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Database: PDB
Entry: 1E29
LinkDB: 1E29
Original site: 1E29 
HEADER    ELECTRON TRANSPORT                      19-MAY-00   1E29              
TITLE     PSII ASSOCIATED CYTOCHROME C549 FROM SYNECHOCYSTIS SP.                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME C549;                                           
COMPND   3 CHAIN: A                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP;                               
SOURCE   3 ORGANISM_TAXID: 1143;                                                
SOURCE   4 STRAIN: PCC 6803                                                     
KEYWDS    ELECTRON TRANSPORT, PSII ASSOCIATED CYTOCHROME, CYTOCHROME, LOW       
KEYWDS   2 POTENTIAL, BIS_HISTIDINYL, PSII MODULATOR                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.FRAZAO,F.J.ENGUITA,R.COELHO,G.M.SHELDRICK                           
REVDAT   9   24-JUL-19 1E29    1       REMARK                                   
REVDAT   8   22-MAY-19 1E29    1       REMARK                                   
REVDAT   7   08-MAY-19 1E29    1       REMARK                                   
REVDAT   6   12-JUL-17 1E29    1                                                
REVDAT   5   24-FEB-09 1E29    1       VERSN                                    
REVDAT   4   24-JUN-03 1E29    1       REMARK LINK   SITE                       
REVDAT   3   10-JUL-02 1E29    1       HET    HETNAM LINK   HETATM              
REVDAT   3 2                   1       ANISOU                                   
REVDAT   2   11-MAY-01 1E29    1       REVDAT REMARK                            
REVDAT   1   04-MAY-01 1E29    0                                                
JRNL        AUTH   C.FRAZAO,F.J.ENGUITA,R.COELHO,G.M.SHELDRICK,J.A.NAVARRO,     
JRNL        AUTH 2 M.HERVAS,M.A.DE LA ROSA,M.A.CARRONDO                         
JRNL        TITL   CRYSTAL STRUCTURE OF LOW-POTENTIAL CYTOCHROME C549 FROM      
JRNL        TITL 2 SYNECHOCYSTIS SP. PCC 6803 AT 1.21A RESOLUTION               
JRNL        REF    J.BIOL.INORG.CHEM.            V.   6   324 2001              
JRNL        REFN                   ISSN 0949-8257                               
JRNL        PMID   11315568                                                     
JRNL        DOI    10.1007/S007750100208                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.21 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.21                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 97.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.8                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R-VALUE                   
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.153                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.149                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.212                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 2158                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 42953                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.149                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.144                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.208                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 1923                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 38228                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 1065                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 46                                            
REMARK   3   SOLVENT ATOMS      : 223                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 1329.9                  
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 1051.0                  
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 3                       
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 12079                   
REMARK   3   NUMBER OF RESTRAINTS                     : 14469                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.013                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.034                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.018                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.028                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.077                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.078                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.043                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.005                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.060                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.115                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-2          
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: HEME TARGET VALUES FROM CYTOCHROME C6, STRUCTURE     
REMARK   3                 3(1995)1159-1169                                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1E29 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-MAY-00.                  
REMARK 100 THE DEPOSITION ID IS D_1290004178.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.83740                            
REMARK 200  MONOCHROMATOR                  : GE SINGLE CRYSTAL                  
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42933                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.210                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 97.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 31.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.21                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIRECT METHODS               
REMARK 200 SOFTWARE USED: SHELXD                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: LOCALIZATION OF FE ATOM BY PATTERSON ANALYSIS OF SUPER-      
REMARK 200  SHARPENED NATIVE OR ANOMALOUS DIFFERENCE MAPS, FOLLOWED BY FE-      
REMARK 200  ANCHORED ROTATION SEARCH OF CYS-GLY-GLY-CYS-HIS+HEME FRAGMENT       
REMARK 200  AND EXPANSION OF THIS SEED FRAGMENT TO FINAL SOLUTION               
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING DROP, VAPOUR DIFFUSION, 16%      
REMARK 280  PEG 8000, O.2 M CALCIUM ACETATE, 0.1 M TRIS/HCL, PH = 8.5, PH       
REMARK 280  8.50, VAPOR DIFFUSION, SITTING DROP                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.83000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       48.83000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       17.11000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       43.43000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       17.11000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       43.43000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       48.83000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       17.11000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       43.43000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       48.83000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       17.11000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       43.43000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 313  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 354  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 479  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 481  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 523  LIES ON A SPECIAL POSITION.                          
