   0.0332                       
REMARK   3      S21:  -0.1596 S22:   0.1203 S23:   0.1898                       
REMARK   3      S31:   0.0154 S32:  -0.2198 S33:   0.1414                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3V92 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB069748.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97915                            
REMARK 200  MONOCHROMATOR                  : FAST MONOCHROMATIC ROTARY BEAM     
REMARK 200                                   SHUTTERS                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41056                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.740                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.350                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.74                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.96                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% TACSIMATE, PH 6.0, VAPOR             
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 295K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000      101.18750            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET B   -17                                                      
REMARK 465     GLY B   -16                                                      
REMARK 465     SER B   -15                                                      
REMARK 465     SER B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     HIS B    -8                                                      
REMARK 465     SER B    -7                                                      
REMARK 465     SER B    -6                                                      
REMARK 465     GLY B    -5                                                      
REMARK 465     LEU B    -4                                                      
REMARK 465     VAL B    -3                                                      
REMARK 465     PRO B    -2                                                      
REMARK 465     ARG B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     HIS B     2                                                      
REMARK 465     MET B     3                                                      
REMARK 465     MET A   -17                                                      
REMARK 465     GLY A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     SER A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     SER A    -7                                                      
REMARK 465     SER A    -6                                                      
REMARK 465     GLY A    -5                                                      
REMARK 465     LEU A    -4                                                      
REMARK 465     VAL A    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     ARG A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     HIS A     2                                                      
REMARK 465     MET A     3                                                      
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   OG   SER B   341     O    HOH B   855              1.92            
REMARK 500   O    HOH A   833     O    HOH A   883              1.96            
REMARK 500   O    ASN B   295     O    HOH B   850              1.97            
REMARK 500   O    ALA A   552     O    HOH A   801              1.97            
REMARK 500   O    GLN A   141     O    HOH A   861              1.98            
REMARK 500   O    ILE A   292     O    HOH A   832              2.02            
REMARK 500   OD1  ASN A   335     O    HOH A   826              2.07            
REMARK 500   O    SER A    31     O    HOH A   840              2.10            
REMARK 500   OD1  ASP A   507     O    HOH A   836              2.13            
