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Database: PDB
Entry: 4ENW
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Original site: 4ENW 
HEADER    OXIDOREDUCTASE                          13-APR-12   4ENW              
TITLE     STRUCTURE OF THE S234N VARIANT OF E. COLI KATE                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CATALASE HPII;                                             
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: HYDROXYPEROXIDASE II;                                       
COMPND   5 EC: 1.11.1.6;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: B1732, JW1721, KATE;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: UM255;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PKS                                       
KEYWDS    CATALASE FOLD, KATE, S234N VARIANT, OXIDOREDUCTASE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.C.LOEWEN,V.JHA                                                      
REVDAT   3   13-SEP-23 4ENW    1       REMARK SEQADV LINK                       
REVDAT   2   27-FEB-13 4ENW    1       JRNL                                     
REVDAT   1   02-MAY-12 4ENW    0                                                
JRNL        AUTH   V.JHA,P.CHELIKANI,X.CARPENA,I.FITA,P.C.LOEWEN                
JRNL        TITL   INFLUENCE OF MAIN CHANNEL STRUCTURE ON H(2)O(2) ACCESS TO    
JRNL        TITL 2 THE HEME CAVITY OF CATALASE KATE OF ESCHERICHIA COLI.        
JRNL        REF    ARCH.BIOCHEM.BIOPHYS.         V. 526    54 2012              
JRNL        REFN                   ISSN 0003-9861                               
JRNL        PMID   22820098                                                     
JRNL        DOI    10.1016/J.ABB.2012.06.010                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.13                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 206533                         
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) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 10355                           
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 12674                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.66                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4090                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 662                          
REMARK   3   BIN FREE R VALUE                    : 0.4400                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 22960                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 176                                     
REMARK   3   SOLVENT ATOMS            : 2752                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.12000                                             
REMARK   3    B22 (A**2) : -0.26000                                             
REMARK   3    B33 (A**2) : 0.68000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.46000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.183         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.159         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.092         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.900         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.939                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.908                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 23841 ; 0.019 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 32505 ; 2.068 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2912 ; 6.568 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1181 ;36.757 ;23.870       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3768 ;14.966 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   176 ;15.161 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3427 ; 0.151 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 18836 ; 0.012 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     28       A     753      4                      
REMARK   3           1     B     28       B     753      4                      
REMARK   3           1     C     28       C     753      4                      
REMARK   3           1     D     28       D     753      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   5736 ; 0.310 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   5736 ; 0.310 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   5736 ; 0.320 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   5736 ; 0.350 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   5736 ; 2.270 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   5736 ; 2.060 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   5736 ; 1.990 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   5736 ; 1.810 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    28        A   753                          
REMARK   3    RESIDUE RANGE :   A   801        A   801                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.5142  -9.1911  31.7428              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0100 T22:   0.0096                                     
REMARK   3      T33:   0.0235 T12:   0.0035                                     
REMARK   3      T13:   0.0108 T23:   0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0575 L22:   0.0814                                     
REMARK   3      L33:   0.0459 L12:   0.0005                                     
REMARK   3      L13:   0.0246 L23:  -0.0186                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0056 S12:  -0.0150 S13:  -0.0245                       
REMARK   3      S21:   0.0225 S22:   0.0121 S23:   0.0247                       
REMARK   3      S31:   0.0012 S32:  -0.0100 S33:  -0.0065                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    28        B   753                          
REMARK   3    RESIDUE RANGE :   B   801        B   801                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.4521  11.7914 -18.8396              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0272 T22:   0.0087                                     
REMARK   3      T33:   0.0218 T12:   0.0001                                     
REMARK   3      T13:  -0.0137 T23:   0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0656 L22:   0.1033                                     
REMARK   3      L33:   0.0513 L12:  -0.0355                                     
REMARK   3      L13:  -0.0257 L23:  -0.0113                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0055 S12:   0.0136 S13:   0.0229                       
REMARK   3      S21:  -0.0474 S22:  -0.0027 S23:   0.0093                       
REMARK   3      S31:   0.0004 S32:  -0.0123 S33:  -0.0029                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    28        C   753                          
REMARK   3    RESIDUE RANGE :   C   801        C   801                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.1321 -11.6795 -19.4655              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0335 T22:   0.0092                                     
REMARK   3      T33:   0.0176 T12:  -0.0057                                     
REMARK   3      T13:   0.0151 T23:  -0.0091                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0610 L22:   0.0942                                     
REMARK   3      L33:   0.0552 L12:  -0.0071                                     
REMARK   3      L13:   0.0031 L23:  -0.0030                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0091 S12:   0.0101 S13:  -0.0241                       
REMARK   3      S21:  -0.0500 S22:   0.0044 S23:  -0.0100                       
REMARK   3      S31:   0.0117 S32:   0.0110 S33:   0.0047                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    28        D   753                          
REMARK   3    RESIDUE RANGE :   D   801        D   801                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.6027   9.0432  31.1587              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0111 T22:   0.0190                                     
REMARK   3      T33:   0.0145 T12:  -0.0032                                     
REMARK   3      T13:  -0.0038 T23:  -0.0091                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0800 L22:   0.0865                                     
REMARK   3      L33:   0.0357 L12:   0.0412                                     
REMARK   3      L13:  -0.0232 L23:   0.0050                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0106 S12:  -0.0181 S13:   0.0135                       
REMARK   3      S21:   0.0226 S22:  -0.0031 S23:  -0.0057                       
REMARK   3      S31:  -0.0078 S32:   0.0216 S33:  -0.0075                       
