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Database: PDB
Entry: 1YE9
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Original site: 1YE9 
HEADER    OXIDOREDUCTASE                          28-DEC-04   1YE9              
TITLE     CRYSTAL STRUCTURE OF PROTEOLYTICALLY TRUNCATED CATALASE               
TITLE    2 HPII FROM E. COLI                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CATALASE HPII;                                             
COMPND   3 CHAIN: A, B, C, D, I, J, K, L;                                       
COMPND   4 FRAGMENT: PROTEOLYTIC FRAGMENT, RESIDUES 75-300;                     
COMPND   5 EC: 1.11.1.6;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CATALASE HPII;                                             
COMPND   9 CHAIN: E, F, G, H, M, N, O, P;                                       
COMPND  10 FRAGMENT: PROTEOLYTIC FRAGMENT, RESIDUES 309-567;                    
COMPND  11 EC: 1.11.1.6;                                                        
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 STRAIN: MP180;                                                       
SOURCE   5 GENE: 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: PBLUESCRIPT;                              
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  13 ORGANISM_TAXID: 562;                                                 
SOURCE  14 STRAIN: MP180;                                                       
SOURCE  15 GENE: KATE;                                                          
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PBLUESCRIPT                               
KEYWDS    CATALASE HPII, PROTEOLYTIC TRUNCATION, BETA BARREL CORE,              
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.C.LOEWEN,P.CHELIKANI,X.CARPENA,I.FITA,R.PEREZ-LUQUE,                
AUTHOR   2 L.J.DONALD,J.SWITALA,H.W.DUCKWORTH                                   
REVDAT   2   24-FEB-09 1YE9    1       VERSN                                    
REVDAT   1   26-APR-05 1YE9    0                                                
JRNL        AUTH   P.CHELIKANI,X.CARPENA,R.PEREZ-LUQUE,L.J.DONALD,              
JRNL        AUTH 2 H.W.DUCKWORTH,J.SWITALA,I.FITA,P.C.LOEWEN                    
JRNL        TITL   CHARACTERIZATION OF A LARGE SUBUNIT CATALASE                 
JRNL        TITL 2 TRUNCATED BY PROTEOLYTIC CLEAVAGE(,)                         
JRNL        REF    BIOCHEMISTRY                  V.  44  5597 2005              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   15823018                                                     
JRNL        DOI    10.1021/BI047277M                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 99638                          
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) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5289                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6917                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3580                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 361                          
REMARK   3   BIN FREE R VALUE                    : 0.4200                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 31183                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 352                                     
REMARK   3   SOLVENT ATOMS            : 180                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.73                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.05000                                              
REMARK   3    B22 (A**2) : -2.62000                                             
REMARK   3    B33 (A**2) : 2.26000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.66000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.432         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.378         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.105        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.914                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.865                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 32563 ; 0.015 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 44390 ; 2.048 ; 1.943       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3816 ; 6.411 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  4485 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 26260 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A): 16371 ; 0.282 ; 0.200       
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):  1385 ; 0.202 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     4 ; 0.173 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    50 ; 0.449 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.381 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 19173 ; 1.036 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31092 ; 1.926 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 13390 ; 3.184 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 13298 ; 5.019 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D I J K L                 
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     75       E     564      1                      
REMARK   3           1     B     75       F     564      1                      
REMARK   3           1     C     75       G     564      1                      
REMARK   3           1     D     75       H     564      1                      
REMARK   3           1     I     75       M     564      1                      
REMARK   3           1     J     75       N     564      1                      
REMARK   3           1     K     75       O     564      1                      
REMARK   3           1     L     75       P     564      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   3851 ;  0.14 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):   3851 ;  0.14 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    C    (A):   3851 ;  0.14 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    D    (A):   3851 ;  0.14 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    I    (A):   3851 ;  0.16 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    J    (A):   3851 ;  0.14 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    K    (A):   3851 ;  0.16 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    L    (A):   3851 ;  0.15 ;  0.05           
REMARK   3   TIGHT THERMAL      1    A (A**2):   3851 ;  0.51 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):   3851 ;  0.41 ;  0.50           
REMARK   3   TIGHT THERMAL      1    C (A**2):   3851 ;  0.46 ;  0.50           
REMARK   3   TIGHT THERMAL      1    D (A**2):   3851 ;  0.42 ;  0.50           
REMARK   3   TIGHT THERMAL      1    I (A**2):   3851 ;  0.49 ;  0.50           
REMARK   3   TIGHT THERMAL      1    J (A**2):   3851 ;  0.43 ;  0.50           
REMARK   3   TIGHT THERMAL      1    K (A**2):   3851 ;  0.51 ;  0.50           
REMARK   3   TIGHT THERMAL      1    L (A**2):   3851 ;  0.41 ;  0.50           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1YE9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-JAN-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB031427.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-SEP-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.931                              
REMARK 200  MONOCHROMATOR                  : DIAMOND(111), GE(220)              
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 104927                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : 0.10600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.87                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.65000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1GGE                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM TRISHCL, 8% PEG 20000, 8% PEG       
REMARK 280  MME 550, 0.2M KSCN, 0.1M DITHIOTHREITOL, PH 7.0, VAPOR              
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
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       76.44400            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: BIOLOGICAL UNIT IS A TETRAMER AND THE ASYMMETRIC UNIT IS     
REMARK 300 COMPOSED OF TWO TRUNCATED TETRAMERS IN WHICH EACH MONOMER IS CUT     
REMARK 300 INTO TWO FRAGMENTS.                                                  
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: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 91390 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 55310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -487.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, B, F, C, G, D, H                
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 91560 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 55320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -490.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, M, J, N, K, O, L, P                
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     GLY A   298                                                      
REMARK 465     LYS A   299                                                      
REMARK 465     ALA A   300                                                      
REMARK 465     GLU E   565                                                      
REMARK 465     LEU E   566                                                      
REMARK 465     THR E   567                                                      
REMARK 465     GLY B   298                                                      
REMARK 465     LYS B   299                                                      
REMARK 465     ALA B   300                                                      
REMARK 465     GLU F   565                                                      
REMARK 465     LEU F   566                                                      
REMARK 465     THR F   567                                                      
REMARK 465     GLY C   298                                                      
REMARK 465     LYS C   299                                                      
REMARK 465     ALA C   300                                                      
REMARK 465     GLU G   565                                                      
REMARK 465     LEU G   566                                                      
REMARK 465     THR G   567                                                      
REMARK 465     GLY D   298                                                      
REMARK 465     LYS D   299                                                      