REMARK 500   O    GLY A   428     O    HOH A   816              2.13            
REMARK 500   OH   TYR B   445     O    HOH B   859              2.15            
REMARK 500   O    ASN B   238     O    HOH B   835              2.16            
REMARK 500   O    HOH A   812     O    HOH A   852              2.17            
REMARK 500   OE2  GLU A   537     O    HOH A   825              2.18            
REMARK 500   O    PRO A   629     O    HOH A   819              2.19            
REMARK 500   ND1  HIS A   550     O    HOH A   860              2.19            
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 B  41      -52.01     68.43                                   
REMARK 500    CYS B  99      -74.43   -126.40                                   
REMARK 500    ASP B 176      115.78   -165.70                                   
REMARK 500    MET B 196       73.15   -103.31                                   
REMARK 500    PRO B 242       54.50    -91.46                                   
REMARK 500    PHE B 286       40.47   -106.50                                   
REMARK 500    ILE B 365      -62.13    -92.81                                   
REMARK 500    THR B 371      -55.18   -130.32                                   
REMARK 500    GLN B 413      -42.12   -130.25                                   
REMARK 500    LEU B 414      -71.25    -80.75                                   
REMARK 500    SER B 547      -81.12   -117.00                                   
REMARK 500    ALA B 567       67.46   -155.89                                   
REMARK 500    TYR B 620       74.40   -119.37                                   
REMARK 500    ASP A  41      -54.26     64.62                                   
REMARK 500    LYS A  42       -1.46     70.84                                   
REMARK 500    CYS A  99      -74.35   -120.06                                   
REMARK 500    PHE A 189       -8.94     70.47                                   
REMARK 500    ASN A 216     -158.42   -101.95                                   
REMARK 500    ILE A 365      -60.24    -98.77                                   
REMARK 500    HIS A 367      -75.50    -94.89                                   
REMARK 500    THR A 371      -53.24   -127.28                                   
REMARK 500    LEU A 414      -64.47    -90.23                                   
REMARK 500    TYR A 467       37.75    -94.85                                   
REMARK 500    ARG A 518       19.73     59.80                                   
REMARK 500    SER A 547      -82.08   -116.66                                   
REMARK 500    ALA A 567       69.73   -153.00                                   
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                             FE2 B 701  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE B 673   O                                                      
REMARK 620 2 HIS B 372   NE2  81.6                                              
REMARK 620 3 HIS B 550   NE2  73.2 101.4                                        
REMARK 620 4 HIS B 367   NE2 141.3 119.4 126.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 A 701  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE A 673   OXT                                                    
REMARK 620 2 ILE A 673   O    53.5                                              
REMARK 620 3 HIS A 372   NE2  80.4  61.4                                        
REMARK 620 4 HIS A 550   NE2  91.0  54.6 104.0                                  
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 FE2 B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 701                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3O8Y   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3V98   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3V99   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 UNP ENTRY P09917 RESIDUES 41-45 (PRO PHE TYR ASN ASP) WERE DELETED   
