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Database: PDB
Entry: 3AK3
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Original site: 3AK3 
HEADER    OXIDOREDUCTASE                          30-JUN-10   3AK3              
TITLE     SUPEROXIDE DISMUTASE FROM AEROPYRUM PERNIX K1, FE-BOUND FORM          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [MN/FE];                              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AEROPYRUM PERNIX;                               
SOURCE   3 ORGANISM_TAXID: 272557;                                              
SOURCE   4 STRAIN: K1;                                                          
SOURCE   5 GENE: APE0741;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3);                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET11                                     
KEYWDS    SUPEROXIDE DISMUTASE, CAMBIALISTIC, OXIDOREDUCTASE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.NAKAMURA,K.UEGAKI                                                   
REVDAT   2   23-FEB-11 3AK3    1       JRNL                                     
REVDAT   1   02-FEB-11 3AK3    0                                                
JRNL        AUTH   T.NAKAMURA,K.TORIKAI,K.UEGAKI,J.MORITA,K.MACHIDA,A.SUZUKI,   
JRNL        AUTH 2 Y.KAWATA                                                     
JRNL        TITL   CRYSTAL STRUCTURE OF THE CAMBIALISTIC SUPEROXIDE DISMUTASE   
JRNL        TITL 2 FROM AEROPYRUM PERNIX K1 - INSIGHTS INTO THE ENZYME          
JRNL        TITL 3 MECHANISM AND STABILITY                                      
JRNL        REF    FEBS J.                       V. 278   598 2011              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        PMID   21182595                                                     
JRNL        DOI    10.1111/J.1742-4658.2010.07977.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.48 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.48                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.75                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 113539                         
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) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5993                            
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) : 1.48                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.52                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7965                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.93                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2950                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 429                          
REMARK   3   BIN FREE R VALUE                    : 0.3270                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6855                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 44                                      
REMARK   3   SOLVENT ATOMS            : 417                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.32                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.46                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.101         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.099         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.071         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.883         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7090 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9602 ; 1.143 ; 1.941       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   839 ; 6.114 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   344 ;36.240 ;24.302       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1180 ;12.941 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;15.700 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   997 ; 0.079 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5440 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3788 ; 0.201 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4858 ; 0.309 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   486 ; 0.128 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     3 ; 0.049 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    36 ; 0.156 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    13 ; 0.193 ; 0.200       
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):  4325 ; 0.694 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6747 ; 0.873 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3245 ; 1.444 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2855 ; 2.103 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3AK3 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-JUL-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB029349.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-FEB-10                          
