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Database: PDB
Entry: 1MZ4
LinkDB: 1MZ4
Original site: 1MZ4 
HEADER    ELECTRON TRANSPORT                      05-OCT-02   1MZ4              
TITLE     CRYSTAL STRUCTURE OF CYTOCHROME C550 FROM THERMOSYNECHOCOCCUS         
TITLE    2 ELONGATUS                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME C550;                                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: C550, LOW POTENTIAL CYTOCHROME C                            
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE   3 ORGANISM_TAXID: 146786                                               
KEYWDS    PSII ASSOCIATED CYTOCHROME, ELECTRON TRANSPORT                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.A.KERFELD,M.R.SAWAYA,H.BOTTIN,K.T.TRAN,M.SUGIURA,D.KIRILOVSKY,      
AUTHOR   2 D.KROGMANN,T.O.YEATES,A.BOUSSAC                                      
REVDAT   3   13-JUL-11 1MZ4    1       VERSN                                    
REVDAT   2   24-FEB-09 1MZ4    1       VERSN                                    
REVDAT   1   23-SEP-03 1MZ4    0                                                
JRNL        AUTH   C.A.KERFELD,M.R.SAWAYA,H.BOTTIN,K.T.TRAN,M.SUGIURA,D.CASCIO, 
JRNL        AUTH 2 A.DESBOIS,T.O.YEATES,D.KIRILOVSKY,A.BOUSSAC                  
JRNL        TITL   STRUCTURAL AND EPR CHARACTERIZATION OF THE SOLUBLE FORM OF   
JRNL        TITL 2 CYTOCHROME C-550 AND OF THE PSBV2 GENE PRODUCT FROM THE      
JRNL        TITL 3 CYANOBACTERIUM THERMOSYNECHOCOCCUS ELONGATUS.                
JRNL        REF    PLANT CELL.PHYSIOL.           V.  44   697 2003              
JRNL        REFN                   ISSN 0032-0781                               
JRNL        PMID   12881497                                                     
JRNL        DOI    10.1093/PCP/PCG084                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.58                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 23890                          
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 SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.202                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 2419                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.91                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3368                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2010                       
REMARK   3   BIN FREE R VALUE                    : 0.2390                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.30                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 387                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.012                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1015                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 102                                     
REMARK   3   SOLVENT ATOMS            : 105                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.05000                                              
REMARK   3    B22 (A**2) : 1.05000                                              
REMARK   3    B33 (A**2) : -2.10000                                             
REMARK   3    B12 (A**2) : 1.30000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.20                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.14                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.80                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.90                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 51.22                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  3  : PARAM19X.HEME                                  
REMARK   3  PARAMETER FILE  4  : BCT.PAR                                        
REMARK   3  PARAMETER FILE  5  : GOL.PAR                                        
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : TOPH19XB.HEME                                  
REMARK   3  TOPOLOGY FILE  4   : BCT.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : GOL.TOP                                        
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1MZ4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-OCT-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB017318.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUN-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X8C                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.100                              
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : COLLIMATING MIRROR                 
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25953                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 7.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.45400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: TWO WAVELENGTH ANOMALOUS     
REMARK 200  DISPERSION                                                          
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M DIHYDROGEN PHOSPHATE, MES, PH 8.5,   
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.89933            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       30.94967            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       30.94967            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       61.89933            
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 300 REMARK: THE BIOLOGICAL UNIT IS THE MONOMER CONTAINED WITHIN THE      
REMARK 300 ASYMMETRIC UNIT.                                                     
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 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 228  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 227  LIES ON A SPECIAL POSITION.                          
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   132                                                      
REMARK 465     GLY A   133                                                      
REMARK 465     LYS A   134                                                      
REMARK 465     VAL A   135                                                      
REMARK 465     TYR A   136                                                      
REMARK 465     TYR A   137                                                      
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    THR A  48      -11.02     74.09                                   
REMARK 500    ASN A  49       67.62   -158.32                                   
REMARK 500    LEU A  52       53.04   -100.02                                   
REMARK 500    ASP A  67       34.00    -95.36                                   
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                             HEM A 151  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  41   NE2                                                    
REMARK 620 2 HEM A 151   NA   89.7                                              
REMARK 620 3 HEM A 151   NB   90.8  90.7                                        
REMARK 620 4 HEM A 151   NC   89.6 179.2  88.8                                  
REMARK 620 5 HEM A 151   ND   88.4  89.3 179.2  91.1                            
REMARK 620 6 HIS A  92   NE2 177.3  87.9  88.0  92.8  92.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 145                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 146                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 147                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 148                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 149                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT A 150                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 151                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 140                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 143                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 144                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1F1C   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CYTOCHROME C549 FROM ARTHROSPIRA MAXIMA         
REMARK 900 RELATED ID: 1E29   RELATED DB: PDB                                   
REMARK 900 PSII ASSOCIATED CYTOCHROME C549 FROM SYNECHOCYSTIS SP.               