REMARK 999 AND REPLACED WITH RESIDUES GS(GLY SER)                               
DBREF  3V92 B    3   673  UNP    P09917   LOX5_HUMAN       1    674             
DBREF  3V92 A    3   673  UNP    P09917   LOX5_HUMAN       1    674             
SEQADV 3V92 MET B  -17  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 GLY B  -16  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 SER B  -15  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 SER B  -14  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 HIS B  -13  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 HIS B  -12  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 HIS B  -11  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 HIS B  -10  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 HIS B   -9  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 HIS B   -8  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 SER B   -7  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 SER B   -6  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 GLY B   -5  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 LEU B   -4  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 VAL B   -3  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 PRO B   -2  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 ARG B   -1  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 GLY B    0  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 SER B    1  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 HIS B    2  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 GLU B   16  UNP  P09917    TRP    14 ENGINEERED MUTATION            
SEQADV 3V92 HIS B   17  UNP  P09917    PHE    15 ENGINEERED MUTATION            
SEQADV 3V92 GLY B   43  UNP  P09917    ASN    44 SEE REMARK 999                 
SEQADV 3V92 SER B   44  UNP  P09917    ASP    45 SEE REMARK 999                 
SEQADV 3V92 GLY B   75  UNP  P09917    TRP    76 ENGINEERED MUTATION            
SEQADV 3V92 SER B   76  UNP  P09917    LEU    77 ENGINEERED MUTATION            
SEQADV 3V92 ALA B  240  UNP  P09917    CYS   241 ENGINEERED MUTATION            
SEQADV 3V92 ALA B  561  UNP  P09917    CYS   562 ENGINEERED MUTATION            
SEQADV 3V92 GLU B  653  UNP  P09917    LYS   654 ENGINEERED MUTATION            
SEQADV 3V92 ASN B  654  UNP  P09917    LYS   655 ENGINEERED MUTATION            
SEQADV 3V92 LEU B  655  UNP  P09917    LYS   656 ENGINEERED MUTATION            
SEQADV 3V92 ALA B  663  UNP  P09917    SER   664 ENGINEERED MUTATION            
SEQADV 3V92 MET A  -17  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 GLY A  -16  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 SER A  -15  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 SER A  -14  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 HIS A  -13  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 HIS A  -12  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 HIS A  -11  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 HIS A  -10  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 HIS A   -9  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 HIS A   -8  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 SER A   -7  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 SER A   -6  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 GLY A   -5  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 LEU A   -4  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 VAL A   -3  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 PRO A   -2  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 ARG A   -1  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 GLY A    0  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 SER A    1  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 HIS A    2  UNP  P09917              EXPRESSION TAG                 