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    GLU A   5   OE1 -  CD  -  OE2 ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ARG A   8   CD  -  NE  -  CZ  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    ARG A   8   NE  -  CZ  -  NH2 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ASP A  35   CB  -  CG  -  OD1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG A  65   NH1 -  CZ  -  NH2 ANGL. DEV. =   7.4 DEGREES          
REMARK 500    ARG A  65   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    TYR A  82   CG  -  CD2 -  CE2 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ASP A  86   C   -  N   -  CA  ANGL. DEV. =  15.7 DEGREES          
REMARK 500    TYR A  88   CB  -  CG  -  CD1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  13     -157.21   -137.02                                   
REMARK 500    ASP A  67       33.61    -93.23                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    GLU A 127         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 523        DISTANCE =  6.33 ANGSTROMS                       
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                              CA A 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  35   O                                                      
REMARK 620 2 ASP A  35   OD1  73.0                                              
REMARK 620 3 HOH A 332   O    72.8  89.4                                        
REMARK 620 4 HOH A 449   O   118.0  74.6  55.6                                  
REMARK 620 5 GLU A 127   OE1  46.3  91.4 115.2 162.6                            
REMARK 620 6 GLU A 127   OE2  49.8  94.1 117.8 166.3   3.8                      
REMARK 620 7 HOH A 371   O    82.3 155.0  87.0 122.3  68.0  66.1                
REMARK 620 8 HOH A 451   O   179.3 107.5 106.7  61.8 134.0 130.4  97.2          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  35   OD1                                                    
REMARK 620 2 ASP A  35   OD2  44.5                                              
REMARK 620 3 HOH A 308   O    51.7  59.9                                        
REMARK 620 4 HOH A 340   O    71.0  86.1 122.2                                  
REMARK 620 5 HOH A 393   O   122.8  90.2 142.1  73.5                            
REMARK 620 6 HOH A 461   O   121.1  84.6  80.7 145.3  73.2                      
REMARK 620 7 HOH A 499   O   100.0 109.7  53.4 147.5 132.2  66.5                
REMARK 620 8 HOH A 514   O   149.9 165.4 123.9 100.9  79.8  82.4  70.8          
REMARK 620 9 HOH A 449   O    72.4 116.5  77.5  79.0 140.1 134.6  68.5  77.6    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC A 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  41   NE2                                                    
REMARK 620 2 HEC A 201   NA   92.2                                              
REMARK 620 3 HEC A 201   NB   91.3  89.4                                        
REMARK 620 4 HEC A 201   NC   90.0 177.4  89.1                                  
REMARK 620 5 HEC A 201   ND   87.3  91.0 178.6  90.5                            
REMARK 620 6 HIS A  92   NE2 176.8  89.6  91.3  88.3  90.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A  49   OD1                                                    
REMARK 620 2 ASN A  50   OD1  69.2                                              
REMARK 620 3 HOH A 415   O    74.6  75.8                                        
REMARK 620 4 HOH A 442   O    83.4 132.0  58.9                                  
REMARK 620 5 HOH A 361   O   110.4  68.8 138.7 159.1                            
REMARK 620 6 HOH A 444   O   140.4  79.9  74.2 100.7  79.1                      
REMARK 620 7 HOH A 509   O   147.1 143.4 111.9  74.3  86.3  68.9                
REMARK 620 8 HOH A 374   O    74.9 122.6 134.0  84.1  84.5 144.5  78.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA Z 225                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA Z 226                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA Z 227                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 136                 
DBREF  1E29 A    1   135  UNP    Q55013   C550_SYNY3      26    160             
SEQRES   1 A  135  VAL GLU LEU THR GLU SER THR ARG THR ILE PRO LEU ASP          
SEQRES   2 A  135  GLU ALA GLY GLY THR THR THR LEU THR ALA ARG GLN PHE          
SEQRES   3 A  135  THR ASN GLY GLN LYS ILE PHE VAL ASP THR CYS THR GLN          
SEQRES   4 A  135  CYS HIS LEU GLN GLY LYS THR LYS THR ASN ASN ASN VAL          
SEQRES   5 A  135  SER LEU GLY LEU ALA ASP LEU ALA GLY ALA GLU PRO ARG          
SEQRES   6 A  135  ARG ASP ASN VAL LEU ALA LEU VAL GLU PHE LEU LYS ASN          
SEQRES   7 A  135  PRO LYS SER TYR ASP GLY GLU ASP ASP TYR SER GLU LEU          
SEQRES   8 A  135  HIS PRO ASN ILE SER ARG PRO ASP ILE TYR PRO GLU MET          
SEQRES   9 A  135  ARG ASN TYR THR GLU ASP ASP ILE PHE ASP VAL ALA GLY          
SEQRES  10 A  135  TYR THR LEU ILE ALA PRO LYS LEU ASP GLU ARG TRP GLY          
SEQRES  11 A  135  GLY THR ILE TYR PHE                                          
HET    HEC  A 201      43                                                       
