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Database: PDB
Entry: 2BPI
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HEADER    OXIDOREDUCTASE                          20-APR-05   2BPI              
TITLE     STRUCTURE OF IRON DEPENDENT SUPEROXIDE DISMUTASE FROM P. FALCIPARUM.  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FE-SUPEROXIDE DISMUTASE;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;                          
SOURCE   3 ORGANISM_TAXID: 36329;                                               
SOURCE   4 STRAIN: 3D7;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET 28C                                   
KEYWDS    DISMUTASE, OXIDOREDUCTASE, METAL-BINDING                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.W.BOUCHER,J.A.BRANNIGAN,A.J.WILKINSON,A.M BRZOZOWSKI                
REVDAT   3   24-APR-13 2BPI    1       TITLE  REMARK VERSN  FORMUL              
REVDAT   2   24-FEB-09 2BPI    1       VERSN                                    
REVDAT   1   11-OCT-06 2BPI    0                                                
JRNL        AUTH   I.W.BOUCHER,A.M.BRZOZOWSKI,J.A.BRANNIGAN,C.SCHNICK,          
JRNL        AUTH 2 D.J.SMITH,S.A.KYES,A.J.WILKINSON                             
JRNL        TITL   THE CRYSTAL STRUCTURE OF SUPEROXIDE DISMUTASE FROM           
JRNL        TITL 2 PLASMODIUM FALCIPARUM.                                       
JRNL        REF    BMC STRUCT.BIOL.              V.   6    20 2006              
JRNL        REFN                   ISSN 1472-6807                               
JRNL        PMID   17020617                                                     
JRNL        DOI    10.1186/1472-6807-6-20                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.52 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 2.52                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 59.76                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 13247                          
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) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 697                             
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) : 2.52                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.58                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 843                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2240                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 50                           
REMARK   3   BIN FREE R VALUE                    : 0.3380                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3202                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 140                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.74000                                             
REMARK   3    B22 (A**2) : 1.37000                                              
REMARK   3    B33 (A**2) : 0.37000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 6.219         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.339         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.229         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.172        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.878                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3262 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4442 ; 1.453 ; 1.901       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   392 ; 6.350 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   169 ;36.632 ;25.385       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   503 ;18.676 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     4 ;14.211 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   459 ; 0.107 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2560 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1624 ; 0.209 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2208 ; 0.309 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   176 ; 0.147 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    19 ; 0.203 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.217 ; 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):  2003 ; 0.689 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3134 ; 1.189 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1493 ; 1.695 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1308 ; 2.542 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2BPI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-APR-05.                  
REMARK 100 THE PDBE ID CODE IS EBI-21292.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JUL-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97600                            
REMARK 200  MONOCHROMATOR                  : LIQUID NITROGEN COOLED             
REMARK 200                                   CHANNEL-CUT SILICON                
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13247                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.520                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1ISC                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH 7.5,38% PEG 600             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       27.97050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.31050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.45500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.31050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.97050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.45500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     LEU A   198                                                      
REMARK 465     GLU A   199                                                      
REMARK 465     HIS A   200                                                      
REMARK 465     HIS A   201                                                      