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 U VALUES: WITH TLS ADDED                                  
REMARK   4                                                                      
REMARK   4 4ENW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000071852.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUL-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.16                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 206796                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.131                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.6                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.23800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1GGE                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% PEG3350, 1.6 M LICL, 0.1 M TRIS,     
REMARK 280  PH 9.0, 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       66.28500            
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: 58830 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 78160 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -277.0 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     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     HIS A     4                                                      
REMARK 465     ASN A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     ASN A     8                                                      
REMARK 465     PRO A     9                                                      
REMARK 465     HIS A    10                                                      
REMARK 465     GLN A    11                                                      
REMARK 465     HIS A    12                                                      
REMARK 465     GLN A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     PRO A    15                                                      
REMARK 465     LEU A    16                                                      
REMARK 465     HIS A    17                                                      
REMARK 465     ASP A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     SER A    20                                                      
REMARK 465     GLU A    21                                                      
REMARK 465     ALA A    22                                                      
REMARK 465     LYS A    23                                                      
REMARK 465     PRO A    24                                                      
REMARK 465     GLY A    25                                                      
REMARK 465     MET A    26                                                      
REMARK 465     ASP A    27                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     GLN B     3                                                      
REMARK 465     HIS B     4                                                      
REMARK 465     ASN B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     ASN B     8                                                      
REMARK 465     PRO B     9                                                      
REMARK 465     HIS B    10                                                      
REMARK 465     GLN B    11                                                      
REMARK 465     HIS B    12                                                      
REMARK 465     GLN B    13                                                      
REMARK 465     SER B    14                                                      
REMARK 465     PRO B    15                                                      
REMARK 465     LEU B    16                                                      
REMARK 465     HIS B    17                                                      
REMARK 465     ASP B    18                                                      
REMARK 465     SER B    19                                                      
REMARK 465     SER B    20                                                      
REMARK 465     GLU B    21                                                      
REMARK 465     ALA B    22                                                      
REMARK 465     LYS B    23                                                      
REMARK 465     PRO B    24                                                      
REMARK 465     GLY B    25                                                      
REMARK 465     MET B    26                                                      
REMARK 465     ASP B    27                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     GLN C     3                                                      
REMARK 465     HIS C     4                                                      
REMARK 465     ASN C     5                                                      
REMARK 465     GLU C     6                                                      
REMARK 465     LYS C     7                                                      
REMARK 465     ASN C     8                                                      
REMARK 465     PRO C     9                                                      
REMARK 465     HIS C    10                                                      
REMARK 465     GLN C    11                                                      
REMARK 465     HIS C    12                                                      
REMARK 465     GLN C    13                                                      
REMARK 465     SER C    14                                                      
REMARK 465     PRO C    15                                                      
REMARK 465     LEU C    16                                                      
REMARK 465     HIS C    17                                                      
REMARK 465     ASP C    18                                                      
REMARK 465     SER C    19                                                      
REMARK 465     SER C    20                                                      
REMARK 465     GLU C    21                                                      
REMARK 465     ALA C    22                                                      
REMARK 465     LYS C    23                                                      
REMARK 465     PRO C    24                                                      
REMARK 465     GLY C    25                                                      
REMARK 465     MET C    26                                                      
REMARK 465     ASP C    27                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     GLN D     3                                                      
REMARK 465     HIS D     4                                                      
REMARK 465     ASN D     5                                                      
REMARK 465     GLU D     6                                                      
REMARK 465     LYS D     7                                                      
REMARK 465     ASN D     8                                                      
REMARK 465     PRO D     9                                                      
REMARK 465     HIS D    10                                                      
REMARK 465     GLN D    11                                                      
REMARK 465     HIS D    12                                                      
REMARK 465     GLN D    13                                                      
REMARK 465     SER D    14                                                      
REMARK 465     PRO D    15                                                      
REMARK 465     LEU D    16                                                      
REMARK 465     HIS D    17                                                      
REMARK 465     ASP D    18                                                      
REMARK 465     SER D    19                                                      
REMARK 465     SER D    20                                                      
REMARK 465     GLU D    21                                                      
REMARK 465     ALA D    22                                                      
REMARK 465     LYS D    23                                                      
REMARK 465     PRO D    24                                                      
REMARK 465     GLY D    25                                                      
REMARK 465     MET D    26                                                      
REMARK 465     ASP D    27                                                      
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   ND1  HIS D   392     CB   TYR D   415              1.69            
REMARK 500   ND1  HIS A   392     CB   TYR A   415              1.71            
