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Database: PDB
Entry: 3KZI
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Original site: 3KZI 
HEADER    ELECTRON TRANSPORT                      08-DEC-09   3KZI              
TITLE     CRYSTAL STRUCTURE OF MONOMERIC FORM OF CYANOBACTERIAL PHOTOSYSTEM II  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOTOSYSTEM Q(B) PROTEIN 1;                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: 32 KDA THYLAKOID MEMBRANE PROTEIN 1, PHOTOSYSTEM II PROTEIN 
COMPND   5 D1 1;                                                                
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PHOTOSYSTEM II CORE LIGHT HARVESTING PROTEIN;              
COMPND   8 CHAIN: B;                                                            
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: PHOTOSYSTEM II CP43 PROTEIN;                               
COMPND  11 CHAIN: C;                                                            
COMPND  12 MOL_ID: 4;                                                           
COMPND  13 MOLECULE: PHOTOSYSTEM II D2 PROTEIN;                                 
COMPND  14 CHAIN: D;                                                            
COMPND  15 SYNONYM: PHOTOSYSTEM II REACTION CENTER D2 PROTEIN, PSII D2 PROTEIN, 
COMPND  16 PHOTOSYSTEM Q(A) PROTEIN;                                            
COMPND  17 MOL_ID: 5;                                                           
COMPND  18 MOLECULE: CYTOCHROME B559 SUBUNIT ALPHA;                             
COMPND  19 CHAIN: E;                                                            
COMPND  20 SYNONYM: PSII REACTION CENTER SUBUNIT V;                             
COMPND  21 MOL_ID: 6;                                                           
COMPND  22 MOLECULE: CYTOCHROME B559 SUBUNIT BETA;                              
COMPND  23 CHAIN: F;                                                            
COMPND  24 SYNONYM: PSII REACTION CENTER SUBUNIT VI;                            
COMPND  25 MOL_ID: 7;                                                           
COMPND  26 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN H;                  
COMPND  27 CHAIN: H;                                                            
COMPND  28 SYNONYM: PSII-H;                                                     
COMPND  29 MOL_ID: 8;                                                           
COMPND  30 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN I;                  
COMPND  31 CHAIN: I;                                                            
COMPND  32 SYNONYM: PSII-I, PSII 4.4 KDA PROTEIN;                               
COMPND  33 MOL_ID: 9;                                                           
COMPND  34 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN J;                  
COMPND  35 CHAIN: J;                                                            
COMPND  36 SYNONYM: PSII-J;                                                     
COMPND  37 MOL_ID: 10;                                                          
COMPND  38 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN K;                  
COMPND  39 CHAIN: K;                                                            
COMPND  40 SYNONYM: PSII-K;                                                     
COMPND  41 MOL_ID: 11;                                                          
COMPND  42 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN L;                  
COMPND  43 CHAIN: L;                                                            
COMPND  44 SYNONYM: PSII-L, PSII 5 KDA PROTEIN;                                 
COMPND  45 MOL_ID: 12;                                                          
COMPND  46 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN M;                  
COMPND  47 CHAIN: M;                                                            
COMPND  48 SYNONYM: PSII-M;                                                     
COMPND  49 MOL_ID: 13;                                                          
COMPND  50 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;          
COMPND  51 CHAIN: O;                                                            
COMPND  52 SYNONYM: MSP;                                                        
COMPND  53 MOL_ID: 14;                                                          
COMPND  54 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN T;                  
COMPND  55 CHAIN: T;                                                            
COMPND  56 SYNONYM: PSII-T, PSII-TC;                                            
COMPND  57 MOL_ID: 15;                                                          
COMPND  58 MOLECULE: PHOTOSYSTEM II 12 KDA EXTRINSIC PROTEIN;                   
COMPND  59 CHAIN: U;                                                            
COMPND  60 SYNONYM: PS II COMPLEX 12 KDA EXTRINSIC PROTEIN, PSII-U;             
COMPND  61 MOL_ID: 16;                                                          
COMPND  62 MOLECULE: CYTOCHROME C-550;                                          
COMPND  63 CHAIN: V;                                                            
COMPND  64 SYNONYM: CYTOCHROME C550, LOW-POTENTIAL CYTOCHROME C, CYTOCHROME C-  
COMPND  65 549;                                                                 
COMPND  66 MOL_ID: 17;                                                          
COMPND  67 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN YCF12;              
COMPND  68 CHAIN: y;                                                            
COMPND  69 SYNONYM: PROTEIN YCF12;                                              
COMPND  70 MOL_ID: 18;                                                          
COMPND  71 MOLECULE: PHOTOSYSTEM II REACTION CENTER X PROTEIN;                  
COMPND  72 CHAIN: X;                                                            
COMPND  73 SYNONYM: PHOTOSYSTEM II PSBX PROTEIN;                                
COMPND  74 MOL_ID: 19;                                                          
COMPND  75 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Z;                  
COMPND  76 CHAIN: Z;                                                            
COMPND  77 SYNONYM: PSII-Z                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE   3 ORGANISM_TAXID: 197221;                                              
SOURCE   4 STRAIN: BP-1;                                                        
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE   7 ORGANISM_TAXID: 197221;                                              
SOURCE   8 STRAIN: BP-1;                                                        
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  11 ORGANISM_TAXID: 197221;                                              
SOURCE  12 STRAIN: BP-1;                                                        
SOURCE  13 MOL_ID: 4;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  15 ORGANISM_TAXID: 197221;                                              
SOURCE  16 STRAIN: BP-1;                                                        
SOURCE  17 MOL_ID: 5;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  19 ORGANISM_TAXID: 197221;                                              
SOURCE  20 STRAIN: BP-1;                                                        
SOURCE  21 MOL_ID: 6;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  23 ORGANISM_TAXID: 197221;                                              
SOURCE  24 STRAIN: BP-1;                                                        
SOURCE  25 MOL_ID: 7;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  27 ORGANISM_TAXID: 197221;                                              
SOURCE  28 STRAIN: BP-1;                                                        
SOURCE  29 MOL_ID: 8;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  31 ORGANISM_TAXID: 197221;                                              
SOURCE  32 STRAIN: BP-1;                                                        
SOURCE  33 MOL_ID: 9;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  35 ORGANISM_TAXID: 197221;                                              
SOURCE  36 STRAIN: BP-1;                                                        
SOURCE  37 MOL_ID: 10;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  39 ORGANISM_TAXID: 197221;                                              
SOURCE  40 STRAIN: BP-1;                                                        
SOURCE  41 MOL_ID: 11;                                                          
SOURCE  42 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  43 ORGANISM_TAXID: 197221;                                              
SOURCE  44 STRAIN: BP-1;                                                        
SOURCE  45 MOL_ID: 12;                                                          
SOURCE  46 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  47 ORGANISM_TAXID: 197221;                                              
SOURCE  48 STRAIN: BP-1;                                                        
SOURCE  49 MOL_ID: 13;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  51 ORGANISM_TAXID: 197221;                                              
SOURCE  52 STRAIN: BP-1;                                                        
SOURCE  53 MOL_ID: 14;                                                          
SOURCE  54 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  55 ORGANISM_TAXID: 197221;                                              
SOURCE  56 STRAIN: BP-1;                                                        
SOURCE  57 MOL_ID: 15;                                                          
SOURCE  58 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  59 ORGANISM_TAXID: 197221;                                              
SOURCE  60 STRAIN: BP-1;                                                        
SOURCE  61 MOL_ID: 16;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  63 ORGANISM_TAXID: 197221;                                              
SOURCE  64 STRAIN: BP-1;                                                        
SOURCE  65 MOL_ID: 17;                                                          
SOURCE  66 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  67 ORGANISM_TAXID: 197221;                                              
SOURCE  68 STRAIN: BP-1;                                                        
SOURCE  69 MOL_ID: 18;                                                          
SOURCE  70 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  71 ORGANISM_TAXID: 197221;                                              
SOURCE  72 STRAIN: BP-1;                                                        
SOURCE  73 MOL_ID: 19;                                                          
SOURCE  74 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  75 ORGANISM_TAXID: 197221;                                              
SOURCE  76 STRAIN: BP-1                                                         
KEYWDS    ELECTRON TRANSPORT PHOTOSYSTEM, PS II, PS2, MEMBRANE COMPLEX,         
KEYWDS   2 TRANSMEMBRANE ALPHA-HELIX, IRON, METAL-BINDING, PHOTOSYNTHESIS,      
KEYWDS   3 PHOTOSYSTEM II, THYLAKOID, HEME, REACTION CENTER, MANGANESE,         
KEYWDS   4 ELECTRON TRANSPORT                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.GABDULKHAKOV,A.GUSKOV,M.BROSER,J.KERN,A.ZOUNI,W.SAENGER             
REVDAT   3   01-SEP-10 3KZI    1       JRNL                                     
REVDAT   2   30-JUN-10 3KZI    1       JRNL                                     
REVDAT   1   16-JUN-10 3KZI    0                                                
JRNL        AUTH   M.BROSER,A.GABDULKHAKOV,J.KERN,A.GUSKOV,F.MUH,W.SAENGER,     
JRNL        AUTH 2 A.ZOUNI                                                      
JRNL        TITL   CRYSTAL STRUCTURE OF MONOMERIC PHOTOSYSTEM II FROM           
JRNL        TITL 2 THERMOSYNECHOCOCCUS ELONGATUS AT 3.6-A RESOLUTION            
JRNL        REF    J.BIOL.CHEM.                  V. 285 26255 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20558739                                                     
JRNL        DOI    10.1074/JBC.M110.127589                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
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) : 3.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.87                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.500                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 11330360.960                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 47332                          
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) : 0.297                           
REMARK   3   FREE R VALUE                     : 0.308                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 946                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
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) : 3.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.83                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 71.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6144                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4540                       
REMARK   3   BIN FREE R VALUE                    : 0.4570                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 2.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 123                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.041                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 20318                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4360                                    
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 162.60                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -16.38000                                            
REMARK   3    B22 (A**2) : -5.03000                                             
REMARK   3    B33 (A**2) : 21.41000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.67                            
REMARK   3   ESD FROM SIGMAA              (A) : 1.25                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.68                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 1.07                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.013                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.10                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 18.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.22                            
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) : 1.140 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.010 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 6.700 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 7.620 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.30                                                 
REMARK   3   BSOL        : 102.89                                               
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  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : COF-NEW6.PARAM                                 
REMARK   3  PARAMETER FILE  4  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  5  : MES.PARAM                                      
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   : COF-NEW6.TOP                                   
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : MES.TOP                                        
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3KZI COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-DEC-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB056642.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-FEB-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97915                            
REMARK 200  MONOCHROMATOR                  : SI(311)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47417                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.2                               