REMARK 465     ALA D   300                                                      
REMARK 465     GLU H   565                                                      
REMARK 465     LEU H   566                                                      
REMARK 465     THR H   567                                                      
REMARK 465     GLY I   298                                                      
REMARK 465     LYS I   299                                                      
REMARK 465     ALA I   300                                                      
REMARK 465     GLU M   565                                                      
REMARK 465     LEU M   566                                                      
REMARK 465     THR M   567                                                      
REMARK 465     GLY J   298                                                      
REMARK 465     LYS J   299                                                      
REMARK 465     ALA J   300                                                      
REMARK 465     GLU N   565                                                      
REMARK 465     LEU N   566                                                      
REMARK 465     THR N   567                                                      
REMARK 465     GLY K   298                                                      
REMARK 465     LYS K   299                                                      
REMARK 465     ALA K   300                                                      
REMARK 465     GLU O   565                                                      
REMARK 465     LEU O   566                                                      
REMARK 465     THR O   567                                                      
REMARK 465     GLY L   298                                                      
REMARK 465     LYS L   299                                                      
REMARK 465     ALA L   300                                                      
REMARK 465     GLU P   565                                                      
REMARK 465     LEU P   566                                                      
REMARK 465     THR P   567                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS E 309    CG   CD   CE   NZ                                   
REMARK 470     ARG E 313    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F 309    CG   CD   CE   NZ                                   
REMARK 470     ARG F 313    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS G 309    CG   CD   CE   NZ                                   
REMARK 470     ARG G 313    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS H 309    CG   CD   CE   NZ                                   
REMARK 470     ARG H 313    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS M 309    CG   CD   CE   NZ                                   
REMARK 470     ARG M 313    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS N 309    CG   CD   CE   NZ                                   
REMARK 470     ARG N 313    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS O 309    CG   CD   CE   NZ                                   
REMARK 470     ARG O 313    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS P 309    CG   CD   CE   NZ                                   
REMARK 470     ARG P 313    CG   CD   NE   CZ   NH1  NH2                        
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 H   392     CB   TYR H   415              1.60            
REMARK 500   ND1  HIS M   392     CB   TYR M   415              1.62            
REMARK 500   ND1  HIS E   392     CB   TYR E   415              1.63            
REMARK 500   ND1  HIS O   392     CB   TYR O   415              1.71            
REMARK 500   ND1  HIS P   392     CB   TYR P   415              1.72            
REMARK 500   ND1  HIS G   392     CB   TYR G   415              1.74            
REMARK 500   ND1  HIS N   392     CB   TYR N   415              1.74            
REMARK 500   O    LEU N   412     NH2  ARG L   111              1.82            
REMARK 500   NH2  ARG N   369     O    HOH N   104              1.83            
REMARK 500   ND1  HIS F   392     CB   TYR F   415              1.88            
REMARK 500   N    ARG J    87     O    HOH J   305              1.99            
REMARK 500   OE1  GLU P   327     O    HOH P   767              2.03            
REMARK 500   O    GLY K   101     O    HOH K   302              2.04            
REMARK 500   N    ALA D   282     O    HOH D   310              2.07            
REMARK 500   NH2  ARG J   278     OE1  GLU N   487              2.09            
REMARK 500   O    ASP H   467     NH1  ARG H   471              2.11            
REMARK 500   OD1  ASN H   456     N    ALA H   458              2.13            
REMARK 500   O    ASP N   467     NH1  ARG N   471              2.13            
REMARK 500   NH1  ARG C   278     O    HOH C   317              2.14            
REMARK 500   CD   ARG F   488     O    HOH F   761              2.15            
REMARK 500   O    ASP E   467     NH1  ARG E   471              2.16            
REMARK 500   O    ASP M   467     NH1  ARG M   471              2.16            
REMARK 500   OE2  GLU H   530     O    HOH H   765              2.17            
REMARK 500   O    LEU M   412     NH2  ARG K   111              2.17            
REMARK 500   O    MET P   448     O    HOH P   763              2.18            
REMARK 500   O    LEU E   412     NH2  ARG C   111              2.18            
REMARK 500   OE2  GLU G   343     O    HOH C   317              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   NH1  ARG O   509     NE   ARG P   521     2756     1.70            
REMARK 500   OD1  ASN D   157     NH2  ARG O   369     2645     2.16            
REMARK 500   NH1  ARG O   509     CD   ARG P   521     2756     2.19            
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    ASP A  90   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP A  91   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG A 111   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ASP A 118   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A 155   CB  -  CG  -  OD2 ANGL. DEV. =   8.4 DEGREES          
REMARK 500    ASP A 177   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP A 237   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A 259   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG A 267   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A 267   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ASP E 314   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP E 525   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP E 545   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP B 146   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP B 151   CB  -  CG  -  OD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP B 155   CB  -  CG  -  OD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ASP B 197   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP B 210   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP B 216   CB  -  CG  -  OD2 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ASP B 259   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP F 330   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP F 355   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP F 446   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP C  90   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ASP C 118   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP C 155   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP C 197   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP C 241   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG C 267   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ASP G 330   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP G 355   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG G 377   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP G 405   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP D  91   CB  -  CG  -  OD2 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ASP D 197   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP D 216   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP D 237   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP D 241   CB  -  CG  -  OD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP H 314   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP H 405   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP H 446   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP H 525   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ASP H 545   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP H 551   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP I  90   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP I  91   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG I 111   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG I 111   NE  -  CZ  -  NH2 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ASP I 155   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP I 216   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      83 ANGLE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 155      120.92   -174.53                                   
REMARK 500    LYS A 222      160.54    -49.96                                   
REMARK 500    PRO A 223      151.55    -44.39                                   
REMARK 500    SER A 258     -172.22    -55.82                                   
REMARK 500    ILE A 274      -66.46     67.98                                   
REMARK 500    VAL E 370      -34.54   -130.91                                   
REMARK 500    ASN E 442     -165.19   -163.37                                   
REMARK 500    ASP E 446     -143.54     68.02                                   
REMARK 500    HIS E 449       50.85     28.51                                   
REMARK 500    GLN E 486       43.56    -81.90                                   
REMARK 500    ASN B  77       85.11     17.38                                   
REMARK 500    GLU B 106        0.70    -69.88                                   
REMARK 500    PHE B 152      -18.25    -48.74                                   
REMARK 500    ASP B 155      129.70   -179.43                                   
REMARK 500    THR B 178       66.33   -108.99                                   
REMARK 500    SER B 258     -168.46    -71.55                                   