REMARK 500   ND1  HIS C   392     CB   TYR C   415              1.71            
REMARK 500   ND1  HIS B   392     CB   TYR B   415              1.72            
REMARK 500   O    HOH D  1252     O    HOH D  1306              1.93            
REMARK 500   O    HOH C  1260     O    HOH C  1549              2.01            
REMARK 500   O    HOH D  1326     O    HOH D  1541              2.02            
REMARK 500   O    HOH A  1536     O    HOH C  1133              2.05            
REMARK 500   OE1  GLN D   368     O    HOH D  1555              2.07            
REMARK 500   O    HOH D  1640     O    HOH D  1641              2.14            
REMARK 500   O    HOH C  1436     O    HOH C  1547              2.15            
REMARK 500   CD   LYS D    73     O    HOH B  1463              2.16            
REMARK 500   O    HOH B  1352     O    HOH B  1401              2.17            
REMARK 500   CG   GLU A   716     O    HOH A  1302              2.18            
REMARK 500   O    HOH D  1492     O    HOH D  1540              2.19            
REMARK 500   O    HOH A  1151     O    HOH A  1353              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CB   ASP C    59     O    HOH B  1526     2545     2.00            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A 135   CG    HIS A 135   CD2     0.063                       
REMARK 500    HIS A 318   CG    HIS A 318   CD2     0.058                       
REMARK 500    GLU A 321   CD    GLU A 321   OE1     0.074                       
REMARK 500    TRP A 323   CE2   TRP A 323   CD2     0.074                       
REMARK 500    TYR A 440   CE1   TYR A 440   CZ      0.094                       
REMARK 500    HIS A 549   CG    HIS A 549   CD2     0.063                       
REMARK 500    TRP A 742   CE2   TRP A 742   CD2     0.076                       
REMARK 500    TRP B 255   CE2   TRP B 255   CD2     0.089                       
REMARK 500    TYR B 440   CE1   TYR B 440   CZ      0.102                       
REMARK 500    HIS B 449   CG    HIS B 449   CD2     0.077                       
REMARK 500    HIS C 449   CG    HIS C 449   CD2     0.059                       
REMARK 500    TRP C 469   CE2   TRP C 469   CD2     0.077                       
REMARK 500    HIS C 522   CG    HIS C 522   CD2     0.056                       
REMARK 500    HIS D 236   CG    HIS D 236   CD2     0.060                       
REMARK 500    HIS D 251   CG    HIS D 251   CD2     0.061                       
REMARK 500    TRP D 293   CE2   TRP D 293   CD2     0.084                       
REMARK 500    TRP D 323   CE2   TRP D 323   CD2     0.078                       
REMARK 500    HIS D 522   CG    HIS D 522   CD2     0.071                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 130   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ASP A 350   CB  -  CG  -  OD1 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ARG A 377   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG A 471   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG A 479   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A 740   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG B 121   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    LEU B 375   CB  -  CG  -  CD1 ANGL. DEV. =  12.0 DEGREES          
REMARK 500    ASP B 401   CB  -  CG  -  OD1 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ASP B 401   CB  -  CG  -  OD2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ARG B 422   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    LEU B 590   CB  -  CG  -  CD2 ANGL. DEV. = -11.2 DEGREES          
REMARK 500    ARG C 471   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    LEU C 552   CA  -  CB  -  CG  ANGL. DEV. =  13.8 DEGREES          
REMARK 500    ARG C 636   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG C 636   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ASP D 401   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    LYS D 478   CD  -  CE  -  NZ  ANGL. DEV. =  23.1 DEGREES          
REMARK 500    LEU D 582   CB  -  CG  -  CD1 ANGL. DEV. =  10.7 DEGREES          
REMARK 500    ARG D 740   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  75      -37.39   -165.95                                   
REMARK 500    THR A 178       36.32    -90.85                                   
REMARK 500    ILE A 274      -64.75     71.72                                   
REMARK 500    ASP A 314       86.06   -155.01                                   
REMARK 500    ASP A 405      113.46    -32.41                                   
REMARK 500    ASP A 446     -153.63     70.66                                   
REMARK 500    ASP A 595       36.86   -159.04                                   
REMARK 500    GLU A 610       58.35   -148.97                                   
REMARK 500    ASP A 725     -169.61    -78.55                                   
REMARK 500    HIS A 739      -64.98     77.64                                   
REMARK 500    VAL A 741       77.21   -102.34                                   
REMARK 500    SER B  35        3.55    -69.88                                   
REMARK 500    SER B  75      -39.69   -163.37                                   
REMARK 500    THR B 178       38.66    -87.37                                   
REMARK 500    ILE B 274      -61.30     68.98                                   
REMARK 500    ASP B 314       88.24   -153.72                                   
REMARK 500    ASN B 442     -167.93   -163.82                                   
REMARK 500    ASP B 446     -151.84     65.24                                   
REMARK 500    HIS B 449       31.57     70.63                                   
REMARK 500    ASP B 595       31.94   -148.67                                   
REMARK 500    GLU B 610       61.22   -152.25                                   
REMARK 500    ARG B 612       89.96    -59.05                                   
REMARK 500    ALA B 724       30.87    -88.66                                   
REMARK 500    ASP B 725     -179.63    -33.18                                   
REMARK 500    HIS B 739      -61.19     67.52                                   
REMARK 500    SER C  75      -36.75   -164.50                                   
REMARK 500    THR C 178       40.95    -91.42                                   
REMARK 500    ILE C 274      -62.17     65.21                                   
REMARK 500    PHE C 277     -169.98   -112.60                                   
REMARK 500    ASP C 314       82.12   -154.49                                   
REMARK 500    ASN C 442     -168.30   -165.32                                   
REMARK 500    ASP C 446     -154.81     67.94                                   
REMARK 500    LYS C 584      155.71    171.95                                   
REMARK 500    ASP C 595       33.63   -150.61                                   
REMARK 500    ASP C 725     -134.81   -144.81                                   
REMARK 500    HIS C 739      -65.86     78.45                                   
REMARK 500    SER D  75      -35.79   -166.80                                   
REMARK 500    VAL D 169      -51.96   -121.19                                   
REMARK 500    THR D 178       38.52    -88.46                                   
REMARK 500    ILE D 274      -60.38     65.41                                   
REMARK 500    ASP D 405      116.22    -37.88                                   
REMARK 500    ASN D 442     -167.73   -163.19                                   
REMARK 500    ASP D 446     -151.47     73.85                                   
REMARK 500    ASP D 595       34.93   -142.58                                   
REMARK 500    GLU D 610       71.49   -154.76                                   
REMARK 500    HIS D 739      -64.62     73.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA C  724     ASP C  725                  146.14                    
REMARK 500 ASP C  725     GLY C  726                 -142.50                    
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                             HDD A 801  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 415   OH                                                     
REMARK 620 2 HDD A 801   NA   95.1                                              
REMARK 620 3 HDD A 801   NB   86.5  88.7                                        
REMARK 620 4 HDD A 801   NC   94.8 170.0  90.7                                  
REMARK 620 5 HDD A 801   ND   95.0  91.0 178.5  89.4                            
REMARK 620 6 HOH A1506   O   160.8  81.7  74.6  88.5 104.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HDD B 801  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR B 415   OH                                                     
REMARK 620 2 HDD B 801   NA   93.5                                              