REMARK 200  DATA REDUNDANCY                : 4.110                              
REMARK 200  R MERGE                    (I) : 0.11200                            
REMARK 200  R SYM                      (I) : 0.07500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.3500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 68.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.24                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.63800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.340                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3BZ1                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, PIPES, MES, CACL2, PH 7,        
REMARK 280  BATCH, TEMPERATURE 291.0K                                           
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      168.64000            
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      168.64000            
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       59.94500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      112.34500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       59.94500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      112.34500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      168.64000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       59.94500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      112.34500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      168.64000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       59.94500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      112.34500            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: NONADECAMERIC                     
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONADECAMERIC              
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 68770 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 104350 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -457.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, I, J,            
REMARK 350                    AND CHAINS: K, L, M, O, T, U, V, y, X, Z          
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     ARG A     7                                                      
REMARK 465     ARG A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B   487                                                      
REMARK 465     PRO B   488                                                      
REMARK 465     GLU B   489                                                      
REMARK 465     GLN B   490                                                      
REMARK 465     VAL B   491                                                      
REMARK 465     GLU B   492                                                      
REMARK 465     TRP B   493                                                      
REMARK 465     GLY B   494                                                      
REMARK 465     PHE B   495                                                      
REMARK 465     TYR B   496                                                      
REMARK 465     GLN B   497                                                      
REMARK 465     LYS B   498                                                      
REMARK 465     VAL B   499                                                      
REMARK 465     GLY B   500                                                      
REMARK 465     ASP B   501                                                      
REMARK 465     VAL B   502                                                      
REMARK 465     THR B   503                                                      
REMARK 465     THR B   504                                                      
REMARK 465     ARG B   505                                                      
REMARK 465     ARG B   506                                                      
REMARK 465     LYS B   507                                                      
REMARK 465     GLU B   508                                                      
REMARK 465     ALA B   509                                                      
REMARK 465     VAL B   510                                                      
REMARK 465     MET C    13                                                      
REMARK 465     VAL C    14                                                      
REMARK 465     THR C    15                                                      
REMARK 465     LEU C    16                                                      
REMARK 465     SER C    17                                                      
REMARK 465     SER C    18                                                      
REMARK 465     ASN C    19                                                      
REMARK 465     SER C    20                                                      
REMARK 465     ILE C    21                                                      
REMARK 465     PHE C    22                                                      
REMARK 465     ALA C    23                                                      
REMARK 465     THR C    24                                                      
REMARK 465     ASN C    25                                                      
REMARK 465     MET D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     ILE D     3                                                      
REMARK 465     ALA D     4                                                      
REMARK 465     ILE D     5                                                      
REMARK 465     GLY D     6                                                      
REMARK 465     ARG D     7                                                      
REMARK 465     ALA D     8                                                      
REMARK 465     PRO D     9                                                      
REMARK 465     ALA D    10                                                      
REMARK 465     GLU D    11                                                      
REMARK 465     ARG D    12                                                      
REMARK 465     ALA E     2                                                      
REMARK 465     GLY E     3                                                      
REMARK 465     THR E     4                                                      
REMARK 465     THR E     5                                                      
REMARK 465     GLY E     6                                                      
REMARK 465     GLU E     7                                                      
REMARK 465     THR F     2                                                      
REMARK 465     SER F     3                                                      
REMARK 465     ASN F     4                                                      
REMARK 465     THR F     5                                                      
REMARK 465     PRO F     6                                                      
REMARK 465     ASN F     7                                                      
REMARK 465     ASP I    36                                                      
REMARK 465     LEU I    37                                                      
REMARK 465     GLU I    38                                                      
REMARK 465     MET J     1                                                      
REMARK 465     MET J     2                                                      
REMARK 465     SER J     3                                                      
REMARK 465     GLU J     4                                                      
REMARK 465     GLY J     5                                                      
REMARK 465     GLY J     6                                                      
REMARK 465     SER M    35                                                      
REMARK 465     SER M    36                                                      
REMARK 465     ALA O    27                                                      
REMARK 465     LYS O    28                                                      
REMARK 465     GLN O    29                                                      
REMARK 465     LYS T    31                                                      
REMARK 465     LYS T    32                                                      
REMARK 465     ALA U    31                                                      
REMARK 465     THR U    32                                                      
REMARK 465     ALA U    33                                                      
REMARK 465     SER U    34                                                      
REMARK 465     THR U    35                                                      
REMARK 465     GLU U    36                                                      
REMARK 465     GLU U    37                                                      
REMARK 465     MET y     1                                                      
REMARK 465     GLY y     2                                                      
REMARK 465     ILE y     3                                                      
REMARK 465     PHE y     4                                                      
REMARK 465     ASN y     5                                                      
REMARK 465     GLY y     6                                                      
REMARK 465     ILE y     7                                                      
REMARK 465     ILE y     8                                                      
REMARK 465     GLU y     9                                                      
REMARK 465     PHE y    10                                                      
REMARK 465     LEU y    11                                                      
REMARK 465     SER y    12                                                      
REMARK 465     ASN y    13                                                      
REMARK 465     ILE y    14                                                      
REMARK 465     ASN y    15                                                      
REMARK 465     PHE y    16                                                      
REMARK 465     GLU y    17                                                      
REMARK 465     VAL y    18                                                      
REMARK 465     VAL X    46                                                      
REMARK 465     GLN X    47                                                      
REMARK 465     ARG X    48                                                      
REMARK 465     SER X    49                                                      
REMARK 465     LEU X    50                                                      
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     TYR C 143    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU C 462    CG   CD   OE1  OE2                                  
REMARK 470     LYS H  20    CG   CD   CE   NZ                                   
REMARK 470     ARG O  53    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU O  80    CG   CD   OE1  OE2                                  
REMARK 470     LYS O  85    CG   CD   CE   NZ                                   
REMARK 470     ARG O 233    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU V  41    CG   CD   OE1  OE2                                  
REMARK 470     ARG y  43    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OXT  ALA A   344    MN2   OEC A   368              1.58            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B 484   C   -  N   -  CA  ANGL. DEV. =  11.0 DEGREES          
REMARK 500    LEU B 486   CA  -  CB  -  CG  ANGL. DEV. =  16.1 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    ASN A  12      105.64    128.38                                   
REMARK 500    LEU A  13      -70.93    -32.43                                   
REMARK 500    TRP A  97       19.72    -69.95                                   
REMARK 500    GLN A 130       -6.12    -55.13                                   
REMARK 500    TRP A 131      -60.41    -99.77                                   
REMARK 500    PRO A 141     -119.35    -70.23                                   
REMARK 500    TRP A 142      -18.05     45.73                                   
REMARK 500    LEU A 159      -46.38   -138.50                                   
REMARK 500    ILE A 176      -71.38    -56.08                                   
REMARK 500    HIS A 215      -71.24    -45.09                                   
REMARK 500    GLU A 226        8.50   -152.08                                   
REMARK 500    GLU A 242      -60.41    -90.96                                   
REMARK 500    ILE A 259      -80.43   -101.46                                   
REMARK 500    PHE A 260      137.24    179.94                                   
REMARK 500    GLN A 261      -64.01    -27.28                                   
REMARK 500    TRP A 278      -71.10    -50.18                                   
REMARK 500    PHE A 302       34.03    -96.42                                   
REMARK 500    ARG A 334      -68.85    -27.10                                   
REMARK 500    LEU A 343       58.99   -107.31                                   
REMARK 500    VAL B  11        2.97    -60.93                                   
REMARK 500    ILE B  13      -26.17    -37.96                                   
REMARK 500    ASN B  14       64.74   -153.12                                   
REMARK 500    ASP B  15       59.59   -147.11                                   
REMARK 500    PRO B  16      -34.48    -33.38                                   
REMARK 500    SER B  48      -19.19    -49.96                                   
REMARK 500    ASP B  49      103.38   -160.55                                   
REMARK 500    ASP B 119       52.22    -94.11                                   
REMARK 500    ARG B 127      -78.81    -56.43                                   
REMARK 500    SER B 177      179.05    178.01                                   
REMARK 500    PRO B 183     -179.06    -50.17                                   
REMARK 500    GLU B 184      101.47   -167.25                                   
REMARK 500    ASP B 188       -0.45    -58.26                                   
REMARK 500    LEU B 218      -68.55   -103.80                                   
REMARK 500    LEU B 229       39.45    -80.21                                   
REMARK 500    ARG B 230       47.31     16.58                                   
REMARK 500    MET B 231     -179.20    -56.11                                   
REMARK 500    GLU B 235       16.18    -67.21                                   
REMARK 500    ALA B 261       -9.69    -59.24                                   
REMARK 500    SER B 294       28.71    -75.28                                   
REMARK 500    ASP B 313       41.15    -92.96                                   
REMARK 500    LYS B 349      -48.32    -21.92                                   
REMARK 500    PHE B 383      -69.44    -90.45                                   
REMARK 500    PRO B 414      -65.28    -15.92                                   
REMARK 500    GLU B 435      -76.00    -59.78                                   
REMARK 500    THR B 436      -73.65    -21.43                                   
REMARK 500    SER B 480      -19.63     75.80                                   
REMARK 500    ILE B 482     -161.16   -119.43                                   
REMARK 500    PRO B 484     -179.09     18.64                                   
REMARK 500    GLU B 485      173.03     67.70                                   
REMARK 500    GLN C  28      114.43   -163.92                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     213 RAMACHANDRAN OUTLIERS.                        
