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Database: PDB
Entry: 2AXT
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HEADER    ELECTRON TRANSPORT                      06-SEP-05   2AXT              
TITLE     CRYSTAL STRUCTURE OF PHOTOSYSTEM II FROM THERMOSYNECHOCOCCUS ELONGATUS
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOTOSYSTEM Q(B) PROTEIN;                                  
COMPND   3 CHAIN: A, a;                                                         
COMPND   4 FRAGMENT: RESIDUES 1-344;                                            
COMPND   5 SYNONYM: REACTION CENTRE SUBUNIT D1, 32 KDA THYLAKOID MEMBRANE       
COMPND   6 PROTEIN, PHOTOSYSTEM II PROTEIN D1;                                  
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CP47 PROTEIN;                                              
COMPND   9 CHAIN: B, b;                                                         
COMPND  10 SYNONYM: ANTENNA SUBUNIT CP47;                                       
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: PHOTOSYSTEM II CP43 PROTEIN;                               
COMPND  13 CHAIN: C, c;                                                         
COMPND  14 SYNONYM: ANTENNA SUBUNIT CP43;                                       
COMPND  15 MOL_ID: 4;                                                           
COMPND  16 MOLECULE: PHOTOSYSTEM II REACTION CENTER D2 PROTEIN;                 
COMPND  17 CHAIN: D, d;                                                         
COMPND  18 SYNONYM: REACTION CENTRE SUBUNIT D2;                                 
COMPND  19 MOL_ID: 5;                                                           
COMPND  20 MOLECULE: CYTOCHROME B559 ALPHA SUBUNIT;                             
COMPND  21 CHAIN: E, e;                                                         
COMPND  22 SYNONYM: CYT B-559 SUBUNIT ALPHA, PSII REACTION CENTER SUBUNIT V;    
COMPND  23 MOL_ID: 6;                                                           
COMPND  24 MOLECULE: CYTOCHROME B559 BETA SUBUNIT;                              
COMPND  25 CHAIN: F, f;                                                         
COMPND  26 SYNONYM: CYT B-559 SUBUNIT BETA, PSII REACTION CENTER SUBUNIT VI;    
COMPND  27 MOL_ID: 7;                                                           
COMPND  28 MOLECULE: PHOTOSYSTEM II REACTION CENTER H PROTEIN;                  
COMPND  29 CHAIN: H, h;                                                         
COMPND  30 SYNONYM: SUBUNIT PSBH, PSII-H;                                       
COMPND  31 MOL_ID: 8;                                                           
COMPND  32 MOLECULE: PHOTOSYSTEM II REACTION CENTER I PROTEIN;                  
COMPND  33 CHAIN: I, i;                                                         
COMPND  34 SYNONYM: SUBUNIT PSBI, PSII 4.4 KDA PROTEIN;                         
COMPND  35 MOL_ID: 9;                                                           
COMPND  36 MOLECULE: PHOTOSYSTEM II REACTION CENTER J PROTEIN;                  
COMPND  37 CHAIN: J, j;                                                         
COMPND  38 SYNONYM: SUBUNIT PSBJ;                                               
COMPND  39 MOL_ID: 10;                                                          
COMPND  40 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN K;                  
COMPND  41 CHAIN: K, k;                                                         
COMPND  42 SYNONYM: SUBUNIT PSBK, PSII-K;                                       
COMPND  43 MOL_ID: 11;                                                          
COMPND  44 MOLECULE: PHOTOSYSTEM II REACTION CENTER L PROTEIN;                  
COMPND  45 CHAIN: L, l;                                                         
COMPND  46 SYNONYM: SUBUNIT PSBL, PSII-L, PSII 5 KDA PROTEIN;                   
COMPND  47 MOL_ID: 12;                                                          
COMPND  48 MOLECULE: PHOTOSYSTEM II REACTION CENTER M PROTEIN;                  
COMPND  49 CHAIN: M, m;                                                         
COMPND  50 SYNONYM: SUBUNIT PSBM, PSII-M;                                       
COMPND  51 MOL_ID: 13;                                                          
COMPND  52 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;          
COMPND  53 CHAIN: O, o;                                                         
COMPND  54 SYNONYM: SUBUNIT PSBO, MSP;                                          
COMPND  55 MOL_ID: 14;                                                          
COMPND  56 MOLECULE: PHOTOSYSTEM II REACTION CENTER T PROTEIN;                  
COMPND  57 CHAIN: T, t;                                                         
COMPND  58 SYNONYM: SUBUNIT PSBT, PSII-T, PSII-TC;                              
COMPND  59 MOL_ID: 15;                                                          
COMPND  60 MOLECULE: PHOTOSYSTEM II 12 KDA EXTRINSIC PROTEIN;                   
COMPND  61 CHAIN: U, u;                                                         
COMPND  62 SYNONYM: SUBUNIT PSBU, PS II COMPLEX 12 KDA EXTRINSIC PROTEIN, PSII- 
COMPND  63 U;                                                                   
COMPND  64 MOL_ID: 16;                                                          
COMPND  65 MOLECULE: CYTOCHROME C-550;                                          
COMPND  66 CHAIN: V, v;                                                         
COMPND  67 SYNONYM: CYT C-550, SUBUNIT PSBV, CYTOCHROME C550, LOW POTENTIAL     
COMPND  68 CYTOCHROME C;                                                        
COMPND  69 MOL_ID: 17;                                                          
COMPND  70 MOLECULE: UNASSIGNED SUBUNITS;                                       
COMPND  71 CHAIN: X, x;                                                         
COMPND  72 MOL_ID: 18;                                                          
COMPND  73 MOLECULE: PHOTOSYSTEM II REACTION CENTER Z PROTEIN;                  
COMPND  74 CHAIN: Z, z;                                                         