REMARK 620 3 HDD B 801   NB   83.6  91.1                                        
REMARK 620 4 HDD B 801   NC   94.0 172.3  91.2                                  
REMARK 620 5 HDD B 801   ND   97.7  88.5 178.6  89.0                            
REMARK 620 6 HOH B1460   O   163.7  84.6  80.2  88.6  98.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HDD C 801  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR C 415   OH                                                     
REMARK 620 2 HDD C 801   NA   93.1                                              
REMARK 620 3 HDD C 801   NB   86.5  89.8                                        
REMARK 620 4 HDD C 801   NC   94.2 172.5  92.4                                  
REMARK 620 5 HDD C 801   ND   94.8  89.6 178.5  88.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HDD D 801  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR D 415   OH                                                     
REMARK 620 2 HDD D 801   NA   95.9                                              
REMARK 620 3 HDD D 801   NB   87.3  90.7                                        
REMARK 620 4 HDD D 801   NC   93.7 170.3  90.5                                  
REMARK 620 5 HDD D 801   ND   94.3  89.0 178.3  89.5                            
REMARK 620 6 HOH D1643   O   160.0  84.9  72.7  86.4 105.7                      
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 HDD A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD C 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD D 801                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4ENP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ENQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ENR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ENS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ENT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ENU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ENV   RELATED DB: PDB                                   
DBREF  4ENW A    1   753  UNP    P21179   CATE_ECOLI       1    753             
DBREF  4ENW B    1   753  UNP    P21179   CATE_ECOLI       1    753             
DBREF  4ENW C    1   753  UNP    P21179   CATE_ECOLI       1    753             
DBREF  4ENW D    1   753  UNP    P21179   CATE_ECOLI       1    753             
SEQADV 4ENW ASN A  234  UNP  P21179    SER   234 ENGINEERED MUTATION            
SEQADV 4ENW ASN B  234  UNP  P21179    SER   234 ENGINEERED MUTATION            
SEQADV 4ENW ASN C  234  UNP  P21179    SER   234 ENGINEERED MUTATION            
SEQADV 4ENW ASN D  234  UNP  P21179    SER   234 ENGINEERED MUTATION            
SEQRES   1 A  753  MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN          
SEQRES   2 A  753  SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET          
SEQRES   3 A  753  ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA          
SEQRES   4 A  753  ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO          
SEQRES   5 A  753  GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU          
SEQRES   6 A  753  ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR          
SEQRES   7 A  753  ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP          
SEQRES   8 A  753  GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU          
SEQRES   9 A  753  LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE THR HIS PHE          
SEQRES  10 A  753  ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG          
SEQRES  11 A  753  GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER          
SEQRES  12 A  753  LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO          
SEQRES  13 A  753  ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL          
SEQRES  14 A  753  GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE          
SEQRES  15 A  753  ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE          
SEQRES  16 A  753  PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE          
SEQRES  17 A  753  GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL          
SEQRES  18 A  753  LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN ASN          
SEQRES  19 A  753  ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO          
SEQRES  20 A  753  GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG          
SEQRES  21 A  753  GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY          
SEQRES  22 A  753  ILE HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA          
SEQRES  23 A  753  THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS          
SEQRES  24 A  753  ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY          
SEQRES  25 A  753  ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA          
SEQRES  26 A  753  ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE          
SEQRES  27 A  753  GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE          
SEQRES  28 A  753  ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU          
SEQRES  29 A  753  VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG          
SEQRES  30 A  753  ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA          
SEQRES  31 A  753  PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR          
SEQRES  32 A  753  ASN ASP PRO LEU LEU GLN GLY ARG LEU PHE SER TYR THR          
SEQRES  33 A  753  ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS          
SEQRES  34 A  753  GLU ILE PRO ILE ASN ARG PRO THR CYS PRO TYR HIS ASN          
SEQRES  35 A  753  PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR          
SEQRES  36 A  753  ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN          
SEQRES  37 A  753  TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY          
SEQRES  38 A  753  PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL          
SEQRES  39 A  753  ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS          
SEQRES  40 A  753  PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN          
SEQRES  41 A  753  ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS          
SEQRES  42 A  753  VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN          
SEQRES  43 A  753  LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA          
SEQRES  44 A  753  LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN          
SEQRES  45 A  753  ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP          
SEQRES  46 A  753  PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL          
SEQRES  47 A  753  LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL          
SEQRES  48 A  753  ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS          
SEQRES  49 A  753  ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET          
SEQRES  50 A  753  GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE          
SEQRES  51 A  753  ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP          
SEQRES  52 A  753  ALA VAL ILE VAL PRO CYS GLY ASN ILE ALA ASP ILE ALA          
SEQRES  53 A  753  ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR          
SEQRES  54 A  753  LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG          
SEQRES  55 A  753  LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU          
SEQRES  56 A  753  GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE          
SEQRES  57 A  753  MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL          
SEQRES  58 A  753  TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA              
SEQRES   1 B  753  MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN          
SEQRES   2 B  753  SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET          
SEQRES   3 B  753  ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA          
SEQRES   4 B  753  ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO          
SEQRES   5 B  753  GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU          
SEQRES   6 B  753  ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR          
SEQRES   7 B  753  ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP          
SEQRES   8 B  753  GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU          
SEQRES   9 B  753  LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE THR HIS PHE          
SEQRES  10 B  753  ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG          
SEQRES  11 B  753  GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER          
SEQRES  12 B  753  LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO          
SEQRES  13 B  753  ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL          
SEQRES  14 B  753  GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE          
SEQRES  15 B  753  ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE          