SEQADV 3V92 GLU A   16  UNP  P09917    TRP    14 ENGINEERED MUTATION            
SEQADV 3V92 HIS A   17  UNP  P09917    PHE    15 ENGINEERED MUTATION            
SEQADV 3V92 GLY A   43  UNP  P09917    ASN    44 SEE REMARK 999                 
SEQADV 3V92 SER A   44  UNP  P09917    ASP    45 SEE REMARK 999                 
SEQADV 3V92 GLY A   75  UNP  P09917    TRP    76 ENGINEERED MUTATION            
SEQADV 3V92 SER A   76  UNP  P09917    LEU    77 ENGINEERED MUTATION            
SEQADV 3V92 ALA A  240  UNP  P09917    CYS   241 ENGINEERED MUTATION            
SEQADV 3V92 ALA A  561  UNP  P09917    CYS   562 ENGINEERED MUTATION            
SEQADV 3V92 GLU A  653  UNP  P09917    LYS   654 ENGINEERED MUTATION            
SEQADV 3V92 ASN A  654  UNP  P09917    LYS   655 ENGINEERED MUTATION            
SEQADV 3V92 LEU A  655  UNP  P09917    LYS   656 ENGINEERED MUTATION            
SEQADV 3V92 ALA A  663  UNP  P09917    SER   664 ENGINEERED MUTATION            
SEQRES   1 B  691  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  691  LEU VAL PRO ARG GLY SER HIS MET PRO SER TYR THR VAL          
SEQRES   3 B  691  THR VAL ALA THR GLY SER GLN GLU HIS ALA GLY THR ASP          
SEQRES   4 B  691  ASP TYR ILE TYR LEU SER LEU VAL GLY SER ALA GLY CYS          
SEQRES   5 B  691  SER GLU LYS HIS LEU LEU ASP LYS GLY SER PHE GLU ARG          
SEQRES   6 B  691  GLY ALA VAL ASP SER TYR ASP VAL THR VAL ASP GLU GLU          
SEQRES   7 B  691  LEU GLY GLU ILE GLN LEU VAL ARG ILE GLU LYS ARG LYS          
SEQRES   8 B  691  TYR GLY SER ASN ASP ASP TRP TYR LEU LYS TYR ILE THR          
SEQRES   9 B  691  LEU LYS THR PRO HIS GLY ASP TYR ILE GLU PHE PRO CYS          
SEQRES  10 B  691  TYR ARG TRP ILE THR GLY ASP VAL GLU VAL VAL LEU ARG          
SEQRES  11 B  691  ASP GLY ARG ALA LYS LEU ALA ARG ASP ASP GLN ILE HIS          
SEQRES  12 B  691  ILE LEU LYS GLN HIS ARG ARG LYS GLU LEU GLU THR ARG          
SEQRES  13 B  691  GLN LYS GLN TYR ARG TRP MET GLU TRP ASN PRO GLY PHE          
SEQRES  14 B  691  PRO LEU SER ILE ASP ALA LYS CYS HIS LYS ASP LEU PRO          
SEQRES  15 B  691  ARG ASP ILE GLN PHE ASP SER GLU LYS GLY VAL ASP PHE          
SEQRES  16 B  691  VAL LEU ASN TYR SER LYS ALA MET GLU ASN LEU PHE ILE          
SEQRES  17 B  691  ASN ARG PHE MET HIS MET PHE GLN SER SER TRP ASN ASP          
SEQRES  18 B  691  PHE ALA ASP PHE GLU LYS ILE PHE VAL LYS ILE SER ASN          
SEQRES  19 B  691  THR ILE SER GLU ARG VAL MET ASN HIS TRP GLN GLU ASP          
SEQRES  20 B  691  LEU MET PHE GLY TYR GLN PHE LEU ASN GLY ALA ASN PRO          
SEQRES  21 B  691  VAL LEU ILE ARG ARG CYS THR GLU LEU PRO GLU LYS LEU          
SEQRES  22 B  691  PRO VAL THR THR GLU MET VAL GLU CYS SER LEU GLU ARG          
SEQRES  23 B  691  GLN LEU SER LEU GLU GLN GLU VAL GLN GLN GLY ASN ILE          
SEQRES  24 B  691  PHE ILE VAL ASP PHE GLU LEU LEU ASP GLY ILE ASP ALA          
SEQRES  25 B  691  ASN LYS THR ASP PRO CYS THR LEU GLN PHE LEU ALA ALA          
SEQRES  26 B  691  PRO ILE CYS LEU LEU TYR LYS ASN LEU ALA ASN LYS ILE          
SEQRES  27 B  691  VAL PRO ILE ALA ILE GLN LEU ASN GLN ILE PRO GLY ASP          
SEQRES  28 B  691  GLU ASN PRO ILE PHE LEU PRO SER ASP ALA LYS TYR ASP          
SEQRES  29 B  691  TRP LEU LEU ALA LYS ILE TRP VAL ARG SER SER ASP PHE          
SEQRES  30 B  691  HIS VAL HIS GLN THR ILE THR HIS LEU LEU ARG THR HIS          
SEQRES  31 B  691  LEU VAL SER GLU VAL PHE GLY ILE ALA MET TYR ARG GLN          
SEQRES  32 B  691  LEU PRO ALA VAL HIS PRO ILE PHE LYS LEU LEU VAL ALA          
SEQRES  33 B  691  HIS VAL ARG PHE THR ILE ALA ILE ASN THR LYS ALA ARG          
SEQRES  34 B  691  GLU GLN LEU ILE CYS GLU CYS GLY LEU PHE ASP LYS ALA          
SEQRES  35 B  691  ASN ALA THR GLY GLY GLY GLY HIS VAL GLN MET VAL GLN          