COMPND  75 SYNONYM: SUBUNIT PSBZ                                                
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE   3 ORGANISM_TAXID: 146786;                                              
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE   6 ORGANISM_TAXID: 197221;                                              
SOURCE   7 STRAIN: BP-1;                                                        
SOURCE   8 MOL_ID: 3;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  10 ORGANISM_TAXID: 197221;                                              
SOURCE  11 STRAIN: BP-1;                                                        
SOURCE  12 MOL_ID: 4;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  14 ORGANISM_TAXID: 197221;                                              
SOURCE  15 STRAIN: BP-1;                                                        
SOURCE  16 MOL_ID: 5;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  18 ORGANISM_TAXID: 146786;                                              
SOURCE  19 MOL_ID: 6;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  21 ORGANISM_TAXID: 146786;                                              
SOURCE  22 MOL_ID: 7;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  24 ORGANISM_TAXID: 146786;                                              
SOURCE  25 MOL_ID: 8;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  27 ORGANISM_TAXID: 146786;                                              
SOURCE  28 MOL_ID: 9;                                                           
SOURCE  29 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  30 ORGANISM_TAXID: 146786;                                              
SOURCE  31 MOL_ID: 10;                                                          
SOURCE  32 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  33 ORGANISM_TAXID: 146786;                                              
SOURCE  34 MOL_ID: 11;                                                          
SOURCE  35 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  36 ORGANISM_TAXID: 146786;                                              
SOURCE  37 MOL_ID: 12;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  39 ORGANISM_TAXID: 146786;                                              
SOURCE  40 MOL_ID: 13;                                                          
SOURCE  41 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  42 ORGANISM_TAXID: 146786;                                              
SOURCE  43 MOL_ID: 14;                                                          
SOURCE  44 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  45 ORGANISM_TAXID: 146786;                                              
SOURCE  46 MOL_ID: 15;                                                          
SOURCE  47 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  48 ORGANISM_TAXID: 146786;                                              
SOURCE  49 MOL_ID: 16;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  51 ORGANISM_TAXID: 146786;                                              
SOURCE  52 MOL_ID: 17;                                                          
SOURCE  53 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  54 ORGANISM_TAXID: 146786;                                              
SOURCE  55 MOL_ID: 18;                                                          
SOURCE  56 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  57 ORGANISM_TAXID: 146786                                               
KEYWDS    PHOTOSYSTEM, PS II, PS2, MEMBRANE COMPLEX, TRANSMEMBRANE ALPHA-HELIX, 
KEYWDS   2 ELECTRON TRANSPORT                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.LOLL,J.KERN,W.SAENGER,A.ZOUNI,J.BIESIADKA                           
REVDAT   4   20-DEC-17 2AXT    1       ATOM                                     
REVDAT   3   13-JUL-11 2AXT    1       VERSN                                    
REVDAT   2   10-FEB-09 2AXT    1       VERSN  ATOM                              
REVDAT   1   27-DEC-05 2AXT    0                                                
JRNL        AUTH   B.LOLL,J.KERN,W.SAENGER,A.ZOUNI,J.BIESIADKA                  
JRNL        TITL   TOWARDS COMPLETE COFACTOR ARRANGEMENT IN THE 3.0 A           
JRNL        TITL 2 RESOLUTION STRUCTURE OF PHOTOSYSTEM II                       
JRNL        REF    NATURE                        V. 438  1040 2005              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   16355230                                                     
JRNL        DOI    10.1038/NATURE04224                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 4628278.020                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 75.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 129965                         
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) : 0.234                           
REMARK   3   FREE R VALUE                     : 0.286                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1620                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
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) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.18                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 50.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 14106                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3430                       
REMARK   3   BIN FREE R VALUE                    : 0.3830                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 1.30                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 182                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.028                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 40684                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 7570                                    
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) : 71.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 27.02000                                             