SEQRES  16 B  753  PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE          
SEQRES  17 B  753  GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL          
SEQRES  18 B  753  LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN ASN          
SEQRES  19 B  753  ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO          
SEQRES  20 B  753  GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG          
SEQRES  21 B  753  GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY          
SEQRES  22 B  753  ILE HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA          
SEQRES  23 B  753  THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS          
SEQRES  24 B  753  ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY          
SEQRES  25 B  753  ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA          
SEQRES  26 B  753  ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE          
SEQRES  27 B  753  GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE          
SEQRES  28 B  753  ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU          
SEQRES  29 B  753  VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG          
SEQRES  30 B  753  ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA          
SEQRES  31 B  753  PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR          
SEQRES  32 B  753  ASN ASP PRO LEU LEU GLN GLY ARG LEU PHE SER TYR THR          
SEQRES  33 B  753  ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS          
SEQRES  34 B  753  GLU ILE PRO ILE ASN ARG PRO THR CYS PRO TYR HIS ASN          
SEQRES  35 B  753  PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR          
SEQRES  36 B  753  ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN          
SEQRES  37 B  753  TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY          
SEQRES  38 B  753  PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL          
SEQRES  39 B  753  ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS          
SEQRES  40 B  753  PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN          
SEQRES  41 B  753  ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS          
SEQRES  42 B  753  VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN          
SEQRES  43 B  753  LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA          
SEQRES  44 B  753  LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN          
SEQRES  45 B  753  ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP          
SEQRES  46 B  753  PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL          
SEQRES  47 B  753  LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL          
SEQRES  48 B  753  ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS          
SEQRES  49 B  753  ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET          
SEQRES  50 B  753  GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE          
SEQRES  51 B  753  ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP          
SEQRES  52 B  753  ALA VAL ILE VAL PRO CYS GLY ASN ILE ALA ASP ILE ALA          
SEQRES  53 B  753  ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR          
SEQRES  54 B  753  LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG          
SEQRES  55 B  753  LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU          
SEQRES  56 B  753  GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE          
SEQRES  57 B  753  MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL          
SEQRES  58 B  753  TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA              
SEQRES   1 C  753  MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN          
SEQRES   2 C  753  SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET          
SEQRES   3 C  753  ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA          
SEQRES   4 C  753  ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO          
SEQRES   5 C  753  GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU          
SEQRES   6 C  753  ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR          
SEQRES   7 C  753  ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP          
SEQRES   8 C  753  GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU          
SEQRES   9 C  753  LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE THR HIS PHE          
SEQRES  10 C  753  ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG          
SEQRES  11 C  753  GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER          
SEQRES  12 C  753  LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO          
SEQRES  13 C  753  ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL          
SEQRES  14 C  753  GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE          
SEQRES  15 C  753  ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE          
SEQRES  16 C  753  PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE          
SEQRES  17 C  753  GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL          
SEQRES  18 C  753  LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN ASN          
SEQRES  19 C  753  ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO          
SEQRES  20 C  753  GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG          
SEQRES  21 C  753  GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY          
SEQRES  22 C  753  ILE HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA          
SEQRES  23 C  753  THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS          
SEQRES  24 C  753  ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY          
SEQRES  25 C  753  ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA          
SEQRES  26 C  753  ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE          
SEQRES  27 C  753  GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE          
SEQRES  28 C  753  ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU          
SEQRES  29 C  753  VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG          
SEQRES  30 C  753  ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA          
SEQRES  31 C  753  PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR          
SEQRES  32 C  753  ASN ASP PRO LEU LEU GLN GLY ARG LEU PHE SER TYR THR          
SEQRES  33 C  753  ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS          
SEQRES  34 C  753  GLU ILE PRO ILE ASN ARG PRO THR CYS PRO TYR HIS ASN          
SEQRES  35 C  753  PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR          
SEQRES  36 C  753  ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN          
SEQRES  37 C  753  TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY          
SEQRES  38 C  753  PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL          
SEQRES  39 C  753  ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS          
SEQRES  40 C  753  PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN          
SEQRES  41 C  753  ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS          
SEQRES  42 C  753  VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN          
SEQRES  43 C  753  LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA          
SEQRES  44 C  753  LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN          
SEQRES  45 C  753  ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP          
SEQRES  46 C  753  PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL          
SEQRES  47 C  753  LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL          
SEQRES  48 C  753  ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS          
SEQRES  49 C  753  ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET          
SEQRES  50 C  753  GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE          
SEQRES  51 C  753  ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP          
SEQRES  52 C  753  ALA VAL ILE VAL PRO CYS GLY ASN ILE ALA ASP ILE ALA          
SEQRES  53 C  753  ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR          
SEQRES  54 C  753  LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG          
SEQRES  55 C  753  LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU          
SEQRES  56 C  753  GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE          
SEQRES  57 C  753  MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL          
SEQRES  58 C  753  TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA              
SEQRES   1 D  753  MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN          
SEQRES   2 D  753  SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET          
SEQRES   3 D  753  ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA          
SEQRES   4 D  753  ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO          