REMARK 500    ILE B 274      -60.93     47.22                                   
REMARK 500    VAL F 370      -27.51   -140.01                                   
REMARK 500    ASN F 386      -72.24    -78.17                                   
REMARK 500    ASP F 446     -151.48     68.71                                   
REMARK 500    GLU F 461      130.31   -170.42                                   
REMARK 500    GLU F 472      178.89    -57.23                                   
REMARK 500    GLN F 486       49.51    -73.51                                   
REMARK 500    ASP C 155      129.27    174.62                                   
REMARK 500    PHE C 185       88.25   -154.97                                   
REMARK 500    ALA C 235       69.82    -68.22                                   
REMARK 500    ILE C 274      -65.92     64.46                                   
REMARK 500    ASN G 442     -167.27   -165.04                                   
REMARK 500    ASP G 446     -145.21     55.75                                   
REMARK 500    GLN G 486       46.65    -82.82                                   
REMARK 500    GLU G 496      129.20   -170.95                                   
REMARK 500    HIS G 549        6.01    -69.00                                   
REMARK 500    ASN D  83       -9.42    -58.73                                   
REMARK 500    GLU D 106        5.19    -69.47                                   
REMARK 500    SER D 145      -27.25    -36.83                                   
REMARK 500    ASP D 155      126.15   -176.25                                   
REMARK 500    THR D 178       69.91   -106.34                                   
REMARK 500    ASP D 181      151.06    175.42                                   
REMARK 500    SER D 258     -171.39    -69.39                                   
REMARK 500    ILE D 274      -52.74     54.06                                   
REMARK 500    ASP H 330       80.54    -69.43                                   
REMARK 500    VAL H 370      -27.40   -141.49                                   
REMARK 500    ASN H 442     -165.41   -160.93                                   
REMARK 500    ASP H 446     -154.22     70.44                                   
REMARK 500    GLU H 461      132.14   -177.28                                   
REMARK 500    GLN H 486       49.21    -72.74                                   
REMARK 500    HIS H 549       -9.39    -51.34                                   
REMARK 500    ASP I  91       40.58   -108.47                                   
REMARK 500    ASP I 107       75.69    -65.25                                   
REMARK 500    ASP I 155      124.37   -178.97                                   
REMARK 500    THR I 178       66.27   -100.56                                   
REMARK 500    ASP I 181      164.29    175.74                                   
REMARK 500    PHE I 185       92.49   -160.03                                   
REMARK 500    GLU I 248      -34.21    -37.39                                   
REMARK 500    SER I 258     -168.92    -62.95                                   
REMARK 500    ILE I 262       58.83   -140.05                                   
REMARK 500    ILE I 274      -48.84     35.65                                   
REMARK 500    GLU M 327      -70.11    -44.96                                   
REMARK 500    ASP M 330       80.95    -68.04                                   
REMARK 500    ARG M 369      123.05    -35.35                                   
REMARK 500    ASN M 404       13.45    -69.43                                   
REMARK 500    ASP M 417      -50.31    -29.88                                   
REMARK 500    ASP M 446     -153.31     55.61                                   
REMARK 500    GLU M 461      134.18    179.24                                   
REMARK 500    GLN M 486       49.09    -67.56                                   
REMARK 500    PRO M 517      -36.10    -36.27                                   
REMARK 500    HIS M 549        0.16    -60.77                                   
REMARK 500    ASP M 551      123.26    177.57                                   
REMARK 500    ASN J  77       75.26     39.81                                   
REMARK 500    ASN J  83       -6.48    -57.62                                   
REMARK 500    ASP J  91       30.92    -97.28                                   
REMARK 500    ASP J 155      121.94   -176.52                                   
REMARK 500    GLN J 246       59.67   -143.89                                   
REMARK 500    SER J 258     -176.59    -68.04                                   
REMARK 500    ILE J 274      -70.31     65.10                                   
REMARK 500    PRO N 379      172.63    -59.84                                   
REMARK 500    ASN N 386      -76.44    -81.32                                   
REMARK 500    ASP N 405      113.16    -33.23                                   
REMARK 500    ASN N 442     -168.22   -160.72                                   
REMARK 500    ASP N 446     -151.78     57.04                                   
REMARK 500    GLN N 486       45.66    -78.21                                   
REMARK 500    GLU N 487      141.57    -35.39                                   
REMARK 500    LYS N 493       92.93    -59.02                                   
REMARK 500    ASP N 551      130.47   -175.36                                   
REMARK 500    ASP K  91       43.24    -98.49                                   
REMARK 500    ASP K 107       86.04    -67.27                                   
REMARK 500    ASP K 151      -67.62    -29.32                                   
REMARK 500    PHE K 152      -18.60    -49.98                                   
REMARK 500    ASP K 155      117.02   -177.48                                   
REMARK 500    THR K 168     -158.62    -79.30                                   
REMARK 500    VAL K 169      -56.89   -127.93                                   
REMARK 500    THR K 178       76.73   -104.11                                   
REMARK 500    ASP K 181      159.55    173.27                                   
REMARK 500    ASN K 201     -159.75   -106.94                                   
REMARK 500    ALA K 235       59.26    -95.14                                   
REMARK 500    ILE K 274      -53.66     46.17                                   
REMARK 500    GLU O 346      -49.95    -28.92                                   
REMARK 500    ARG O 369      121.08    -28.00                                   
REMARK 500    ASN O 386      -71.53    -67.33                                   
REMARK 500    ILE O 396     -163.61   -111.84                                   
REMARK 500    ASP O 405      107.37    -51.64                                   
REMARK 500    PRO O 432      -82.54    -36.65                                   
REMARK 500    ASP O 446     -156.12     68.08                                   
REMARK 500    MET O 451      -60.12    -96.90                                   
REMARK 500    GLU O 461      137.84   -177.61                                   
REMARK 500    GLU O 472      174.72    -52.47                                   
REMARK 500    GLN O 486       31.77    -68.62                                   
REMARK 500    GLU O 487      129.76    -34.35                                   
REMARK 500    ASN L  77       75.04     51.65                                   
REMARK 500    ASN L  83       -7.87    -56.20                                   
REMARK 500    HIS L 128       48.94     38.28                                   
REMARK 500    ASP L 155      132.30   -178.39                                   
REMARK 500    PRO L 223      157.29    -44.06                                   
REMARK 500    GLU L 248      -35.24    -34.77                                   
REMARK 500    SER L 258     -169.66    -68.32                                   
REMARK 500    ILE L 274      -65.13     66.76                                   
REMARK 500    ASN P 386      -71.61    -82.22                                   
REMARK 500    ILE P 396     -169.34   -106.08                                   
REMARK 500    ASP P 405      115.21    -38.87                                   
REMARK 500    LEU P 412      -28.02    -38.77                                   
REMARK 500    ASN P 442     -168.72   -163.42                                   
REMARK 500    ASP P 446     -150.40     56.51                                   
REMARK 500    GLN P 486       47.85    -73.87                                   
REMARK 500    HIS P 549        4.15    -53.81                                   
REMARK 500    ILE P 550      -62.13   -106.40                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD E 760                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD F 760                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD G 760                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD H 760                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD M 760                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD N 760                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD O 760                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD P 760                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1GGE   RELATED DB: PDB                                   
REMARK 900 CATALASE HPII FROM E. COLI                                           
DBREF  1YE9 A   75   300  UNP    P21179   CATE_ECOLI      75    300             
DBREF  1YE9 B   75   300  UNP    P21179   CATE_ECOLI      75    300             
DBREF  1YE9 C   75   300  UNP    P21179   CATE_ECOLI      75    300             
DBREF  1YE9 D   75   300  UNP    P21179   CATE_ECOLI      75    300             
DBREF  1YE9 I   75   300  UNP    P21179   CATE_ECOLI      75    300             
DBREF  1YE9 J   75   300  UNP    P21179   CATE_ECOLI      75    300             
DBREF  1YE9 K   75   300  UNP    P21179   CATE_ECOLI      75    300             
DBREF  1YE9 L   75   300  UNP    P21179   CATE_ECOLI      75    300             
DBREF  1YE9 E  309   567  UNP    P21179   CATE_ECOLI     309    567             
DBREF  1YE9 F  309   567  UNP    P21179   CATE_ECOLI     309    567             
DBREF  1YE9 G  309   567  UNP    P21179   CATE_ECOLI     309    567             
DBREF  1YE9 H  309   567  UNP    P21179   CATE_ECOLI     309    567             