REMARK   3    B22 (A**2) : -2.46000                                             
REMARK   3    B33 (A**2) : -24.56000                                            
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) : 0.43                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.65                            
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) : 0.52                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.78                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.014                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.500                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 18.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.800                           
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) : 1.070 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.820 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.750 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.520 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.30                                                 
REMARK   3   BSOL        : 39.65                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : CONSTR                                                  
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-NEW2.PARAM                                 
REMARK   3  PARAMETER FILE  4  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2AXT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-OCT-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000034441.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-FEB-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : SI                                 
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 155380                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.2                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.8300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 73.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.46600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.170                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS                        
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.76                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 2000, PIPES, MAGNESIUM CHLORIDE,     
REMARK 280  PH 7.0, BATCH, TEMPERATURE 298K                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       63.84600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      153.05300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      112.70150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      153.05300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       63.84600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      112.70150            
REMARK 290   SMTRY3   4  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: 36-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, I, J, K,         
REMARK 350                    AND CHAINS: L, M, O, T, U, V, X, Z, a,            
REMARK 350                    AND CHAINS: b, c, d, e, f, h, i, j, k, l,         
REMARK 350                    AND CHAINS: m, o, t, u, v, 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     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     1                                                      
REMARK 465     LYS C     2                                                      
REMARK 465     THR C     3                                                      
REMARK 465     LEU C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     GLN C     7                                                      
REMARK 465     LYS C     8                                                      
REMARK 465     ARG C     9                                                      
REMARK 465     TYR C    10                                                      
REMARK 465     SER C    11                                                      
REMARK 465     PRO C    12                                                      
REMARK 465     VAL 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     ARG C    26                                                      
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     MET E     1                                                      
REMARK 465     ALA E     2                                                      
REMARK 465     MET F     1                                                      
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     GLN F     8                                                      
REMARK 465     GLU F     9                                                      
REMARK 465     PRO F    10                                                      
REMARK 465     MET H     1                                                      
REMARK 465     GLY H    66                                                      
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     ALA O    26                                                      
REMARK 465     ALA O    27                                                      
REMARK 465     LYS O    28                                                      
REMARK 465     GLN O    29                                                      
REMARK 465     ALA O   272                                                      
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     UNK X    32                                                      
REMARK 465     UNK X    33                                                      
REMARK 465     UNK X    34                                                      
REMARK 465     UNK X    35                                                      
REMARK 465     UNK X    36                                                      
REMARK 465     UNK X    37                                                      
REMARK 465     UNK X    38                                                      
REMARK 465     UNK X    39                                                      
REMARK 465     UNK X    40                                                      