SEQRES   5 D  753  GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU          
SEQRES   6 D  753  ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR          
SEQRES   7 D  753  ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP          
SEQRES   8 D  753  GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU          
SEQRES   9 D  753  LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE THR HIS PHE          
SEQRES  10 D  753  ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG          
SEQRES  11 D  753  GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER          
SEQRES  12 D  753  LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO          
SEQRES  13 D  753  ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL          
SEQRES  14 D  753  GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE          
SEQRES  15 D  753  ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE          
SEQRES  16 D  753  PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE          
SEQRES  17 D  753  GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL          
SEQRES  18 D  753  LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN ASN          
SEQRES  19 D  753  ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO          
SEQRES  20 D  753  GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG          
SEQRES  21 D  753  GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY          
SEQRES  22 D  753  ILE HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA          
SEQRES  23 D  753  THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS          
SEQRES  24 D  753  ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY          
SEQRES  25 D  753  ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA          
SEQRES  26 D  753  ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE          
SEQRES  27 D  753  GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE          
SEQRES  28 D  753  ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU          
SEQRES  29 D  753  VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG          
SEQRES  30 D  753  ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA          
SEQRES  31 D  753  PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR          
SEQRES  32 D  753  ASN ASP PRO LEU LEU GLN GLY ARG LEU PHE SER TYR THR          
SEQRES  33 D  753  ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS          
SEQRES  34 D  753  GLU ILE PRO ILE ASN ARG PRO THR CYS PRO TYR HIS ASN          
SEQRES  35 D  753  PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR          
SEQRES  36 D  753  ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN          
SEQRES  37 D  753  TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY          
SEQRES  38 D  753  PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL          
SEQRES  39 D  753  ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS          
SEQRES  40 D  753  PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN          
SEQRES  41 D  753  ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS          
SEQRES  42 D  753  VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN          
SEQRES  43 D  753  LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA          
SEQRES  44 D  753  LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN          
SEQRES  45 D  753  ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP          
SEQRES  46 D  753  PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL          
SEQRES  47 D  753  LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL          
SEQRES  48 D  753  ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS          
SEQRES  49 D  753  ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET          
SEQRES  50 D  753  GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE          
SEQRES  51 D  753  ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP          
SEQRES  52 D  753  ALA VAL ILE VAL PRO CYS GLY ASN ILE ALA ASP ILE ALA          
SEQRES  53 D  753  ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR          
SEQRES  54 D  753  LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG          
SEQRES  55 D  753  LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU          
SEQRES  56 D  753  GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE          
SEQRES  57 D  753  MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL          
SEQRES  58 D  753  TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA              
HET    HDD  A 801      44                                                       
HET    HDD  B 801      44                                                       
HET    HDD  C 801      44                                                       
HET    HDD  D 801      44                                                       
HETNAM     HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE                     
HETSYN     HDD HEME                                                             
FORMUL   5  HDD    4(C34 H32 FE N4 O5)                                          
FORMUL   9  HOH   *2752(H2 O)                                                   
HELIX    1   1 PRO A   52  ALA A   57  1                                   6    
HELIX    2   2 ASN A   62  LEU A   68  1                                   7    
HELIX    3   3 ASP A  107  HIS A  119  1                                  13    
HELIX    4   4 ALA A  150  SER A  154  5                                   5    
HELIX    5   5 ASP A  210  HIS A  212  5                                   3    
HELIX    6   6 LYS A  213  LYS A  222  1                                  10    
HELIX    7   7 HIS A  236  GLN A  246  1                                  11    
HELIX    8   8 THR A  249  SER A  258  1                                  10    
HELIX    9   9 ASP A  259  ILE A  262  5                                   4    
HELIX   10  10 SER A  265  MET A  269  5                                   5    
HELIX   11  11 VAL A  303  ASP A  314  1                                  12    
HELIX   12  12 ASP A  316  GLY A  329  1                                  14    
HELIX   13  13 GLU A  344  GLU A  346  5                                   3    
HELIX   14  14 ASN A  381  ASN A  386  1                                   6    
HELIX   15  15 ASP A  405  THR A  418  1                                  14    
HELIX   16  16 THR A  418  LEU A  423  1                                   6    
HELIX   17  17 ASN A  427  ARG A  435  5                                   9    
HELIX   18  18 SER A  498  GLY A  502  5                                   5    
HELIX   19  19 TYR A  505  SER A  514  1                                  10    
HELIX   20  20 THR A  516  LYS A  533  1                                  18    
HELIX   21  21 ARG A  536  ASP A  551  1                                  16    
HELIX   22  22 ASP A  551  LEU A  562  1                                  12    
HELIX   23  23 THR A  567  ASN A  572  1                                   6    
HELIX   24  24 ASP A  585  SER A  589  5                                   5    
HELIX   25  25 ARG A  612  LYS A  626  1                                  15    
HELIX   26  26 PRO A  658  VAL A  662  5                                   5    
HELIX   27  27 ILE A  672  ASP A  677  1                                   6    
HELIX   28  28 ASN A  678  HIS A  691  1                                  14    
HELIX   29  29 ASP A  700  LYS A  709  5                                  10    
HELIX   30  30 ASP A  725  ALA A  738  1                                  14    
HELIX   31  31 VAL A  741  SER A  743  5                                   3    
HELIX   32  32 ARG A  744  ASP A  749  1                                   6    
HELIX   33  33 PRO B   52  ALA B   57  1                                   6    
HELIX   34  34 ASN B   62  LEU B   68  1                                   7    
HELIX   35  35 ASP B  107  HIS B  119  1                                  13    
HELIX   36  36 ALA B  150  SER B  154  5                                   5    
HELIX   37  37 ASP B  210  HIS B  212  5                                   3    
HELIX   38  38 LYS B  213  LYS B  222  1                                  10    
HELIX   39  39 HIS B  236  GLN B  246  1                                  11    
HELIX   40  40 THR B  249  SER B  258  1                                  10    
HELIX   41  41 ASP B  259  ILE B  262  5                                   4    
HELIX   42  42 SER B  265  MET B  269  5                                   5    
HELIX   43  43 VAL B  303  ASP B  314  1                                  12    
HELIX   44  44 ASP B  316  GLY B  329  1                                  14    
HELIX   45  45 GLU B  344  GLU B  346  5                                   3    