SEQRES  36 B  691  ARG ALA MET LYS ASP LEU THR TYR ALA SER LEU CYS PHE          
SEQRES  37 B  691  PRO GLU ALA ILE LYS ALA ARG GLY MET GLU SER LYS GLU          
SEQRES  38 B  691  ASP ILE PRO TYR TYR PHE TYR ARG ASP ASP GLY LEU LEU          
SEQRES  39 B  691  VAL TRP GLU ALA ILE ARG THR PHE THR ALA GLU VAL VAL          
SEQRES  40 B  691  ASP ILE TYR TYR GLU GLY ASP GLN VAL VAL GLU GLU ASP          
SEQRES  41 B  691  PRO GLU LEU GLN ASP PHE VAL ASN ASP VAL TYR VAL TYR          
SEQRES  42 B  691  GLY MET ARG GLY ARG LYS SER SER GLY PHE PRO LYS SER          
SEQRES  43 B  691  VAL LYS SER ARG GLU GLN LEU SER GLU TYR LEU THR VAL          
SEQRES  44 B  691  VAL ILE PHE THR ALA SER ALA GLN HIS ALA ALA VAL ASN          
SEQRES  45 B  691  PHE GLY GLN TYR ASP TRP ALA SER TRP ILE PRO ASN ALA          
SEQRES  46 B  691  PRO PRO THR MET ARG ALA PRO PRO PRO THR ALA LYS GLY          
SEQRES  47 B  691  VAL VAL THR ILE GLU GLN ILE VAL ASP THR LEU PRO ASP          
SEQRES  48 B  691  ARG GLY ARG SER CYS TRP HIS LEU GLY ALA VAL TRP ALA          
SEQRES  49 B  691  LEU SER GLN PHE GLN GLU ASN GLU LEU PHE LEU GLY MET          
SEQRES  50 B  691  TYR PRO GLU GLU HIS PHE ILE GLU LYS PRO VAL LYS GLU          
SEQRES  51 B  691  ALA MET ALA ARG PHE ARG LYS ASN LEU GLU ALA ILE VAL          
SEQRES  52 B  691  SER VAL ILE ALA GLU ARG ASN GLU ASN LEU GLN LEU PRO          
SEQRES  53 B  691  TYR TYR TYR LEU ALA PRO ASP ARG ILE PRO ASN SER VAL          
SEQRES  54 B  691  ALA ILE                                                      
SEQRES   1 A  691  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  691  LEU VAL PRO ARG GLY SER HIS MET PRO SER TYR THR VAL          
SEQRES   3 A  691  THR VAL ALA THR GLY SER GLN GLU HIS ALA GLY THR ASP          
SEQRES   4 A  691  ASP TYR ILE TYR LEU SER LEU VAL GLY SER ALA GLY CYS          
SEQRES   5 A  691  SER GLU LYS HIS LEU LEU ASP LYS GLY SER PHE GLU ARG          
SEQRES   6 A  691  GLY ALA VAL ASP SER TYR ASP VAL THR VAL ASP GLU GLU          
SEQRES   7 A  691  LEU GLY GLU ILE GLN LEU VAL ARG ILE GLU LYS ARG LYS          
SEQRES   8 A  691  TYR GLY SER ASN ASP ASP TRP TYR LEU LYS TYR ILE THR          
SEQRES   9 A  691  LEU LYS THR PRO HIS GLY ASP TYR ILE GLU PHE PRO CYS          
SEQRES  10 A  691  TYR ARG TRP ILE THR GLY ASP VAL GLU VAL VAL LEU ARG          
SEQRES  11 A  691  ASP GLY ARG ALA LYS LEU ALA ARG ASP ASP GLN ILE HIS          
SEQRES  12 A  691  ILE LEU LYS GLN HIS ARG ARG LYS GLU LEU GLU THR ARG          
SEQRES  13 A  691  GLN LYS GLN TYR ARG TRP MET GLU TRP ASN PRO GLY PHE          
SEQRES  14 A  691  PRO LEU SER ILE ASP ALA LYS CYS HIS LYS ASP LEU PRO          
SEQRES  15 A  691  ARG ASP ILE GLN PHE ASP SER GLU LYS GLY VAL ASP PHE          
SEQRES  16 A  691  VAL LEU ASN TYR SER LYS ALA MET GLU ASN LEU PHE ILE          
SEQRES  17 A  691  ASN ARG PHE MET HIS MET PHE GLN SER SER TRP ASN ASP          
SEQRES  18 A  691  PHE ALA ASP PHE GLU LYS ILE PHE VAL LYS ILE SER ASN          
SEQRES  19 A  691  THR ILE SER GLU ARG VAL MET ASN HIS TRP GLN GLU ASP          
SEQRES  20 A  691  LEU MET PHE GLY TYR GLN PHE LEU ASN GLY ALA ASN PRO          
SEQRES  21 A  691  VAL LEU ILE ARG ARG CYS THR GLU LEU PRO GLU LYS LEU          
SEQRES  22 A  691  PRO VAL THR THR GLU MET VAL GLU CYS SER LEU GLU ARG          
SEQRES  23 A  691  GLN LEU SER LEU GLU GLN GLU VAL GLN GLN GLY ASN ILE          
SEQRES  24 A  691  PHE ILE VAL ASP PHE GLU LEU LEU ASP GLY ILE ASP ALA          
SEQRES  25 A  691  ASN LYS THR ASP PRO CYS THR LEU GLN PHE LEU ALA ALA          
SEQRES  26 A  691  PRO ILE CYS LEU LEU TYR LYS ASN LEU ALA ASN LYS ILE          
SEQRES  27 A  691  VAL PRO ILE ALA ILE GLN LEU ASN GLN ILE PRO GLY ASP          
SEQRES  28 A  691  GLU ASN PRO ILE PHE LEU PRO SER ASP ALA LYS TYR ASP          
SEQRES  29 A  691  TRP LEU LEU ALA LYS ILE TRP VAL ARG SER SER ASP PHE          
SEQRES  30 A  691  HIS VAL HIS GLN THR ILE THR HIS LEU LEU ARG THR HIS          