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               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL44XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 119558                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.480                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3AK1                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES, 10% PEG 6000, 8% ETHYLENE   
REMARK 280  GLYCOL, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K     
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       35.87750            
REMARK 290   SMTRY3   2  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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15760 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 26960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     LEU A   211                                                      
REMARK 465     LEU A   212                                                      
REMARK 465     PRO A   213                                                      
REMARK 465     GLN A   214                                                      
REMARK 465     GLN B   214                                                      
REMARK 465     LEU C   211                                                      
REMARK 465     LEU C   212                                                      
REMARK 465     PRO C   213                                                      
REMARK 465     GLN C   214                                                      
REMARK 465     LEU D   211                                                      
REMARK 465     LEU D   212                                                      
REMARK 465     PRO D   213                                                      
REMARK 465     GLN D   214                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   225     O    HOH B   251              2.07            
REMARK 500   O    HOH B   234     O    HOH B   251              2.09            
REMARK 500   O    LEU C   209     O    HOH C   238              2.14            
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    LYS A  34      -60.26   -100.65                                   
REMARK 500    LYS A 149     -127.55     48.27                                   
REMARK 500    ASN A 151       33.98   -147.81                                   
REMARK 500    LEU A 153      -16.81     79.60                                   
REMARK 500    TYR A 171      -20.85   -140.11                                   
REMARK 500    LYS A 176     -135.85     52.46                                   
REMARK 500    SER B   3     -116.73     87.59                                   
REMARK 500    LYS B  34      -61.41   -107.43                                   
REMARK 500    LYS B 149     -128.01     46.32                                   
REMARK 500    ASN B 151       33.13   -145.60                                   
REMARK 500    LEU B 153      -15.21     79.38                                   
REMARK 500    TYR B 171      -20.16   -143.70                                   
REMARK 500    LYS B 176     -134.94     55.36                                   
REMARK 500    LYS C  34      -60.54    -96.19                                   
REMARK 500    LYS C 149     -124.85     48.17                                   
REMARK 500    ASN C 151       31.51   -146.53                                   
REMARK 500    LEU C 153      -13.06     81.61                                   
REMARK 500    TYR C 171      -16.97   -147.30                                   
REMARK 500    LYS C 176     -134.99     53.55                                   
REMARK 500    LYS D  34      -60.90    -99.79                                   
REMARK 500    LYS D 149     -128.69     50.90                                   
REMARK 500    ASN D 151       31.99   -148.57                                   
REMARK 500    LEU D 153      -12.81     78.52                                   
REMARK 500    TYR D 171      -17.83   -145.40                                   
REMARK 500    LYS D 176     -132.20     52.82                                   
REMARK 500    LEU D 209      -22.92   -145.73                                   
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                              FE C 215  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 165   OD2                                                    
REMARK 620 2 HIS C  31   NE2  81.7                                              
REMARK 620 3 HIS C  79   NE2  94.3  90.9                                        
REMARK 620 4 HIS C 169   NE2 113.0  94.1 152.6                                  
REMARK 620 5 HOH C 253   O   171.6  99.0  77.3  75.3                            