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    TYR A 161         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    TYR U  72        22.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OEC A  368                                                       
REMARK 610     DGD C  474                                                       
REMARK 610     LHG A  371                                                       
REMARK 610     SQD C  475                                                       
REMARK 610     LMG A  373                                                       
REMARK 610     LHG C  476                                                       
REMARK 610     DGD A  375                                                       
REMARK 610     LMG B  531                                                       
REMARK 610     DGD C  491                                                       
REMARK 610     DGD C  492                                                       
REMARK 610     LMG J  492                                                       
REMARK 610     LMG C  494                                                       
REMARK 610     LMG D  359                                                       
REMARK 610     LMG D  360                                                       
REMARK 610     SQD D  361                                                       
REMARK 610     DGD D  362                                                       
REMARK 610     LMT D  363                                                       
REMARK 610     SQD F  224                                                       
REMARK 610     DGD B  528                                                       
REMARK 610     LMG I  220                                                       
REMARK 610     LMG M  217                                                       
REMARK 610     SQD L  213                                                       
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                             OEC A 368  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 189   OE2                                                    
REMARK 620 2 HIS A 332   NE2 101.1                                              
REMARK 620 3 ASP A 342   OD2  76.7  92.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM V 164  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS V  67   NE2                                                    
REMARK 620 2 HEM V 164   NA   84.1                                              
REMARK 620 3 HEM V 164   NB   94.2  90.0                                        
REMARK 620 4 HEM V 164   NC   94.9 178.0  91.7                                  
REMARK 620 5 HEM V 164   ND   88.1  88.9 177.4  89.4                            
REMARK 620 6 HIS V 118   NE2 163.1  80.7  93.4 100.0  84.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 A 361  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 BCT D 353   O3                                                     
REMARK 620 2 HIS D 214   NE2  90.0                                              
REMARK 620 3 HIS A 215   NE2 125.8 132.1                                        
REMARK 620 4 HIS A 272   NE2  92.9  99.9 107.6                                  
REMARK 620 5 HIS D 268   NE2  68.8  91.7  76.5 158.4                            
REMARK 620 6 BCT D 353   O2   53.9 143.9  78.7  83.6  76.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC A 368  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 354   OE2                                                    
REMARK 620 2 GLU A 333   OE1  78.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC A 368  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 342   OD1                                                    
REMARK 620 2 GLU C 354   OE1  75.2                                              
REMARK 620 3 ALA A 344   O   116.0 124.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM F  85  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  23   NE2                                                    
REMARK 620 2 HEM F  85   NA   93.9                                              
REMARK 620 3 HEM F  85   NB  104.4  88.7                                        
REMARK 620 4 HEM F  85   NC   86.2 178.6  89.9                                  
REMARK 620 5 HEM F  85   ND   78.0  92.5 177.2  88.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC A 368  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 189   OE1                                                    
REMARK 620 2 ALA A 344   O   133.0                                              
REMARK 620 3 ASP A 170   OD1 140.6  78.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 486  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C  39   OD1                                                    
REMARK 620 2 CLA C 486   NA   99.4                                              
REMARK 620 3 CLA C 486   NB   76.2  88.7                                        
REMARK 620 4 CLA C 486   NC   86.4 174.3  92.9                                  
REMARK 620 5 CLA C 486   ND  108.8  87.0 173.8  91.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA K  56  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP K  19   OD2                                                    
REMARK 620 2 ASP K  23   OD1 151.7                                              
REMARK 620 3 ASP K  23   OD2 132.7  43.5                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 361                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 362                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 363                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO A 365                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 366                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 367                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OEC A 368                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR A 369                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 474                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG A 371                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD C 475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG A 373                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG C 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD A 375                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT A 376                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 522                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 523                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 524                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 525                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 526                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 527                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 529                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 530                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG B 531                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD B 533                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 535                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT D 536                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 484                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 485                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA K 483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 486                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 487                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 488                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR C 489                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR C 490                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 491                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 492                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 493                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG J 492                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG C 494                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT D 353                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA D 354                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 364                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO D 355                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA D 356                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 D 357                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR D 358                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG D 359                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG D 360                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD D 361                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD D 362                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT D 363                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM F 85                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD F 224                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 225                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR X 107                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD B 528                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG I 220                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR J 115                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA K 56                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR J 112                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG M 217                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT T 226                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA O 273                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT I 274                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD L 213                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT O 274                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM V 164                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR Z 116                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3BZ1   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CYANOBACTERIAL PHOTOSYSTEM II (PART 1           
REMARK 900 OF 2). THIS FILE CONTAINS FIRST MONOMER OF PSII DIMER                
REMARK 900 RELATED ID: 3BZ2   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CYANOBACTERIAL PHOTOSYSTEM II (PART 2           
REMARK 900 OF 2). THIS FILE CONTAINS SECOND MONOMER OF PSII DIMER               
DBREF  3KZI A    1   344  UNP    P0A444   PSBA1_THEEB      1    344             
DBREF  3KZI B    1   510  UNP    Q8DIQ1   Q8DIQ1_THEEB     1    510             
DBREF  3KZI C   13   473  UNP    Q8DIF8   Q8DIF8_THEEB     1    461             
DBREF  3KZI D    1   352  UNP    Q8CM25   PSBD_THEEB       1    352             
DBREF  3KZI E    2    84  UNP    Q8DIP0   PSBE_THEEB       2     84             
DBREF  3KZI F    2    45  UNP    Q8DIN9   PSBF_THEEB       2     45             
DBREF  3KZI H    2    66  UNP    Q8DJ43   PSBH_THEEB       2     66             
DBREF  3KZI I    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  3KZI J    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  3KZI K   10    46  UNP    Q9F1K9   PSBK_THEEB      10     46             
DBREF  3KZI L    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  3KZI M    1    36  UNP    Q8DHA7   PSBM_THEEB       1     36             
DBREF  3KZI O   27   272  UNP    P0A431   PSBO_THEEB      27    272             
DBREF  3KZI T    1    32  UNP    Q8DIQ0   PSBT_THEEB       1     32             
DBREF  3KZI U   31   134  UNP    Q9F1L5   PSBU_THEEB      31    134             
DBREF  3KZI V   27   163  UNP    P0A386   CY550_THEEB     27    163             
DBREF  3KZI y    1    46  UNP    Q8DJI1   YCF12_THEEB      1     46             
DBREF  3KZI X   11    50  UNP    Q9F1R6   PSBX_THEEB       2     41             
DBREF  3KZI Z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
SEQRES   1 A  344  MET THR THR THR LEU GLN ARG ARG GLU SER ALA ASN LEU          
SEQRES   2 A  344  TRP GLU ARG PHE CYS ASN TRP VAL THR SER THR ASP ASN          
SEQRES   3 A  344  ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE MET ILE PRO          
SEQRES   4 A  344  THR LEU LEU ALA ALA THR ILE CYS PHE VAL ILE ALA PHE          
SEQRES   5 A  344  ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY ILE ARG GLU          
SEQRES   6 A  344  PRO VAL SER GLY SER LEU LEU TYR GLY ASN ASN ILE ILE          
SEQRES   7 A  344  THR GLY ALA VAL VAL PRO SER SER ASN ALA ILE GLY LEU          
SEQRES   8 A  344  HIS PHE TYR PRO ILE TRP GLU ALA ALA SER LEU ASP GLU          
SEQRES   9 A  344  TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU ILE ILE PHE          
SEQRES  10 A  344  HIS PHE LEU LEU GLY ALA SER CYS TYR MET GLY ARG GLN          
SEQRES  11 A  344  TRP GLU LEU SER TYR ARG LEU GLY MET ARG PRO TRP ILE          
SEQRES  12 A  344  CYS VAL ALA TYR SER ALA PRO LEU ALA SER ALA PHE ALA          
SEQRES  13 A  344  VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY SER PHE SER          
