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Database: PDB
Entry: 4LJI
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Original site: 4LJI 
HEADER    ELECTRON TRANSPORT                      04-JUL-13   4LJI              
TITLE     CRYSTAL STRUCTURE AT 1.5 ANGSTROM RESOLUTION OF THE PSBV2 CYTOCHROME  
TITLE    2 FROM THE CYANOBACTERIUM THERMOSYNECHOCOCCUS ELONGATUS                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME C-550-LIKE PROTEIN;                             
COMPND   3 CHAIN: A, B                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE   3 ORGANISM_TAXID: 197221;                                              
SOURCE   4 STRAIN: BP-1                                                         
KEYWDS    CYTOCHROME C, ELECTRON TRANSPORT                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.SUGA,T.-L.LAI,M.SUGIURA,J.-R.SHEN,A.BOUSSAC                         
REVDAT   4   02-OCT-19 4LJI    1       COMPND HET    HETNAM HETSYN              
REVDAT   4 2                   1       FORMUL LINK   ATOM                       
REVDAT   3   16-OCT-13 4LJI    1       JRNL                                     
REVDAT   2   18-SEP-13 4LJI    1       JRNL                                     
REVDAT   1   28-AUG-13 4LJI    0                                                
JRNL        AUTH   M.SUGA,T.-L.LAI,M.SUGIURA,J.-R.SHEN,A.BOUSSAC                
JRNL        TITL   CRYSTAL STRUCTURE AT 1.5 ANGSTROM RESOLUTION OF THE PSBV2    
JRNL        TITL 2 CYTOCHROME FROM THE CYANOBACTERIUM THERMOSYNECHOCOCCUS       
JRNL        TITL 3 ELONGATUS                                                    
JRNL        REF    FEBS LETT.                    V. 587  3267 2013              
JRNL        REFN                   ISSN 0014-5793                               
JRNL        PMID   23994160                                                     
JRNL        DOI    10.1016/J.FEBSLET.2013.08.023                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.51 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.51                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.39                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.970                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 72652                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.218                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3653                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 45.4059 -  4.4652    0.94     2638   157  0.1866 0.2006        
REMARK   3     2  4.4652 -  3.5446    0.93     2587   153  0.1783 0.1914        
REMARK   3     3  3.5446 -  3.0967    0.96     2700   128  0.2169 0.2364        
REMARK   3     4  3.0967 -  2.8136    0.97     2645   180  0.2166 0.2556        
REMARK   3     5  2.8136 -  2.6119    0.97     2706   148  0.2221 0.3230        
REMARK   3     6  2.6119 -  2.4580    0.96     2712   148  0.2202 0.2438        
REMARK   3     7  2.4580 -  2.3349    0.96     2670   155  0.2236 0.2860        
REMARK   3     8  2.3349 -  2.2332    0.96     2721   139  0.2204 0.2504        
REMARK   3     9  2.2332 -  2.1473    0.97     2712   129  0.2145 0.2480        
REMARK   3    10  2.1473 -  2.0732    0.97     2729   136  0.2252 0.2940        
REMARK   3    11  2.0732 -  2.0083    0.98     2714   167  0.2206 0.2698        
REMARK   3    12  2.0083 -  1.9509    0.98     2820   131  0.2298 0.2646        
REMARK   3    13  1.9509 -  1.8996    0.99     2673   132  0.2348 0.2723        
REMARK   3    14  1.8996 -  1.8532    0.99     2840   161  0.2367 0.2635        
REMARK   3    15  1.8532 -  1.8111    0.99     2743   128  0.2335 0.3242        
REMARK   3    16  1.8111 -  1.7726    0.98     2748   140  0.2370 0.3290        
REMARK   3    17  1.7726 -  1.7371    0.94     2612   161  0.2419 0.2886        
REMARK   3    18  1.7371 -  1.7043    0.94     2631   119  0.2452 0.2545        
REMARK   3    19  1.7043 -  1.6739    0.94     2654   141  0.2453 0.3115        
REMARK   3    20  1.6739 -  1.6455    0.94     2655   133  0.2547 0.2824        
REMARK   3    21  1.6455 -  1.6190    0.94     2575   149  0.2531 0.3294        