REMARK 620 6 HOH C 219   O    86.1 167.7  92.0  88.8  93.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A 215  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 165   OD2                                                    
REMARK 620 2 HIS A  79   NE2 101.2                                              
REMARK 620 3 HIS A 169   NE2 110.3 148.4                                        
REMARK 620 4 HIS A  31   NE2  81.8  90.7  90.6                                  
REMARK 620 5 HOH A 217   O    88.4  93.2  90.9 170.0                            
REMARK 620 6 HOH A 288   O   174.0  74.1  74.3  94.3  95.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE D 215  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 165   OD2                                                    
REMARK 620 2 HIS D  31   NE2  83.7                                              
REMARK 620 3 HIS D 169   NE2 111.7  90.8                                        
REMARK 620 4 HIS D  79   NE2  96.0  91.4 152.3                                  
REMARK 620 5 HOH D 219   O    84.9 168.5  92.2  91.1                            
REMARK 620 6 HOH D 267   O   173.1  93.9  74.7  77.5  97.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 215  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 165   OD2                                                    
REMARK 620 2 HIS B  31   NE2  81.7                                              
REMARK 620 3 HIS B  79   NE2  97.9  93.1                                        
REMARK 620 4 HIS B 169   NE2 109.3  88.6 152.7                                  
REMARK 620 5 HOH B 221   O    91.6 171.9  92.3  89.3                            
REMARK 620 6 HOH B 250   O   176.0  98.7  78.1  74.7  88.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 215                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 216                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 215                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 216                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 217                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 218                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 219                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 220                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE C 215                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 216                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE D 215                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 216                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 217                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 218                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3AK1   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN, APO-FORM                                               
REMARK 900 RELATED ID: 3AK2   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN, MN-BOUND FORM                                          
DBREF  3AK3 A    1   214  UNP    Q9Y8H8   SODF_AERPE       1    214             
DBREF  3AK3 B    1   214  UNP    Q9Y8H8   SODF_AERPE       1    214             
DBREF  3AK3 C    1   214  UNP    Q9Y8H8   SODF_AERPE       1    214             
DBREF  3AK3 D    1   214  UNP    Q9Y8H8   SODF_AERPE       1    214             
SEQRES   1 A  214  MET VAL SER PHE LYS ARG TYR GLU LEU PRO PRO LEU PRO          
SEQRES   2 A  214  TYR ASN TYR ASN ALA LEU GLU PRO TYR ILE ILE GLU GLU          
SEQRES   3 A  214  ILE MET LYS LEU HIS HIS GLN LYS HIS HIS ASN THR TYR          
SEQRES   4 A  214  VAL LYS GLY ALA ASN ALA ALA LEU GLU LYS ILE GLU LYS          
SEQRES   5 A  214  HIS LEU LYS GLY GLU ILE GLN ILE ASP VAL ARG ALA VAL          
SEQRES   6 A  214  MET ARG ASP PHE SER PHE ASN TYR ALA GLY HIS ILE MET          
SEQRES   7 A  214  HIS THR ILE PHE TRP PRO ASN MET ALA PRO PRO GLY LYS          
SEQRES   8 A  214  GLY GLY GLY THR PRO GLY GLY ARG VAL ALA ASP LEU ILE          
SEQRES   9 A  214  GLU LYS GLN PHE GLY GLY PHE GLU LYS PHE LYS ALA LEU          
SEQRES  10 A  214  PHE SER ALA ALA ALA LYS THR VAL GLU GLY VAL GLY TRP          
SEQRES  11 A  214  GLY VAL LEU ALA PHE ASP PRO LEU THR GLU GLU LEU ARG          
SEQRES  12 A  214  ILE LEU GLN VAL GLU LYS HIS ASN VAL LEU MET THR ALA          
SEQRES  13 A  214  GLY LEU VAL PRO ILE LEU VAL ILE ASP VAL TRP GLU HIS          
SEQRES  14 A  214  ALA TYR TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR          
SEQRES  15 A  214  VAL GLU ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL          
SEQRES  16 A  214  GLU LYS ARG LEU GLU GLN ALA LEU ASN ASN ALA LYS PRO          
SEQRES  17 A  214  LEU TYR LEU LEU PRO GLN                                      
SEQRES   1 B  214  MET VAL SER PHE LYS ARG TYR GLU LEU PRO PRO LEU PRO          
SEQRES   2 B  214  TYR ASN TYR ASN ALA LEU GLU PRO TYR ILE ILE GLU GLU          
SEQRES   3 B  214  ILE MET LYS LEU HIS HIS GLN LYS HIS HIS ASN THR TYR          