DBREF  1YE9 M  309   567  UNP    P21179   CATE_ECOLI     309    567             
DBREF  1YE9 N  309   567  UNP    P21179   CATE_ECOLI     309    567             
DBREF  1YE9 O  309   567  UNP    P21179   CATE_ECOLI     309    567             
DBREF  1YE9 P  309   567  UNP    P21179   CATE_ECOLI     309    567             
SEQRES   1 A  226  SER GLU ASN TYR ALA LEU THR THR ASN GLN GLY VAL ARG          
SEQRES   2 A  226  ILE ALA ASP ASP GLN ASN SER LEU ARG ALA GLY SER ARG          
SEQRES   3 A  226  GLY PRO THR LEU LEU GLU ASP PHE ILE LEU ARG GLU LYS          
SEQRES   4 A  226  ILE THR HIS PHE ASP HIS GLU ARG ILE PRO GLU ARG ILE          
SEQRES   5 A  226  VAL HIS ALA ARG GLY SER ALA ALA HIS GLY TYR PHE GLN          
SEQRES   6 A  226  PRO TYR LYS SER LEU SER ASP ILE THR LYS ALA ASP PHE          
SEQRES   7 A  226  LEU SER ASP PRO ASN LYS ILE THR PRO VAL PHE VAL ARG          
SEQRES   8 A  226  PHE SER THR VAL GLN GLY GLY ALA GLY SER ALA ASP THR          
SEQRES   9 A  226  VAL ARG ASP ILE ARG GLY PHE ALA THR LYS PHE TYR THR          
SEQRES  10 A  226  GLU GLU GLY ILE PHE ASP LEU VAL GLY ASN ASN THR PRO          
SEQRES  11 A  226  ILE PHE PHE ILE GLN ASP ALA HIS LYS PHE PRO ASP PHE          
SEQRES  12 A  226  VAL HIS ALA VAL LYS PRO GLU PRO HIS TRP ALA ILE PRO          
SEQRES  13 A  226  GLN GLY GLN SER ALA HIS ASP THR PHE TRP ASP TYR VAL          
SEQRES  14 A  226  SER LEU GLN PRO GLU THR LEU HIS ASN VAL MET TRP ALA          
SEQRES  15 A  226  MET SER ASP ARG GLY ILE PRO ARG SER TYR ARG THR MET          
SEQRES  16 A  226  GLU GLY PHE GLY ILE HIS THR PHE ARG LEU ILE ASN ALA          
SEQRES  17 A  226  GLU GLY LYS ALA THR PHE VAL ARG PHE HIS TRP LYS PRO          
SEQRES  18 A  226  LEU ALA GLY LYS ALA                                          
SEQRES   1 E  259  LYS LEU THR GLY ARG ASP PRO ASP PHE HIS ARG ARG GLU          
SEQRES   2 E  259  LEU TRP GLU ALA ILE GLU ALA GLY ASP PHE PRO GLU TYR          
SEQRES   3 E  259  GLU LEU GLY PHE GLN LEU ILE PRO GLU GLU ASP GLU PHE          
SEQRES   4 E  259  LYS PHE ASP PHE ASP LEU LEU ASP PRO THR LYS LEU ILE          
SEQRES   5 E  259  PRO GLU GLU LEU VAL PRO VAL GLN ARG VAL GLY LYS MET          
SEQRES   6 E  259  VAL LEU ASN ARG ASN PRO ASP ASN PHE PHE ALA GLU ASN          
SEQRES   7 E  259  GLU GLN ALA ALA PHE HIS PRO GLY HIS ILE VAL PRO GLY          
SEQRES   8 E  259  LEU ASP PHE THR ASN ASP PRO LEU LEU GLN GLY ARG LEU          
SEQRES   9 E  259  PHE SER TYR THR ASP THR GLN ILE SER ARG LEU GLY GLY          
SEQRES  10 E  259  PRO ASN PHE HIS GLU ILE PRO ILE ASN ARG PRO THR CYS          
SEQRES  11 E  259  PRO TYR HIS ASN PHE GLN ARG ASP GLY MET HIS ARG MET          
SEQRES  12 E  259  GLY ILE ASP THR ASN PRO ALA ASN TYR GLU PRO ASN SER          
SEQRES  13 E  259  ILE ASN ASP ASN TRP PRO ARG GLU THR PRO PRO GLY PRO          
SEQRES  14 E  259  LYS ARG GLY GLY PHE GLU SER TYR GLN GLU ARG VAL GLU          
SEQRES  15 E  259  GLY ASN LYS VAL ARG GLU ARG SER PRO SER PHE GLY GLU          
SEQRES  16 E  259  TYR TYR SER HIS PRO ARG LEU PHE TRP LEU SER GLN THR          
SEQRES  17 E  259  PRO PHE GLU GLN ARG HIS ILE VAL ASP GLY PHE SER PHE          
SEQRES  18 E  259  GLU LEU SER LYS VAL VAL ARG PRO TYR ILE ARG GLU ARG          
SEQRES  19 E  259  VAL VAL ASP GLN LEU ALA HIS ILE ASP LEU THR LEU ALA          
SEQRES  20 E  259  GLN ALA VAL ALA LYS ASN LEU GLY ILE GLU LEU THR              
SEQRES   1 B  226  SER GLU ASN TYR ALA LEU THR THR ASN GLN GLY VAL ARG          
SEQRES   2 B  226  ILE ALA ASP ASP GLN ASN SER LEU ARG ALA GLY SER ARG          
SEQRES   3 B  226  GLY PRO THR LEU LEU GLU ASP PHE ILE LEU ARG GLU LYS          
SEQRES   4 B  226  ILE THR HIS PHE ASP HIS GLU ARG ILE PRO GLU ARG ILE          
SEQRES   5 B  226  VAL HIS ALA ARG GLY SER ALA ALA HIS GLY TYR PHE GLN          
SEQRES   6 B  226  PRO TYR LYS SER LEU SER ASP ILE THR LYS ALA ASP PHE          
SEQRES   7 B  226  LEU SER ASP PRO ASN LYS ILE THR PRO VAL PHE VAL ARG          
SEQRES   8 B  226  PHE SER THR VAL GLN GLY GLY ALA GLY SER ALA ASP THR          
SEQRES   9 B  226  VAL ARG ASP ILE ARG GLY PHE ALA THR LYS PHE TYR THR          
SEQRES  10 B  226  GLU GLU GLY ILE PHE ASP LEU VAL GLY ASN ASN THR PRO          
SEQRES  11 B  226  ILE PHE PHE ILE GLN ASP ALA HIS LYS PHE PRO ASP PHE          
SEQRES  12 B  226  VAL HIS ALA VAL LYS PRO GLU PRO HIS TRP ALA ILE PRO          
SEQRES  13 B  226  GLN GLY GLN SER ALA HIS ASP THR PHE TRP ASP TYR VAL          
SEQRES  14 B  226  SER LEU GLN PRO GLU THR LEU HIS ASN VAL MET TRP ALA          
SEQRES  15 B  226  MET SER ASP ARG GLY ILE PRO ARG SER TYR ARG THR MET          
SEQRES  16 B  226  GLU GLY PHE GLY ILE HIS THR PHE ARG LEU ILE ASN ALA          
SEQRES  17 B  226  GLU GLY LYS ALA THR PHE VAL ARG PHE HIS TRP LYS PRO          
SEQRES  18 B  226  LEU ALA GLY LYS ALA                                          
SEQRES   1 F  259  LYS LEU THR GLY ARG ASP PRO ASP PHE HIS ARG ARG GLU          
SEQRES   2 F  259  LEU TRP GLU ALA ILE GLU ALA GLY ASP PHE PRO GLU TYR          
SEQRES   3 F  259  GLU LEU GLY PHE GLN LEU ILE PRO GLU GLU ASP GLU PHE          
SEQRES   4 F  259  LYS PHE ASP PHE ASP LEU LEU ASP PRO THR LYS LEU ILE          
SEQRES   5 F  259  PRO GLU GLU LEU VAL PRO VAL GLN ARG VAL GLY LYS MET          
SEQRES   6 F  259  VAL LEU ASN ARG ASN PRO ASP ASN PHE PHE ALA GLU ASN          
SEQRES   7 F  259  GLU GLN ALA ALA PHE HIS PRO GLY HIS ILE VAL PRO GLY          
SEQRES   8 F  259  LEU ASP PHE THR ASN ASP PRO LEU LEU GLN GLY ARG LEU          
SEQRES   9 F  259  PHE SER TYR THR ASP THR GLN ILE SER ARG LEU GLY GLY          
SEQRES  10 F  259  PRO ASN PHE HIS GLU ILE PRO ILE ASN ARG PRO THR CYS          
SEQRES  11 F  259  PRO TYR HIS ASN PHE GLN ARG ASP GLY MET HIS ARG MET          
SEQRES  12 F  259  GLY ILE ASP THR ASN PRO ALA ASN TYR GLU PRO ASN SER          
SEQRES  13 F  259  ILE ASN ASP ASN TRP PRO ARG GLU THR PRO PRO GLY PRO          
SEQRES  14 F  259  LYS ARG GLY GLY PHE GLU SER TYR GLN GLU ARG VAL GLU          
SEQRES  15 F  259  GLY ASN LYS VAL ARG GLU ARG SER PRO SER PHE GLY GLU          
SEQRES  16 F  259  TYR TYR SER HIS PRO ARG LEU PHE TRP LEU SER GLN THR          
SEQRES  17 F  259  PRO PHE GLU GLN ARG HIS ILE VAL ASP GLY PHE SER PHE          
SEQRES  18 F  259  GLU LEU SER LYS VAL VAL ARG PRO TYR ILE ARG GLU ARG          
SEQRES  19 F  259  VAL VAL ASP GLN LEU ALA HIS ILE ASP LEU THR LEU ALA          
SEQRES  20 F  259  GLN ALA VAL ALA LYS ASN LEU GLY ILE GLU LEU THR              
SEQRES   1 C  226  SER GLU ASN TYR ALA LEU THR THR ASN GLN GLY VAL ARG          
SEQRES   2 C  226  ILE ALA ASP ASP GLN ASN SER LEU ARG ALA GLY SER ARG          
SEQRES   3 C  226  GLY PRO THR LEU LEU GLU ASP PHE ILE LEU ARG GLU LYS          
SEQRES   4 C  226  ILE THR HIS PHE ASP HIS GLU ARG ILE PRO GLU ARG ILE          
SEQRES   5 C  226  VAL HIS ALA ARG GLY SER ALA ALA HIS GLY TYR PHE GLN          
SEQRES   6 C  226  PRO TYR LYS SER LEU SER ASP ILE THR LYS ALA ASP PHE          
SEQRES   7 C  226  LEU SER ASP PRO ASN LYS ILE THR PRO VAL PHE VAL ARG          
SEQRES   8 C  226  PHE SER THR VAL GLN GLY GLY ALA GLY SER ALA ASP THR          
SEQRES   9 C  226  VAL ARG ASP ILE ARG GLY PHE ALA THR LYS PHE TYR THR          
SEQRES  10 C  226  GLU GLU GLY ILE PHE ASP LEU VAL GLY ASN ASN THR PRO          
SEQRES  11 C  226  ILE PHE PHE ILE GLN ASP ALA HIS LYS PHE PRO ASP PHE          
SEQRES  12 C  226  VAL HIS ALA VAL LYS PRO GLU PRO HIS TRP ALA ILE PRO          
SEQRES  13 C  226  GLN GLY GLN SER ALA HIS ASP THR PHE TRP ASP TYR VAL          
SEQRES  14 C  226  SER LEU GLN PRO GLU THR LEU HIS ASN VAL MET TRP ALA          
SEQRES  15 C  226  MET SER ASP ARG GLY ILE PRO ARG SER TYR ARG THR MET          
SEQRES  16 C  226  GLU GLY PHE GLY ILE HIS THR PHE ARG LEU ILE ASN ALA          
SEQRES  17 C  226  GLU GLY LYS ALA THR PHE VAL ARG PHE HIS TRP LYS PRO          
SEQRES  18 C  226  LEU ALA GLY LYS ALA                                          
SEQRES   1 G  259  LYS LEU THR GLY ARG ASP PRO ASP PHE HIS ARG ARG GLU          
SEQRES   2 G  259  LEU TRP GLU ALA ILE GLU ALA GLY ASP PHE PRO GLU TYR          
SEQRES   3 G  259  GLU LEU GLY PHE GLN LEU ILE PRO GLU GLU ASP GLU PHE          
SEQRES   4 G  259  LYS PHE ASP PHE ASP LEU LEU ASP PRO THR LYS LEU ILE          
SEQRES   5 G  259  PRO GLU GLU LEU VAL PRO VAL GLN ARG VAL GLY LYS MET          
SEQRES   6 G  259  VAL LEU ASN ARG ASN PRO ASP ASN PHE PHE ALA GLU ASN          
SEQRES   7 G  259  GLU GLN ALA ALA PHE HIS PRO GLY HIS ILE VAL PRO GLY          
SEQRES   8 G  259  LEU ASP PHE THR ASN ASP PRO LEU LEU GLN GLY ARG LEU          
SEQRES   9 G  259  PHE SER TYR THR ASP THR GLN ILE SER ARG LEU GLY GLY          
SEQRES  10 G  259  PRO ASN PHE HIS GLU ILE PRO ILE ASN ARG PRO THR CYS          
SEQRES  11 G  259  PRO TYR HIS ASN PHE GLN ARG ASP GLY MET HIS ARG MET          
SEQRES  12 G  259  GLY ILE ASP THR ASN PRO ALA ASN TYR GLU PRO ASN SER          
SEQRES  13 G  259  ILE ASN ASP ASN TRP PRO ARG GLU THR PRO PRO GLY PRO          
SEQRES  14 G  259  LYS ARG GLY GLY PHE GLU SER TYR GLN GLU ARG VAL GLU          
SEQRES  15 G  259  GLY ASN LYS VAL ARG GLU ARG SER PRO SER PHE GLY GLU          
SEQRES  16 G  259  TYR TYR SER HIS PRO ARG LEU PHE TRP LEU SER GLN THR          
SEQRES  17 G  259  PRO PHE GLU GLN ARG HIS ILE VAL ASP GLY PHE SER PHE          
SEQRES  18 G  259  GLU LEU SER LYS VAL VAL ARG PRO TYR ILE ARG GLU ARG          
SEQRES  19 G  259  VAL VAL ASP GLN LEU ALA HIS ILE ASP LEU THR LEU ALA          
SEQRES  20 G  259  GLN ALA VAL ALA LYS ASN LEU GLY ILE GLU LEU THR              
SEQRES   1 D  226  SER GLU ASN TYR ALA LEU THR THR ASN GLN GLY VAL ARG          
SEQRES   2 D  226  ILE ALA ASP ASP GLN ASN SER LEU ARG ALA GLY SER ARG          
SEQRES   3 D  226  GLY PRO THR LEU LEU GLU ASP PHE ILE LEU ARG GLU LYS          
SEQRES   4 D  226  ILE THR HIS PHE ASP HIS GLU ARG ILE PRO GLU ARG ILE          
SEQRES   5 D  226  VAL HIS ALA ARG GLY SER ALA ALA HIS GLY TYR PHE GLN          
SEQRES   6 D  226  PRO TYR LYS SER LEU SER ASP ILE THR LYS ALA ASP PHE          
SEQRES   7 D  226  LEU SER ASP PRO ASN LYS ILE THR PRO VAL PHE VAL ARG          
SEQRES   8 D  226  PHE SER THR VAL GLN GLY GLY ALA GLY SER ALA ASP THR          
SEQRES   9 D  226  VAL ARG ASP ILE ARG GLY PHE ALA THR LYS PHE TYR THR          
SEQRES  10 D  226  GLU GLU GLY ILE PHE ASP LEU VAL GLY ASN ASN THR PRO          
SEQRES  11 D  226  ILE PHE PHE ILE GLN ASP ALA HIS LYS PHE PRO ASP PHE          
SEQRES  12 D  226  VAL HIS ALA VAL LYS PRO GLU PRO HIS TRP ALA ILE PRO          
SEQRES  13 D  226  GLN GLY GLN SER ALA HIS ASP THR PHE TRP ASP TYR VAL          
