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Database: PDB
Entry: 4YIP
LinkDB: 4YIP
Original site: 4YIP 
HEADER    OXIDOREDUCTASE                          02-MAR-15   4YIP              
TITLE     X-RAY STRUCTURE OF THE IRON/MANGANESE CAMBIALISTIC SUPEROXIDE         
TITLE    2 DISMUTASE FROM STREPTOCOCCUS MUTANS                                  
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: STREPTOCOCCUS MUTANS;                           
SOURCE   3 ORGANISM_TAXID: 1309;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    OXIDOREDUCTASE, CAMBIALISTIC                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.RUSSO KRAUSS,A.MERLINO,A.PICA,F.SICA                                
REVDAT   1   13-JAN-16 4YIP    0                                                
JRNL        AUTH   I.RUSSO KRAUSS,A.MERLINO,A.PICA,R.RULLO,A.BERTONI,A.CAPASSO, 
JRNL        AUTH 2 M.AMATO,F.RICCITIELLO,E.DE VENDITTIS,F.SICA                  
JRNL        TITL   FINE TUNING OF METAL-SPECIFIC ACTIVITY IN THE MN-LIKE GROUP  
JRNL        TITL 2 OF CAMBIALISTIC SUPEROXIDE DISMUTASES                        
JRNL        REF    RSC ADV                       V.   5 87876 2015              
JRNL        REFN                   ESSN 2046-2069                               
JRNL        DOI    10.1039/C5RA13559A                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.39                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 41189                          
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) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2181                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2842                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.87                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2620                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 156                          
REMARK   3   BIN FREE R VALUE                    : 0.3480                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6395                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 277                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.37                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.40000                                             
REMARK   3    B22 (A**2) : 1.11000                                              
REMARK   3    B33 (A**2) : 0.33000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.62000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.290         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.229         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.165         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.424         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.911                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6593 ; 0.015 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9026 ; 1.731 ; 1.935       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   814 ; 6.670 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   321 ;35.700 ;25.016       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1001 ;15.977 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;17.204 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1014 ; 0.120 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5112 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 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 USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4YIP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000206885.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JAN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43458                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.13500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.64700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
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: 3LIO                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 28-33% PEG 8000, 0.1 M SODIUM            
REMARK 280  CACODYLATE BUFFER AT PH 6.0, 3% ACETONITRILE, VAPOR DIFFUSION,      
REMARK 280  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       41.43950            
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     MET A     0                                                      
REMARK 465     HIS A   204                                                      
REMARK 465     HIS A   205                                                      