SEQRES   4 B  214  VAL LYS GLY ALA ASN ALA ALA LEU GLU LYS ILE GLU LYS          
SEQRES   5 B  214  HIS LEU LYS GLY GLU ILE GLN ILE ASP VAL ARG ALA VAL          
SEQRES   6 B  214  MET ARG ASP PHE SER PHE ASN TYR ALA GLY HIS ILE MET          
SEQRES   7 B  214  HIS THR ILE PHE TRP PRO ASN MET ALA PRO PRO GLY LYS          
SEQRES   8 B  214  GLY GLY GLY THR PRO GLY GLY ARG VAL ALA ASP LEU ILE          
SEQRES   9 B  214  GLU LYS GLN PHE GLY GLY PHE GLU LYS PHE LYS ALA LEU          
SEQRES  10 B  214  PHE SER ALA ALA ALA LYS THR VAL GLU GLY VAL GLY TRP          
SEQRES  11 B  214  GLY VAL LEU ALA PHE ASP PRO LEU THR GLU GLU LEU ARG          
SEQRES  12 B  214  ILE LEU GLN VAL GLU LYS HIS ASN VAL LEU MET THR ALA          
SEQRES  13 B  214  GLY LEU VAL PRO ILE LEU VAL ILE ASP VAL TRP GLU HIS          
SEQRES  14 B  214  ALA TYR TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR          
SEQRES  15 B  214  VAL GLU ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL          
SEQRES  16 B  214  GLU LYS ARG LEU GLU GLN ALA LEU ASN ASN ALA LYS PRO          
SEQRES  17 B  214  LEU TYR LEU LEU PRO GLN                                      
SEQRES   1 C  214  MET VAL SER PHE LYS ARG TYR GLU LEU PRO PRO LEU PRO          
SEQRES   2 C  214  TYR ASN TYR ASN ALA LEU GLU PRO TYR ILE ILE GLU GLU          
SEQRES   3 C  214  ILE MET LYS LEU HIS HIS GLN LYS HIS HIS ASN THR TYR          
SEQRES   4 C  214  VAL LYS GLY ALA ASN ALA ALA LEU GLU LYS ILE GLU LYS          
SEQRES   5 C  214  HIS LEU LYS GLY GLU ILE GLN ILE ASP VAL ARG ALA VAL          
SEQRES   6 C  214  MET ARG ASP PHE SER PHE ASN TYR ALA GLY HIS ILE MET          
SEQRES   7 C  214  HIS THR ILE PHE TRP PRO ASN MET ALA PRO PRO GLY LYS          
SEQRES   8 C  214  GLY GLY GLY THR PRO GLY GLY ARG VAL ALA ASP LEU ILE          
SEQRES   9 C  214  GLU LYS GLN PHE GLY GLY PHE GLU LYS PHE LYS ALA LEU          
SEQRES  10 C  214  PHE SER ALA ALA ALA LYS THR VAL GLU GLY VAL GLY TRP          
SEQRES  11 C  214  GLY VAL LEU ALA PHE ASP PRO LEU THR GLU GLU LEU ARG          
SEQRES  12 C  214  ILE LEU GLN VAL GLU LYS HIS ASN VAL LEU MET THR ALA          
SEQRES  13 C  214  GLY LEU VAL PRO ILE LEU VAL ILE ASP VAL TRP GLU HIS          
SEQRES  14 C  214  ALA TYR TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR          
SEQRES  15 C  214  VAL GLU ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL          
SEQRES  16 C  214  GLU LYS ARG LEU GLU GLN ALA LEU ASN ASN ALA LYS PRO          
SEQRES  17 C  214  LEU TYR LEU LEU PRO GLN                                      
SEQRES   1 D  214  MET VAL SER PHE LYS ARG TYR GLU LEU PRO PRO LEU PRO          
SEQRES   2 D  214  TYR ASN TYR ASN ALA LEU GLU PRO TYR ILE ILE GLU GLU          
SEQRES   3 D  214  ILE MET LYS LEU HIS HIS GLN LYS HIS HIS ASN THR TYR          
SEQRES   4 D  214  VAL LYS GLY ALA ASN ALA ALA LEU GLU LYS ILE GLU LYS          
SEQRES   5 D  214  HIS LEU LYS GLY GLU ILE GLN ILE ASP VAL ARG ALA VAL          
SEQRES   6 D  214  MET ARG ASP PHE SER PHE ASN TYR ALA GLY HIS ILE MET          
SEQRES   7 D  214  HIS THR ILE PHE TRP PRO ASN MET ALA PRO PRO GLY LYS          
SEQRES   8 D  214  GLY GLY GLY THR PRO GLY GLY ARG VAL ALA ASP LEU ILE          
SEQRES   9 D  214  GLU LYS GLN PHE GLY GLY PHE GLU LYS PHE LYS ALA LEU          
SEQRES  10 D  214  PHE SER ALA ALA ALA LYS THR VAL GLU GLY VAL GLY TRP          
SEQRES  11 D  214  GLY VAL LEU ALA PHE ASP PRO LEU THR GLU GLU LEU ARG          
SEQRES  12 D  214  ILE LEU GLN VAL GLU LYS HIS ASN VAL LEU MET THR ALA          
SEQRES  13 D  214  GLY LEU VAL PRO ILE LEU VAL ILE ASP VAL TRP GLU HIS          
SEQRES  14 D  214  ALA TYR TYR LEU GLN TYR LYS ASN ASP ARG GLY SER TYR          
SEQRES  15 D  214  VAL GLU ASN TRP TRP ASN VAL VAL ASN TRP ASP ASP VAL          
SEQRES  16 D  214  GLU LYS ARG LEU GLU GLN ALA LEU ASN ASN ALA LYS PRO          
SEQRES  17 D  214  LEU TYR LEU LEU PRO GLN                                      
HET     FE  A 215       1                                                       
HET    EDO  A 216       4                                                       
HET     FE  B 215       1                                                       
HET    EDO  B 216       4                                                       
HET    EDO  B 217       4                                                       
HET    EDO  B 218       4                                                       
HET    EDO  B 219       4                                                       
HET    EDO  B 220       4                                                       
HET     FE  C 215       1                                                       
HET    EDO  C 216       4                                                       
HET     FE  D 215       1                                                       
HET    EDO  D 216       4                                                       