SEQRES  14 D  226  SER LEU GLN PRO GLU THR LEU HIS ASN VAL MET TRP ALA          
SEQRES  15 D  226  MET SER ASP ARG GLY ILE PRO ARG SER TYR ARG THR MET          
SEQRES  16 D  226  GLU GLY PHE GLY ILE HIS THR PHE ARG LEU ILE ASN ALA          
SEQRES  17 D  226  GLU GLY LYS ALA THR PHE VAL ARG PHE HIS TRP LYS PRO          
SEQRES  18 D  226  LEU ALA GLY LYS ALA                                          
SEQRES   1 H  259  LYS LEU THR GLY ARG ASP PRO ASP PHE HIS ARG ARG GLU          
SEQRES   2 H  259  LEU TRP GLU ALA ILE GLU ALA GLY ASP PHE PRO GLU TYR          
SEQRES   3 H  259  GLU LEU GLY PHE GLN LEU ILE PRO GLU GLU ASP GLU PHE          
SEQRES   4 H  259  LYS PHE ASP PHE ASP LEU LEU ASP PRO THR LYS LEU ILE          
SEQRES   5 H  259  PRO GLU GLU LEU VAL PRO VAL GLN ARG VAL GLY LYS MET          
SEQRES   6 H  259  VAL LEU ASN ARG ASN PRO ASP ASN PHE PHE ALA GLU ASN          
SEQRES   7 H  259  GLU GLN ALA ALA PHE HIS PRO GLY HIS ILE VAL PRO GLY          
SEQRES   8 H  259  LEU ASP PHE THR ASN ASP PRO LEU LEU GLN GLY ARG LEU          
SEQRES   9 H  259  PHE SER TYR THR ASP THR GLN ILE SER ARG LEU GLY GLY          
SEQRES  10 H  259  PRO ASN PHE HIS GLU ILE PRO ILE ASN ARG PRO THR CYS          
SEQRES  11 H  259  PRO TYR HIS ASN PHE GLN ARG ASP GLY MET HIS ARG MET          
SEQRES  12 H  259  GLY ILE ASP THR ASN PRO ALA ASN TYR GLU PRO ASN SER          
SEQRES  13 H  259  ILE ASN ASP ASN TRP PRO ARG GLU THR PRO PRO GLY PRO          
SEQRES  14 H  259  LYS ARG GLY GLY PHE GLU SER TYR GLN GLU ARG VAL GLU          
SEQRES  15 H  259  GLY ASN LYS VAL ARG GLU ARG SER PRO SER PHE GLY GLU          
SEQRES  16 H  259  TYR TYR SER HIS PRO ARG LEU PHE TRP LEU SER GLN THR          
SEQRES  17 H  259  PRO PHE GLU GLN ARG HIS ILE VAL ASP GLY PHE SER PHE          
SEQRES  18 H  259  GLU LEU SER LYS VAL VAL ARG PRO TYR ILE ARG GLU ARG          
SEQRES  19 H  259  VAL VAL ASP GLN LEU ALA HIS ILE ASP LEU THR LEU ALA          
SEQRES  20 H  259  GLN ALA VAL ALA LYS ASN LEU GLY ILE GLU LEU THR              
SEQRES   1 I  226  SER GLU ASN TYR ALA LEU THR THR ASN GLN GLY VAL ARG          
SEQRES   2 I  226  ILE ALA ASP ASP GLN ASN SER LEU ARG ALA GLY SER ARG          
SEQRES   3 I  226  GLY PRO THR LEU LEU GLU ASP PHE ILE LEU ARG GLU LYS          
SEQRES   4 I  226  ILE THR HIS PHE ASP HIS GLU ARG ILE PRO GLU ARG ILE          
SEQRES   5 I  226  VAL HIS ALA ARG GLY SER ALA ALA HIS GLY TYR PHE GLN          
SEQRES   6 I  226  PRO TYR LYS SER LEU SER ASP ILE THR LYS ALA ASP PHE          
SEQRES   7 I  226  LEU SER ASP PRO ASN LYS ILE THR PRO VAL PHE VAL ARG          
SEQRES   8 I  226  PHE SER THR VAL GLN GLY GLY ALA GLY SER ALA ASP THR          
SEQRES   9 I  226  VAL ARG ASP ILE ARG GLY PHE ALA THR LYS PHE TYR THR          
SEQRES  10 I  226  GLU GLU GLY ILE PHE ASP LEU VAL GLY ASN ASN THR PRO          
SEQRES  11 I  226  ILE PHE PHE ILE GLN ASP ALA HIS LYS PHE PRO ASP PHE          
SEQRES  12 I  226  VAL HIS ALA VAL LYS PRO GLU PRO HIS TRP ALA ILE PRO          
SEQRES  13 I  226  GLN GLY GLN SER ALA HIS ASP THR PHE TRP ASP TYR VAL          
SEQRES  14 I  226  SER LEU GLN PRO GLU THR LEU HIS ASN VAL MET TRP ALA          
SEQRES  15 I  226  MET SER ASP ARG GLY ILE PRO ARG SER TYR ARG THR MET          
SEQRES  16 I  226  GLU GLY PHE GLY ILE HIS THR PHE ARG LEU ILE ASN ALA          
SEQRES  17 I  226  GLU GLY LYS ALA THR PHE VAL ARG PHE HIS TRP LYS PRO          
SEQRES  18 I  226  LEU ALA GLY LYS ALA                                          
SEQRES   1 M  259  LYS LEU THR GLY ARG ASP PRO ASP PHE HIS ARG ARG GLU          
SEQRES   2 M  259  LEU TRP GLU ALA ILE GLU ALA GLY ASP PHE PRO GLU TYR          
SEQRES   3 M  259  GLU LEU GLY PHE GLN LEU ILE PRO GLU GLU ASP GLU PHE          
SEQRES   4 M  259  LYS PHE ASP PHE ASP LEU LEU ASP PRO THR LYS LEU ILE          
SEQRES   5 M  259  PRO GLU GLU LEU VAL PRO VAL GLN ARG VAL GLY LYS MET          
SEQRES   6 M  259  VAL LEU ASN ARG ASN PRO ASP ASN PHE PHE ALA GLU ASN          
SEQRES   7 M  259  GLU GLN ALA ALA PHE HIS PRO GLY HIS ILE VAL PRO GLY          
SEQRES   8 M  259  LEU ASP PHE THR ASN ASP PRO LEU LEU GLN GLY ARG LEU          
SEQRES   9 M  259  PHE SER TYR THR ASP THR GLN ILE SER ARG LEU GLY GLY          
SEQRES  10 M  259  PRO ASN PHE HIS GLU ILE PRO ILE ASN ARG PRO THR CYS          
SEQRES  11 M  259  PRO TYR HIS ASN PHE GLN ARG ASP GLY MET HIS ARG MET          
SEQRES  12 M  259  GLY ILE ASP THR ASN PRO ALA ASN TYR GLU PRO ASN SER          
SEQRES  13 M  259  ILE ASN ASP ASN TRP PRO ARG GLU THR PRO PRO GLY PRO          
SEQRES  14 M  259  LYS ARG GLY GLY PHE GLU SER TYR GLN GLU ARG VAL GLU          
SEQRES  15 M  259  GLY ASN LYS VAL ARG GLU ARG SER PRO SER PHE GLY GLU          
SEQRES  16 M  259  TYR TYR SER HIS PRO ARG LEU PHE TRP LEU SER GLN THR          
SEQRES  17 M  259  PRO PHE GLU GLN ARG HIS ILE VAL ASP GLY PHE SER PHE          
SEQRES  18 M  259  GLU LEU SER LYS VAL VAL ARG PRO TYR ILE ARG GLU ARG          
SEQRES  19 M  259  VAL VAL ASP GLN LEU ALA HIS ILE ASP LEU THR LEU ALA          
SEQRES  20 M  259  GLN ALA VAL ALA LYS ASN LEU GLY ILE GLU LEU THR              
SEQRES   1 J  226  SER GLU ASN TYR ALA LEU THR THR ASN GLN GLY VAL ARG          
SEQRES   2 J  226  ILE ALA ASP ASP GLN ASN SER LEU ARG ALA GLY SER ARG          
SEQRES   3 J  226  GLY PRO THR LEU LEU GLU ASP PHE ILE LEU ARG GLU LYS          
SEQRES   4 J  226  ILE THR HIS PHE ASP HIS GLU ARG ILE PRO GLU ARG ILE          
SEQRES   5 J  226  VAL HIS ALA ARG GLY SER ALA ALA HIS GLY TYR PHE GLN          
SEQRES   6 J  226  PRO TYR LYS SER LEU SER ASP ILE THR LYS ALA ASP PHE          
SEQRES   7 J  226  LEU SER ASP PRO ASN LYS ILE THR PRO VAL PHE VAL ARG          
SEQRES   8 J  226  PHE SER THR VAL GLN GLY GLY ALA GLY SER ALA ASP THR          
SEQRES   9 J  226  VAL ARG ASP ILE ARG GLY PHE ALA THR LYS PHE TYR THR          
SEQRES  10 J  226  GLU GLU GLY ILE PHE ASP LEU VAL GLY ASN ASN THR PRO          
SEQRES  11 J  226  ILE PHE PHE ILE GLN ASP ALA HIS LYS PHE PRO ASP PHE          
SEQRES  12 J  226  VAL HIS ALA VAL LYS PRO GLU PRO HIS TRP ALA ILE PRO          
SEQRES  13 J  226  GLN GLY GLN SER ALA HIS ASP THR PHE TRP ASP TYR VAL          
SEQRES  14 J  226  SER LEU GLN PRO GLU THR LEU HIS ASN VAL MET TRP ALA          
SEQRES  15 J  226  MET SER ASP ARG GLY ILE PRO ARG SER TYR ARG THR MET          
SEQRES  16 J  226  GLU GLY PHE GLY ILE HIS THR PHE ARG LEU ILE ASN ALA          
SEQRES  17 J  226  GLU GLY LYS ALA THR PHE VAL ARG PHE HIS TRP LYS PRO          
SEQRES  18 J  226  LEU ALA GLY LYS ALA                                          
SEQRES   1 N  259  LYS LEU THR GLY ARG ASP PRO ASP PHE HIS ARG ARG GLU          
SEQRES   2 N  259  LEU TRP GLU ALA ILE GLU ALA GLY ASP PHE PRO GLU TYR          
SEQRES   3 N  259  GLU LEU GLY PHE GLN LEU ILE PRO GLU GLU ASP GLU PHE          
SEQRES   4 N  259  LYS PHE ASP PHE ASP LEU LEU ASP PRO THR LYS LEU ILE          
SEQRES   5 N  259  PRO GLU GLU LEU VAL PRO VAL GLN ARG VAL GLY LYS MET          
SEQRES   6 N  259  VAL LEU ASN ARG ASN PRO ASP ASN PHE PHE ALA GLU ASN          
SEQRES   7 N  259  GLU GLN ALA ALA PHE HIS PRO GLY HIS ILE VAL PRO GLY          
SEQRES   8 N  259  LEU ASP PHE THR ASN ASP PRO LEU LEU GLN GLY ARG LEU          
SEQRES   9 N  259  PHE SER TYR THR ASP THR GLN ILE SER ARG LEU GLY GLY          
SEQRES  10 N  259  PRO ASN PHE HIS GLU ILE PRO ILE ASN ARG PRO THR CYS          
SEQRES  11 N  259  PRO TYR HIS ASN PHE GLN ARG ASP GLY MET HIS ARG MET          
SEQRES  12 N  259  GLY ILE ASP THR ASN PRO ALA ASN TYR GLU PRO ASN SER          
SEQRES  13 N  259  ILE ASN ASP ASN TRP PRO ARG GLU THR PRO PRO GLY PRO          
SEQRES  14 N  259  LYS ARG GLY GLY PHE GLU SER TYR GLN GLU ARG VAL GLU          
SEQRES  15 N  259  GLY ASN LYS VAL ARG GLU ARG SER PRO SER PHE GLY GLU          
SEQRES  16 N  259  TYR TYR SER HIS PRO ARG LEU PHE TRP LEU SER GLN THR          
SEQRES  17 N  259  PRO PHE GLU GLN ARG HIS ILE VAL ASP GLY PHE SER PHE          
SEQRES  18 N  259  GLU LEU SER LYS VAL VAL ARG PRO TYR ILE ARG GLU ARG          
SEQRES  19 N  259  VAL VAL ASP GLN LEU ALA HIS ILE ASP LEU THR LEU ALA          
SEQRES  20 N  259  GLN ALA VAL ALA LYS ASN LEU GLY ILE GLU LEU THR              
SEQRES   1 K  226  SER GLU ASN TYR ALA LEU THR THR ASN GLN GLY VAL ARG          
SEQRES   2 K  226  ILE ALA ASP ASP GLN ASN SER LEU ARG ALA GLY SER ARG          
SEQRES   3 K  226  GLY PRO THR LEU LEU GLU ASP PHE ILE LEU ARG GLU LYS          
SEQRES   4 K  226  ILE THR HIS PHE ASP HIS GLU ARG ILE PRO GLU ARG ILE          
SEQRES   5 K  226  VAL HIS ALA ARG GLY SER ALA ALA HIS GLY TYR PHE GLN          
SEQRES   6 K  226  PRO TYR LYS SER LEU SER ASP ILE THR LYS ALA ASP PHE          
SEQRES   7 K  226  LEU SER ASP PRO ASN LYS ILE THR PRO VAL PHE VAL ARG          
SEQRES   8 K  226  PHE SER THR VAL GLN GLY GLY ALA GLY SER ALA ASP THR          
SEQRES   9 K  226  VAL ARG ASP ILE ARG GLY PHE ALA THR LYS PHE TYR THR          
SEQRES  10 K  226  GLU GLU GLY ILE PHE ASP LEU VAL GLY ASN ASN THR PRO          
SEQRES  11 K  226  ILE PHE PHE ILE GLN ASP ALA HIS LYS PHE PRO ASP PHE          
SEQRES  12 K  226  VAL HIS ALA VAL LYS PRO GLU PRO HIS TRP ALA ILE PRO          
SEQRES  13 K  226  GLN GLY GLN SER ALA HIS ASP THR PHE TRP ASP TYR VAL          
SEQRES  14 K  226  SER LEU GLN PRO GLU THR LEU HIS ASN VAL MET TRP ALA          
SEQRES  15 K  226  MET SER ASP ARG GLY ILE PRO ARG SER TYR ARG THR MET          
SEQRES  16 K  226  GLU GLY PHE GLY ILE HIS THR PHE ARG LEU ILE ASN ALA          
SEQRES  17 K  226  GLU GLY LYS ALA THR PHE VAL ARG PHE HIS TRP LYS PRO          
SEQRES  18 K  226  LEU ALA GLY LYS ALA                                          
SEQRES   1 O  259  LYS LEU THR GLY ARG ASP PRO ASP PHE HIS ARG ARG GLU          
SEQRES   2 O  259  LEU TRP GLU ALA ILE GLU ALA GLY ASP PHE PRO GLU TYR          
SEQRES   3 O  259  GLU LEU GLY PHE GLN LEU ILE PRO GLU GLU ASP GLU PHE          
SEQRES   4 O  259  LYS PHE ASP PHE ASP LEU LEU ASP PRO THR LYS LEU ILE          
SEQRES   5 O  259  PRO GLU GLU LEU VAL PRO VAL GLN ARG VAL GLY LYS MET          
SEQRES   6 O  259  VAL LEU ASN ARG ASN PRO ASP ASN PHE PHE ALA GLU ASN          
SEQRES   7 O  259  GLU GLN ALA ALA PHE HIS PRO GLY HIS ILE VAL PRO GLY          
SEQRES   8 O  259  LEU ASP PHE THR ASN ASP PRO LEU LEU GLN GLY ARG LEU          
SEQRES   9 O  259  PHE SER TYR THR ASP THR GLN ILE SER ARG LEU GLY GLY          
SEQRES  10 O  259  PRO ASN PHE HIS GLU ILE PRO ILE ASN ARG PRO THR CYS          
SEQRES  11 O  259  PRO TYR HIS ASN PHE GLN ARG ASP GLY MET HIS ARG MET          
SEQRES  12 O  259  GLY ILE ASP THR ASN PRO ALA ASN TYR GLU PRO ASN SER          