HELIX   46  46 ASN B  381  ASN B  386  1                                   6    
HELIX   47  47 ASP B  405  THR B  418  1                                  14    
HELIX   48  48 THR B  418  LEU B  423  1                                   6    
HELIX   49  49 ASN B  427  ARG B  435  5                                   9    
HELIX   50  50 SER B  498  GLY B  502  5                                   5    
HELIX   51  51 TYR B  505  SER B  514  1                                  10    
HELIX   52  52 THR B  516  LYS B  533  1                                  18    
HELIX   53  53 ARG B  536  ALA B  548  1                                  13    
HELIX   54  54 ASP B  551  LEU B  562  1                                  12    
HELIX   55  55 THR B  567  ASN B  572  1                                   6    
HELIX   56  56 ASP B  585  SER B  589  5                                   5    
HELIX   57  57 ARG B  612  LYS B  626  1                                  15    
HELIX   58  58 PRO B  658  VAL B  662  5                                   5    
HELIX   59  59 ILE B  672  ASP B  677  1                                   6    
HELIX   60  60 ASN B  678  HIS B  691  1                                  14    
HELIX   61  61 ASP B  700  THR B  707  5                                   8    
HELIX   62  62 ASP B  725  ALA B  738  1                                  14    
HELIX   63  63 VAL B  741  SER B  743  5                                   3    
HELIX   64  64 ARG B  744  ASP B  749  1                                   6    
HELIX   65  65 PRO C   52  ALA C   57  1                                   6    
HELIX   66  66 ASN C   62  LEU C   68  1                                   7    
HELIX   67  67 ASP C  107  HIS C  119  1                                  13    
HELIX   68  68 ALA C  150  SER C  154  5                                   5    
HELIX   69  69 ASP C  210  HIS C  212  5                                   3    
HELIX   70  70 LYS C  213  LYS C  222  1                                  10    
HELIX   71  71 HIS C  236  GLN C  246  1                                  11    
HELIX   72  72 THR C  249  SER C  258  1                                  10    
HELIX   73  73 ASP C  259  ILE C  262  5                                   4    
HELIX   74  74 SER C  265  MET C  269  5                                   5    
HELIX   75  75 VAL C  303  ASP C  314  1                                  12    
HELIX   76  76 ASP C  316  GLY C  329  1                                  14    
HELIX   77  77 GLU C  344  GLU C  346  5                                   3    
HELIX   78  78 ASN C  381  ASN C  386  1                                   6    
HELIX   79  79 ASP C  405  THR C  418  1                                  14    
HELIX   80  80 THR C  418  LEU C  423  1                                   6    
HELIX   81  81 ASN C  427  ARG C  435  5                                   9    
HELIX   82  82 SER C  498  GLY C  502  5                                   5    
HELIX   83  83 TYR C  505  SER C  514  1                                  10    
HELIX   84  84 THR C  516  LYS C  533  1                                  18    
HELIX   85  85 ARG C  536  HIS C  549  1                                  14    
HELIX   86  86 ASP C  551  LEU C  562  1                                  12    
HELIX   87  87 THR C  567  ASN C  572  1                                   6    
HELIX   88  88 ASP C  585  SER C  589  5                                   5    
HELIX   89  89 ARG C  612  GLY C  627  1                                  16    
HELIX   90  90 PRO C  658  VAL C  662  5                                   5    
HELIX   91  91 ILE C  672  ASP C  677  1                                   6    
HELIX   92  92 ASN C  678  HIS C  691  1                                  14    
HELIX   93  93 ASP C  700  ALA C  706  5                                   7    
HELIX   94  94 SER C  727  ALA C  738  1                                  12    
HELIX   95  95 VAL C  741  ILE C  748  5                                   8    
HELIX   96  96 PRO D   52  ALA D   57  1                                   6    
HELIX   97  97 ASN D   62  LEU D   68  1                                   7    
HELIX   98  98 ASP D  107  HIS D  119  1                                  13    
HELIX   99  99 ALA D  150  SER D  154  5                                   5    
HELIX  100 100 ASP D  210  HIS D  212  5                                   3    
HELIX  101 101 LYS D  213  LYS D  222  1                                  10    
HELIX  102 102 HIS D  236  GLN D  246  1                                  11    
HELIX  103 103 THR D  249  SER D  258  1                                  10    
HELIX  104 104 ASP D  259  ILE D  262  5                                   4    
HELIX  105 105 SER D  265  MET D  269  5                                   5    
HELIX  106 106 VAL D  303  ASP D  314  1                                  12    
HELIX  107 107 ASP D  316  GLY D  329  1                                  14    
HELIX  108 108 GLU D  344  GLU D  346  5                                   3    
HELIX  109 109 ASN D  381  ASN D  386  1                                   6    
HELIX  110 110 ASP D  405  LEU D  423  1                                  19    
HELIX  111 111 ASN D  427  ARG D  435  5                                   9    
HELIX  112 112 SER D  498  GLY D  502  5                                   5    
HELIX  113 113 TYR D  505  GLN D  515  1                                  11    
HELIX  114 114 THR D  516  LYS D  533  1                                  18    
HELIX  115 115 ARG D  536  HIS D  549  1                                  14    
HELIX  116 116 ASP D  551  LEU D  562  1                                  12    
HELIX  117 117 THR D  567  ASN D  572  1                                   6    
HELIX  118 118 ASP D  585  SER D  589  5                                   5    
HELIX  119 119 ARG D  612  LYS D  626  1                                  15    
HELIX  120 120 PRO D  658  VAL D  662  5                                   5    
HELIX  121 121 ILE D  672  ASP D  677  1                                   6    
HELIX  122 122 ASN D  678  HIS D  691  1                                  14    
HELIX  123 123 ASP D  700  THR D  707  5                                   8    
HELIX  124 124 SER D  727  ALA D  738  1                                  12    
HELIX  125 125 VAL D  741  SER D  743  5                                   3    
HELIX  126 126 ARG D  744  ASP D  749  1                                   6    
SHEET    1   A 2 ARG A  72  LYS A  73  0                                        
SHEET    2   A 2 ILE C 453  ASP C 454  1  O  ILE C 453   N  LYS A  73           
SHEET    1   B 4 LEU A  95  ALA A  97  0                                        
SHEET    2   B 4 ARG D 488  ARG D 495 -1  O  VAL D 494   N  ARG A  96           
SHEET    3   B 4 ARG C 488  ARG C 495 -1  N  VAL C 489   O  GLY D 491           
SHEET    4   B 4 LEU B  95  ALA B  97 -1  N  ARG B  96   O  VAL C 494           
SHEET    1   C11 LEU A 400  ASP A 401  0                                        
SHEET    2   C11 PHE A 277  ILE A 280 -1  N  ARG A 278   O  ASP A 401           
SHEET    3   C11 ALA A 286  PRO A 295 -1  O  VAL A 289   N  PHE A 277           
SHEET    4   C11 GLU A 333  PRO A 342 -1  O  GLU A 335   N  LYS A 294           
SHEET    5   C11 GLN A 368  ARG A 377 -1  O  VAL A 370   N  LEU A 336           
SHEET    6   C11 GLY A 131  PRO A 140 -1  N  HIS A 135   O  ARG A 377           
SHEET    7   C11 THR A 160  SER A 167 -1  O  THR A 160   N  PHE A 138           
SHEET    8   C11 GLY A 184  THR A 191 -1  O  LYS A 188   N  PHE A 163           
SHEET    9   C11 GLY A 194  ASN A 201 -1  O  PHE A 196   N  PHE A 189           
SHEET   10   C11 GLY A 271  PHE A 272 -1  O  PHE A 272   N  ASN A 201           
SHEET   11   C11 ALA A 286  PRO A 295 -1  O  TRP A 293   N  GLY A 271           
SHEET    1   D 2 ILE A 453  ASP A 454  0                                        
SHEET    2   D 2 ARG C  72  LYS C  73  1  O  LYS C  73   N  ILE A 453           
SHEET    1   E 4 LEU C  95  ALA C  97  0                                        
SHEET    2   E 4 ARG B 488  ARG B 495 -1  N  VAL B 494   O  ARG C  96           
SHEET    3   E 4 ARG A 488  VAL A 494 -1  N  GLY A 491   O  VAL B 489           
SHEET    4   E 4 ARG D  96  ALA D  97 -1  O  ARG D  96   N  VAL A 494           
SHEET    1   F 6 ALA A 652  THR A 653  0                                        
SHEET    2   F 6 HIS A 629  TYR A 634  1  N  TYR A 634   O  ALA A 652           
SHEET    3   F 6 VAL A 602  LEU A 606  1  N  ILE A 605   O  LEU A 633           
SHEET    4   F 6 ALA A 664  VAL A 667  1  O  ILE A 666   N  ALA A 604           
SHEET    5   F 6 ILE A 695  ALA A 698  1  O  ALA A 696   N  VAL A 665           
SHEET    6   F 6 ILE A 718  ALA A 721  1  O  VAL A 719   N  LEU A 697           