REMARK   3    22  1.6190 -  1.5940    0.93     2620   123  0.2521 0.2732        
REMARK   3    23  1.5940 -  1.5706    0.92     2663   120  0.2457 0.2741        
REMARK   3    24  1.5706 -  1.5485    0.92     2519   127  0.2579 0.2833        
REMARK   3    25  1.5485 -  1.5276    0.92     2666   143  0.2646 0.2514        
REMARK   3    26  1.5276 -  1.5077    0.74     2046   105  0.2829 0.3397        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.320           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.68                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.67                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.011           2202                                  
REMARK   3   ANGLE     :  1.415           3026                                  
REMARK   3   CHIRALITY :  0.101            338                                  
REMARK   3   PLANARITY :  0.008            384                                  
REMARK   3   DIHEDRAL  : 13.455            822                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.0045  -0.4565   0.0780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1138 T22:   0.1172                                     
REMARK   3      T33:   0.1234 T12:   0.0101                                     
REMARK   3      T13:  -0.0225 T23:   0.0301                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6825 L22:   1.1149                                     
REMARK   3      L33:   1.8456 L12:   0.1188                                     
REMARK   3      L13:  -0.4319 L23:   0.9227                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0324 S12:  -0.0286 S13:  -0.0073                       
REMARK   3      S21:  -0.0002 S22:   0.0601 S23:  -0.0275                       
REMARK   3      S31:   0.0055 S32:   0.0289 S33:  -0.0870                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE ENTRY CONTAINS FRIEDEL PAIRS IN       
REMARK   3  F_PLUS/MINUS COLUMNS                                                
REMARK   4                                                                      
REMARK   4 4LJI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JUL-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000080707.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-13                          
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               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 72721                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 3ARC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THE ENTRY CONTAINS FRIEDEL PAIRS IN F_PLUS/MINUS COLUMNS     
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.5, VAPOR DIFFUSION, SITTING DROP,   
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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     ALA A     1                                                      
REMARK 465     SER A   135                                                      
REMARK 465     PHE A   136                                                      
REMARK 465     PRO A   137                                                      
REMARK 465     ASP A   138                                                      
REMARK 465     SER A   139                                                      
REMARK 465     ALA A   140                                                      
REMARK 465     PRO A   141                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     GLU B   134                                                      
REMARK 465     SER B   135                                                      
REMARK 465     PHE B   136                                                      
REMARK 465     PRO B   137                                                      
REMARK 465     ASP B   138                                                      
REMARK 465     SER B   139                                                      
REMARK 465     ALA B   140                                                      
REMARK 465     PRO B   141                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 134    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 133    CG1  CG2                                            