REMARK 465     HIS A   206                                                      
REMARK 465     HIS A   207                                                      
REMARK 465     HIS A   208                                                      
REMARK 465     HIS A   209                                                      
REMARK 465     MET B     0                                                      
REMARK 465     HIS B   204                                                      
REMARK 465     HIS B   205                                                      
REMARK 465     HIS B   206                                                      
REMARK 465     HIS B   207                                                      
REMARK 465     HIS B   208                                                      
REMARK 465     HIS B   209                                                      
REMARK 465     MET C     0                                                      
REMARK 465     LEU C   202                                                      
REMARK 465     GLU C   203                                                      
REMARK 465     HIS C   204                                                      
REMARK 465     HIS C   205                                                      
REMARK 465     HIS C   206                                                      
REMARK 465     HIS C   207                                                      
REMARK 465     HIS C   208                                                      
REMARK 465     HIS C   209                                                      
REMARK 465     MET D     0                                                      
REMARK 465     HIS D   204                                                      
REMARK 465     HIS D   205                                                      
REMARK 465     HIS D   206                                                      
REMARK 465     HIS D   207                                                      
REMARK 465     HIS D   208                                                      
REMARK 465     HIS D   209                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP B 162   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 146     -113.37     53.62                                   
REMARK 500    TYR A 168       -5.02   -145.44                                   
REMARK 500    ARG A 173     -130.73     57.99                                   
REMARK 500    PRO B   8       38.68    -87.77                                   
REMARK 500    LYS B  29      -62.94   -108.82                                   
REMARK 500    GLU B  50       15.69   -142.09                                   
REMARK 500    ASN B 146     -119.46     56.94                                   
REMARK 500    ARG B 173     -129.50     51.14                                   
REMARK 500    GLU C 136       34.84    -93.38                                   
REMARK 500    ASN C 146     -124.66     53.28                                   
REMARK 500    TYR C 168      -14.07   -150.11                                   
REMARK 500    ARG C 173     -136.28     47.70                                   
REMARK 500    ASN D 146     -123.06     48.78                                   
REMARK 500    TYR D 168       -4.40   -144.32                                   
REMARK 500    ARG D 173     -140.57     50.94                                   
REMARK 500    LEU D 202      -61.74    161.31                                   
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 A 301  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  26   NE2                                                    
REMARK 620 2 HIS A  80   NE2  85.3                                              
REMARK 620 3 ASP A 162   OD2  88.3  94.6                                        
REMARK 620 4 HIS A 166   NE2  89.4 140.4 124.5                                  
REMARK 620 5 HOH A 412   O   178.0  95.2  89.8  91.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 301  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  26   NE2                                                    
REMARK 620 2 HIS B  80   NE2  81.1                                              
REMARK 620 3 ASP B 162   OD2  82.6 108.4                                        
REMARK 620 4 HIS B 166   NE2  96.4 135.7 115.2                                  