REMARK 465     UNK X    41                                                      
REMARK 465     UNK X    42                                                      
REMARK 465     UNK X    43                                                      
REMARK 465     UNK X    44                                                      
REMARK 465     UNK X    45                                                      
REMARK 465     UNK X    46                                                      
REMARK 465     UNK X    47                                                      
REMARK 465     UNK X    48                                                      
REMARK 465     UNK X    49                                                      
REMARK 465     UNK X    93                                                      
REMARK 465     UNK X    94                                                      
REMARK 465     UNK X    95                                                      
REMARK 465     UNK X    96                                                      
REMARK 465     UNK X    97                                                      
REMARK 465     UNK X    98                                                      
REMARK 465     UNK X    99                                                      
REMARK 465     MET a  5001                                                      
REMARK 465     THR a  5002                                                      
REMARK 465     THR a  5003                                                      
REMARK 465     THR a  5004                                                      
REMARK 465     LEU a  5005                                                      
REMARK 465     GLN a  5006                                                      
REMARK 465     ARG a  5007                                                      
REMARK 465     ARG a  5008                                                      
REMARK 465     GLU a  5009                                                      
REMARK 465     MET b  5001                                                      
REMARK 465     GLN b  5490                                                      
REMARK 465     VAL b  5491                                                      
REMARK 465     GLU b  5492                                                      
REMARK 465     TRP b  5493                                                      
REMARK 465     GLY b  5494                                                      
REMARK 465     PHE b  5495                                                      
REMARK 465     TYR b  5496                                                      
REMARK 465     GLN b  5497                                                      
REMARK 465     LYS b  5498                                                      
REMARK 465     VAL b  5499                                                      
REMARK 465     GLY b  5500                                                      
REMARK 465     ASP b  5501                                                      
REMARK 465     VAL b  5502                                                      
REMARK 465     THR b  5503                                                      
REMARK 465     THR b  5504                                                      
REMARK 465     ARG b  5505                                                      
REMARK 465     ARG b  5506                                                      
REMARK 465     LYS b  5507                                                      
REMARK 465     GLU b  5508                                                      
REMARK 465     ALA b  5509                                                      
REMARK 465     VAL b  5510                                                      
REMARK 465     MET c  5001                                                      
REMARK 465     LYS c  5002                                                      
REMARK 465     THR c  5003                                                      
REMARK 465     LEU c  5004                                                      
REMARK 465     SER c  5005                                                      
REMARK 465     SER c  5006                                                      
REMARK 465     GLN c  5007                                                      
REMARK 465     LYS c  5008                                                      
REMARK 465     ARG c  5009                                                      
REMARK 465     TYR c  5010                                                      
REMARK 465     SER c  5011                                                      
REMARK 465     PRO c  5012                                                      
REMARK 465     VAL c  5013                                                      
REMARK 465     VAL c  5014                                                      
REMARK 465     THR c  5015                                                      
REMARK 465     LEU c  5016                                                      
REMARK 465     SER c  5017                                                      
REMARK 465     SER c  5018                                                      
REMARK 465     ASN c  5019                                                      
REMARK 465     SER c  5020                                                      
REMARK 465     ILE c  5021                                                      
REMARK 465     PHE c  5022                                                      
REMARK 465     ALA c  5023                                                      
REMARK 465     THR c  5024                                                      
REMARK 465     ASN c  5025                                                      
REMARK 465     ARG c  5026                                                      
REMARK 465     MET d  5001                                                      
REMARK 465     THR d  5002                                                      