SEQRES  14 A  344  ASP GLY MET PRO LEU GLY ILE SER GLY THR PHE ASN PHE          
SEQRES  15 A  344  MET ILE VAL PHE GLN ALA GLU HIS ASN ILE LEU MET HIS          
SEQRES  16 A  344  PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL PHE GLY GLY          
SEQRES  17 A  344  ALA LEU PHE CYS ALA MET HIS GLY SER LEU VAL THR SER          
SEQRES  18 A  344  SER LEU ILE ARG GLU THR THR GLU THR GLU SER ALA ASN          
SEQRES  19 A  344  TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU THR TYR ASN          
SEQRES  20 A  344  ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG LEU ILE PHE          
SEQRES  21 A  344  GLN TYR ALA SER PHE ASN ASN SER ARG SER LEU HIS PHE          
SEQRES  22 A  344  PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL TRP PHE THR          
SEQRES  23 A  344  ALA LEU GLY ILE SER THR MET ALA PHE ASN LEU ASN GLY          
SEQRES  24 A  344  PHE ASN PHE ASN HIS SER VAL ILE ASP ALA LYS GLY ASN          
SEQRES  25 A  344  VAL ILE ASN THR TRP ALA ASP ILE ILE ASN ARG ALA ASN          
SEQRES  26 A  344  LEU GLY MET GLU VAL MET HIS GLU ARG ASN ALA HIS ASN          
SEQRES  27 A  344  PHE PRO LEU ASP LEU ALA                                      
SEQRES   1 B  510  MET GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE          
SEQRES   2 B  510  ASN ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS          
SEQRES   3 B  510  THR ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU          
SEQRES   4 B  510  TYR GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU          
SEQRES   5 B  510  ASN PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE          
SEQRES   6 B  510  MET ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP          
SEQRES   7 B  510  SER ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP          
SEQRES   8 B  510  SER PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER          
SEQRES   9 B  510  GLY LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR          
SEQRES  10 B  510  TRP ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU          
SEQRES  11 B  510  PRO ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU          
SEQRES  12 B  510  PHE LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE          
SEQRES  13 B  510  HIS LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER          
SEQRES  14 B  510  ASP PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA          
SEQRES  15 B  510  PRO GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO          
SEQRES  16 B  510  GLY GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL          
SEQRES  17 B  510  GLY ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO          
SEQRES  18 B  510  PRO GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE          
SEQRES  19 B  510  GLU THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE          
SEQRES  20 B  510  ALA ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER          
SEQRES  21 B  510  ALA THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR          
SEQRES  22 B  510  GLN TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG          
SEQRES  23 B  510  ARG VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU          
SEQRES  24 B  510  GLU ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR          
SEQRES  25 B  510  ASP TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE          
SEQRES  26 B  510  ARG THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN          
SEQRES  27 B  510  ALA TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY          
SEQRES  28 B  510  GLU GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU          
SEQRES  29 B  510  SER PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL          
SEQRES  30 B  510  LYS ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR          
SEQRES  31 B  510  SER PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY          
SEQRES  32 B  510  GLY GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR          
SEQRES  33 B  510  VAL LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE          
SEQRES  34 B  510  PHE GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE          
SEQRES  35 B  510  PHE ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS          
SEQRES  36 B  510  ALA VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP          
SEQRES  37 B  510  HIS GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY          
SEQRES  38 B  510  ILE ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY          
SEQRES  39 B  510  PHE TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG LYS          
SEQRES  40 B  510  GLU ALA VAL                                                  
SEQRES   1 C  461  MET VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN          
SEQRES   2 C  461  ARG ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY          
SEQRES   3 C  461  ASN ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY          
SEQRES   4 C  461  ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA          
SEQRES   5 C  461  GLY ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO          
SEQRES   6 C  461  GLU LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO          
SEQRES   7 C  461  HIS ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY          
SEQRES   8 C  461  GLU VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL          
SEQRES   9 C  461  VAL HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY          
SEQRES  10 C  461  VAL TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU          
SEQRES  11 C  461  TYR SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN          
SEQRES  12 C  461  LYS MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU          
SEQRES  13 C  461  GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE          
SEQRES  14 C  461  PHE GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY          
SEQRES  15 C  461  ASP VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG          
SEQRES  16 C  461  VAL ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY          
SEQRES  17 C  461  GLU GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL          
SEQRES  18 C  461  VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA          
SEQRES  19 C  461  GLY GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP          
SEQRES  20 C  461  ALA ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU          
SEQRES  21 C  461  SER TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE          
SEQRES  22 C  461  ALA THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO          
SEQRES  23 C  461  SER GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN          
SEQRES  24 C  461  ALA GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU          
SEQRES  25 C  461  GLY ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU          
SEQRES  26 C  461  GLY LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE          
SEQRES  27 C  461  PHE GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY          
SEQRES  28 C  461  PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP          
SEQRES  29 C  461  LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU          
SEQRES  30 C  461  ARG ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY          
SEQRES  31 C  461  SER LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN          
SEQRES  32 C  461  SER VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR          
SEQRES  33 C  461  SER HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS          
SEQRES  34 C  461  LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY          
SEQRES  35 C  461  PHE GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU          
SEQRES  36 C  461  SER MET PRO SER LEU ASP                                      
SEQRES   1 D  352  MET THR ILE ALA ILE GLY ARG ALA PRO ALA GLU ARG GLY          
SEQRES   2 D  352  TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS ARG ASP ARG          
SEQRES   3 D  352  PHE VAL PHE VAL GLY TRP SER GLY ILE LEU LEU PHE PRO          
SEQRES   4 D  352  CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU THR GLY THR          
SEQRES   5 D  352  THR PHE VAL THR SER TRP TYR THR HIS GLY LEU ALA SER          
SEQRES   6 D  352  SER TYR LEU GLU GLY CYS ASN PHE LEU THR VAL ALA VAL          
SEQRES   7 D  352  SER THR PRO ALA ASN SER MET GLY HIS SER LEU LEU LEU          
SEQRES   8 D  352  LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE THR ARG TRP          
SEQRES   9 D  352  CYS GLN LEU GLY GLY LEU TRP THR PHE ILE ALA LEU HIS          
SEQRES  10 D  352  GLY ALA PHE GLY LEU ILE GLY PHE MET LEU ARG GLN PHE          
SEQRES  11 D  352  GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO TYR ASN ALA          
SEQRES  12 D  352  ILE ALA PHE SER ALA PRO ILE ALA VAL PHE VAL SER VAL          
SEQRES  13 D  352  PHE LEU ILE TYR PRO LEU GLY GLN SER SER TRP PHE PHE          
SEQRES  14 D  352  ALA PRO SER PHE GLY VAL ALA ALA ILE PHE ARG PHE LEU          
SEQRES  15 D  352  LEU PHE PHE GLN GLY PHE HIS ASN TRP THR LEU ASN PRO          
SEQRES  16 D  352  PHE HIS MET MET GLY VAL ALA GLY VAL LEU GLY GLY ALA          
SEQRES  17 D  352  LEU LEU CYS ALA ILE HIS GLY ALA THR VAL GLU ASN THR          
SEQRES  18 D  352  LEU PHE GLN ASP GLY GLU GLY ALA SER THR PHE ARG ALA          
SEQRES  19 D  352  PHE ASN PRO THR GLN ALA GLU GLU THR TYR SER MET VAL          
SEQRES  20 D  352  THR ALA ASN ARG PHE TRP SER GLN ILE PHE GLY ILE ALA          
SEQRES  21 D  352  PHE SER ASN LYS ARG TRP LEU HIS PHE PHE MET LEU PHE          
SEQRES  22 D  352  VAL PRO VAL THR GLY LEU TRP MET SER ALA ILE GLY VAL          
SEQRES  23 D  352  VAL GLY LEU ALA LEU ASN LEU ARG SER TYR ASP PHE ILE          
SEQRES  24 D  352  SER GLN GLU ILE ARG ALA ALA GLU ASP PRO GLU PHE GLU          
SEQRES  25 D  352  THR PHE TYR THR LYS ASN LEU LEU LEU ASN GLU GLY ILE          
SEQRES  26 D  352  ARG ALA TRP MET ALA PRO GLN ASP GLN PRO HIS GLU ASN          
SEQRES  27 D  352  PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG GLY ASN ALA          
SEQRES  28 D  352  LEU                                                          
SEQRES   1 E   83  ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE ILE          
SEQRES   2 E   83  THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR ILE          
SEQRES   3 E   83  PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER THR          
SEQRES   4 E   83  GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO ASP          
SEQRES   5 E   83  SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU VAL          
SEQRES   6 E   83  THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR PHE          
SEQRES   7 E   83  LEU GLU GLN LEU LYS                                          
SEQRES   1 F   44  THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR PRO          
SEQRES   2 F   44  ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU ALA          
SEQRES   3 F   44  VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA MET          
SEQRES   4 F   44  GLN PHE ILE GLN ARG                                          
SEQRES   1 H   65  ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO LEU          
SEQRES   2 H   65  ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY THR          
SEQRES   3 H   65  THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU VAL          
SEQRES   4 H   65  PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR LEU          
SEQRES   5 H   65  ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU GLY          
SEQRES   1 I   38  MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR          
SEQRES   2 I   38  PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY          
SEQRES   3 I   38  ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU              
SEQRES   1 J   40  MET MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL          
SEQRES   2 J   40  ALA THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY          
SEQRES   3 J   40  LEU PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER          
SEQRES   4 J   40  LEU                                                          
SEQRES   1 K   37  LYS LEU PRO GLU ALA TYR ALA ILE PHE ASP PRO LEU VAL          
SEQRES   2 K   37  ASP VAL LEU PRO VAL ILE PRO VAL LEU PHE LEU ALA LEU          
SEQRES   3 K   37  ALA PHE VAL TRP GLN ALA ALA VAL GLY PHE ARG                  
SEQRES   1 L   37  MET GLU PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN          
SEQRES   2 L   37  ARG THR SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL          
SEQRES   3 L   37  LEU ALA LEU LEU PHE SER SER TYR PHE PHE ASN                  
SEQRES   1 M   36  MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU          
SEQRES   2 M   36  PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR          
SEQRES   3 M   36  VAL GLN THR GLU SER GLN GLN LYS SER SER                      
SEQRES   1 O  246  ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY THR          
SEQRES   2 O  246  GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR ALA          
SEQRES   3 O  246  ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR ARG          
SEQRES   4 O  246  ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU VAL          
SEQRES   5 O  246  LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE          
SEQRES   6 O  246  VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER LEU          
SEQRES   7 O  246  ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP GLY          