REMARK 620 5 HOH B 415   O   174.4  98.0  92.4  88.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE C 301  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  26   NE2                                                    
REMARK 620 2 HIS C  80   NE2  88.8                                              
REMARK 620 3 ASP C 162   OD2  88.5 108.9                                        
REMARK 620 4 HIS C 166   NE2 105.1 138.5 110.3                                  
REMARK 620 5 HOH C 410   O   169.6  89.9  82.1  82.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE D 301  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  26   NE2                                                    
REMARK 620 2 HIS D  80   NE2  93.4                                              
REMARK 620 3 ASP D 162   OD2  87.4 102.3                                        
REMARK 620 4 HIS D 166   NE2  89.3 137.8 119.9                                  
REMARK 620 5 HOH D 418   O   168.0  95.1  82.4  90.2                            
REMARK 620 N                    1     2     3     4                             
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 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE C 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE D 301                  
DBREF  4YIP A    0   201  UNP    P09738   SODM_STRMU       1    202             
DBREF  4YIP B    0   201  UNP    P09738   SODM_STRMU       1    202             
DBREF  4YIP C    0   201  UNP    P09738   SODM_STRMU       1    202             
DBREF  4YIP D    0   201  UNP    P09738   SODM_STRMU       1    202             
SEQADV 4YIP LEU A  202  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP GLU A  203  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS A  204  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS A  205  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS A  206  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS A  207  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS A  208  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS A  209  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP LEU B  202  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP GLU B  203  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS B  204  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS B  205  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS B  206  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS B  207  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS B  208  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS B  209  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP LEU C  202  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP GLU C  203  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS C  204  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS C  205  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS C  206  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS C  207  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS C  208  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS C  209  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP LEU D  202  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP GLU D  203  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS D  204  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS D  205  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS D  206  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS D  207  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS D  208  UNP  P09738              EXPRESSION TAG                 
SEQADV 4YIP HIS D  209  UNP  P09738              EXPRESSION TAG                 
SEQRES   1 A  210  MET ALA ILE LEU LEU PRO ASP LEU PRO TYR ALA TYR ASP          
SEQRES   2 A  210  ALA LEU GLU PRO TYR ILE ASP ALA GLU THR MET THR LEU          
SEQRES   3 A  210  HIS HIS ASP LYS HIS HIS ALA THR TYR VAL ALA ASN ALA          
SEQRES   4 A  210  ASN ALA ALA LEU GLU LYS HIS PRO GLU ILE GLY GLU ASN          
SEQRES   5 A  210  LEU GLU VAL LEU LEU ALA ASP VAL GLU GLN ILE PRO ALA          
SEQRES   6 A  210  ASP ILE ARG GLN SER LEU ILE ASN ASN GLY GLY GLY HIS          
SEQRES   7 A  210  LEU ASN HIS ALA LEU PHE TRP GLU LEU LEU SER PRO GLU          
SEQRES   8 A  210  LYS THR LYS VAL THR ALA GLU VAL ALA ALA ALA ILE ASN          
SEQRES   9 A  210  GLU ALA PHE GLY SER PHE ASP ASP PHE LYS ALA ALA PHE          
SEQRES  10 A  210  THR ALA ALA ALA THR THR ARG PHE GLY SER GLY TRP ALA          
SEQRES  11 A  210  TRP LEU VAL VAL ASP LYS GLU GLY LYS LEU GLU VAL THR          