REMARK 465     HIS A   202                                                      
REMARK 465     HIS A   203                                                      
REMARK 465     HIS A   204                                                      
REMARK 465     HIS A   205                                                      
REMARK 465     MET B     0                                                      
REMARK 465     LEU B   198                                                      
REMARK 465     GLU B   199                                                      
REMARK 465     HIS B   200                                                      
REMARK 465     HIS B   201                                                      
REMARK 465     HIS B   202                                                      
REMARK 465     HIS B   203                                                      
REMARK 465     HIS B   204                                                      
REMARK 465     HIS B   205                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A    6   CG   CD   CE   NZ                                   
REMARK 480     LYS A   43   CD   CE   NZ                                        
REMARK 480     ASP A   44   CB   CG   OD1  OD2                                  
REMARK 480     LYS A   50   CG   CD   CE   NZ                                   
REMARK 480     LYS A  176   CD   CE   NZ                                        
REMARK 480     LYS A  193   CD   CE   NZ                                        
REMARK 480     LYS B   37   CE   NZ                                             
REMARK 480     LYS B   43   CD   CE   NZ                                        
REMARK 480     LYS B   50   CG   CD   CE   NZ                                   
REMARK 480     GLU B   91   CD   OE1  OE2                                       
REMARK 480     LYS B  176   CE   NZ                                             
REMARK 480     GLN B  196   CD   OE1  NE2                                       
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   OD1  ASP A    44     NE2  GLN B   196     1455     1.95            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU B  91   CG    GLU B  91   CD     -0.172                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  29      -66.38   -102.47                                   
REMARK 500    LYS A  43      -72.44    -13.84                                   
REMARK 500    CYS A  84     -140.29   -124.10                                   
REMARK 500    ASP A 140     -112.82     57.83                                   
REMARK 500    ARG A 168     -130.67     48.44                                   
REMARK 500    LYS B  29      -69.75   -104.57                                   
REMARK 500    LYS B  43      -65.99    -27.28                                   
REMARK 500    CYS B  84     -151.62   -123.64                                   
REMARK 500    ASN B 128     -161.84    -79.56                                   
REMARK 500    ASP B 140     -112.32     57.94                                   
REMARK 500    TYR B 163      -10.10   -142.65                                   
REMARK 500    ARG B 168     -135.23     49.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A1198  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  26   NE2                                                    
REMARK 620 2 HIS A  73   NE2  88.8                                              
REMARK 620 3 HIS A 161   NE2  99.8 127.6                                        
REMARK 620 4 ASP A 157   OD2  85.5 106.5 125.6                                  
REMARK 620 5 HOH A2055   O   167.5  94.0  88.1  82.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B1198  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 157   OD2                                                    
REMARK 620 2 HIS B 161   NE2 114.8                                              
REMARK 620 3 HOH B2054   O    82.2  94.9                                        
REMARK 620 4 HIS B  26   NE2  90.9  93.8 170.6                                  
REMARK 620 5 HIS B  73   NE2 110.7 133.2  80.7  95.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE A1198                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE B1198                 
DBREF  2BPI A    0   197  UNP    Q8IAY6   Q8IAY6_PLAF7     1    198             
DBREF  2BPI A  198   205  PDB    2BPI     2BPI           198    205             
DBREF  2BPI B    0   197  UNP    Q8IAY6   Q8IAY6_PLAF7     1    198             
DBREF  2BPI B  198   205  PDB    2BPI     2BPI           198    205             
SEQRES   1 A  206  MET VAL ILE THR LEU PRO LYS LEU LYS TYR ALA LEU ASN          
SEQRES   2 A  206  ALA LEU SER PRO HIS ILE SER GLU GLU THR LEU ASN PHE          
SEQRES   3 A  206  HIS TYR ASN LYS HIS HIS ALA GLY TYR VAL ASN LYS LEU          
SEQRES   4 A  206  ASN THR LEU ILE LYS ASP THR PRO PHE ALA GLU LYS SER          
SEQRES   5 A  206  LEU LEU ASP ILE VAL LYS GLU SER SER GLY ALA ILE PHE          
SEQRES   6 A  206  ASN ASN ALA ALA GLN ILE TRP ASN HIS THR PHE TYR TRP          
SEQRES   7 A  206  ASP SER MET GLY PRO ASP CYS GLY GLY GLU PRO HIS GLY          
SEQRES   8 A  206  GLU ILE LYS GLU LYS ILE GLN GLU ASP PHE GLY SER PHE          
SEQRES   9 A  206  ASN ASN PHE LYS GLU GLN PHE SER ASN ILE LEU CYS GLY          
SEQRES  10 A  206  HIS PHE GLY SER GLY TRP GLY TRP LEU ALA LEU ASN ASN          
SEQRES  11 A  206  ASN ASN LYS LEU VAL ILE LEU GLN THR HIS ASP ALA GLY          
SEQRES  12 A  206  ASN PRO ILE LYS ASP ASN THR GLY ILE PRO ILE LEU THR          
SEQRES  13 A  206  CYS ASP ILE TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG          
SEQRES  14 A  206  ASN ASP ARG ALA SER TYR VAL LYS ALA TRP TRP ASN LEU          
SEQRES  15 A  206  VAL ASN TRP ASN PHE ALA ASN GLU ASN LEU LYS LYS ALA          