SEQRES   8 O  246  SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN          
SEQRES   9 O  246  PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE PRO          
SEQRES  10 O  246  LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR GLN          
SEQRES  11 O  246  PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE LYS          
SEQRES  12 O  246  GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN PHE          
SEQRES  13 O  246  LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR ASP          
SEQRES  14 O  246  SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU          
SEQRES  15 O  246  ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS GLY          
SEQRES  16 O  246  GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG THR          
SEQRES  17 O  246  GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU SER          
SEQRES  18 O  246  ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL LYS          
SEQRES  19 O  246  ILE GLN GLY VAL PHE TYR ALA SER ILE GLU PRO ALA              
SEQRES   1 T   32  MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE          
SEQRES   2 T   32  ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO          
SEQRES   3 T   32  PRO ARG ILE THR LYS LYS                                      
SEQRES   1 U  104  ALA THR ALA SER THR GLU GLU GLU LEU VAL ASN VAL VAL          
SEQRES   2 U  104  ASP GLU LYS LEU GLY THR ALA TYR GLY GLU LYS ILE ASP          
SEQRES   3 U  104  LEU ASN ASN THR ASN ILE ALA ALA PHE ILE GLN TYR ARG          
SEQRES   4 U  104  GLY LEU TYR PRO THR LEU ALA LYS LEU ILE VAL LYS ASN          
SEQRES   5 U  104  ALA PRO TYR GLU SER VAL GLU ASP VAL LEU ASN ILE PRO          
SEQRES   6 U  104  GLY LEU THR GLU ARG GLN LYS GLN ILE LEU ARG GLU ASN          
SEQRES   7 U  104  LEU GLU HIS PHE THR VAL THR GLU VAL GLU THR ALA LEU          
SEQRES   8 U  104  VAL GLU GLY GLY ASP ARG TYR ASN ASN GLY LEU TYR LYS          
SEQRES   1 V  137  ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN          
SEQRES   2 V  137  SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR          
SEQRES   3 V  137  LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER          
SEQRES   4 V  137  CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU          
SEQRES   5 V  137  ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO          
SEQRES   6 V  137  ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN          
SEQRES   7 V  137  PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL          
SEQRES   8 V  137  HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET          
SEQRES   9 V  137  ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY          
SEQRES  10 V  137  HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP          
SEQRES  11 V  137  GLY GLY GLY LYS VAL TYR TYR                                  
SEQRES   1 y   46  MET GLY ILE PHE ASN GLY ILE ILE GLU PHE LEU SER ASN          
SEQRES   2 y   46  ILE ASN PHE GLU VAL ILE ALA GLN LEU THR MET ILE ALA          
SEQRES   3 y   46  MET ILE GLY ILE ALA GLY PRO MET ILE ILE PHE LEU LEU          
SEQRES   4 y   46  ALA VAL ARG ARG GLY ASN LEU                                  
SEQRES   1 X   40  THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY LEU          
SEQRES   2 X   40  LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA VAL          
SEQRES   3 X   40  LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG SER          
SEQRES   4 X   40  LEU                                                          
SEQRES   1 Z   62  MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL          
SEQRES   2 Z   62  ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA          
SEQRES   3 Z   62  TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU          
SEQRES   4 Z   62  ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU          
SEQRES   5 Z   62  VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL                      
HET    FE2  A 361       1                                                       
HET    CLA  A 362      65                                                       
HET    CLA  A 363      65                                                       
HET    PHO  A 365      64                                                       
HET    CLA  A 366      65                                                       
HET    MES  A 367      12                                                       
HET    OEC  A 368       5                                                       
HET    BCR  A 369      40                                                       
HET    DGD  C 474      56                                                       
HET    LHG  A 371      39                                                       
HET    SQD  C 475      51                                                       
HET    LMG  A 373      51                                                       
HET    LHG  C 476      37                                                       
HET    DGD  A 375      52                                                       
HET    LMT  A 376      35                                                       
HET    CLA  B 511      65                                                       
HET    CLA  B 512      65                                                       
HET    CLA  B 513      65                                                       
HET    CLA  B 514      65                                                       
HET    CLA  B 515      65                                                       
HET    CLA  B 516      65                                                       
HET    CLA  B 517      65                                                       
HET    CLA  B 518      65                                                       
HET    CLA  B 519      65                                                       
HET    CLA  B 520      65                                                       
HET    CLA  B 521      65                                                       
HET    CLA  B 522      65                                                       
HET    CLA  B 523      65                                                       
HET    CLA  B 524      65                                                       
HET    CLA  B 525      65                                                       
HET    CLA  B 526      65                                                       
HET    BCR  B 527      40                                                       
HET    BCR  B 529      40                                                       
HET    BCR  B 530      40                                                       
HET    LMG  B 531      49                                                       
HET    DGD  B 533      66                                                       
HET    LMT  B 535      35                                                       
HET    LMT  D 536      35                                                       
HET    CLA  C 477      65                                                       
HET    CLA  C 478      65                                                       
HET    CLA  C 479      65                                                       
HET    CLA  C 480      65                                                       
HET    CLA  C 481      65                                                       
HET    CLA  C 482      65                                                       
HET    CLA  C 483      65                                                       
HET    CLA  C 484      65                                                       
HET    CLA  C 485      65                                                       
HET    CLA  K 483      65                                                       
HET    CLA  C 486      65                                                       
HET    CLA  C 487      65                                                       
HET    CLA  C 488      65                                                       
HET    BCR  C 489      40                                                       
HET    BCR  C 490      40                                                       
HET    DGD  C 491      53                                                       
HET    DGD  C 492      62                                                       
HET    DGD  C 493      66                                                       
HET    LMG  J 492      48                                                       
HET    LMG  C 494      45                                                       
HET    BCT  D 353       4                                                       
HET    CLA  D 354      65                                                       
HET    CLA  A 364      65                                                       
HET    PHO  D 355      64                                                       
HET    CLA  D 356      65                                                       
HET    PL9  D 357      55                                                       
HET    BCR  D 358      40                                                       
HET    LMG  D 359      46                                                       
HET    LMG  D 360      48                                                       
HET    SQD  D 361      43                                                       
HET    DGD  D 362      63                                                       
HET    LMT  D 363      31                                                       
HET    HEM  F  85      43                                                       
HET    SQD  F 224      45                                                       
HET     CA  F 225       1                                                       
HET    BCR  X 107      40                                                       
HET    DGD  B 528      58                                                       
HET    LMG  I 220      43                                                       
HET    BCR  J 115      40                                                       
HET     CA  K  56       1                                                       
HET    BCR  J 112      40                                                       
HET    LMG  M 217      42                                                       
HET    LMT  T 226      35                                                       
HET     CA  O 273       1                                                       
HET    LMT  I 274      35                                                       
HET    SQD  L 213      47                                                       
HET    LMT  O 274      35                                                       
HET    HEM  V 164      43                                                       
HET    BCR  Z 116      40                                                       
HETNAM     FE2 FE (II) ION                                                      
HETNAM     CLA CHLOROPHYLL A                                                    
HETNAM     PHO PHEOPHYTIN A                                                     
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM     OEC OXYGEN EVOLVING SYSTEM                                           
HETNAM     BCR BETA-CAROTENE                                                    
HETNAM     DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)                              
HETNAM     LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE                           
HETNAM     SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-                      
HETNAM   2 SQD  GLUCOPYRANOSYL]-SN-GLYCEROL                                     
HETNAM     LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE                        
HETNAM     LMT DODECYL-BETA-D-MALTOSIDE                                         
HETNAM     BCT BICARBONATE ION                                                  
HETNAM     PL9 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,           
HETNAM   2 PL9  6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-               
HETNAM   3 PL9  CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-          
HETNAM   4 PL9  BENZOQUINONE                                                    
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM      CA CALCIUM ION                                                      
HETSYN     SQD SULFOQUINOVOSYLDIACYLGLYCEROL                                    
HETSYN     PL9 PLASTOQUINONE 9                                                  
HETSYN     HEM HEME                                                             
FORMUL  20  FE2    FE 2+                                                        
FORMUL  21  CLA    35(C55 H72 MG N4 O5 2+)                                      
FORMUL  23  PHO    2(C55 H74 N4 O5)                                             
FORMUL  25  MES    C6 H13 N O4 S                                                
FORMUL  26  OEC    CA MN4 O4                                                    
FORMUL  27  BCR    11(C40 H56)                                                  
FORMUL  28  DGD    8(C51 H96 O15)                                               
FORMUL  29  LHG    2(C38 H75 O10 P)                                             
FORMUL  30  SQD    4(C41 H78 O12 S)                                             
FORMUL  31  LMG    8(C45 H86 O10)                                               
FORMUL  34  LMT    7(C24 H46 O11)                                               