HET    EDO  D 217       4                                                       
HET    EDO  D 218       4                                                       
HETNAM      FE FE (III) ION                                                     
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5   FE    4(FE 3+)                                                     
FORMUL   6  EDO    10(C2 H6 O2)                                                 
FORMUL  19  HOH   *417(H2 O)                                                    
HELIX    1   1 ILE A   24  LYS A   34  1                                  11    
HELIX    2   2 LYS A   34  LYS A   55  1                                  22    
HELIX    3   3 ASP A   61  TRP A   83  1                                  23    
HELIX    4   4 GLY A   97  GLY A  109  1                                  13    
HELIX    5   5 GLY A  110  THR A  124  1                                  15    
HELIX    6   6 TRP A  167  ALA A  170  5                                   4    
HELIX    7   7 TYR A  171  LYS A  176  1                                   6    
HELIX    8   8 ASP A  178  TRP A  187  1                                  10    
HELIX    9   9 ASN A  188  VAL A  190  5                                   3    
HELIX   10  10 ASN A  191  ALA A  206  1                                  16    
HELIX   11  11 LYS A  207  TYR A  210  5                                   4    
HELIX   12  12 ILE B   24  LYS B   34  1                                  11    
HELIX   13  13 LYS B   34  LYS B   55  1                                  22    
HELIX   14  14 ASP B   61  TRP B   83  1                                  23    
HELIX   15  15 GLY B   97  GLY B  109  1                                  13    
HELIX   16  16 GLY B  110  THR B  124  1                                  15    
HELIX   17  17 TRP B  167  ALA B  170  5                                   4    
HELIX   18  18 TYR B  171  LYS B  176  1                                   6    
HELIX   19  19 ASP B  178  TRP B  187  1                                  10    
HELIX   20  20 ASN B  188  VAL B  190  5                                   3    
HELIX   21  21 ASN B  191  ALA B  206  1                                  16    
HELIX   22  22 LYS B  207  TYR B  210  5                                   4    
HELIX   23  23 ILE C   24  LYS C   34  1                                  11    
HELIX   24  24 LYS C   34  LYS C   55  1                                  22    
HELIX   25  25 ASP C   61  TRP C   83  1                                  23    
HELIX   26  26 GLY C   97  GLY C  109  1                                  13    
HELIX   27  27 GLY C  110  THR C  124  1                                  15    
HELIX   28  28 TRP C  167  ALA C  170  5                                   4    
HELIX   29  29 TYR C  171  LYS C  176  1                                   6    
HELIX   30  30 ASP C  178  TRP C  187  1                                  10    
HELIX   31  31 ASN C  188  VAL C  190  5                                   3    
HELIX   32  32 ASN C  191  ALA C  206  1                                  16    
HELIX   33  33 ILE D   24  LYS D   34  1                                  11    
HELIX   34  34 LYS D   34  LYS D   55  1                                  22    
HELIX   35  35 ASP D   61  TRP D   83  1                                  23    
HELIX   36  36 GLY D   97  GLY D  109  1                                  13    
HELIX   37  37 GLY D  110  THR D  124  1                                  15    
HELIX   38  38 TRP D  167  ALA D  170  5                                   4    
HELIX   39  39 TYR D  171  LYS D  176  1                                   6    
HELIX   40  40 ASP D  178  TRP D  187  1                                  10    
HELIX   41  41 ASN D  188  VAL D  190  5                                   3    
HELIX   42  42 ASN D  191  ALA D  206  1                                  16    
SHEET    1   A 3 GLU A 141  GLU A 148  0                                        
SHEET    2   A 3 GLY A 129  ASP A 136 -1  N  ASP A 136   O  GLU A 141           
SHEET    3   A 3 VAL A 159  ASP A 165 -1  O  ILE A 161   N  LEU A 133           
SHEET    1   B 3 GLU B 141  GLU B 148  0                                        
SHEET    2   B 3 GLY B 129  ASP B 136 -1  N  ALA B 134   O  ARG B 143           
SHEET    3   B 3 VAL B 159  ASP B 165 -1  O  LEU B 162   N  LEU B 133           
SHEET    1   C 3 LEU C 142  GLU C 148  0                                        
SHEET    2   C 3 GLY C 129  PHE C 135 -1  N  ALA C 134   O  ARG C 143           
SHEET    3   C 3 VAL C 159  ASP C 165 -1  O  LEU C 162   N  LEU C 133           
SHEET    1   D 3 LEU D 142  GLU D 148  0                                        
SHEET    2   D 3 GLY D 129  PHE D 135 -1  N  ALA D 134   O  ARG D 143           
SHEET    3   D 3 VAL D 159  ASP D 165 -1  O  ILE D 161   N  LEU D 133           