SEQRES  31 A  691  LEU VAL SER GLU VAL PHE GLY ILE ALA MET TYR ARG GLN          
SEQRES  32 A  691  LEU PRO ALA VAL HIS PRO ILE PHE LYS LEU LEU VAL ALA          
SEQRES  33 A  691  HIS VAL ARG PHE THR ILE ALA ILE ASN THR LYS ALA ARG          
SEQRES  34 A  691  GLU GLN LEU ILE CYS GLU CYS GLY LEU PHE ASP LYS ALA          
SEQRES  35 A  691  ASN ALA THR GLY GLY GLY GLY HIS VAL GLN MET VAL GLN          
SEQRES  36 A  691  ARG ALA MET LYS ASP LEU THR TYR ALA SER LEU CYS PHE          
SEQRES  37 A  691  PRO GLU ALA ILE LYS ALA ARG GLY MET GLU SER LYS GLU          
SEQRES  38 A  691  ASP ILE PRO TYR TYR PHE TYR ARG ASP ASP GLY LEU LEU          
SEQRES  39 A  691  VAL TRP GLU ALA ILE ARG THR PHE THR ALA GLU VAL VAL          
SEQRES  40 A  691  ASP ILE TYR TYR GLU GLY ASP GLN VAL VAL GLU GLU ASP          
SEQRES  41 A  691  PRO GLU LEU GLN ASP PHE VAL ASN ASP VAL TYR VAL TYR          
SEQRES  42 A  691  GLY MET ARG GLY ARG LYS SER SER GLY PHE PRO LYS SER          
SEQRES  43 A  691  VAL LYS SER ARG GLU GLN LEU SER GLU TYR LEU THR VAL          
SEQRES  44 A  691  VAL ILE PHE THR ALA SER ALA GLN HIS ALA ALA VAL ASN          
SEQRES  45 A  691  PHE GLY GLN TYR ASP TRP ALA SER TRP ILE PRO ASN ALA          
SEQRES  46 A  691  PRO PRO THR MET ARG ALA PRO PRO PRO THR ALA LYS GLY          
SEQRES  47 A  691  VAL VAL THR ILE GLU GLN ILE VAL ASP THR LEU PRO ASP          
SEQRES  48 A  691  ARG GLY ARG SER CYS TRP HIS LEU GLY ALA VAL TRP ALA          
SEQRES  49 A  691  LEU SER GLN PHE GLN GLU ASN GLU LEU PHE LEU GLY MET          
SEQRES  50 A  691  TYR PRO GLU GLU HIS PHE ILE GLU LYS PRO VAL LYS GLU          
SEQRES  51 A  691  ALA MET ALA ARG PHE ARG LYS ASN LEU GLU ALA ILE VAL          
SEQRES  52 A  691  SER VAL ILE ALA GLU ARG ASN GLU ASN LEU GLN LEU PRO          
SEQRES  53 A  691  TYR TYR TYR LEU ALA PRO ASP ARG ILE PRO ASN SER VAL          
SEQRES  54 A  691  ALA ILE                                                      
HET    FE2  B 701       1                                                       
HET    FE2  A 701       1                                                       
HETNAM     FE2 FE (II) ION                                                      
FORMUL   3  FE2    2(FE 2+)                                                     
FORMUL   5  HOH   *161(H2 O)                                                    
HELIX    1   1 LEU B  118  ASP B  122  5                                   5    
HELIX    2   2 ILE B  124  TYR B  142  1                                  19    
HELIX    3   3 CYS B  159  LEU B  163  5                                   5    
HELIX    4   4 PRO B  164  GLN B  168  5                                   5    
HELIX    5   5 ASP B  176  LEU B  188  1                                  13    
HELIX    6   6 ILE B  190  MET B  194  5                                   5    
HELIX    7   7 ASP B  203  SER B  215  1                                  13    
HELIX    8   8 ASN B  216  TRP B  226  1                                  11    
HELIX    9   9 GLU B  228  GLY B  239  1                                  12    
HELIX   10  10 THR B  258  GLU B  263  1                                   6    
HELIX   11  11 SER B  271  GLN B  278  1                                   8    
HELIX   12  12 GLU B  287  ASP B  290  5                                   4    
HELIX   13  13 ALA B  343  ILE B  365  1                                  23    
HELIX   14  14 THR B  371  LEU B  386  1                                  16    
HELIX   15  15 HIS B  390  VAL B  397  1                                   8    
HELIX   16  16 ALA B  398  VAL B  400  5                                   3    
HELIX   17  17 PHE B  402  LEU B  414  1                                  13    
HELIX   18  18 LEU B  420  ASN B  425  1                                   6    
HELIX   19  19 GLY B  430  LYS B  441  1                                  12    