FORMUL  78  BCT    C H O3 1-                                                    
FORMUL  83  PL9    C53 H80 O2                                                   
FORMUL  90  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL  92   CA    3(CA 2+)                                                     
HELIX    1   1 ASN A   12  THR A   22  1                                  11    
HELIX    2   2 PHE A   33  ALA A   55  1                                  23    
HELIX    3   3 SER A   70  GLY A   74  5                                   5    
HELIX    4   4 PRO A   95  ALA A   99  5                                   5    
HELIX    5   5 SER A  101  ASN A  108  1                                   8    
HELIX    6   6 GLY A  109  LEU A  137  1                                  29    
HELIX    7   7 TRP A  142  TYR A  147  1                                   6    
HELIX    8   8 TYR A  147  LEU A  159  1                                  13    
HELIX    9   9 LEU A  159  GLY A  166  1                                   8    
HELIX   10  10 SER A  167  GLY A  171  5                                   5    
HELIX   11  11 ILE A  176  ASN A  191  1                                  16    
HELIX   12  12 ILE A  192  MET A  194  5                                   3    
HELIX   13  13 HIS A  195  SER A  222  1                                  28    
HELIX   14  14 ASN A  247  ILE A  259  1                                  13    
HELIX   15  15 PHE A  260  SER A  264  5                                   5    
HELIX   16  16 ASN A  267  MET A  293  1                                  27    
HELIX   17  17 THR A  316  HIS A  332  1                                  17    
HELIX   18  18 PRO B    4  ILE B   13  5                                  10    
HELIX   19  19 ASP B   15  ALA B   43  1                                  29    
HELIX   20  20 PRO B   54  GLN B   58  5                                   5    
HELIX   21  21 VAL B   62  ARG B   68  1                                   7    
HELIX   22  22 SER B   92  TYR B  117  1                                  26    
HELIX   23  23 LEU B  120  ARG B  124  5                                   5    
HELIX   24  24 ASP B  134  HIS B  157  1                                  24    
HELIX   25  25 GLY B  186  ASN B  191  5                                   6    
HELIX   26  26 ASN B  194  VAL B  219  1                                  26    
HELIX   27  27 PRO B  222  LEU B  229  1                                   8    
HELIX   28  28 ASN B  233  GLY B  259  1                                  27    
HELIX   29  29 PRO B  264  GLY B  269  1                                   6    
HELIX   30  30 THR B  271  SER B  277  1                                   7    
HELIX   31  31 SER B  278  SER B  294  1                                  17    
HELIX   32  32 THR B  297  ILE B  305  1                                   9    
HELIX   33  33 PRO B  306  ASP B  313  1                                   8    
HELIX   34  34 TYR B  314  ASN B  318  5                                   5    
HELIX   35  35 PRO B  329  GLY B  333  5                                   5    
HELIX   36  36 ARG B  384  SER B  388  5                                   5    
HELIX   37  37 SER B  391  GLY B  396  1                                   6    
HELIX   38  38 ASP B  413  ILE B  425  1                                  13    
HELIX   39  39 SER B  446  PHE B  475  1                                  30    
HELIX   40  40 ALA C   34  ILE C   43  5                                  10    
HELIX   41  41 GLY C   47  PHE C   75  1                                  29    
HELIX   42  42 MET C   81  GLY C   85  5                                   5    
HELIX   43  43 LEU C   88  LEU C   95  1                                   8    
HELIX   44  44 GLY C  100  GLU C  104  5                                   5    
HELIX   45  45 THR C  108  ARG C  135  1                                  28    
HELIX   46  46 ASP C  153  PHE C  181  1                                  29    
HELIX   47  47 ASP C  205  PHE C  210  1                                   6    
HELIX   48  48 GLY C  211  LYS C  215  5                                   5    
HELIX   49  49 GLY C  222  VAL C  227  5                                   6    
HELIX   50  50 ASN C  229  LEU C  253  1                                  25    
HELIX   51  51 GLY C  258  PHE C  264  1                                   7    
HELIX   52  52 SER C  267  ASN C  293  1                                  27    
HELIX   53  53 THR C  305  LEU C  324  1                                  20    
HELIX   54  54 ASN C  327  ALA C  331  5                                   5    
HELIX   55  55 GLY C  353  TRP C  359  5                                   7    
HELIX   56  56 LEU C  366  ARG C  370  5                                   5    
HELIX   57  57 ASP C  376  ASP C  383  1                                   8    
HELIX   58  58 GLN C  385  THR C  397  1                                  13    
HELIX   59  59 SER C  421  GLY C  454  1                                  34    
HELIX   60  60 GLU C  464  MET C  469  5                                   6    
HELIX   61  61 GLY D   13  LYS D   23  1                                  11    
HELIX   62  62 VAL D   30  PHE D   54  1                                  25    
HELIX   63  63 SER D   57  GLY D   62  1                                   6    
HELIX   64  64 SER D   66  GLY D   70  5                                   5    
HELIX   65  65 ASP D  100  LEU D  107  1                                   8    
HELIX   66  66 GLY D  108  GLY D  137  1                                  30    
HELIX   67  67 PRO D  140  PHE D  146  1                                   7    
HELIX   68  68 PHE D  146  LEU D  158  1                                  13    
HELIX   69  69 LEU D  158  GLN D  164  1                                   7    
HELIX   70  70 SER D  166  ALA D  170  5                                   5    
HELIX   71  71 VAL D  175  ASN D  190  1                                  16    
HELIX   72  72 TRP D  191  LEU D  193  5                                   3    
HELIX   73  73 ASN D  194  ASN D  220  1                                  27    
HELIX   74  74 SER D  245  PHE D  257  1                                  13    
HELIX   75  75 ASN D  263  LEU D  291  1                                  29    
HELIX   76  76 PHE D  298  ASP D  308  1                                  11    
HELIX   77  77 THR D  313  GLN D  334  1                                  22    
HELIX   78  78 PRO D  335  ASN D  338  5                                   4    
HELIX   79  79 PRO E    9  SER E   16  1                                   8    
HELIX   80  80 SER E   16  THR E   40  1                                  25    
HELIX   81  81 GLY E   41  PHE E   47  1                                   7    
HELIX   82  82 GLU E   71  GLN E   82  1                                  12    
HELIX   83  83 VAL F   18  LEU F   26  1                                   9    
HELIX   84  84 ALA F   27  GLY F   35  1                                   9    
HELIX   85  85 GLY F   35  GLN F   41  1                                   7    
HELIX   86  86 THR H    5  ARG H   12  1                                   8    
HELIX   87  87 THR H   27  ASN H   50  1                                  24    
HELIX   88  88 MET I    1  SER I   25  1                                  25    
HELIX   89  89 PRO J    9  ALA J   32  1                                  24    
HELIX   90  90 PRO K   12  ILE K   17  5                                   6    
HELIX   91  91 PHE K   18  ASP K   23  1                                   6    
HELIX   92  92 VAL K   24  PRO K   26  5                                   3    
HELIX   93  93 VAL K   27  VAL K   43  1                                  17    
HELIX   94  94 ASN L   13  ASN L   37  1                                  25    
HELIX   95  95 LEU M    6  SER M   31  1                                  26    
HELIX   96  96 THR O   32  ILE O   36  5                                   5    
HELIX   97  97 GLY O   40  LYS O   44  5                                   5    
HELIX   98  98 LEU O  208  VAL O  213  1                                   6    
HELIX   99  99 MET T    1  PHE T   23  1                                  23    
HELIX  100 100 ASN U   41  LEU U   47  1                                   7    
HELIX  101 101 ASN U   61  TYR U   68  5                                   8    
HELIX  102 102 TYR U   72  ASN U   82  1                                  11    
HELIX  103 103 SER U   87  ILE U   94  5                                   8    
HELIX  104 104 THR U   98  LEU U  109  1                                  12    
HELIX  105 105 GLU U  118  GLU U  123  1                                   6    
HELIX  106 106 GLY U  124  ASP U  126  5                                   3    
HELIX  107 107 THR V   30  LEU V   34  1                                   5    
HELIX  108 108 THR V   48  CYS V   63  1                                  16    
HELIX  109 109 CYS V   63  VAL V   68  1                                   6    
HELIX  110 110 GLY V   69  ILE V   71  5                                   3    
HELIX  111 111 ARG V   81  LEU V   87  1                                   7    
HELIX  112 112 ASN V   94  MET V  102  1                                   9    
HELIX  113 113 SER V  120  ALA V  124  5                                   5    
HELIX  114 114 PRO V  128  LEU V  133  1                                   6    
HELIX  115 115 THR V  134  GLY V  153  1                                  20    
HELIX  116 116 GLY V  153  GLY V  158  1                                   6    
HELIX  117 117 GLN y   21  ARG y   42  1                                  22    
HELIX  118 118 THR X   13  GLN X   42  1                                  30    
HELIX  119 119 MET Z    1  SER Z   29  1                                  29    
HELIX  120 120 ARG Z   35  VAL Z   62  1                                  28    
SHEET    1   A 2 ALA A  81  VAL A  82  0                                        
SHEET    2   A 2 LEU A 174  GLY A 175 -1  O  LEU A 174   N  VAL A  82           
SHEET    1   B 2 LEU A 297  ASN A 298  0                                        
SHEET    2   B 2 GLY C 402  SER C 403  1  O  GLY C 402   N  ASN A 298           
SHEET    1   C 2 MET B 166  VAL B 168  0                                        
SHEET    2   C 2 SER B 177  GLN B 179 -1  O  SER B 177   N  VAL B 168           
SHEET    1   D 2 ILE B 336  TRP B 340  0                                        
SHEET    2   D 2 PHE B 430  ASP B 433 -1  O  GLU B 431   N  GLN B 338           
SHEET    1   E 6 VAL B 377  ASP B 380  0                                        
SHEET    2   E 6 ILE B 369  THR B 371 -1  N  LEU B 370   O  ALA B 379           
SHEET    3   E 6 GLU B 353  VAL B 356 -1  N  PHE B 355   O  THR B 371           
SHEET    4   E 6 HIS B 343  ARG B 347 -1  N  PHE B 346   O  LEU B 354           
SHEET    5   E 6 THR B 398  TYR B 402 -1  O  SER B 400   N  VAL B 345           
SHEET    6   E 6 THR B 410  PHE B 411 -1  O  PHE B 411   N  VAL B 399           
SHEET    1   F 2 LEU C 185  ASP C 187  0                                        
SHEET    2   F 2 ASP C 195  ARG C 197 -1  O  ARG C 197   N  LEU C 185           
SHEET    1   G 2 LEU C 341  ARG C 343  0                                        
SHEET    2   G 2 ILE C 349  PHE C 351 -1  O  ILE C 350   N  MET C 342           
SHEET    1   H 2 ALA D  77  VAL D  78  0                                        
SHEET    2   H 2 PHE D 173  GLY D 174 -1  O  PHE D 173   N  VAL D  78           
SHEET    1   I 2 TYR O  56  PRO O  57  0                                        
SHEET    2   I 2 SER O 161  ILE O 162 -1  O  ILE O 162   N  TYR O  56           
SHEET    1   J10 PHE O  91  PRO O  93  0                                        
SHEET    2   J10 ARG O  65  LYS O  79 -1  N  VAL O  78   O  VAL O  92           
SHEET    3   J10 GLU O 258  GLU O 270 -1  O  VAL O 264   N  GLN O  72           
SHEET    4   J10 GLU O 236  LEU O 246 -1  N  SER O 243   O  ILE O 261           
SHEET    5   J10 LEU O 218  LYS O 229 -1  N  LYS O 229   O  ALA O 238           
SHEET    6   J10 PHE O 168  PRO O 175 -1  N  VAL O 174   O  THR O 219           
SHEET    7   J10 LYS O 149  SER O 154 -1  N  LYS O 149   O  ASN O 173           
SHEET    8   J10 THR O 120  ILE O 127 -1  N  PHE O 121   O  ALA O 153           
SHEET    9   J10 LEU O 104  GLU O 110 -1  N  GLN O 108   O  GLU O 124           
SHEET   10   J10 ARG O  65  LYS O  79 -1  N  ILE O  66   O  GLY O 109           
SHEET    1   K 3 LYS O  95  LEU O  96  0                                        
SHEET    2   K 3 PHE O 129  GLN O 135 -1  O  GLN O 135   N  LYS O  95           
SHEET    3   K 3 ARG O 141  THR O 147 -1  O  ILE O 142   N  VAL O 134           
SHEET    1   L 2 ILE U  55  ASP U  56  0                                        
SHEET    2   L 2 PHE U 112  THR U 113  1  O  THR U 113   N  ILE U  55           
SHEET    1   M 2 THR V  35  PRO V  37  0                                        
SHEET    2   M 2 THR V  44  THR V  46 -1  O  ILE V  45   N  VAL V  36           
SSBOND   1 CYS O   45    CYS O   70                          1555   1555  2.04  
LINK         OE2 GLU A 189                MN1  OEC A 368     1555   1555  1.73  
LINK         NE2 HIS V  67                FE   HEM V 164     1555   1555  2.05  
LINK        FE   FE2 A 361                 O3  BCT D 353     1555   1555  2.08  
LINK         OE2 GLU C 354                MN3  OEC A 368     1555   1555  2.18  
LINK         OD1 ASP A 342                MN2  OEC A 368     1555   1555  2.23  