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  16      -86.53   -103.79                                   
REMARK 500    ASN A  59       84.98   -150.54                                   
REMARK 500    VAL A  62       73.84   -119.18                                   
REMARK 500    ARG A  76       49.77   -107.27                                   
REMARK 500    SER A  88       86.01   -152.50                                   
REMARK 500    ASP B  16      -79.46   -110.89                                   
REMARK 500    CYS B  47      -31.81   -132.78                                   
REMARK 500    ASN B  59       80.60   -162.38                                   
REMARK 500    VAL B  62       64.95   -111.86                                   
REMARK 500    ARG B  76       53.59   -106.08                                   
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                             HEC A 301  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  51   NE2                                                    
REMARK 620 2 HEC A 301   NA   90.1                                              
REMARK 620 3 HEC A 301   NB   86.8  90.2                                        
REMARK 620 4 HEC A 301   NC   85.6 174.9  86.8                                  
REMARK 620 5 HEC A 301   ND   90.1  89.7 176.9  93.1                            
REMARK 620 6 CYS A 101   SG  174.2  88.4  87.6  95.5  95.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC B 301  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  51   NE2                                                    
REMARK 620 2 HEC B 301   NA   89.8                                              
REMARK 620 3 HEC B 301   NB   88.8  91.3                                        
REMARK 620 4 HEC B 301   NC   87.3 176.2  86.1                                  
REMARK 620 5 HEC B 301   ND   89.6  89.5 178.1  92.9                            
REMARK 620 6 CYS B 101   SG  173.7  90.4  85.0  92.2  96.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 301                 
DBREF  4LJI A    1   141  UNP    Q8DJE2   PSBV2_THEEB     35    175             
DBREF  4LJI B    1   141  UNP    Q8DJE2   PSBV2_THEEB     35    175             
SEQRES   1 A  141  ALA ALA GLY VAL ASP ASN TYR VAL ILE GLN TYR LEU LYS          
SEQRES   2 A  141  VAL THR ASP THR VAL GLU LEU PRO VAL ASN ASP ARG GLY          
SEQRES   3 A  141  GLU THR LYS THR PHE THR ALA VAL ASP LEU THR ARG GLY          
SEQRES   4 A  141  LYS ARG LEU PHE GLU GLU ASN CYS LYS ASN CYS HIS VAL          
SEQRES   5 A  141  GLY GLY SER THR LEU PRO ASN PRO LEU VAL SER LEU SER          
SEQRES   6 A  141  LEU LYS ASP LEU LYS GLY ALA THR PRO PRO ARG ASP THR          
SEQRES   7 A  141  ILE ALA SER LEU VAL ALA PHE GLN ARG SER PRO LYS SER          
SEQRES   8 A  141  TYR ASP GLY SER GLU GLU SER TYR SER CYS ARG ARG VAL          
SEQRES   9 A  141  SER GLU ASP TRP LEU THR THR GLU GLN LEU GLU THR LEU          
SEQRES  10 A  141  ALA ALA PHE ILE LEU ARG ALA ALA ALA VAL ALA PRO GLY          
SEQRES  11 A  141  TRP GLY VAL GLU SER PHE PRO ASP SER ALA PRO                  
SEQRES   1 B  141  ALA ALA GLY VAL ASP ASN TYR VAL ILE GLN TYR LEU LYS          
SEQRES   2 B  141  VAL THR ASP THR VAL GLU LEU PRO VAL ASN ASP ARG GLY          
SEQRES   3 B  141  GLU THR LYS THR PHE THR ALA VAL ASP LEU THR ARG GLY          
SEQRES   4 B  141  LYS ARG LEU PHE GLU GLU ASN CYS LYS ASN CYS HIS VAL          
SEQRES   5 B  141  GLY GLY SER THR LEU PRO ASN PRO LEU VAL SER LEU SER          
SEQRES   6 B  141  LEU LYS ASP LEU LYS GLY ALA THR PRO PRO ARG ASP THR          
SEQRES   7 B  141  ILE ALA SER LEU VAL ALA PHE GLN ARG SER PRO LYS SER          
SEQRES   8 B  141  TYR ASP GLY SER GLU GLU SER TYR SER CYS ARG ARG VAL          
SEQRES   9 B  141  SER GLU ASP TRP LEU THR THR GLU GLN LEU GLU THR LEU          
SEQRES  10 B  141  ALA ALA PHE ILE LEU ARG ALA ALA ALA VAL ALA PRO GLY          
SEQRES  11 B  141  TRP GLY VAL GLU SER PHE PRO ASP SER ALA PRO                  
HET    HEC  A 301      43                                                       
HET     CL  A 302       1                                                       