HELIX   20  20 TYR B  445  LEU B  448  5                                   4    
HELIX   21  21 CYS B  449  ALA B  456  1                                   8    
HELIX   22  22 TYR B  468  TYR B  493  1                                  26    
HELIX   23  23 GLY B  495  ASP B  502  1                                   8    
HELIX   24  24 ASP B  502  TYR B  515  1                                  14    
HELIX   25  25 ARG B  520  GLY B  524  5                                   5    
HELIX   26  26 SER B  531  SER B  547  1                                  17    
HELIX   27  27 SER B  547  VAL B  553  1                                   7    
HELIX   28  28 GLY B  556  SER B  562  1                                   7    
HELIX   29  29 TRP B  563  ALA B  567  5                                   5    
HELIX   30  30 THR B  583  LEU B  591  1                                   9    
HELIX   31  31 ASP B  593  LEU B  607  1                                  15    
HELIX   32  32 GLU B  627  ASN B  654  1                                  28    
HELIX   33  33 LEU A  118  ASP A  122  5                                   5    
HELIX   34  34 ILE A  124  TYR A  142  1                                  19    
HELIX   35  35 CYS A  159  LEU A  163  5                                   5    
HELIX   36  36 PRO A  164  GLN A  168  5                                   5    
HELIX   37  37 ASP A  176  LEU A  188  1                                  13    
HELIX   38  38 ASP A  203  SER A  215  1                                  13    
HELIX   39  39 ASN A  216  TRP A  226  1                                  11    
HELIX   40  40 GLU A  228  GLY A  239  1                                  12    
HELIX   41  41 THR A  258  GLU A  263  1                                   6    
HELIX   42  42 SER A  271  GLN A  277  1                                   7    
HELIX   43  43 GLU A  287  ASP A  290  5                                   4    
HELIX   44  44 ALA A  343  ILE A  365  1                                  23    
HELIX   45  45 THR A  371  LEU A  386  1                                  16    
HELIX   46  46 HIS A  390  VAL A  397  1                                   8    
HELIX   47  47 ALA A  398  VAL A  400  5                                   3    
HELIX   48  48 PHE A  402  LEU A  414  1                                  13    
HELIX   49  49 LEU A  420  ASN A  425  1                                   6    
HELIX   50  50 GLY A  430  LYS A  441  1                                  12    
HELIX   51  51 THR A  444  CYS A  449  1                                   6    
HELIX   52  52 CYS A  449  ARG A  457  1                                   9    
HELIX   53  53 TYR A  468  TYR A  493  1                                  26    
HELIX   54  54 GLY A  495  GLU A  501  1                                   7    
HELIX   55  55 ASP A  502  TYR A  515  1                                  14    
HELIX   56  56 ARG A  520  GLY A  524  5                                   5    
HELIX   57  57 SER A  531  SER A  547  1                                  17    
HELIX   58  58 SER A  547  PHE A  555  1                                   9    
HELIX   59  59 GLY A  556  SER A  562  1                                   7    
HELIX   60  60 TRP A  563  ALA A  567  5                                   5    
HELIX   61  61 THR A  583  LEU A  591  1                                   9    
HELIX   62  62 ASP A  593  SER A  608  1                                  16    
HELIX   63  63 GLU A  627  GLU A  653  1                                  27    
HELIX   64  64 ALA A  663  ILE A  667  5                                   5    
SHEET    1   A 4 VAL B  50  THR B  56  0                                        
SHEET    2   A 4 SER B   5  THR B  12 -1  N  VAL B  10   O  ASP B  51           
SHEET    3   A 4 TRP B  80  LYS B  88 -1  O  LYS B  83   N  ALA B  11           