LINK         OD2 ASP C 165                FE    FE C 215     1555   1555  1.88  
LINK         OD2 ASP A 165                FE    FE A 215     1555   1555  1.93  
LINK         OD2 ASP D 165                FE    FE D 215     1555   1555  2.00  
LINK         OD2 ASP B 165                FE    FE B 215     1555   1555  2.01  
LINK         NE2 HIS B  31                FE    FE B 215     1555   1555  2.13  
LINK         NE2 HIS A  79                FE    FE A 215     1555   1555  2.14  
LINK         NE2 HIS D  31                FE    FE D 215     1555   1555  2.15  
LINK         NE2 HIS C  31                FE    FE C 215     1555   1555  2.16  
LINK         NE2 HIS A 169                FE    FE A 215     1555   1555  2.17  
LINK         NE2 HIS D 169                FE    FE D 215     1555   1555  2.18  
LINK         NE2 HIS A  31                FE    FE A 215     1555   1555  2.18  
LINK         NE2 HIS B  79                FE    FE B 215     1555   1555  2.19  
LINK         NE2 HIS B 169                FE    FE B 215     1555   1555  2.20  
LINK         NE2 HIS C  79                FE    FE C 215     1555   1555  2.22  
LINK         NE2 HIS D  79                FE    FE D 215     1555   1555  2.22  
LINK         NE2 HIS C 169                FE    FE C 215     1555   1555  2.31  
LINK        FE    FE C 215                 O   HOH C 253     1555   1555  1.95  
LINK        FE    FE C 215                 O   HOH C 219     1555   1555  2.00  
LINK        FE    FE D 215                 O   HOH D 219     1555   1555  2.04  
LINK        FE    FE B 215                 O   HOH B 221     1555   1555  2.07  
LINK        FE    FE A 215                 O   HOH A 217     1555   1555  2.10  
LINK        FE    FE A 215                 O   HOH A 288     1555   1555  2.22  
LINK        FE    FE D 215                 O   HOH D 267     1555   1555  2.24  
LINK        FE    FE B 215                 O   HOH B 250     1555   1555  2.26  
CISPEP   1 GLU A   20    PRO A   21          0         4.60                     
CISPEP   2 GLU B   20    PRO B   21          0         4.23                     
CISPEP   3 GLU C   20    PRO C   21          0         7.12                     
CISPEP   4 GLU D   20    PRO D   21          0         1.91                     
SITE     1 AC1  6 HIS A  31  HIS A  79  ASP A 165  HIS A 169                    
SITE     2 AC1  6 HOH A 217  HOH A 288                                          
SITE     1 AC2  5 GLU A 148  LYS A 149  HOH A 394  GLU C 148                    
SITE     2 AC2  5 VAL C 152                                                     
SITE     1 AC3  6 HIS B  31  HIS B  79  ASP B 165  HIS B 169                    
SITE     2 AC3  6 HOH B 221  HOH B 250                                          
SITE     1 AC4  4 PRO B  21  ASN B 185  HOH B 305  HOH B 424                    
SITE     1 AC5  5 LYS B  49  ILE B  60  ASP B  61  VAL B  65                    
SITE     2 AC5  5 HOH B 297                                                     
SITE     1 AC6  9 LEU A 153  ARG B  67  LYS B 149  ASN B 151                    
SITE     2 AC6  9 HOH B 306  ARG C  67  HOH C 266  GLU D 126                    
SITE     3 AC6  9 HOH D 223                                                     
SITE     1 AC7  5 PRO A  89  GLY A  90  GLU B  20  GLU B  25                    
SITE     2 AC7  5 HOH B 233                                                     
SITE     1 AC8  8 ALA B  64  ARG B  67  ASP B  68  HOH B 243                    
SITE     2 AC8  8 HOH B 291  ALA C  64  ARG C  67  ASP C  68                    
SITE     1 AC9  6 HIS C  31  HIS C  79  ASP C 165  HIS C 169                    
SITE     2 AC9  6 HOH C 219  HOH C 253                                          
SITE     1 BC1  7 LEU C 142  ARG C 143  HOH C 281  LEU D  47                    
SITE     2 BC1  7 ILE D  50  GLU D  51  HOH D 269                               
SITE     1 BC2  6 HIS D  31  HIS D  79  ASP D 165  HIS D 169                    
SITE     2 BC2  6 HOH D 219  HOH D 267                                          
SITE     1 BC3  9 ARG A  67  HOH B 225  HOH B 251  GLU C 148                    
SITE     2 BC3  9 LEU C 153  ARG D  67  LYS D 149  HOH D 261                    
SITE     3 BC3  9 HOH D 284                                                     
SITE     1 BC4  4 ASN B 177  LYS D  34  HIS D  35  THR D  38                    
SITE     1 BC5  5 ARG C  63  LYS D 123  VAL D 125  GLU D 126                    
SITE     2 BC5  5 HOH D 268                                                     
CRYST1   69.057   71.755   76.404  90.00  91.72  90.00 P 1 21 1      8          
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      0.014481  0.000000  0.000435        0.00000                         
SCALE2      0.000000  0.013936  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013094        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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