HET    HEC  B 301      43                                                       
HETNAM     HEC HEME C                                                           
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3  HEC    2(C34 H34 FE N4 O4)                                          
FORMUL   4   CL    CL 1-                                                        
FORMUL   6  HOH   *121(H2 O)                                                    
HELIX    1   1 ASP A    5  TYR A   11  1                                   7    
HELIX    2   2 ALA A   33  CYS A   47  1                                  15    
HELIX    3   3 CYS A   47  VAL A   52  1                                   6    
HELIX    4   4 GLY A   53  SER A   55  5                                   3    
HELIX    5   5 SER A   65  GLY A   71  1                                   7    
HELIX    6   6 THR A   78  SER A   88  1                                  11    
HELIX    7   7 THR A  110  ALA A  128  1                                  19    
HELIX    8   8 ASP B    5  TYR B   11  1                                   7    
HELIX    9   9 ALA B   33  CYS B   47  1                                  15    
HELIX   10  10 CYS B   47  VAL B   52  1                                   6    
HELIX   11  11 GLY B   53  SER B   55  5                                   3    
HELIX   12  12 SER B   65  LYS B   70  1                                   6    
HELIX   13  13 THR B   78  SER B   88  1                                  11    
HELIX   14  14 THR B  110  ALA B  128  1                                  19    
SHEET    1   A 2 THR A  17  PRO A  21  0                                        
SHEET    2   A 2 THR A  28  THR A  32 -1  O  PHE A  31   N  VAL A  18           
SHEET    1   B 2 THR B  17  PRO B  21  0                                        
SHEET    2   B 2 THR B  28  THR B  32 -1  O  PHE B  31   N  VAL B  18           
LINK         SG  CYS A  47                 CAB HEC A 301     1555   1555  1.67  
LINK         SG  CYS A  50                 CAC HEC A 301     1555   1555  1.86  
LINK         SG  CYS B  47                 CAB HEC B 301     1555   1555  1.66  
LINK         SG  CYS B  50                 CAC HEC B 301     1555   1555  1.85  
LINK         NE2 HIS A  51                FE   HEC A 301     1555   1555  2.11  
LINK         SG  CYS A 101                FE   HEC A 301     1555   1555  2.22  
LINK         NE2 HIS B  51                FE   HEC B 301     1555   1555  2.15  
LINK         SG  CYS B 101                FE   HEC B 301     1555   1555  2.19  
CISPEP   1 THR A   73    PRO A   74          0       -10.00                     
CISPEP   2 THR B   73    PRO B   74          0        -7.36                     
SITE     1 AC1 22 ASN A  46  CYS A  47  CYS A  50  HIS A  51                    
SITE     2 AC1 22 THR A  56  VAL A  62  SER A  63  LEU A  64                    
SITE     3 AC1 22 ASP A  68  ARG A  76  LEU A  82  PHE A  85                    
SITE     4 AC1 22 GLN A  86  TYR A  92  SER A  98  SER A 100                    
SITE     5 AC1 22 CYS A 101  ARG A 102  ILE A 121  HOH A 401                    
SITE     6 AC1 22 HOH A 404  ASN B  49                                          
SITE     1 AC2  2 ASN A  46  ARG A 102                                          
SITE     1 AC3 23 ASN B  46  CYS B  47  CYS B  50  HIS B  51                    
SITE     2 AC3 23 THR B  56  VAL B  62  SER B  63  LEU B  64                    
SITE     3 AC3 23 ASP B  68  LEU B  69  ALA B  72  ARG B  76                    
SITE     4 AC3 23 LEU B  82  PHE B  85  GLN B  86  TYR B  92                    
SITE     5 AC3 23 SER B  98  SER B 100  CYS B 101  ARG B 102                    
SITE     6 AC3 23 ILE B 121  HOH B 401  HOH B 402                               
CRYST1   38.421   38.430   47.779  71.86  82.22  69.38 P 1           2          
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      0.026027 -0.009793 -0.000805        0.00000                         
SCALE2      0.000000  0.027802 -0.008245        0.00000                         
SCALE3      0.000000  0.000000  0.022034        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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