SEQRES  13 O  259  ILE ASN ASP ASN TRP PRO ARG GLU THR PRO PRO GLY PRO          
SEQRES  14 O  259  LYS ARG GLY GLY PHE GLU SER TYR GLN GLU ARG VAL GLU          
SEQRES  15 O  259  GLY ASN LYS VAL ARG GLU ARG SER PRO SER PHE GLY GLU          
SEQRES  16 O  259  TYR TYR SER HIS PRO ARG LEU PHE TRP LEU SER GLN THR          
SEQRES  17 O  259  PRO PHE GLU GLN ARG HIS ILE VAL ASP GLY PHE SER PHE          
SEQRES  18 O  259  GLU LEU SER LYS VAL VAL ARG PRO TYR ILE ARG GLU ARG          
SEQRES  19 O  259  VAL VAL ASP GLN LEU ALA HIS ILE ASP LEU THR LEU ALA          
SEQRES  20 O  259  GLN ALA VAL ALA LYS ASN LEU GLY ILE GLU LEU THR              
SEQRES   1 L  226  SER GLU ASN TYR ALA LEU THR THR ASN GLN GLY VAL ARG          
SEQRES   2 L  226  ILE ALA ASP ASP GLN ASN SER LEU ARG ALA GLY SER ARG          
SEQRES   3 L  226  GLY PRO THR LEU LEU GLU ASP PHE ILE LEU ARG GLU LYS          
SEQRES   4 L  226  ILE THR HIS PHE ASP HIS GLU ARG ILE PRO GLU ARG ILE          
SEQRES   5 L  226  VAL HIS ALA ARG GLY SER ALA ALA HIS GLY TYR PHE GLN          
SEQRES   6 L  226  PRO TYR LYS SER LEU SER ASP ILE THR LYS ALA ASP PHE          
SEQRES   7 L  226  LEU SER ASP PRO ASN LYS ILE THR PRO VAL PHE VAL ARG          
SEQRES   8 L  226  PHE SER THR VAL GLN GLY GLY ALA GLY SER ALA ASP THR          
SEQRES   9 L  226  VAL ARG ASP ILE ARG GLY PHE ALA THR LYS PHE TYR THR          
SEQRES  10 L  226  GLU GLU GLY ILE PHE ASP LEU VAL GLY ASN ASN THR PRO          
SEQRES  11 L  226  ILE PHE PHE ILE GLN ASP ALA HIS LYS PHE PRO ASP PHE          
SEQRES  12 L  226  VAL HIS ALA VAL LYS PRO GLU PRO HIS TRP ALA ILE PRO          
SEQRES  13 L  226  GLN GLY GLN SER ALA HIS ASP THR PHE TRP ASP TYR VAL          
SEQRES  14 L  226  SER LEU GLN PRO GLU THR LEU HIS ASN VAL MET TRP ALA          
SEQRES  15 L  226  MET SER ASP ARG GLY ILE PRO ARG SER TYR ARG THR MET          
SEQRES  16 L  226  GLU GLY PHE GLY ILE HIS THR PHE ARG LEU ILE ASN ALA          
SEQRES  17 L  226  GLU GLY LYS ALA THR PHE VAL ARG PHE HIS TRP LYS PRO          
SEQRES  18 L  226  LEU ALA GLY LYS ALA                                          
SEQRES   1 P  259  LYS LEU THR GLY ARG ASP PRO ASP PHE HIS ARG ARG GLU          
SEQRES   2 P  259  LEU TRP GLU ALA ILE GLU ALA GLY ASP PHE PRO GLU TYR          
SEQRES   3 P  259  GLU LEU GLY PHE GLN LEU ILE PRO GLU GLU ASP GLU PHE          
SEQRES   4 P  259  LYS PHE ASP PHE ASP LEU LEU ASP PRO THR LYS LEU ILE          
SEQRES   5 P  259  PRO GLU GLU LEU VAL PRO VAL GLN ARG VAL GLY LYS MET          
SEQRES   6 P  259  VAL LEU ASN ARG ASN PRO ASP ASN PHE PHE ALA GLU ASN          
SEQRES   7 P  259  GLU GLN ALA ALA PHE HIS PRO GLY HIS ILE VAL PRO GLY          
SEQRES   8 P  259  LEU ASP PHE THR ASN ASP PRO LEU LEU GLN GLY ARG LEU          
SEQRES   9 P  259  PHE SER TYR THR ASP THR GLN ILE SER ARG LEU GLY GLY          
SEQRES  10 P  259  PRO ASN PHE HIS GLU ILE PRO ILE ASN ARG PRO THR CYS          
SEQRES  11 P  259  PRO TYR HIS ASN PHE GLN ARG ASP GLY MET HIS ARG MET          
SEQRES  12 P  259  GLY ILE ASP THR ASN PRO ALA ASN TYR GLU PRO ASN SER          
SEQRES  13 P  259  ILE ASN ASP ASN TRP PRO ARG GLU THR PRO PRO GLY PRO          
SEQRES  14 P  259  LYS ARG GLY GLY PHE GLU SER TYR GLN GLU ARG VAL GLU          
SEQRES  15 P  259  GLY ASN LYS VAL ARG GLU ARG SER PRO SER PHE GLY GLU          
SEQRES  16 P  259  TYR TYR SER HIS PRO ARG LEU PHE TRP LEU SER GLN THR          
SEQRES  17 P  259  PRO PHE GLU GLN ARG HIS ILE VAL ASP GLY PHE SER PHE          
SEQRES  18 P  259  GLU LEU SER LYS VAL VAL ARG PRO TYR ILE ARG GLU ARG          
SEQRES  19 P  259  VAL VAL ASP GLN LEU ALA HIS ILE ASP LEU THR LEU ALA          
SEQRES  20 P  259  GLN ALA VAL ALA LYS ASN LEU GLY ILE GLU LEU THR              
HET    HDD  E 760      44                                                       
HET    HDD  F 760      44                                                       
HET    HDD  G 760      44                                                       
HET    HDD  H 760      44                                                       
HET    HDD  M 760      44                                                       
HET    HDD  N 760      44                                                       
HET    HDD  O 760      44                                                       
HET    HDD  P 760      44                                                       
HETNAM     HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE                     
HETSYN     HDD HEME                                                             
FORMUL  17  HDD    8(C34 H32 FE N4 O5)                                          
FORMUL  25  HOH   *180(H2 O)                                                    
HELIX    1   1 ASP A  107  HIS A  119  1                                  13    
HELIX    2   2 ALA A  150  SER A  154  5                                   5    
HELIX    3   3 ASP A  210  HIS A  212  5                                   3    
HELIX    4   4 LYS A  213  LYS A  222  1                                  10    
HELIX    5   5 HIS A  236  LEU A  245  1                                  10    
HELIX    6   6 GLN A  246  GLU A  248  5                                   3    
HELIX    7   7 THR A  249  SER A  258  1                                  10    
HELIX    8   8 ASP A  259  ILE A  262  5                                   4    
HELIX    9   9 SER A  265  MET A  269  5                                   5    
HELIX   10  10 LYS E  309  ASP E  314  1                                   6    
HELIX   11  11 ASP E  316  GLY E  329  1                                  14    
HELIX   12  12 GLU E  344  GLU E  346  5                                   3    
HELIX   13  13 ASN E  381  ASN E  386  1                                   6    
HELIX   14  14 ASP E  405  THR E  418  1                                  14    
HELIX   15  15 THR E  418  LEU E  423  1                                   6    
HELIX   16  16 ASN E  427  ARG E  435  5                                   9    
HELIX   17  17 SER E  498  GLY E  502  5                                   5    
HELIX   18  18 TYR E  505  LEU E  513  1                                   9    
HELIX   19  19 THR E  516  LYS E  533  1                                  18    
HELIX   20  20 ARG E  536  HIS E  549  1                                  14    
HELIX   21  21 ASP E  551  GLY E  563  1                                  13    
HELIX   22  22 ASP B  107  HIS B  119  1                                  13    
HELIX   23  23 ALA B  150  SER B  154  5                                   5    
HELIX   24  24 ASP B  210  HIS B  212  5                                   3    
HELIX   25  25 LYS B  213  LYS B  222  1                                  10    
HELIX   26  26 HIS B  236  GLN B  246  1                                  11    
HELIX   27  27 THR B  249  SER B  258  1                                  10    
HELIX   28  28 ASP B  259  ILE B  262  5                                   4    
HELIX   29  29 SER B  265  MET B  269  5                                   5    
HELIX   30  30 LYS F  309  ASP F  314  1                                   6    
HELIX   31  31 ASP F  316  GLY F  329  1                                  14    
HELIX   32  32 GLU F  344  GLU F  346  5                                   3    
HELIX   33  33 ASN F  381  ASN F  386  1                                   6    
HELIX   34  34 ASP F  405  LEU F  423  1                                  19    
HELIX   35  35 ASN F  427  ARG F  435  5                                   9    
HELIX   36  36 SER F  498  GLY F  502  5                                   5    
HELIX   37  37 TYR F  505  LEU F  513  1                                   9    
HELIX   38  38 THR F  516  LYS F  533  1                                  18    
HELIX   39  39 ARG F  536  HIS F  549  1                                  14    
HELIX   40  40 ASP F  551  GLY F  563  1                                  13    
HELIX   41  41 ASP C  107  HIS C  119  1                                  13    
HELIX   42  42 ALA C  150  SER C  154  5                                   5    
HELIX   43  43 ASP C  210  HIS C  212  5                                   3    
HELIX   44  44 LYS C  213  LYS C  222  1                                  10    
HELIX   45  45 HIS C  236  GLN C  246  1                                  11    
HELIX   46  46 THR C  249  SER C  258  1                                  10    
HELIX   47  47 ASP C  259  ILE C  262  5                                   4    
HELIX   48  48 SER C  265  MET C  269  5                                   5    
HELIX   49  49 LYS G  309  ASP G  314  1                                   6    
HELIX   50  50 ASP G  316  GLY G  329  1                                  14    
HELIX   51  51 GLU G  344  LYS G  348  5                                   5    
HELIX   52  52 ASN G  381  ASN G  386  1                                   6    
HELIX   53  53 ASP G  405  THR G  418  1                                  14    
HELIX   54  54 THR G  418  LEU G  423  1                                   6    
HELIX   55  55 ASN G  427  ARG G  435  5                                   9    
HELIX   56  56 SER G  498  GLY G  502  5                                   5    
HELIX   57  57 TYR G  505  SER G  514  1                                  10    
HELIX   58  58 THR G  516  LYS G  533  1                                  18    
HELIX   59  59 ARG G  536  HIS G  549  1                                  14    
HELIX   60  60 ASP G  551  GLY G  563  1                                  13    
HELIX   61  61 ASP D  107  HIS D  119  1                                  13    
HELIX   62  62 ALA D  150  SER D  154  5                                   5    
HELIX   63  63 ASP D  210  HIS D  212  5                                   3    
HELIX   64  64 LYS D  213  LYS D  222  1                                  10    
HELIX   65  65 HIS D  236  GLN D  246  1                                  11    
HELIX   66  66 THR D  249  SER D  258  1                                  10    
HELIX   67  67 ASP D  259  ILE D  262  5                                   4    
HELIX   68  68 SER D  265  MET D  269  5                                   5    
HELIX   69  69 LYS H  309  ASP H  314  1                                   6    
HELIX   70  70 ASP H  316  GLY H  329  1                                  14    
HELIX   71  71 GLU H  344  GLU H  346  5                                   3    
HELIX   72  72 ASN H  381  ASN H  386  1                                   6    
HELIX   73  73 ASP H  405  THR H  418  1                                  14    