SEQRES  12 A  210  SER THR ALA ASN GLN ASP THR PRO ILE SER GLN GLY LEU          
SEQRES  13 A  210  LYS PRO ILE LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  14 A  210  TYR LEU ASN TYR ARG ASN VAL ARG PRO ASN TYR ILE LYS          
SEQRES  15 A  210  ALA PHE PHE GLU VAL ILE ASN TRP ASN THR VAL ALA ARG          
SEQRES  16 A  210  LEU TYR ALA GLU ALA LEU THR LEU GLU HIS HIS HIS HIS          
SEQRES  17 A  210  HIS HIS                                                      
SEQRES   1 B  210  MET ALA ILE LEU LEU PRO ASP LEU PRO TYR ALA TYR ASP          
SEQRES   2 B  210  ALA LEU GLU PRO TYR ILE ASP ALA GLU THR MET THR LEU          
SEQRES   3 B  210  HIS HIS ASP LYS HIS HIS ALA THR TYR VAL ALA ASN ALA          
SEQRES   4 B  210  ASN ALA ALA LEU GLU LYS HIS PRO GLU ILE GLY GLU ASN          
SEQRES   5 B  210  LEU GLU VAL LEU LEU ALA ASP VAL GLU GLN ILE PRO ALA          
SEQRES   6 B  210  ASP ILE ARG GLN SER LEU ILE ASN ASN GLY GLY GLY HIS          
SEQRES   7 B  210  LEU ASN HIS ALA LEU PHE TRP GLU LEU LEU SER PRO GLU          
SEQRES   8 B  210  LYS THR LYS VAL THR ALA GLU VAL ALA ALA ALA ILE ASN          
SEQRES   9 B  210  GLU ALA PHE GLY SER PHE ASP ASP PHE LYS ALA ALA PHE          
SEQRES  10 B  210  THR ALA ALA ALA THR THR ARG PHE GLY SER GLY TRP ALA          
SEQRES  11 B  210  TRP LEU VAL VAL ASP LYS GLU GLY LYS LEU GLU VAL THR          
SEQRES  12 B  210  SER THR ALA ASN GLN ASP THR PRO ILE SER GLN GLY LEU          
SEQRES  13 B  210  LYS PRO ILE LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  14 B  210  TYR LEU ASN TYR ARG ASN VAL ARG PRO ASN TYR ILE LYS          
SEQRES  15 B  210  ALA PHE PHE GLU VAL ILE ASN TRP ASN THR VAL ALA ARG          
SEQRES  16 B  210  LEU TYR ALA GLU ALA LEU THR LEU GLU HIS HIS HIS HIS          
SEQRES  17 B  210  HIS HIS                                                      
SEQRES   1 C  210  MET ALA ILE LEU LEU PRO ASP LEU PRO TYR ALA TYR ASP          
SEQRES   2 C  210  ALA LEU GLU PRO TYR ILE ASP ALA GLU THR MET THR LEU          
SEQRES   3 C  210  HIS HIS ASP LYS HIS HIS ALA THR TYR VAL ALA ASN ALA          
SEQRES   4 C  210  ASN ALA ALA LEU GLU LYS HIS PRO GLU ILE GLY GLU ASN          
SEQRES   5 C  210  LEU GLU VAL LEU LEU ALA ASP VAL GLU GLN ILE PRO ALA          
SEQRES   6 C  210  ASP ILE ARG GLN SER LEU ILE ASN ASN GLY GLY GLY HIS          
SEQRES   7 C  210  LEU ASN HIS ALA LEU PHE TRP GLU LEU LEU SER PRO GLU          
SEQRES   8 C  210  LYS THR LYS VAL THR ALA GLU VAL ALA ALA ALA ILE ASN          
SEQRES   9 C  210  GLU ALA PHE GLY SER PHE ASP ASP PHE LYS ALA ALA PHE          
SEQRES  10 C  210  THR ALA ALA ALA THR THR ARG PHE GLY SER GLY TRP ALA          
SEQRES  11 C  210  TRP LEU VAL VAL ASP LYS GLU GLY LYS LEU GLU VAL THR          
SEQRES  12 C  210  SER THR ALA ASN GLN ASP THR PRO ILE SER GLN GLY LEU          
SEQRES  13 C  210  LYS PRO ILE LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  14 C  210  TYR LEU ASN TYR ARG ASN VAL ARG PRO ASN TYR ILE LYS          
SEQRES  15 C  210  ALA PHE PHE GLU VAL ILE ASN TRP ASN THR VAL ALA ARG          
SEQRES  16 C  210  LEU TYR ALA GLU ALA LEU THR LEU GLU HIS HIS HIS HIS          
SEQRES  17 C  210  HIS HIS                                                      
SEQRES   1 D  210  MET ALA ILE LEU LEU PRO ASP LEU PRO TYR ALA TYR ASP          
SEQRES   2 D  210  ALA LEU GLU PRO TYR ILE ASP ALA GLU THR MET THR LEU          
SEQRES   3 D  210  HIS HIS ASP LYS HIS HIS ALA THR TYR VAL ALA ASN ALA          
SEQRES   4 D  210  ASN ALA ALA LEU GLU LYS HIS PRO GLU ILE GLY GLU ASN          
SEQRES   5 D  210  LEU GLU VAL LEU LEU ALA ASP VAL GLU GLN ILE PRO ALA          
SEQRES   6 D  210  ASP ILE ARG GLN SER LEU ILE ASN ASN GLY GLY GLY HIS          
SEQRES   7 D  210  LEU ASN HIS ALA LEU PHE TRP GLU LEU LEU SER PRO GLU          
SEQRES   8 D  210  LYS THR LYS VAL THR ALA GLU VAL ALA ALA ALA ILE ASN          
SEQRES   9 D  210  GLU ALA PHE GLY SER PHE ASP ASP PHE LYS ALA ALA PHE          
SEQRES  10 D  210  THR ALA ALA ALA THR THR ARG PHE GLY SER GLY TRP ALA          
SEQRES  11 D  210  TRP LEU VAL VAL ASP LYS GLU GLY LYS LEU GLU VAL THR          
SEQRES  12 D  210  SER THR ALA ASN GLN ASP THR PRO ILE SER GLN GLY LEU          
SEQRES  13 D  210  LYS PRO ILE LEU ALA LEU ASP VAL TRP GLU HIS ALA TYR          
SEQRES  14 D  210  TYR LEU ASN TYR ARG ASN VAL ARG PRO ASN TYR ILE LYS          
SEQRES  15 D  210  ALA PHE PHE GLU VAL ILE ASN TRP ASN THR VAL ALA ARG          
SEQRES  16 D  210  LEU TYR ALA GLU ALA LEU THR LEU GLU HIS HIS HIS HIS          