HET     CA  A 202       1                                                       
HET     CA  A 203       1                                                       
HET     CA  A 204       1                                                       
HETNAM     HEC HEME C                                                           
HETNAM      CA CALCIUM ION                                                      
FORMUL   2  HEC    C34 H34 FE N4 O4                                             
FORMUL   3   CA    3(CA 2+)                                                     
FORMUL   6  HOH   *223(H2 O)                                                    
HELIX    1   1 THR A   22  CYS A   37  1                                  16    
HELIX    2   2 CYS A   37  LEU A   42  1                                   6    
HELIX    3   3 GLN A   43  LYS A   45  5                                   3    
HELIX    4   4 GLY A   55  GLY A   61  1                                   7    
HELIX    5   5 ASN A   68  ASN A   78  1                                  11    
HELIX    6   6 TYR A  101  ARG A  105  5                                   5    
HELIX    7   7 THR A  108  ASP A  126  1                                  19    
SHEET    1   A 2 THR A   9  PRO A  11  0                                        
SHEET    2   A 2 THR A  18  THR A  20 -1  N  THR A  19   O  ILE A  10           
LINK         O   ASP A  35                CA    CA A 203     1555   1555  2.35  
LINK         OD1 ASP A  35                CA    CA A 204     1555   1555  2.93  
LINK         OD1 ASP A  35                CA    CA A 203     1555   1555  2.39  
LINK         OD2 ASP A  35                CA    CA A 204     1555   1555  2.69  
LINK         SG  CYS A  37                 CAB HEC A 201     1555   1555  1.80  
LINK         SG  CYS A  40                 CAC HEC A 201     1555   1555  1.82  
LINK         NE2 HIS A  41                FE   HEC A 201     1555   1555  1.97  
LINK         OD1 ASN A  49                CA    CA A 202     1555   1555  2.47  
LINK         OD1 ASN A  50                CA    CA A 202     1555   1555  2.51  
LINK         NE2 HIS A  92                FE   HEC A 201     1555   1555  2.00  
LINK        CA    CA A 202                 O   HOH A 415     1555   1555  2.42  
LINK        CA    CA A 202                 O   HOH A 442     1555   1555  2.39  
LINK        CA    CA A 202                 O   HOH A 361     1555   1555  2.36  
LINK        CA    CA A 202                 O   HOH A 444     1555   1555  2.44  
LINK        CA    CA A 202                 O   HOH A 509     1555   1555  2.33  
LINK        CA    CA A 203                 O   HOH A 332     1555   1555  2.04  
LINK        CA    CA A 203                 O   HOH A 449     1555   1555  2.89  
LINK        CA    CA A 204                 O   HOH A 308     1555   1555  2.11  
LINK        CA    CA A 204                 O   HOH A 340     1555   1555  2.41  
LINK        CA    CA A 204                 O   HOH A 393     1555   1555  2.32  
LINK        CA    CA A 204                 O  BHOH A 461     1555   1555  2.35  
LINK        CA    CA A 204                 O   HOH A 499     1555   1555  2.80  
LINK        CA    CA A 204                 O  BHOH A 514     1555   1555  2.41  
LINK        CA    CA A 204                 O   HOH A 449     1555   1555  2.50  
LINK         OE1 GLU A 127                CA    CA A 203     1555   8456  2.48  
LINK         OE2 GLU A 127                CA    CA A 203     1555   8456  3.20  
LINK        CA    CA A 202                 O   HOH A 374     1555   4566  2.36  
LINK        CA    CA A 203                 O   HOH A 371     1555   8556  2.37  
LINK        CA    CA A 203                 O   HOH A 451     1555   8556  2.05  
CISPEP   1 GLU A   63    PRO A   64          0       -11.46                     
SITE     1 AC1  8 ASN A  49  ASN A  50  HOH A 509  HOH A 442                    
SITE     2 AC1  8 HOH A 444  HOH A 415  HOH A 361  HOH A 374                    
SITE     1 AC2  6 ASP A  35  GLU A 127  HOH A 449  HOH A 332                    
SITE     2 AC2  6 HOH A 451  HOH A 371                                          
SITE     1 AC3  8 ASP A  35  HOH A 499  HOH A 514  HOH A 449                    
SITE     2 AC3  8 HOH A 308  HOH A 461  HOH A 340  HOH A 393                    
SITE     1 AC4 21 THR A  36  CYS A  37  CYS A  40  HIS A  41                    
SITE     2 AC4 21 THR A  48  ASN A  49  VAL A  52  SER A  53                    
SITE     3 AC4 21 LEU A  54  ASP A  58  LEU A  59  ALA A  62                    
SITE     4 AC4 21 ARG A  66  LEU A  72  PHE A  75  TYR A  82                    
SITE     5 AC4 21 GLU A  90  HIS A  92  HOH A 362  HOH A 406                    
SITE     6 AC4 21 HOH A 319                                                     
CRYST1   34.220   86.860   97.660  90.00  90.00  90.00 C 2 2 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      0.029223  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011513  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010240        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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