REMARK 465     ILE d  5003                                                      
REMARK 465     ALA d  5004                                                      
REMARK 465     ILE d  5005                                                      
REMARK 465     GLY d  5006                                                      
REMARK 465     ARG d  5007                                                      
REMARK 465     ALA d  5008                                                      
REMARK 465     PRO d  5009                                                      
REMARK 465     ALA d  5010                                                      
REMARK 465     GLU d  5011                                                      
REMARK 465     ARG d  5012                                                      
REMARK 465     MET e  5001                                                      
REMARK 465     ALA e  5002                                                      
REMARK 465     MET f  5001                                                      
REMARK 465     THR f  5002                                                      
REMARK 465     SER f  5003                                                      
REMARK 465     ASN f  5004                                                      
REMARK 465     THR f  5005                                                      
REMARK 465     PRO f  5006                                                      
REMARK 465     ASN f  5007                                                      
REMARK 465     GLN f  5008                                                      
REMARK 465     GLU f  5009                                                      
REMARK 465     PRO f  5010                                                      
REMARK 465     MET h  5001                                                      
REMARK 465     GLY h  5066                                                      
REMARK 465     ASP i  5036                                                      
REMARK 465     LEU i  5037                                                      
REMARK 465     GLU i  5038                                                      
REMARK 465     MET j  5001                                                      
REMARK 465     MET j  5002                                                      
REMARK 465     SER j  5003                                                      
REMARK 465     GLU j  5004                                                      
REMARK 465     GLY j  5005                                                      
REMARK 465     GLY j  5006                                                      
REMARK 465     ALA o  5026                                                      
REMARK 465     ALA o  5027                                                      
REMARK 465     LYS o  5028                                                      
REMARK 465     GLN o  5029                                                      
REMARK 465     ALA o  5272                                                      
REMARK 465     LYS t  5031                                                      
REMARK 465     LYS t  5032                                                      
REMARK 465     ALA u  5031                                                      
REMARK 465     THR u  5032                                                      
REMARK 465     ALA u  5033                                                      
REMARK 465     SER u  5034                                                      
REMARK 465     THR u  5035                                                      
REMARK 465     GLU u  5036                                                      
REMARK 465     UNK x  5032                                                      
REMARK 465     UNK x  5033                                                      
REMARK 465     UNK x  5034                                                      
REMARK 465     UNK x  5035                                                      
REMARK 465     UNK x  5036                                                      
REMARK 465     UNK x  5037                                                      
REMARK 465     UNK x  5038                                                      
REMARK 465     UNK x  5039                                                      
REMARK 465     UNK x  5040                                                      
REMARK 465     UNK x  5041                                                      
REMARK 465     UNK x  5042                                                      
REMARK 465     UNK x  5043                                                      
REMARK 465     UNK x  5044                                                      
REMARK 465     UNK x  5045                                                      
REMARK 465     UNK x  5046                                                      
REMARK 465     UNK x  5047                                                      
REMARK 465     UNK x  5048                                                      
REMARK 465     UNK x  5049                                                      
REMARK 465     UNK x  5093                                                      
REMARK 465     UNK x  5094                                                      
REMARK 465     UNK x  5095                                                      
REMARK 465     UNK x  5096                                                      
REMARK 465     UNK x  5097                                                      
REMARK 465     UNK x  5098                                                      
REMARK 465     UNK x  5099                                                      
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     SER A  10    OG                                                  
REMARK 470     GLU A 229    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 127    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 224    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B 297    OG1  CG2                                            