SEQRES  17 D  210  HIS HIS                                                      
HET     FE  A 301       1                                                       
HET     FE  B 301       1                                                       
HET     FE  C 301       1                                                       
HET     FE  D 301       1                                                       
HETNAM      FE FE (III) ION                                                     
FORMUL   5   FE    4(FE 3+)                                                     
FORMUL   9  HOH   *277(H2 O)                                                    
HELIX    1 AA1 ASP A   19  LYS A   29  1                                  11    
HELIX    2 AA2 LYS A   29  HIS A   45  1                                  17    
HELIX    3 AA3 PRO A   46  GLY A   49  5                                   4    
HELIX    4 AA4 ASN A   51  ASP A   58  1                                   8    
HELIX    5 AA5 VAL A   59  ILE A   62  5                                   4    
HELIX    6 AA6 PRO A   63  LEU A   87  1                                  25    
HELIX    7 AA7 THR A   95  GLY A  107  1                                  13    
HELIX    8 AA8 SER A  108  ARG A  123  1                                  16    
HELIX    9 AA9 THR A  149  GLY A  154  5                                   6    
HELIX   10 AB1 TRP A  164  ALA A  167  5                                   4    
HELIX   11 AB2 TYR A  168  ARG A  173  1                                   6    
HELIX   12 AB3 VAL A  175  PHE A  184  1                                  10    
HELIX   13 AB4 GLU A  185  ILE A  187  5                                   3    
HELIX   14 AB5 ASN A  188  LEU A  202  1                                  15    
HELIX   15 AB6 ASP B   19  LYS B   29  1                                  11    
HELIX   16 AB7 LYS B   29  LYS B   44  1                                  16    
HELIX   17 AB8 HIS B   45  GLY B   49  5                                   5    
HELIX   18 AB9 ASN B   51  LEU B   56  1                                   6    
HELIX   19 AC1 ALA B   57  ILE B   62  5                                   6    
HELIX   20 AC2 PRO B   63  LEU B   86  1                                  24    
HELIX   21 AC3 THR B   95  GLY B  107  1                                  13    
HELIX   22 AC4 SER B  108  THR B  122  1                                  15    
HELIX   23 AC5 THR B  149  GLY B  154  5                                   6    
HELIX   24 AC6 TRP B  164  ALA B  167  5                                   4    
HELIX   25 AC7 TYR B  168  ARG B  173  1                                   6    
HELIX   26 AC8 VAL B  175  ILE B  187  1                                  13    
HELIX   27 AC9 ASN B  188  LEU B  202  1                                  15    
HELIX   28 AD1 ASP C   19  LYS C   29  1                                  11    
HELIX   29 AD2 LYS C   29  GLU C   43  1                                  15    
HELIX   30 AD3 LYS C   44  GLY C   49  5                                   6    
HELIX   31 AD4 ASN C   51  ASP C   58  1                                   8    
HELIX   32 AD5 VAL C   59  ILE C   62  5                                   4    
HELIX   33 AD6 PRO C   63  ASP C   65  5                                   3    
HELIX   34 AD7 ILE C   66  LEU C   87  1                                  22    
HELIX   35 AD8 THR C   95  GLY C  107  1                                  13    
HELIX   36 AD9 SER C  108  THR C  122  1                                  15    
HELIX   37 AE1 THR C  149  GLY C  154  5                                   6    
HELIX   38 AE2 TRP C  164  ALA C  167  5                                   4    
HELIX   39 AE3 TYR C  168  ARG C  173  1                                   6    
HELIX   40 AE4 VAL C  175  VAL C  186  1                                  12    
HELIX   41 AE5 ASN C  188  THR C  201  1                                  14    
HELIX   42 AE6 ASP D   19  LYS D   29  1                                  11    
HELIX   43 AE7 LYS D   29  GLU D   43  1                                  15    
HELIX   44 AE8 LYS D   44  GLY D   49  5                                   6    
HELIX   45 AE9 ASN D   51  LEU D   56  1                                   6    
HELIX   46 AF1 ALA D   57  ILE D   62  5                                   6    
HELIX   47 AF2 ILE D   66  LEU D   87  1                                  22    