LINK         NE2 HIS A 332                MN1  OEC A 368     1555   1555  2.24  
LINK         NE2 HIS D 214                FE   FE2 A 361     1555   1555  2.25  
LINK         OD2 ASP A 170                MN4  OEC A 368     1555   1555  2.26  
LINK         OE1 GLU A 333                MN3  OEC A 368     1555   1555  2.27  
LINK         NE2 HIS A 215                FE   FE2 A 361     1555   1555  2.29  
LINK         NE2 HIS E  23                FE   HEM F  85     1555   1555  2.33  
LINK         NE2 HIS V 118                FE   HEM V 164     1555   1555  2.35  
LINK         OE1 GLU A 189                CA1  OEC A 368     1555   1555  2.36  
LINK         NE2 HIS A 272                FE   FE2 A 361     1555   1555  2.43  
LINK         O   ALA A 344                CA1  OEC A 368     1555   1555  2.43  
LINK         OD2 ASP A 342                MN1  OEC A 368     1555   1555  2.50  
LINK         NE2 HIS D 268                FE   FE2 A 361     1555   1555  2.55  
LINK         OE1 GLU C 354                MN2  OEC A 368     1555   1555  2.55  
LINK         OD1 ASN C  39                MG   CLA C 486     1555   1555  2.65  
LINK        FE   FE2 A 361                 O2  BCT D 353     1555   1555  2.69  
LINK         OD2 ASP K  19                CA    CA K  56     1555   1555  2.74  
LINK         O   ALA A 344                MN2  OEC A 368     1555   1555  2.78  
LINK         OE1 GLU O 140                CA    CA O 273     1555   1555  2.84  
LINK         OD1 ASP A 170                CA1  OEC A 368     1555   1555  2.94  
LINK         OD1 ASP K  23                CA    CA K  56     1555   1555  2.95  
LINK         OD2 ASP K  23                CA    CA K  56     1555   1555  2.98  
LINK         O   ARG F  45                CA    CA F 225     1555   1555  3.16  
CISPEP   1 THR V   89    PRO V   90          0        -0.04                     
SITE     1 AC1  5 HIS A 215  HIS A 272  HIS D 214  HIS D 268                    
SITE     2 AC1  5 BCT D 353                                                     
SITE     1 AC2 22 PHE A 119  TYR A 147  PRO A 150  SER A 153                    
SITE     2 AC2 22 ALA A 154  VAL A 157  PHE A 182  MET A 183                    
SITE     3 AC2 22 PHE A 186  GLN A 187  LEU A 193  HIS A 198                    
SITE     4 AC2 22 VAL A 205  THR A 286  ALA A 287  ILE A 290                    
SITE     5 AC2 22 CLA A 363  CLA A 364  PHO A 365  LEU D 182                    
SITE     6 AC2 22 CLA D 354  PHE T  17                                          
SITE     1 AC3 18 THR A  45  VAL A 157  PHE A 158  MET A 172                    
SITE     2 AC3 18 ILE A 176  THR A 179  MET A 183  CLA A 362                    
SITE     3 AC3 18 PHO A 365  MET D 198  VAL D 201  ALA D 202                    
SITE     4 AC3 18 CLA D 354  PL9 D 357  LMG D 360  LEU L  30                    
SITE     5 AC3 18 PHE T  10  ILE T  14                                          
SITE     1 AC4 19 LEU A  41  THR A  45  PHE A  48  PHE A 119                    
SITE     2 AC4 19 TYR A 126  GLN A 130  TYR A 147  PRO A 150                    
SITE     3 AC4 19 LEU A 174  CLA A 362  CLA A 363  LEU D 205                    
SITE     4 AC4 19 ALA D 208  LEU D 209  ALA D 212  ILE D 213                    
SITE     5 AC4 19 TRP D 253  PHE D 257  LMG D 360                               
SITE     1 AC5 18 VAL A  35  ILE A  36  PRO A  39  THR A  40                    
SITE     2 AC5 18 PHE A  93  ILE A  96  TRP A  97  LEU A 114                    
SITE     3 AC5 18 PHE A 117  HIS A 118  LEU A 121  BCR A 369                    
SITE     4 AC5 18 DGD C 474  CLA C 481  VAL I   8  TYR I   9                    
SITE     5 AC5 18 VAL I  12  PHE I  15                                          
SITE     1 AC6  7 MET A 214  HIS A 215  LEU A 218  VAL A 219                    
SITE     2 AC6  7 TYR A 246  ALA A 251  LEU A 271                               
SITE     1 AC7  7 ASP A 170  GLU A 189  HIS A 332  GLU A 333                    
SITE     2 AC7  7 ASP A 342  ALA A 344  GLU C 354                               
SITE     1 AC8 11 VAL A  35  ILE A  38  PRO A  39  LEU A  42                    
SITE     2 AC8 11 ALA A  43  ILE A  46  ALA A  51  ALA A  55                    
SITE     3 AC8 11 TRP A 105  LEU A 106  CLA A 366                               
SITE     1 AC9 18 PHE A  93  PRO A  95  TRP A  97  GLU A  98                    
SITE     2 AC9 18 LEU A 121  PHE A 155  CLA A 366  LEU C 213                    
SITE     3 AC9 18 LEU C 214  LYS C 215  SER C 216  PRO C 217                    
SITE     4 AC9 18 TRP C 223  MET C 281  PHE C 284  CLA C 481                    
SITE     5 AC9 18 DGD C 491  LYS I   5                                          
SITE     1 BC1 14 ARG A 140  TRP A 142  PHE A 273  TRP C  36                    
SITE     2 BC1 14 PHE C 436  TRP C 443  ARG C 447  SQD C 475                    
SITE     3 BC1 14 CLA C 480  CLA C 484  ALA D 229  SER D 230                    
SITE     4 BC1 14 THR D 231  PHE D 232                                          
SITE     1 BC2 10 PHE A 273  LHG A 371  ALA C  34  TRP C  36                    
SITE     2 BC2 10 LHG C 476  CLA C 484  PHE D 232  ARG D 233                    
SITE     3 BC2 10 LMG D 359  BCR J 115                                          
SITE     1 BC3 20 SER A 232  ASN A 234  TYR A 235  PRO B   4                    
SITE     2 BC3 20 TRP B   5  TYR B   6  CLA B 521  TRP D 266                    
SITE     3 BC3 20 PHE D 273  PL9 D 357  LMG D 360  GLU L  11                    
SITE     4 BC3 20 ASN L  13  SER L  16  GLY L  20  LEU L  23                    
SITE     5 BC3 20 ILE L  24  VAL L  26  PRO M  18  LEU M  22                    
SITE     1 BC4  3 SQD C 475  DGD C 492  BCR J 115                               
SITE     1 BC5  6 ILE A  46  ILE A  50  LMT A 376  LMG I 220                    
SITE     2 BC5  6 LMT I 274  LMT O 274                                          
SITE     1 BC6  3 ALA A  54  ASP A 103  DGD A 375                               
SITE     1 BC7  6 TRP B 185  PRO B 187  PHE B 190  ALA B 204                    
SITE     2 BC7  6 CLA B 512  BCR X 107                                          
SITE     1 BC8 17 GLY B 189  PHE B 190  PRO B 192  HIS B 201                    
SITE     2 BC8 17 ALA B 204  VAL B 208  PHE B 247  PHE B 250                    
SITE     3 BC8 17 CLA B 511  CLA B 513  DGD B 528  PHE H  38                    
SITE     4 BC8 17 PHE H  41  LEU H  42  ILE H  45  TYR H  49                    
SITE     5 BC8 17 BCR X 107                                                     
SITE     1 BC9 21 ARG B  68  LEU B  69  LEU B 149  CYS B 150                    
SITE     2 BC9 21 PHE B 153  MET B 166  HIS B 201  HIS B 202                    
SITE     3 BC9 21 PHE B 247  ALA B 248  VAL B 251  VAL B 252                    
SITE     4 BC9 21 THR B 255  THR B 262  CLA B 512  CLA B 514                    
SITE     5 BC9 21 CLA B 515  CLA B 516  CLA B 519  CLA B 520                    
SITE     6 BC9 21 PHE H  38                                                     
SITE     1 CC1 23 TRP B  33  PHE B  61  PHE B  65  ARG B  68                    
SITE     2 CC1 23 LEU B 148  LEU B 149  VAL B 245  ALA B 248                    
SITE     3 CC1 23 ALA B 249  VAL B 252  PHE B 451  HIS B 455                    
SITE     4 CC1 23 PHE B 458  ALA B 459  PHE B 462  CLA B 513                    
SITE     5 CC1 23 CLA B 515  CLA B 517  CLA B 520  CLA B 521                    
SITE     6 CC1 23 CLA B 522  CLA B 523  CLA B 525                               
SITE     1 CC2 21 THR B  27  VAL B  30  ALA B  31  TRP B  33                    
SITE     2 CC2 21 ALA B  34  VAL B  62  PHE B  65  MET B  66                    
SITE     3 CC2 21 ARG B  68  LEU B  69  HIS B 100  LEU B 103                    
SITE     4 CC2 21 GLY B 147  ALA B 205  CLA B 513  CLA B 514                    
SITE     5 CC2 21 CLA B 516  CLA B 519  CLA B 520  CLA B 522                    
SITE     6 CC2 21 BCR B 530                                                     
SITE     1 CC3 16 TRP B  91  VAL B  96  ALA B  99  HIS B 100                    
SITE     2 CC3 16 LEU B 103  LEU B 106  LEU B 149  GLY B 152                    
SITE     3 CC3 16 PHE B 153  PHE B 156  HIS B 157  PHE B 162                    
SITE     4 CC3 16 PRO B 164  CLA B 513  CLA B 515  CLA B 526                    
SITE     1 CC4 22 TRP B  33  MET B  37  TYR B  40  GLN B  58                    
SITE     2 CC4 22 GLY B  59  PHE B  61  PHE B 325  ARG B 326                    
SITE     3 CC4 22 THR B 327  GLY B 328  PRO B 329  TRP B 450                    
SITE     4 CC4 22 PHE B 451  ALA B 454  CLA B 514  CLA B 523                    
SITE     5 CC4 22 BCR B 529  LMG B 531  DGD B 533  MET D 199                    
SITE     6 CC4 22 MET D 281  PHE M  14                                          
SITE     1 CC5 17 THR B 236  SER B 239  SER B 240  ALA B 243                    
SITE     2 CC5 17 PHE B 246  PHE B 247  HIS B 466  CLA B 519                    
SITE     3 CC5 17 CLA B 520  PHE D 120  ILE D 123  MET D 126                    
SITE     4 CC5 17 LEU D 127  PHE D 130  CLA D 356  SQD D 361                    
SITE     5 CC5 17 LEU H  43                                                     
SITE     1 CC6 20 PHE B 139  VAL B 208  ALA B 212  PHE B 215                    
SITE     2 CC6 20 HIS B 216  ARG B 220  PRO B 221  PRO B 222                    
SITE     3 CC6 20 LEU B 225  LEU B 229  CLA B 513  CLA B 515                    
SITE     4 CC6 20 CLA B 518  CLA B 520  THR H  27  THR H  28                    
SITE     5 CC6 20 MET H  31  PHE H  34  LEU H  46  BCR X 107                    
SITE     1 CC7 14 PHE B 139  HIS B 142  LEU B 143  MET B 231                    
SITE     2 CC7 14 ILE B 234  VAL B 237  SER B 240  CLA B 513                    
SITE     3 CC7 14 CLA B 514  CLA B 515  CLA B 518  CLA B 519                    
SITE     4 CC7 14 CLA B 522  CLA B 525                                          
SITE     1 CC8 20 LMG A 373  TRP B   5  TYR B   6  ARG B   7                    
SITE     2 CC8 20 HIS B   9  ILE B 242  LEU B 461  PHE B 462                    
SITE     3 CC8 20 PHE B 464  GLY B 465  TRP B 468  HIS B 469                    
SITE     4 CC8 20 ARG B 472  PHE B 479  CLA B 514  CLA B 522                    
SITE     5 CC8 20 CLA B 523  CLA B 524  LMG B 531  PHE M  21                    
SITE     1 CC9 17 HIS B   9  HIS B  23  HIS B  26  THR B  27                    
SITE     2 CC9 17 ILE B 234  GLU B 235  VAL B 237  LEU B 238                    
SITE     3 CC9 17 SER B 241  ILE B 242  CLA B 514  CLA B 515                    
SITE     4 CC9 17 CLA B 520  CLA B 521  CLA B 523  CLA B 524                    
SITE     5 CC9 17 CLA B 525                                                     
SITE     1 DC1 12 HIS B   9  HIS B  26  VAL B  30  TRP B  33                    
SITE     2 DC1 12 PHE B 462  CLA B 514  CLA B 517  CLA B 521                    
SITE     3 DC1 12 CLA B 522  CLA B 524  BCR B 527  LMG B 531                    
SITE     1 DC2 12 VAL B   8  HIS B   9  ALA B  22  TRP B 115                    
SITE     2 DC2 12 CLA B 521  CLA B 522  CLA B 523  BCR B 527                    
SITE     3 DC2 12 DGD B 533  VAL L  10  PHE M  21  LEU M  25                    
SITE     1 DC3 11 HIS B  23  LEU B  24  MET B 138  HIS B 142                    
SITE     2 DC3 11 LEU B 145  CLA B 514  CLA B 520  CLA B 522                    
SITE     3 DC3 11 CLA B 526  BCR B 530  LEU H  14                               
SITE     1 DC4 10 LEU B  24  ALA B 110  TRP B 113  HIS B 114                    
SITE     2 DC4 10 CLA B 516  CLA B 525  BCR B 530  THR H   5                    
SITE     3 DC4 10 LEU H   7  GLY H   8                                          
SITE     1 DC5  9 MET B  25  LEU B  29  ALA B 111  TRP B 115                    
SITE     2 DC5  9 CLA B 523  CLA B 524  BCR B 529  DGD B 533                    
SITE     3 DC5  9 LEU M  13                                                     
SITE     1 DC6  6 LEU B  29  TRP B  33  GLY B 105  CLA B 517                    
SITE     2 DC6  6 BCR B 527  DGD B 533                                          
SITE     1 DC7  4 CLA B 515  CLA B 525  CLA B 526  LMT B 535                    
SITE     1 DC8 17 ALA A 233  TYR B   6  ARG B   7  PHE B 464                    
SITE     2 DC8 17 TRP B 468  PHE B 479  CLA B 517  CLA B 521                    
SITE     3 DC8 17 CLA B 523  DGD B 533  ARG D 139  TYR D 141                    
SITE     4 DC8 17 PHE D 269  LEU D 272  VAL D 276  PHE M  14                    
SITE     5 DC8 17 PRO M  18                                                     
SITE     1 DC9 16 THR B 327  LYS B 332  LEU B 461  CLA B 517                    
SITE     2 DC9 16 CLA B 524  BCR B 527  BCR B 529  LMG B 531                    
SITE     3 DC9 16 ILE D 284  PHE L  35  ASN M   4  LEU M   6                    
SITE     4 DC9 16 ALA M  10  LEU M  13  PHE M  14  VAL M  17                    
SITE     1 EC1  3 TRP B  91  LEU B 149  BCR B 530                               
SITE     1 EC2  6 LYS B 227  ASP D  19  ASP D  20  LYS D  23                    
SITE     2 EC2  6 SQD D 361  MET H  35                                          
SITE     1 EC3 16 LEU C  95  LEU C 168  GLY C 171  ALA C 172                    
SITE     2 EC3 16 TRP C 223  ILE C 224  HIS C 237  ILE C 240                    
SITE     3 EC3 16 PHE C 289  VAL C 296  TYR C 297  CLA C 478                    
SITE     4 EC3 16 CLA C 479  CLA C 482  CLA C 483  BCR C 490                    
SITE     1 EC4 20 TRP C  63  HIS C  91  LEU C 174  LEU C 175                    