SHEET    4   A 4 TYR B  94  ILE B 103 -1  O  ILE B 103   N  TRP B  80           
SHEET    1   B 4 HIS B  38  LEU B  40  0                                        
SHEET    2   B 4 TYR B  23  GLY B  30 -1  N  LEU B  26   O  HIS B  38           
SHEET    3   B 4 ILE B  64  ARG B  72 -1  O  GLU B  70   N  TYR B  25           
SHEET    4   B 4 GLU B 108  LEU B 111 -1  O  VAL B 109   N  ILE B  69           
SHEET    1   C 2 TRP B 144  MET B 145  0                                        
SHEET    2   C 2 SER B 154  ILE B 155 -1  O  SER B 154   N  MET B 145           
SHEET    1   D 5 ARG B 246  ARG B 247  0                                        
SHEET    2   D 5 ILE B 281  ASP B 285 -1  O  ILE B 283   N  ARG B 246           
SHEET    3   D 5 ILE B 309  LYS B 314 -1  O  LEU B 312   N  PHE B 282           
SHEET    4   D 5 ILE B 320  GLN B 326 -1  O  GLN B 326   N  ILE B 309           
SHEET    5   D 5 ILE B 337  PHE B 338 -1  O  PHE B 338   N  ILE B 325           
SHEET    1   E 5 HIS A -11  HIS A  -9  0                                        
SHEET    2   E 5 VAL A  50  THR A  56  1  O  SER A  52   N  HIS A  -9           
SHEET    3   E 5 SER A   5  THR A  12 -1  N  TYR A   6   O  VAL A  55           
SHEET    4   E 5 TRP A  80  LYS A  88 -1  O  LYS A  83   N  ALA A  11           
SHEET    5   E 5 TYR A  94  ILE A 103 -1  O  ILE A 103   N  TRP A  80           
SHEET    1   F 3 GLY A  33  CYS A  34  0                                        
SHEET    2   F 3 TYR A  23  GLY A  30 -1  N  GLY A  30   O  GLY A  33           
SHEET    3   F 3 HIS A  38  LEU A  40 -1  O  HIS A  38   N  LEU A  26           
SHEET    1   G 4 GLY A  33  CYS A  34  0                                        
SHEET    2   G 4 TYR A  23  GLY A  30 -1  N  GLY A  30   O  GLY A  33           
SHEET    3   G 4 ILE A  64  ARG A  72 -1  O  GLU A  70   N  TYR A  25           
SHEET    4   G 4 GLU A 108  LEU A 111 -1  O  VAL A 109   N  ILE A  69           
SHEET    1   H 2 TRP A 144  MET A 145  0                                        
SHEET    2   H 2 SER A 154  ILE A 155 -1  O  SER A 154   N  MET A 145           
SHEET    1   I 5 ARG A 246  ARG A 247  0                                        
SHEET    2   I 5 ILE A 281  ASP A 285 -1  O  ILE A 283   N  ARG A 246           
SHEET    3   I 5 ILE A 309  LYS A 314 -1  O  LEU A 312   N  PHE A 282           
SHEET    4   I 5 ILE A 320  GLN A 326 -1  O  ALA A 324   N  LEU A 311           
SHEET    5   I 5 ILE A 337  PHE A 338 -1  O  PHE A 338   N  ILE A 325           
LINK         O   ILE B 673                FE   FE2 B 701     1555   1555  2.32  
LINK         OXT ILE A 673                FE   FE2 A 701     1555   1555  2.33  
LINK         O   ILE A 673                FE   FE2 A 701     1555   1555  2.46  
LINK         NE2 HIS A 372                FE   FE2 A 701     1555   1555  2.48  
LINK         NE2 HIS B 372                FE   FE2 B 701     1555   1555  2.53  
LINK         NE2 HIS B 550                FE   FE2 B 701     1555   1555  2.54  
LINK         NE2 HIS A 550                FE   FE2 A 701     1555   1555  2.61  
LINK         NE2 HIS B 367                FE   FE2 B 701     1555   1555  2.65  
SITE     1 AC1  5 HIS B 367  HIS B 372  HIS B 550  ASN B 554                    
SITE     2 AC1  5 ILE B 673                                                     
SITE     1 AC2  5 HIS A 367  HIS A 372  HIS A 550  ASN A 554                    
SITE     2 AC2  5 ILE A 673                                                     
CRYST1   55.191  202.375   76.986  90.00 109.91  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018119  0.000000  0.006563        0.00000                         
SCALE2      0.000000  0.004941  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013815        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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