HELIX   48 AF3 THR D   95  GLY D  107  1                                  13    
HELIX   49 AF4 SER D  108  ARG D  123  1                                  16    
HELIX   50 AF5 THR D  149  GLY D  154  5                                   6    
HELIX   51 AF6 TRP D  164  ALA D  167  5                                   4    
HELIX   52 AF7 TYR D  168  ARG D  173  1                                   6    
HELIX   53 AF8 VAL D  175  PHE D  184  1                                  10    
HELIX   54 AF9 ASN D  188  LEU D  200  1                                  13    
SHEET    1 AA1 3 LEU A 139  ALA A 145  0                                        
SHEET    2 AA1 3 GLY A 127  VAL A 133 -1  N  VAL A 132   O  GLU A 140           
SHEET    3 AA1 3 LYS A 156  ASP A 162 -1  O  ILE A 158   N  LEU A 131           
SHEET    1 AA2 3 LEU B 139  ALA B 145  0                                        
SHEET    2 AA2 3 GLY B 127  VAL B 133 -1  N  TRP B 130   O  THR B 142           
SHEET    3 AA2 3 LYS B 156  ASP B 162 -1  O  ILE B 158   N  LEU B 131           
SHEET    1 AA3 3 LEU C 139  ALA C 145  0                                        
SHEET    2 AA3 3 GLY C 127  VAL C 133 -1  N  TRP C 130   O  THR C 142           
SHEET    3 AA3 3 LYS C 156  ASP C 162 -1  O  ILE C 158   N  LEU C 131           
SHEET    1 AA4 3 LEU D 139  ALA D 145  0                                        
SHEET    2 AA4 3 GLY D 127  VAL D 133 -1  N  VAL D 132   O  GLU D 140           
SHEET    3 AA4 3 LYS D 156  ASP D 162 -1  O  LEU D 161   N  ALA D 129           
LINK         NE2 HIS A  26                FE    FE A 301     1555   1555  2.15  
LINK         NE2 HIS A  80                FE    FE A 301     1555   1555  2.20  
LINK         OD2 ASP A 162                FE    FE A 301     1555   1555  1.94  
LINK         NE2 HIS A 166                FE    FE A 301     1555   1555  2.28  
LINK         NE2 HIS B  26                FE    FE B 301     1555   1555  2.23  
LINK         NE2 HIS B  80                FE    FE B 301     1555   1555  2.29  
LINK         OD2 ASP B 162                FE    FE B 301     1555   1555  2.03  
LINK         NE2 HIS B 166                FE    FE B 301     1555   1555  2.37  
LINK         NE2 HIS C  26                FE    FE C 301     1555   1555  2.07  
LINK         NE2 HIS C  80                FE    FE C 301     1555   1555  2.28  
LINK         OD2 ASP C 162                FE    FE C 301     1555   1555  2.08  
LINK         NE2 HIS C 166                FE    FE C 301     1555   1555  2.35  
LINK         NE2 HIS D  26                FE    FE D 301     1555   1555  2.16  
LINK         NE2 HIS D  80                FE    FE D 301     1555   1555  2.27  
LINK         OD2 ASP D 162                FE    FE D 301     1555   1555  1.98  
LINK         NE2 HIS D 166                FE    FE D 301     1555   1555  2.25  
LINK        FE    FE A 301                 O   HOH A 412     1555   1555  2.15  
LINK        FE    FE B 301                 O   HOH B 415     1555   1555  2.25  
LINK        FE    FE C 301                 O   HOH C 410     1555   1555  2.28  
LINK        FE    FE D 301                 O   HOH D 418     1555   1555  2.01  
CISPEP   1 GLU A   15    PRO A   16          0         2.62                     
CISPEP   2 GLU B   15    PRO B   16          0        -4.30                     
CISPEP   3 GLU C   15    PRO C   16          0        -4.50                     
CISPEP   4 GLU D   15    PRO D   16          0         2.67                     
SITE     1 AC1  6 HIS A  26  HIS A  80  ASP A 162  HIS A 166                    
SITE     2 AC1  6 HOH A 412  HOH A 470                                          
SITE     1 AC2  5 HIS B  26  HIS B  80  ASP B 162  HIS B 166                    
SITE     2 AC2  5 HOH B 415                                                     
SITE     1 AC3  5 HIS C  26  HIS C  80  ASP C 162  HIS C 166                    
SITE     2 AC3  5 HOH C 410                                                     
SITE     1 AC4  5 HIS D  26  HIS D  80  ASP D 162  HIS D 166                    
SITE     2 AC4  5 HOH D 418                                                     
CRYST1   67.964   82.879   72.779  90.00  94.25  90.00 P 1 21 1      6          
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      0.014714  0.000000  0.001092        0.00000                         
SCALE2      0.000000  0.012066  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013778        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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