SITE     2 EC4 20 LYS C 178  PHE C 182  LEU C 279  MET C 282                    
SITE     3 EC4 20 GLY C 283  ALA C 286  VAL C 290  TYR C 297                    
SITE     4 EC4 20 HIS C 430  LEU C 433  ALA C 434  PHE C 437                    
SITE     5 EC4 20 CLA C 477  CLA C 479  CLA C 480  CLA K 483                    
SITE     1 EC5 14 ILE C  60  VAL C  61  TRP C  63  ALA C  64                    
SITE     2 EC5 14 THR C  68  LEU C  88  HIS C  91  LEU C  95                    
SITE     3 EC5 14 VAL C 114  HIS C 118  CLA C 477  CLA C 478                    
SITE     4 EC5 14 LMG C 494  CLA K 483                                          
SITE     1 EC6 18 VAL A 281  LHG A 371  TRP C  63  MET C  67                    
SITE     2 EC6 18 PHE C  70  GLN C  84  GLY C  85  LEU C 404                    
SITE     3 EC6 18 TRP C 425  LEU C 426  SER C 429  CLA C 478                    
SITE     4 EC6 18 CLA C 484  DGD C 492  DGD C 493  LMG J 492                    
SITE     5 EC6 18 PRO K  26  CLA K 483                                          
SITE     1 EC7 18 PHE A  33  MET A 127  GLY A 128  TRP A 131                    
SITE     2 EC7 18 CLA A 366  PHE C 264  ILE C 265  TYR C 274                    
SITE     3 EC7 18 GLY C 277  MET C 281  HIS C 441  LEU C 442                    
SITE     4 EC7 18 ALA C 445  ARG C 449  DGD C 474  CLA C 483                    
SITE     5 EC7 18 BCR C 490  PHE I  23                                          
SITE     1 EC8 15 LEU C 161  LEU C 165  ILE C 243  CYS C 244                    
SITE     2 EC8 15 TRP C 250  HIS C 251  THR C 255  PRO C 256                    
SITE     3 EC8 15 PHE C 257  TRP C 259  ALA C 260  PHE C 264                    
SITE     4 EC8 15 CLA C 477  CLA C 483  BCR C 490                               
SITE     1 EC9 16 MET C 157  LEU C 161  HIS C 164  LEU C 165                    
SITE     2 EC9 16 LEU C 168  ILE C 240  PHE C 264  TRP C 266                    
SITE     3 EC9 16 TYR C 271  TYR C 274  SER C 275  CLA C 477                    
SITE     4 EC9 16 CLA C 481  CLA C 482  CLA C 485  BCR C 490                    
SITE     1 FC1 19 LHG A 371  TRP C  36  ALA C  37  GLY C  38                    
SITE     2 FC1 19 ASN C  39  ALA C  40  GLU C 269  LEU C 276                    
SITE     3 FC1 19 PHE C 436  PHE C 437  GLY C 440  TRP C 443                    
SITE     4 FC1 19 HIS C 444  ARG C 447  SQD C 475  CLA C 480                    
SITE     5 FC1 19 CLA C 485  CLA C 486  CLA K 483                               
SITE     1 FC2 18 ASN C  39  ILE C  43  LEU C  49  ALA C  52                    
SITE     2 FC2 18 HIS C  53  HIS C  56  TRP C 151  HIS C 164                    
SITE     3 FC2 18 GLY C 268  TYR C 271  LEU C 272  SER C 275                    
SITE     4 FC2 18 LEU C 276  LEU C 279  CLA C 483  CLA C 484                    
SITE     5 FC2 18 CLA C 487  CLA K 483                                          
SITE     1 FC3 16 HIS C  56  LEU C  59  ILE C  60  TRP C  63                    
SITE     2 FC3 16 LEU C 279  PHE C 436  PHE C 437  CLA C 478                    
SITE     3 FC3 16 CLA C 479  CLA C 480  CLA C 484  CLA C 485                    
SITE     4 FC3 16 CLA C 486  PRO K  29  VAL K  30  LEU K  33                    
SITE     1 FC4 28 GLN C  28  TRP C  35  GLY C  38  ASN C  39                    
SITE     2 FC4 28 ARG C  41  LEU C  42  LEU C  45  LYS C  48                    
SITE     3 FC4 28 ALA C  52  ALA C 123  PHE C 127  VAL C 130                    
SITE     4 FC4 28 ALA C 133  ILE C 134  CLA C 484  BCR C 489                    
SITE     5 FC4 28 PHE K  32  LEU K  33  PHE K  37  TRP K  39                    
SITE     6 FC4 28 GLN K  40  CLA K 483  MET Z  19  VAL Z  20                    
SITE     7 FC4 28 PRO Z  24  ILE y  35  LEU y  39  ASN y  45                    
SITE     1 FC5 14 HIS C  53  VAL C  54  ALA C  57  LEU C 125                    
SITE     2 FC5 14 ILE C 160  PHE C 163  HIS C 164  VAL C 167                    
SITE     3 FC5 14 ILE C 170  GLY C 171  LEU C 174  CLA C 485                    
SITE     4 FC5 14 CLA C 488  BCR Z 116                                          
SITE     1 FC6  9 VAL C  54  VAL C 124  LEU C 125  GLY C 128                    
SITE     2 FC6  9 TYR C 131  HIS C 132  PHE C 147  CLA C 487                    
SITE     3 FC6  9 BCR Z 116                                                     
SITE     1 FC7 15 ALA C  55  GLY C  58  LEU C  59  VAL C 116                    
SITE     2 FC7 15 LEU C 119  SER C 122  ALA C 123  CLA C 486                    
SITE     3 FC7 15 BCR J 112  TYR K  15  PHE K  18  LEU K  21                    
SITE     4 FC7 15 LEU Z   9  VAL Z  13  VAL Z  20                               
SITE     1 FC8 15 ILE C 209  PHE C 210  TYR C 212  LEU C 213                    
SITE     2 FC8 15 VAL C 227  ASP C 232  VAL C 233  HIS C 237                    
SITE     3 FC8 15 ILE C 240  PHE C 264  CLA C 477  CLA C 481                    
SITE     4 FC8 15 CLA C 482  CLA C 483  PHE I  23                               
SITE     1 FC9 18 PHE A 155  ILE A 160  PRO C 217  PHE C 218                    
SITE     2 FC9 18 GLY C 219  GLY C 220  TRP C 223  VAL C 225                    
SITE     3 FC9 18 PHE C 284  CYS C 288  PHE C 292  ASN C 293                    
SITE     4 FC9 18 ASN C 294  THR C 295  ASP C 360  ARG C 362                    
SITE     5 FC9 18 LEU C 438  DGD C 474                                          
SITE     1 GC1 18 PHE A 197  THR A 292  GLU C  83  GLN C  84                    
SITE     2 GC1 18 GLY C  85  SER C 406  ASN C 418  PHE C 419                    
SITE     3 GC1 18 VAL C 420  TRP C 425  VAL C 432  LHG C 476                    
SITE     4 GC1 18 CLA C 480  DGD C 493  PHE J  29  TYR J  33                    
SITE     5 GC1 18 BCR J 115  LMG J 492                                          
SITE     1 GC2 24 LEU A 200  ALA A 203  TRP A 278  VAL A 281                    
SITE     2 GC2 24 PHE A 300  CLA A 364  LEU C 404  ASN C 405                    
SITE     3 GC2 24 SER C 406  VAL C 407  ASN C 415  SER C 416                    
SITE     4 GC2 24 VAL C 417  ASN C 418  CLA C 480  DGD C 492                    
SITE     5 GC2 24 LMG D 359  PHE J  29  ALA J  32  TYR J  33                    
SITE     6 GC2 24 GLY J  37  SER J  38  SER J  39  LEU J  40                    
SITE     1 GC3  7 HIS C  74  CLA C 480  DGD C 492  ILE J  22                    
SITE     2 GC3  7 BCR J 115  VAL K  30  ILE y  25                               
SITE     1 GC4  7 PHE C 109  PRO C 110  VAL C 113  VAL C 114                    
SITE     2 GC4  7 VAL C 117  CLA C 479  BCR Z 116                               
SITE     1 GC5  8 HIS A 215  TYR A 246  HIS A 272  FE2 A 361                    
SITE     2 GC5  8 HIS D 214  TYR D 244  LYS D 264  HIS D 268                    
SITE     1 GC6 25 PHE A 206  CLA A 362  CLA A 363  CLA A 364                    
SITE     2 GC6 25 TRP D  48  LEU D 122  PRO D 149  VAL D 152                    
SITE     3 GC6 25 SER D 155  VAL D 156  PHE D 181  LEU D 182                    
SITE     4 GC6 25 PHE D 185  GLN D 186  TRP D 191  THR D 192                    
SITE     5 GC6 25 HIS D 197  VAL D 201  VAL D 204  LEU D 279                    
SITE     6 GC6 25 SER D 282  ALA D 283  VAL D 286  PHO D 355                    
SITE     7 GC6 25 LMG D 359                                                     
SITE     1 GC7 14 GLN A 199  VAL A 202  ALA A 203  CLA A 362                    
SITE     2 GC7 14 DGD C 493  PHE D 153  PHE D 157  VAL D 175                    
SITE     3 GC7 14 ILE D 178  PHE D 181  LEU D 182  CLA D 354                    
SITE     4 GC7 14 PHO D 355  LMG D 359                                          
SITE     1 GC8 20 LEU A 210  MET A 214  ILE A 259  CLA A 364                    
SITE     2 GC8 20 LEU D  37  ALA D  41  ALA D  44  TRP D  48                    
SITE     3 GC8 20 GLY D 118  GLY D 121  LEU D 122  PHE D 125                    
SITE     4 GC8 20 ASN D 142  PHE D 146  ALA D 148  PRO D 149                    
SITE     5 GC8 20 GLY D 174  PRO D 275  LEU D 279  CLA D 354                    
SITE     1 GC9 16 CLA B 518  ILE D  35  PRO D  39  LEU D  43                    
SITE     2 GC9 16 LEU D  89  LEU D  90  LEU D  91  LEU D  92                    
SITE     3 GC9 16 TRP D  93  TRP D 104  THR D 112  PHE D 113                    
SITE     4 GC9 16 HIS D 117  VAL H  40  LEU X  23  GLY X  26                    
SITE     1 HC1 18 ILE A  53  CLA A 363  LMG A 373  ALA D 202                    
SITE     2 HC1 18 LEU D 210  ILE D 213  HIS D 214  THR D 217                    
SITE     3 HC1 18 MET D 246  TRP D 253  ALA D 260  PHE D 261                    
SITE     4 HC1 18 LEU D 267  VAL D 274  LMG D 360  VAL L  26                    
SITE     5 HC1 18 LEU L  29  PHE T  10                                          
SITE     1 HC2 12 TYR D  42  GLY D  46  GLY D  47  LEU D  49                    
SITE     2 HC2 12 THR D  50  PHE D 113  LMG D 359  PRO F  29                    
SITE     3 HC2 12 PHE F  33  LEU F  34  VAL J  21  VAL J  25                    
SITE     1 HC3 15 CLA A 364  SQD C 475  DGD C 493  TYR D  67                    
SITE     2 HC3 15 CYS D  71  CLA D 354  BCR D 358  LEU F  26                    
SITE     3 HC3 15 ILE F  37  MET F  40  GLN F  41  PHE J  28                    
SITE     4 HC3 15 GLY J  31  ALA J  32  GLY J  37                               
SITE     1 HC4 18 CLA A 363  PHO A 365  LMG A 373  ILE D 259                    
SITE     2 HC4 18 ALA D 260  PHE D 261  SER D 262  ASN D 263                    
SITE     3 HC4 18 TRP D 266  PL9 D 357  THR L  15  LEU L  19                    
SITE     4 HC4 18 LEU L  22  PHE T  10  ILE T  13  PHE T  17                    
SITE     5 HC4 18 ALA T  20  ILE T  21                                          
SITE     1 HC5  9 LYS B 227  ARG B 230  CLA B 518  LYS D  23                    
SITE     2 HC5  9 TRP D  32  ARG D 134  LEU D 135  LMT D 536                    
SITE     3 HC5  9 PHE X  34                                                     
SITE     1 HC6  3 PHE D 101  ARG D 103  SQD F 224                               
SITE     1 HC7  4 GLU B 350  GLN D  98  GLY D  99  ILE X  21                    
SITE     1 HC8 14 ARG E   8  PHE E  10  ILE E  13  ARG E  18                    
SITE     2 HC8 14 TYR E  19  HIS E  23  THR E  26  LEU E  30                    
SITE     3 HC8 14 PHE F  16  ARG F  19  TRP F  20  HIS F  24                    
SITE     4 HC8 14 ALA F  27  ILE F  31                                          
SITE     1 HC9  9 TRP D  21  ARG D  24  DGD D 362  PRO F  14                    
SITE     2 HC9  9 PHE F  16  THR F  17  VAL F  18  TRP F  20                    
SITE     3 HC9  9 ILE X  40                                                     
SITE     1 IC1  2 ARG F  45  GLU V  49                                          
SITE     1 IC2 10 CLA B 511  CLA B 512  CLA B 519  MET H  35                    
SITE     2 IC2 10 PHE H  38  PHE H  41  THR X  11  ILE X  12                    
SITE     3 IC2 10 LEU X  16  PHE X  20                                          
SITE     1 IC3 18 TYR B 193  PHE B 250  GLY B 254  TYR B 258                    
SITE     2 IC3 18 TYR B 273  SER B 277  PHE B 463  CLA B 512                    
SITE     3 IC3 18 GLY D  86  HIS D  87  PHE D 120  ILE D 159                    
SITE     4 IC3 18 LEU D 162  SER D 165  LEU H  46  TYR H  49                    
SITE     5 IC3 18 VAL H  60  SER H  61                                          
SITE     1 IC4  2 DGD A 375  LMT I 274                                          
SITE     1 IC5  9 SQD C 475  LHG C 476  DGD C 492  VAL J  21                    
SITE     2 IC5  9 ILE J  22  PHE J  29  TYR J  30  TYR J  33                    
SITE     3 IC5  9 LMG J 492                                                     
SITE     1 IC6  2 ASP K  19  ASP K  23                                          
SITE     1 IC7 15 BCR C 489  ALA J  14  THR J  15  GLY J  18                    
SITE     2 IC7 15 MET J  19  LEU K  21  LEU K  31  PHE K  32                    
SITE     3 IC7 15 PHE K  37  VAL K  38  SER Z  16  PHE Z  17                    
SITE     4 IC7 15 ILE y  28  GLY y  29  GLY y  32                               
SITE     1 IC8  4 SQD L 213  ILE M  23  GLU M  30  SER M  31                    
SITE     1 IC9  3 MET M   1  MET T   1  PHE T   8                               
SITE     1 JC1  2 GLU O 140  HIS O 257                                          
SITE     1 JC2  6 ALA A 100  DGD A 375  MET I   1  LEU I   4                    
SITE     2 JC2  6 LMG I 220  LYS O  95                                          
SITE     1 JC3  4 ARG L  14  LEU L  21  LMG M 217  PHE T  19                    
SITE     1 JC4  1 DGD A 375                                                     
SITE     1 JC5 14 ALA C 393  ALA V  62  CYS V  63  CYS V  66                    
SITE     2 JC5 14 HIS V  67  THR V  74  ASN V  75  LEU V  78                    
SITE     3 JC5 14 LEU V  80  LEU V  85  TYR V 101  MET V 102                    
SITE     4 JC5 14 TYR V 108  HIS V 118                                          
SITE     1 JC6 11 VAL C 116  SER C 121  LEU C 125  CLA C 487                    
SITE     2 JC6 11 CLA C 488  LMG C 494  TYR K  15  VAL Z  51                    
SITE     3 JC6 11 VAL Z  54  GLY Z  55  ASN Z  58                               
CRYST1  119.890  224.690  337.280  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      0.008341  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004451  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002965        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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