SEQRES  16 A  206  MET GLN LYS LEU GLU HIS HIS HIS HIS HIS HIS                  
SEQRES   1 B  206  MET VAL ILE THR LEU PRO LYS LEU LYS TYR ALA LEU ASN          
SEQRES   2 B  206  ALA LEU SER PRO HIS ILE SER GLU GLU THR LEU ASN PHE          
SEQRES   3 B  206  HIS TYR ASN LYS HIS HIS ALA GLY TYR VAL ASN LYS LEU          
SEQRES   4 B  206  ASN THR LEU ILE LYS ASP THR PRO PHE ALA GLU LYS SER          
SEQRES   5 B  206  LEU LEU ASP ILE VAL LYS GLU SER SER GLY ALA ILE PHE          
SEQRES   6 B  206  ASN ASN ALA ALA GLN ILE TRP ASN HIS THR PHE TYR TRP          
SEQRES   7 B  206  ASP SER MET GLY PRO ASP CYS GLY GLY GLU PRO HIS GLY          
SEQRES   8 B  206  GLU ILE LYS GLU LYS ILE GLN GLU ASP PHE GLY SER PHE          
SEQRES   9 B  206  ASN ASN PHE LYS GLU GLN PHE SER ASN ILE LEU CYS GLY          
SEQRES  10 B  206  HIS PHE GLY SER GLY TRP GLY TRP LEU ALA LEU ASN ASN          
SEQRES  11 B  206  ASN ASN LYS LEU VAL ILE LEU GLN THR HIS ASP ALA GLY          
SEQRES  12 B  206  ASN PRO ILE LYS ASP ASN THR GLY ILE PRO ILE LEU THR          
SEQRES  13 B  206  CYS ASP ILE TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG          
SEQRES  14 B  206  ASN ASP ARG ALA SER TYR VAL LYS ALA TRP TRP ASN LEU          
SEQRES  15 B  206  VAL ASN TRP ASN PHE ALA ASN GLU ASN LEU LYS LYS ALA          
SEQRES  16 B  206  MET GLN LYS LEU GLU HIS HIS HIS HIS HIS HIS                  
HET     FE  A1198       1                                                       
HET     FE  B1198       1                                                       
HETNAM      FE FE (III) ION                                                     
FORMUL   3   FE    2(FE 3+)                                                     
FORMUL   5  HOH   *140(H2 O)                                                    
HELIX    1   1 SER A   19  LYS A   29  1                                  11    
HELIX    2   2 LYS A   29  LYS A   43  1                                  15    
HELIX    3   3 SER A   51  SER A   59  1                                   9    
HELIX    4   4 SER A   60  SER A   79  1                                  20    
HELIX    5   5 GLY A   90  GLY A  101  1                                  12    
HELIX    6   6 SER A  102  HIS A  117  1                                  16    
HELIX    7   7 TRP A  159  ALA A  162  5                                   4    
HELIX    8   8 TYR A  163  ARG A  168  1                                   6    
HELIX    9   9 ASP A  170  TRP A  179  1                                  10    
HELIX   10  10 ASN A  183  LYS A  197  1                                  15    
HELIX   11  11 SER B   19  LYS B   29  1                                  11    
HELIX   12  12 LYS B   29  LYS B   43  1                                  15    
HELIX   13  13 THR B   45  GLU B   49  5                                   5    
HELIX   14  14 SER B   51  SER B   59  1                                   9    
HELIX   15  15 SER B   60  SER B   79  1                                  20    
HELIX   16  16 GLY B   90  GLY B  101  1                                  12    
HELIX   17  17 SER B  102  GLY B  116  1                                  15    
HELIX   18  18 ASN B  143  ASN B  148  1                                   6    
HELIX   19  19 TRP B  159  ALA B  162  5                                   4    
HELIX   20  20 TYR B  163  ARG B  168  1                                   6    
HELIX   21  21 ASP B  170  TRP B  179  1                                  10    
HELIX   22  22 ASN B  183  LYS B  197  1                                  15    
SHEET    1  AA 3 LEU A 133  HIS A 139  0                                        
SHEET    2  AA 3 GLY A 121  LEU A 127 -1  O  TRP A 122   N  THR A 138           
SHEET    3  AA 3 ILE A 151  ASP A 157 -1  O  ILE A 151   N  LEU A 127           
SHEET    1  BA 3 LEU B 133  HIS B 139  0                                        
SHEET    2  BA 3 GLY B 121  LEU B 127 -1  O  TRP B 122   N  THR B 138           
SHEET    3  BA 3 ILE B 151  ASP B 157 -1  O  ILE B 151   N  LEU B 127           
LINK        FE    FE A1198                 NE2 HIS A  26     1555   1555  2.29  
LINK        FE    FE A1198                 NE2 HIS A  73     1555   1555  2.10  
LINK        FE    FE A1198                 NE2 HIS A 161     1555   1555  2.08  
LINK        FE    FE A1198                 OD2 ASP A 157     1555   1555  1.81  
LINK        FE    FE A1198                 O   HOH A2055     1555   1555  2.15  
LINK        FE    FE B1198                 NE2 HIS B 161     1555   1555  2.02  
LINK        FE    FE B1198                 O   HOH B2054     1555   1555  2.25  
LINK        FE    FE B1198                 NE2 HIS B  26     1555   1555  2.07  
LINK        FE    FE B1198                 NE2 HIS B  73     1555   1555  2.13  
LINK        FE    FE B1198                 OD2 ASP B 157     1555   1555  2.03  
CISPEP   1 SER A   15    PRO A   16          0         0.85                     
CISPEP   2 SER B   15    PRO B   16          0       -15.85                     
SITE     1 AC1  5 HIS A  26  HIS A  73  ASP A 157  HIS A 161                    
SITE     2 AC1  5 HOH A2055                                                     
SITE     1 AC2  5 HIS B  26  HIS B  73  ASP B 157  HIS B 161                    
SITE     2 AC2  5 HOH B2054                                                     
CRYST1   55.941   78.910   90.621  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017876  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012673  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011035        0.00000                         
MTRIX1   1 -0.999820  0.010060 -0.016290       48.63206    1                    
MTRIX2   1 -0.014930  0.123230  0.992270       -5.72955    1                    
MTRIX3   1  0.011990  0.992330 -0.123060        6.67508    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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