HELIX   74  74 THR H  418  LEU H  423  1                                   6    
HELIX   75  75 ASN H  427  ILE H  431  5                                   5    
HELIX   76  76 SER H  498  GLY H  502  5                                   5    
HELIX   77  77 TYR H  505  SER H  514  1                                  10    
HELIX   78  78 THR H  516  LYS H  533  1                                  18    
HELIX   79  79 ARG H  536  HIS H  549  1                                  14    
HELIX   80  80 ASP H  551  GLY H  563  1                                  13    
HELIX   81  81 ASP I  107  HIS I  119  1                                  13    
HELIX   82  82 ALA I  150  SER I  154  5                                   5    
HELIX   83  83 ASP I  210  HIS I  212  5                                   3    
HELIX   84  84 LYS I  213  LYS I  222  1                                  10    
HELIX   85  85 HIS I  236  GLN I  246  1                                  11    
HELIX   86  86 THR I  249  SER I  258  1                                  10    
HELIX   87  87 LYS M  309  ASP M  314  1                                   6    
HELIX   88  88 ASP M  316  GLY M  329  1                                  14    
HELIX   89  89 GLU M  344  GLU M  346  5                                   3    
HELIX   90  90 ASN M  381  ASN M  386  1                                   6    
HELIX   91  91 ASP M  405  LEU M  423  1                                  19    
HELIX   92  92 ASN M  427  ARG M  435  5                                   9    
HELIX   93  93 SER M  498  GLY M  502  5                                   5    
HELIX   94  94 TYR M  505  SER M  514  1                                  10    
HELIX   95  95 THR M  516  LYS M  533  1                                  18    
HELIX   96  96 ARG M  536  HIS M  549  1                                  14    
HELIX   97  97 ASP M  551  GLY M  563  1                                  13    
HELIX   98  98 ASP J  107  HIS J  119  1                                  13    
HELIX   99  99 ALA J  150  SER J  154  5                                   5    
HELIX  100 100 ASP J  210  HIS J  212  5                                   3    
HELIX  101 101 LYS J  213  LYS J  222  1                                  10    
HELIX  102 102 HIS J  236  LEU J  245  1                                  10    
HELIX  103 103 GLN J  246  GLU J  248  5                                   3    
HELIX  104 104 THR J  249  SER J  258  1                                  10    
HELIX  105 105 ASP J  259  ILE J  262  5                                   4    
HELIX  106 106 SER J  265  MET J  269  5                                   5    
HELIX  107 107 LYS N  309  ASP N  314  1                                   6    
HELIX  108 108 ASP N  316  GLY N  329  1                                  14    
HELIX  109 109 GLU N  344  LYS N  348  5                                   5    
HELIX  110 110 ASN N  381  ASN N  386  1                                   6    
HELIX  111 111 ASP N  405  LEU N  423  1                                  19    
HELIX  112 112 ASN N  427  ARG N  435  5                                   9    
HELIX  113 113 SER N  498  GLY N  502  5                                   5    
HELIX  114 114 TYR N  505  SER N  514  1                                  10    
HELIX  115 115 THR N  516  VAL N  534  1                                  19    
HELIX  116 116 ARG N  536  HIS N  549  1                                  14    
HELIX  117 117 ASP N  551  GLY N  563  1                                  13    
HELIX  118 118 ASP K  107  HIS K  119  1                                  13    
HELIX  119 119 ALA K  150  SER K  154  5                                   5    
HELIX  120 120 ASP K  210  HIS K  212  5                                   3    
HELIX  121 121 LYS K  213  LYS K  222  1                                  10    
HELIX  122 122 HIS K  236  GLN K  246  1                                  11    
HELIX  123 123 THR K  249  SER K  258  1                                  10    
HELIX  124 124 ASP K  259  ILE K  262  5                                   4    
HELIX  125 125 LYS O  309  ASP O  314  1                                   6    
HELIX  126 126 ASP O  316  GLY O  329  1                                  14    
HELIX  127 127 GLU O  344  LYS O  348  5                                   5    
HELIX  128 128 ASN O  381  ASN O  386  1                                   6    
HELIX  129 129 ASP O  405  THR O  418  1                                  14    
HELIX  130 130 THR O  418  LEU O  423  1                                   6    
HELIX  131 131 ASN O  427  ARG O  435  5                                   9    
HELIX  132 132 SER O  498  GLY O  502  5                                   5    
HELIX  133 133 TYR O  505  SER O  514  1                                  10    
HELIX  134 134 THR O  516  LYS O  533  1                                  18    
HELIX  135 135 ARG O  536  HIS O  549  1                                  14    
HELIX  136 136 ASP O  551  GLY O  563  1                                  13    
HELIX  137 137 ASP L  107  HIS L  119  1                                  13    
HELIX  138 138 ALA L  150  SER L  154  5                                   5    
HELIX  139 139 ASP L  210  HIS L  212  5                                   3    
HELIX  140 140 LYS L  213  LYS L  222  1                                  10    
HELIX  141 141 HIS L  236  GLN L  246  1                                  11    
HELIX  142 142 THR L  249  SER L  258  1                                  10    
HELIX  143 143 SER L  265  MET L  269  5                                   5    
HELIX  144 144 LYS P  309  ASP P  314  1                                   6    
HELIX  145 145 ASP P  316  GLY P  329  1                                  14    
HELIX  146 146 GLU P  344  GLU P  346  5                                   3    
HELIX  147 147 ASN P  381  ASN P  386  1                                   6    
HELIX  148 148 ASP P  405  LEU P  423  1                                  19    
HELIX  149 149 ASN P  427  ARG P  435  5                                   9    
HELIX  150 150 SER P  498  GLY P  502  5                                   5    
HELIX  151 151 TYR P  505  SER P  514  1                                  10    
HELIX  152 152 THR P  516  LYS P  533  1                                  18    
HELIX  153 153 ARG P  536  HIS P  549  1                                  14    
HELIX  154 154 ASP P  551  GLY P  563  1                                  13    
SHEET    1   A 4 ARG A  96  ALA A  97  0                                        
SHEET    2   A 4 ARG H 488  VAL H 494 -1  O  VAL H 494   N  ARG A  96           
SHEET    3   A 4 ARG G 488  ARG G 495 -1  N  GLY G 491   O  VAL H 489           
SHEET    4   A 4 LEU B  95  ALA B  97 -1  N  ARG B  96   O  VAL G 494           
SHEET    1   B10 LEU E 400  ASP E 401  0                                        
SHEET    2   B10 GLY A 271  ILE A 280 -1  N  ARG A 278   O  ASP E 401           
SHEET    3   B10 ALA A 286  PRO A 295 -1  O  TRP A 293   N  GLY A 271           
SHEET    4   B10 GLU E 333  PRO E 342 -1  O  GLU E 335   N  LYS A 294           
SHEET    5   B10 VAL E 367  ARG E 377 -1  O  GLN E 368   N  PHE E 338           
SHEET    6   B10 GLY A 131  PRO A 140 -1  N  HIS A 135   O  ARG E 377           
SHEET    7   B10 THR A 160  SER A 167 -1  O  VAL A 162   N  GLY A 136           
SHEET    8   B10 GLY A 184  THR A 191 -1  O  ALA A 186   N  ARG A 165           
SHEET    9   B10 GLY A 194  ASN A 201 -1  O  PHE A 196   N  PHE A 189           
SHEET   10   B10 GLY A 271  ILE A 280 -1  O  PHE A 272   N  ASN A 201           
SHEET    1   C 4 LEU C  95  ALA C  97  0                                        
SHEET    2   C 4 ARG F 488  ARG F 495 -1  N  VAL F 494   O  ARG C  96           
SHEET    3   C 4 ARG E 488  VAL E 494 -1  N  VAL E 489   O  GLY F 491           
SHEET    4   C 4 ARG D  96  ALA D  97 -1  O  ARG D  96   N  VAL E 494           
SHEET    1   D11 LEU F 400  ASP F 401  0                                        
SHEET    2   D11 PHE B 277  ILE B 280 -1  N  ARG B 278   O  ASP F 401           
SHEET    3   D11 ALA B 286  PRO B 295 -1  O  VAL B 289   N  PHE B 277           
SHEET    4   D11 GLU F 333  PRO F 342 -1  O  GLU F 335   N  LYS B 294           
SHEET    5   D11 GLN F 368  ARG F 377 -1  O  MET F 373   N  TYR F 334           
SHEET    6   D11 GLY B 131  PRO B 140 -1  N  HIS B 135   O  ARG F 377           
SHEET    7   D11 THR B 160  THR B 168 -1  O  PHE B 166   N  SER B 132           
SHEET    8   D11 ARG B 183  THR B 191 -1  O  LYS B 188   N  PHE B 163           
SHEET    9   D11 GLY B 194  ASN B 201 -1  O  PHE B 196   N  PHE B 189           
SHEET   10   D11 GLY B 271  PHE B 272 -1  O  PHE B 272   N  ASN B 201           
SHEET   11   D11 ALA B 286  PRO B 295 -1  O  TRP B 293   N  GLY B 271           
SHEET    1   E11 LEU G 400  ASP G 401  0                                        
SHEET    2   E11 PHE C 277  ILE C 280 -1  N  ARG C 278   O  ASP G 401           
SHEET    3   E11 ALA C 286  PRO C 295 -1  O  VAL C 289   N  PHE C 277           
SHEET    4   E11 GLU G 333  PRO G 342 -1  O  GLU G 335   N  LYS C 294           
SHEET    5   E11 VAL G 367  ARG G 377 -1  O  MET G 373   N  TYR G 334           
SHEET    6   E11 GLY C 131  PRO C 140 -1  N  HIS C 135   O  ARG G 377           
SHEET    7   E11 THR C 160  THR C 168 -1  O  PHE C 166   N  SER C 132           
SHEET    8   E11 ARG C 183  THR C 191 -1  O  LYS C 188   N  PHE C 163           
SHEET    9   E11 GLY C 194  ASN C 201 -1  O  GLY C 200   N  PHE C 185           
SHEET   10   E11 GLY C 271  PHE C 272 -1  O  PHE C 272   N  ASN C 201           
SHEET   11   E11 ALA C 286  PRO C 295 -1  O  TRP C 293   N  GLY C 271           
SHEET    1   F11 LEU H 400  ASP H 401  0                                        
SHEET    2   F11 PHE D 277  ILE D 280 -1  N  ARG D 278   O  ASP H 401           
SHEET    3   F11 ALA D 286  PRO D 295 -1  O  VAL D 289   N  PHE D 277           
SHEET    4   F11 GLU H 333  PRO H 342 -1  O  GLU H 335   N  LYS D 294           
SHEET    5   F11 VAL H 367  ARG H 377 -1  O  MET H 373   N  TYR H 334           
SHEET    6   F11 GLY D 131  PRO D 140 -1  N  HIS D 135   O  ARG H 377           
SHEET    7   F11 THR D 160  SER D 167 -1  O  THR D 160   N  PHE D 138           
SHEET    8   F11 GLY D 184  THR D 191 -1  O  LYS D 188   N  PHE D 163           
SHEET    9   F11 GLY D 194  ASN D 201 -1  O  GLY D 200   N  PHE D 185           
SHEET   10   F11 GLY D 271  PHE D 272 -1  O  PHE D 272   N  ASN D 201           