DBREF  1MZ4 A    1   137  UNP    P0A386   CY550_SYNEL     27    163             
SEQRES   1 A  137  ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN          
SEQRES   2 A  137  SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR          
SEQRES   3 A  137  LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER          
SEQRES   4 A  137  CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU          
SEQRES   5 A  137  ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO          
SEQRES   6 A  137  ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN          
SEQRES   7 A  137  PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL          
SEQRES   8 A  137  HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET          
SEQRES   9 A  137  ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY          
SEQRES  10 A  137  HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP          
SEQRES  11 A  137  GLY GLY GLY LYS VAL TYR TYR                                  
HET    PO4  A 145       5                                                       
HET    PO4  A 146       5                                                       
HET    PO4  A 147       5                                                       
HET    PO4  A 148       5                                                       
HET    PO4  A 149       5                                                       
HET    BCT  A 150       4                                                       
HET    HEM  A 151      43                                                       
HET    GOL  A 140       6                                                       
HET    GOL  A 141       6                                                       
HET    GOL  A 142       6                                                       
HET    GOL  A 143       6                                                       
HET    GOL  A 144       6                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     BCT BICARBONATE ION                                                  
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     GOL GLYCEROL                                                         
HETSYN     HEM HEME                                                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  PO4    5(O4 P 3-)                                                   
FORMUL   7  BCT    C H O3 1-                                                    
FORMUL   8  HEM    C34 H32 FE N4 O4                                             
FORMUL   9  GOL    5(C3 H8 O3)                                                  
FORMUL  14  HOH   *105(H2 O)                                                    
HELIX    1   1 THR A    4  LEU A    8  1                                   5    
HELIX    2   2 THR A   22  CYS A   37  1                                  16    
HELIX    3   3 CYS A   37  VAL A   42  1                                   6    
HELIX    4   4 GLY A   43  ILE A   45  5                                   3    
HELIX    5   5 ASN A   49  ASP A   53  5                                   5    
HELIX    6   6 ARG A   55  LEU A   61  1                                   7    
HELIX    7   7 ASN A   68  ASN A   78  1                                  11    
HELIX    8   8 SER A   94  ALA A   98  5                                   5    
HELIX    9   9 PHE A  101  ARG A  105  5                                   5    
HELIX   10  10 THR A  108  GLY A  127  1                                  20    
HELIX   11  11 ASP A  128  TRP A  130  5                                   3    
SHEET    1   A 2 THR A   9  PRO A  11  0                                        
SHEET    2   A 2 THR A  18  THR A  20 -1  O  ILE A  19   N  VAL A  10           
LINK         NE2 HIS A  41                FE   HEM A 151     1555   1555  2.02  
LINK         NE2 HIS A  92                FE   HEM A 151     1555   1555  2.02  
LINK         SG  CYS A  37                 CAB HEM A 151     1555   1555  1.83  
LINK         SG  CYS A  40                 CAC HEM A 151     1555   1555  1.83  
CISPEP   1 THR A   63    PRO A   64          0        -0.65                     
SITE     1 AC1 10 THR A   4  PRO A   5  GLU A   6  GLU A  23                    
SITE     2 AC1 10 GLU A  87  ILE A  88  ALA A  89  GLU A  90                    
SITE     3 AC1 10 HOH A 167  HOH A 185                                          
SITE     1 AC2  7 THR A  22  GLU A  23  LYS A  24  GLU A  90                    
SITE     2 AC2  7 HOH A 169  HOH A 172  HOH A 181                               
SITE     1 AC3  9 TYR A  26  LYS A  30  ASP A  83  GLU A  85                    
SITE     2 AC3  9 GLN A  86  GLU A 122  LEU A 126  PO4 A 148                    
SITE     3 AC3  9 HOH A 245                                                     
SITE     1 AC4  6 HIS A 118  GLU A 122  LEU A 126  PO4 A 147                    
SITE     2 AC4  6 HOH A 176  HOH A 256                                          
SITE     1 AC5  4 LYS A  24  GLU A  28  HOH A 159  HOH A 181                    
SITE     1 AC6  8 LYS A  30  LEU A  52  THR A  81  TYR A  82                    
SITE     2 AC6  8 HEM A 151  HOH A 162  HOH A 208  HOH A 248                    
SITE     1 AC7 22 ALA A  36  CYS A  37  SER A  39  CYS A  40                    
SITE     2 AC7 22 HIS A  41  THR A  46  THR A  48  LEU A  52                    
SITE     3 AC7 22 ASP A  53  LEU A  54  THR A  58  LEU A  59                    
SITE     4 AC7 22 LEU A  72  TYR A  75  TYR A  82  HIS A  92                    
SITE     5 AC7 22 ILE A 115  ILE A 119  GOL A 141  BCT A 150                    
SITE     6 AC7 22 HOH A 153  HOH A 154                                          
SITE     1 AC8  6 THR A  56  ARG A 105  HOH A 220  HOH A 229                    
SITE     2 AC8  6 HOH A 236  HOH A 239                                          
SITE     1 AC9  6 LYS A  24  GLU A  28  ARG A  31  THR A  48                    
SITE     2 AC9  6 ASN A  49  HEM A 151                                          
SITE     1 BC1  7 ASN A  13  SER A  14  GLY A  16  ASP A  67                    
SITE     2 BC1  7 ASN A  68  ARG A 105  HOH A 216                               
SITE     1 BC2  2 ARG A  31  TYR A  35                                          
SITE     1 BC3  2 GLU A  87  ARG A  96                                          
CRYST1   69.641   69.641   92.849  90.00  90.00 120.00 P 32 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014359  0.008290  0.000000        0.00000                         
SCALE2      0.000000  0.016581  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010770        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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