SHEET    1   G 2 GLU A 639  THR A 641  0                                        
SHEET    2   G 2 VAL A 647  PRO A 649 -1  O  LEU A 648   N  VAL A 640           
SHEET    1   H 2 ARG B  72  LYS B  73  0                                        
SHEET    2   H 2 ILE D 453  ASP D 454  1  O  ILE D 453   N  LYS B  73           
SHEET    1   I11 LEU B 400  ASP B 401  0                                        
SHEET    2   I11 PHE B 277  ILE B 280 -1  N  ARG B 278   O  ASP B 401           
SHEET    3   I11 ALA B 286  PRO B 295 -1  O  VAL B 289   N  PHE B 277           
SHEET    4   I11 GLU B 333  PRO B 342 -1  O  GLU B 335   N  LYS B 294           
SHEET    5   I11 GLN B 368  ARG B 377 -1  O  VAL B 370   N  LEU B 336           
SHEET    6   I11 GLY B 131  PRO B 140 -1  N  HIS B 135   O  ARG B 377           
SHEET    7   I11 THR B 160  SER B 167 -1  O  PHE B 166   N  SER B 132           
SHEET    8   I11 GLY B 184  THR B 191 -1  O  LYS B 188   N  PHE B 163           
SHEET    9   I11 GLY B 194  ASN B 201 -1  O  PHE B 196   N  PHE B 189           
SHEET   10   I11 GLY B 271  PHE B 272 -1  O  PHE B 272   N  ASN B 201           
SHEET   11   I11 ALA B 286  PRO B 295 -1  O  TRP B 293   N  GLY B 271           
SHEET    1   J 2 ILE B 453  ASP B 454  0                                        
SHEET    2   J 2 ARG D  72  LYS D  73  1  O  LYS D  73   N  ILE B 453           
SHEET    1   K 6 ALA B 652  THR B 653  0                                        
SHEET    2   K 6 HIS B 629  TYR B 634  1  N  TYR B 634   O  ALA B 652           
SHEET    3   K 6 VAL B 602  LEU B 606  1  N  ILE B 605   O  LEU B 633           
SHEET    4   K 6 ALA B 664  VAL B 667  1  O  ILE B 666   N  ALA B 604           
SHEET    5   K 6 ILE B 695  ALA B 698  1  O  ALA B 696   N  VAL B 667           
SHEET    6   K 6 ILE B 718  ALA B 721  1  O  VAL B 719   N  LEU B 697           
SHEET    1   L 2 GLU B 639  THR B 641  0                                        
SHEET    2   L 2 VAL B 647  PRO B 649 -1  O  LEU B 648   N  VAL B 640           
SHEET    1   M10 LEU C 400  ASP C 401  0                                        
SHEET    2   M10 GLY C 271  ILE C 280 -1  N  ARG C 278   O  ASP C 401           
SHEET    3   M10 ALA C 286  PRO C 295 -1  O  TRP C 293   N  GLY C 271           
SHEET    4   M10 GLU C 333  PRO C 342 -1  O  GLU C 335   N  LYS C 294           
SHEET    5   M10 VAL C 367  ARG C 377 -1  O  VAL C 370   N  LEU C 336           
SHEET    6   M10 GLY C 131  PRO C 140 -1  N  HIS C 135   O  ARG C 377           
SHEET    7   M10 THR C 160  SER C 167 -1  O  PHE C 166   N  SER C 132           
SHEET    8   M10 GLY C 184  THR C 191 -1  O  LYS C 188   N  PHE C 163           
SHEET    9   M10 GLY C 194  ASN C 201 -1  O  PHE C 196   N  PHE C 189           
SHEET   10   M10 GLY C 271  ILE C 280 -1  O  PHE C 272   N  ASN C 201           
SHEET    1   N 6 ALA C 652  THR C 653  0                                        
SHEET    2   N 6 HIS C 629  TYR C 634  1  N  TYR C 634   O  ALA C 652           
SHEET    3   N 6 VAL C 602  LEU C 606  1  N  ILE C 605   O  LYS C 631           
SHEET    4   N 6 ALA C 664  VAL C 667  1  O  ILE C 666   N  ALA C 604           
SHEET    5   N 6 ILE C 695  ALA C 698  1  O  ALA C 696   N  VAL C 667           
SHEET    6   N 6 ILE C 718  ALA C 721  1  O  VAL C 719   N  LEU C 697           
SHEET    1   O 2 GLU C 639  THR C 641  0                                        
SHEET    2   O 2 VAL C 647  PRO C 649 -1  O  LEU C 648   N  VAL C 640           
SHEET    1   P11 LEU D 400  ASP D 401  0                                        
SHEET    2   P11 PHE D 277  ILE D 280 -1  N  ARG D 278   O  ASP D 401           
SHEET    3   P11 ALA D 286  PRO D 295 -1  O  VAL D 289   N  PHE D 277           
SHEET    4   P11 GLU D 333  PRO D 342 -1  O  GLU D 335   N  LYS D 294           
SHEET    5   P11 GLN D 368  ARG D 377 -1  O  MET D 373   N  TYR D 334           
SHEET    6   P11 GLY D 131  PRO D 140 -1  N  HIS D 135   O  ARG D 377           
SHEET    7   P11 THR D 160  SER D 167 -1  O  THR D 160   N  PHE D 138           
SHEET    8   P11 GLY D 184  THR D 191 -1  O  ALA D 186   N  ARG D 165           
SHEET    9   P11 GLY D 194  ASN D 201 -1  O  PHE D 196   N  PHE D 189           
SHEET   10   P11 GLY D 271  PHE D 272 -1  O  PHE D 272   N  ASN D 201           
SHEET   11   P11 ALA D 286  PRO D 295 -1  O  TRP D 293   N  GLY D 271           
SHEET    1   Q 6 ALA D 652  THR D 653  0                                        
SHEET    2   Q 6 HIS D 629  TYR D 634  1  N  TYR D 634   O  ALA D 652           
SHEET    3   Q 6 VAL D 602  LEU D 606  1  N  ILE D 605   O  LEU D 633           
SHEET    4   Q 6 ALA D 664  VAL D 667  1  O  ILE D 666   N  ALA D 604           
SHEET    5   Q 6 ILE D 695  ALA D 698  1  O  ALA D 696   N  VAL D 667           
SHEET    6   Q 6 ILE D 718  ALA D 721  1  O  VAL D 719   N  ILE D 695           
SHEET    1   R 2 GLU D 639  THR D 641  0                                        
SHEET    2   R 2 VAL D 647  PRO D 649 -1  O  LEU D 648   N  VAL D 640           
LINK         OH  TYR A 415                FE   HDD A 801     1555   1555  1.98  
LINK        FE   HDD A 801                 O   HOH A1506     1555   1555  2.52  
LINK         OH  TYR B 415                FE   HDD B 801     1555   1555  2.02  
LINK        FE   HDD B 801                 O   HOH B1460     1555   1555  2.29  
LINK         OH  TYR C 415                FE   HDD C 801     1555   1555  1.93  
LINK         OH  TYR D 415                FE   HDD D 801     1555   1555  1.98  
LINK        FE   HDD D 801                 O   HOH D1643     1555   1555  2.74  
CISPEP   1 ILE A  229    PRO A  230          0         1.83                     
CISPEP   2 GLU A  461    PRO A  462          0         3.87                     
CISPEP   3 TRP A  469    PRO A  470          0        -3.18                     
CISPEP   4 ILE B  229    PRO B  230          0         4.29                     
CISPEP   5 GLU B  461    PRO B  462          0         8.51                     
CISPEP   6 TRP B  469    PRO B  470          0        -5.65                     
CISPEP   7 ILE C  229    PRO C  230          0         5.53                     
CISPEP   8 GLU C  461    PRO C  462          0         8.20                     
CISPEP   9 TRP C  469    PRO C  470          0        -3.70                     
CISPEP  10 ILE D  229    PRO D  230          0         3.61                     
CISPEP  11 GLU D  461    PRO D  462          0         7.24                     
CISPEP  12 TRP D  469    PRO D  470          0        -5.22                     
SITE     1 AC1 24 ARG A 125  VAL A 127  HIS A 128  ARG A 165                    
SITE     2 AC1 24 GLY A 184  VAL A 199  GLY A 200  ASN A 201                    
SITE     3 AC1 24 PHE A 206  PHE A 214  ILE A 274  HIS A 275                    
SITE     4 AC1 24 PHE A 391  LEU A 407  ARG A 411  SER A 414                    
SITE     5 AC1 24 TYR A 415  THR A 418  GLN A 419  ARG A 422                    
SITE     6 AC1 24 HOH A 924  HOH A 968  HOH A 996  HOH A1506                    
SITE     1 AC2 23 ARG B 125  VAL B 127  HIS B 128  ARG B 165                    
SITE     2 AC2 23 GLY B 184  VAL B 199  GLY B 200  ASN B 201                    
SITE     3 AC2 23 PHE B 206  PHE B 214  ILE B 274  HIS B 275                    
SITE     4 AC2 23 PHE B 391  LEU B 407  ARG B 411  SER B 414                    
SITE     5 AC2 23 TYR B 415  THR B 418  GLN B 419  ARG B 422                    
SITE     6 AC2 23 HOH B 963  HOH B1010  HOH B1460                               
SITE     1 AC3 24 ASP B 118  ARG C 125  VAL C 127  HIS C 128                    
SITE     2 AC3 24 ARG C 165  GLY C 184  VAL C 199  GLY C 200                    
SITE     3 AC3 24 ASN C 201  PHE C 206  PHE C 214  ILE C 274                    
SITE     4 AC3 24 HIS C 275  PHE C 391  LEU C 407  ARG C 411                    
SITE     5 AC3 24 SER C 414  TYR C 415  THR C 418  GLN C 419                    
SITE     6 AC3 24 ARG C 422  HOH C1010  HOH C1054  HOH C1083                    
SITE     1 AC4 23 ARG D 125  VAL D 127  HIS D 128  ARG D 165                    
SITE     2 AC4 23 GLY D 184  VAL D 199  GLY D 200  ASN D 201                    
SITE     3 AC4 23 PHE D 206  PHE D 214  HIS D 275  PHE D 391                    
SITE     4 AC4 23 LEU D 407  GLY D 410  ARG D 411  SER D 414                    
SITE     5 AC4 23 TYR D 415  THR D 418  GLN D 419  HOH D1066                    
SITE     6 AC4 23 HOH D1109  HOH D1139  HOH D1643                               
CRYST1   93.393  132.570  122.567  90.00 109.23  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      0.010707  0.000000  0.003735        0.00000                         
SCALE2      0.000000  0.007543  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008641        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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