SHEET   11   F11 ALA D 286  PRO D 295 -1  O  TRP D 293   N  GLY D 271           
SHEET    1   G 4 ARG I  96  ALA I  97  0                                        
SHEET    2   G 4 ARG P 488  VAL P 494 -1  O  VAL P 494   N  ARG I  96           
SHEET    3   G 4 ARG O 488  VAL O 494 -1  N  GLY O 491   O  VAL P 489           
SHEET    4   G 4 ARG J  96  ALA J  97 -1  N  ARG J  96   O  VAL O 494           
SHEET    1   H11 LEU M 400  ASP M 401  0                                        
SHEET    2   H11 PHE I 277  ILE I 280 -1  N  ARG I 278   O  ASP M 401           
SHEET    3   H11 ALA I 286  PRO I 295 -1  O  THR I 287   N  LEU I 279           
SHEET    4   H11 GLU M 333  PRO M 342 -1  O  GLU M 335   N  LYS I 294           
SHEET    5   H11 VAL M 367  ARG M 377 -1  O  MET M 373   N  TYR M 334           
SHEET    6   H11 GLY I 131  PRO I 140 -1  N  HIS I 135   O  ARG M 377           
SHEET    7   H11 THR I 160  SER I 167 -1  O  THR I 160   N  PHE I 138           
SHEET    8   H11 GLY I 184  THR I 191 -1  O  LYS I 188   N  PHE I 163           
SHEET    9   H11 GLY I 194  ASN I 201 -1  O  GLY I 200   N  PHE I 185           
SHEET   10   H11 GLY I 271  PHE I 272 -1  O  PHE I 272   N  ASN I 201           
SHEET   11   H11 ALA I 286  PRO I 295 -1  O  TRP I 293   N  GLY I 271           
SHEET    1   I 4 ARG K  96  ALA K  97  0                                        
SHEET    2   I 4 ARG N 488  VAL N 494 -1  N  VAL N 494   O  ARG K  96           
SHEET    3   I 4 ARG M 488  ARG M 495 -1  N  VAL M 489   O  GLY N 491           
SHEET    4   I 4 LEU L  95  ALA L  97 -1  O  ARG L  96   N  VAL M 494           
SHEET    1   J11 LEU N 400  ASP N 401  0                                        
SHEET    2   J11 PHE J 277  ILE J 280 -1  N  ARG J 278   O  ASP N 401           
SHEET    3   J11 ALA J 286  PRO J 295 -1  O  THR J 287   N  LEU J 279           
SHEET    4   J11 GLU N 333  PRO N 342 -1  O  GLY N 337   N  HIS J 292           
SHEET    5   J11 VAL N 367  ARG N 377 -1  O  GLY N 371   N  LEU N 336           
SHEET    6   J11 GLY J 131  PRO J 140 -1  N  HIS J 135   O  ARG N 377           
SHEET    7   J11 THR J 160  THR J 168 -1  O  PHE J 166   N  SER J 132           
SHEET    8   J11 ARG J 183  THR J 191 -1  O  ALA J 186   N  ARG J 165           
SHEET    9   J11 GLY J 194  ASN J 201 -1  O  GLY J 200   N  PHE J 185           
SHEET   10   J11 GLY J 271  PHE J 272 -1  O  PHE J 272   N  ASN J 201           
SHEET   11   J11 ALA J 286  PRO J 295 -1  O  TRP J 293   N  GLY J 271           
SHEET    1   K11 LEU O 400  ASP O 401  0                                        
SHEET    2   K11 PHE K 277  ASN K 281 -1  N  ARG K 278   O  ASP O 401           
SHEET    3   K11 LYS K 285  PRO K 295 -1  O  THR K 287   N  LEU K 279           
SHEET    4   K11 GLU O 333  PRO O 342 -1  O  GLU O 335   N  LYS K 294           
SHEET    5   K11 VAL O 367  ARG O 377 -1  O  MET O 373   N  TYR O 334           
SHEET    6   K11 GLY K 131  PRO K 140 -1  N  HIS K 135   O  ARG O 377           
SHEET    7   K11 THR K 160  SER K 167 -1  O  VAL K 162   N  GLY K 136           
SHEET    8   K11 GLY K 184  THR K 191 -1  O  LYS K 188   N  PHE K 163           
SHEET    9   K11 GLY K 194  ASN K 201 -1  O  GLY K 200   N  PHE K 185           
SHEET   10   K11 GLY K 271  PHE K 272 -1  O  PHE K 272   N  ASN K 201           
SHEET   11   K11 LYS K 285  PRO K 295 -1  O  TRP K 293   N  GLY K 271           
SHEET    1   L11 LEU P 400  ASP P 401  0                                        
SHEET    2   L11 PHE L 277  ILE L 280 -1  N  ARG L 278   O  ASP P 401           
SHEET    3   L11 ALA L 286  PRO L 295 -1  O  THR L 287   N  LEU L 279           
SHEET    4   L11 GLU P 333  PRO P 342 -1  O  GLY P 337   N  HIS L 292           
SHEET    5   L11 GLN P 368  ARG P 377 -1  O  GLN P 368   N  PHE P 338           
SHEET    6   L11 GLY L 131  PRO L 140 -1  N  HIS L 135   O  ARG P 377           
SHEET    7   L11 THR L 160  SER L 167 -1  O  PHE L 166   N  SER L 132           
SHEET    8   L11 GLY L 184  THR L 191 -1  O  LYS L 188   N  PHE L 163           
SHEET    9   L11 GLY L 194  ASN L 201 -1  O  GLY L 200   N  PHE L 185           
SHEET   10   L11 GLY L 271  PHE L 272 -1  O  PHE L 272   N  ASN L 201           
SHEET   11   L11 ALA L 286  PRO L 295 -1  O  TRP L 293   N  GLY L 271           
LINK        FE   HDD E 760                 OH  TYR E 415     1555   1555  1.91  
LINK        FE   HDD F 760                 OH  TYR F 415     1555   1555  2.20  
LINK        FE   HDD G 760                 OH  TYR G 415     1555   1555  1.96  
LINK        FE   HDD H 760                 OH  TYR H 415     1555   1555  1.74  
LINK        FE   HDD M 760                 OH  TYR M 415     1555   1555  1.73  
LINK        FE   HDD N 760                 OH  TYR N 415     1555   1555  1.98  
LINK        FE   HDD O 760                 OH  TYR O 415     1555   1555  1.84  
LINK        FE   HDD P 760                 OH  TYR P 415     1555   1555  2.05  
CISPEP   1 ILE A  229    PRO A  230          0        -2.13                     
CISPEP   2 GLU E  461    PRO E  462          0        12.68                     
CISPEP   3 TRP E  469    PRO E  470          0         0.83                     
CISPEP   4 ILE B  229    PRO B  230          0        -2.13                     
CISPEP   5 GLU F  461    PRO F  462          0        19.99                     
CISPEP   6 TRP F  469    PRO F  470          0        -0.13                     
CISPEP   7 ILE C  229    PRO C  230          0        -2.94                     
CISPEP   8 GLU G  461    PRO G  462          0         8.14                     
CISPEP   9 TRP G  469    PRO G  470          0         2.53                     
CISPEP  10 ILE D  229    PRO D  230          0         0.87                     
CISPEP  11 GLU H  461    PRO H  462          0        13.12                     
CISPEP  12 TRP H  469    PRO H  470          0         2.49                     
CISPEP  13 ILE I  229    PRO I  230          0        -2.39                     
CISPEP  14 GLU M  461    PRO M  462          0        12.35                     
CISPEP  15 TRP M  469    PRO M  470          0        -5.34                     
CISPEP  16 ILE J  229    PRO J  230          0       -11.54                     
CISPEP  17 GLU N  461    PRO N  462          0        14.78                     
CISPEP  18 TRP N  469    PRO N  470          0         2.39                     
CISPEP  19 ILE K  229    PRO K  230          0         1.93                     
CISPEP  20 GLU O  461    PRO O  462          0        10.21                     
CISPEP  21 TRP O  469    PRO O  470          0         1.05                     
CISPEP  22 ILE L  229    PRO L  230          0        -5.82                     
CISPEP  23 GLU P  461    PRO P  462          0        10.65                     
CISPEP  24 TRP P  469    PRO P  470          0        -0.84                     
SITE     1 AC1 20 ARG A 125  VAL A 127  HIS A 128  ARG A 165                    
SITE     2 AC1 20 GLY A 184  VAL A 199  GLY A 200  ASN A 201                    
SITE     3 AC1 20 PHE A 206  PHE A 214  ILE A 274  HOH A 303                    
SITE     4 AC1 20 PHE D 117  HOH E 137  PHE E 391  LEU E 407                    
SITE     5 AC1 20 ARG E 411  SER E 414  TYR E 415  GLN E 419                    
SITE     1 AC2 20 ARG B 125  ILE B 126  VAL B 127  HIS B 128                    
SITE     2 AC2 20 ARG B 165  GLY B 184  VAL B 199  GLY B 200                    
SITE     3 AC2 20 ASN B 201  PHE B 206  PHE B 214  ILE B 274                    
SITE     4 AC2 20 PHE F 391  LEU F 407  ARG F 411  SER F 414                    
SITE     5 AC2 20 TYR F 415  THR F 418  GLN F 419  ARG F 422                    
SITE     1 AC3 21 PHE B 117  ARG C 125  ILE C 126  VAL C 127                    
SITE     2 AC3 21 HIS C 128  ARG C 165  GLY C 184  VAL C 199                    
SITE     3 AC3 21 GLY C 200  ASN C 201  PHE C 206  PHE C 214                    
SITE     4 AC3 21 ILE C 274  HIS C 275  PHE G 391  LEU G 407                    
SITE     5 AC3 21 ARG G 411  SER G 414  TYR G 415  THR G 418                    
SITE     6 AC3 21 GLN G 419                                                     
SITE     1 AC4 19 ARG D 125  ILE D 126  VAL D 127  HIS D 128                    
SITE     2 AC4 19 ARG D 165  GLY D 184  VAL D 199  GLY D 200                    
SITE     3 AC4 19 ASN D 201  PHE D 206  PHE D 214  PHE H 391                    
SITE     4 AC4 19 LEU H 407  ARG H 411  SER H 414  TYR H 415                    
SITE     5 AC4 19 THR H 418  GLN H 419  ARG H 422                               
SITE     1 AC5 18 ARG I 125  ILE I 126  VAL I 127  HIS I 128                    
SITE     2 AC5 18 ARG I 165  GLY I 184  VAL I 199  GLY I 200                    
SITE     3 AC5 18 ASN I 201  PHE I 214  HIS I 275  PHE M 391                    
SITE     4 AC5 18 LEU M 407  ARG M 411  SER M 414  TYR M 415                    
SITE     5 AC5 18 THR M 418  GLN M 419                                          
SITE     1 AC6 18 ARG J 125  VAL J 127  HIS J 128  ARG J 165                    
SITE     2 AC6 18 GLY J 184  VAL J 199  GLY J 200  ASN J 201                    
SITE     3 AC6 18 PHE J 206  PHE J 214  ILE J 274  PHE K 117                    
SITE     4 AC6 18 PHE N 391  LEU N 407  ARG N 411  SER N 414                    
SITE     5 AC6 18 TYR N 415  GLN N 419                                          
SITE     1 AC7 20 ARG K 125  VAL K 127  HIS K 128  ARG K 165                    
SITE     2 AC7 20 GLY K 184  VAL K 199  GLY K 200  ASN K 201                    
SITE     3 AC7 20 PHE K 206  PHE K 214  HIS K 275  PHE O 391                    
SITE     4 AC7 20 LEU O 407  ARG O 411  SER O 414  TYR O 415                    
SITE     5 AC7 20 THR O 418  GLN O 419  ARG O 422  HOH O 761                    
SITE     1 AC8 20 ARG L 125  ILE L 126  VAL L 127  HIS L 128                    
SITE     2 AC8 20 ARG L 165  GLY L 184  ALA L 186  VAL L 199                    
SITE     3 AC8 20 GLY L 200  ASN L 201  PHE L 206  PHE L 214                    
SITE     4 AC8 20 ILE L 274  PHE P 391  ARG P 411  SER P 414                    
SITE     5 AC8 20 TYR P 415  THR P 418  GLN P 419  ARG P 422                    
CRYST1  111.011  152.888  135.287  90.00  97.54  90.00 P 1 21 1     16          
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      0.009008  0.000000  0.001192        0.00000                         
SCALE2      0.000000  0.006541  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007456        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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