REMARK 470     ILE B 482    CG1  CG2  CD1                                       
REMARK 470     ASP B 483    CG   OD1  OD2                                       
REMARK 470     GLU B 485    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 486    CG   CD1  CD2                                       
REMARK 470     SER B 487    OG                                                  
REMARK 470     PRO B 488    CG   CD                                             
REMARK 470     GLU B 489    CG   CD   OE1  OE2                                  
REMARK 470     GLN C  28    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 104    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 135    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 141    CG   CD   OE1  OE2                                  
REMARK 470     TYR C 143    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER C 144    OG                                                  
REMARK 470     LYS C 156    CG   CD   CE   NZ                                   
REMARK 470     GLU C 462    CG   CD   OE1  OE2                                  
REMARK 470     ARG D  24    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN D 239    CG   CD   OE1  NE2                                  
REMARK 470     ARG E   8    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP E  12    CG   OD1  OD2                                       
REMARK 470     ARG E  61    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E  84    CG   CD   CE   NZ                                   
REMARK 470     SER F  12    OG                                                  
REMARK 470     ILE F  15    CG1  CG2  CD1                                       
REMARK 470     ARG H   4    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS H  20    CG   CD   CE   NZ                                   
REMARK 470     SER H  61    OG                                                  
REMARK 470     LEU H  65    CG   CD1  CD2                                       
REMARK 470     ARG J   7    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU J  10    CG   CD1  CD2                                       
REMARK 470     LYS K  10    CG   CD   CE   NZ                                   
REMARK 470     MET L   1    CG   SD   CE                                        
REMARK 470     LYS M  34    CG   CD   CE   NZ                                   
REMARK 470     LEU O  31    CG   CD1  CD2                                       
REMARK 470     ASP O  49    CG   OD1  OD2                                       
REMARK 470     ARG O  53    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE O  58    CG1  CG2  CD1                                       
REMARK 470     SER O  61    OG                                                  
REMARK 470     GLN O  62    CG   CD   OE1  NE2                                  
REMARK 470     LYS O  79    CG   CD   CE   NZ                                   
REMARK 470     GLU O  80    CG   CD   OE1  OE2                                  
REMARK 470     LYS O  83    CG   CD   CE   NZ                                   
REMARK 470     ASN O  84    CG   OD1  ND2                                       
REMARK 470     LYS O  85    CG   CD   CE   NZ                                   
REMARK 470     ARG O  86    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN O  87    CG   CD   OE1  NE2                                  
REMARK 470     GLU O  88    CG   CD   OE1  OE2                                  
REMARK 470     GLU O  90    CG   CD   OE1  OE2                                  
REMARK 470     LYS O  95    CG   CD   CE   NZ                                   
REMARK 470     GLU O 124    CG   CD   OE1  OE2                                  
REMARK 470     VAL O 159    CG1  CG2                                            
REMARK 470     SER O 161    OG                                                  
REMARK 470     SER O 165    OG                                                  
REMARK 470     GLN O 222    CG   CD   OE1  NE2                                  
REMARK 470     ASN O 226    CG   OD1  ND2                                       
REMARK 470     LYS O 229    CG   CD   CE   NZ                                   
REMARK 470     ARG O 233    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER O 247    OG                                                  
REMARK 470     THR T  30    OG1  CG2                                            
REMARK 470     GLU U  37    CG   CD   OE1  OE2                                  
REMARK 470     GLU U  99    CG   CD   OE1  OE2                                  
REMARK 470     GLN Z  31    CG   CD   OE1  NE2                                  
REMARK 470     ASP Z  32    CG   OD1  OD2                                       
REMARK 470     TRP Z  33    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP Z  33    CZ3  CH2                                            
REMARK 470     ASP Z  34    CG   OD1  OD2                                       
REMARK 470     ARG Z  35    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER Z  36    OG                                                  
REMARK 470     LYS Z  37    CG   CD   CE   NZ                                   
REMARK 470     GLN Z  38    CG   CD   OE1  NE2                                  
REMARK 470     VAL Z  62    CG1  CG2                                            
REMARK 470     SER a5010    OG                                                  
REMARK 470     GLU a5229    CG   CD   OE1  OE2                                  
REMARK 470     ARG b5127    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG b5224    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR b5297    OG1  CG2                                            
REMARK 470     ILE b5482    CG1  CG2  CD1                                       
REMARK 470     ASP b5483    CG   OD1  OD2                                       
REMARK 470     GLU b5485    CG   CD   OE1  OE2                                  
REMARK 470     LEU b5486    CG   CD1  CD2                                       
REMARK 470     SER b5487    OG                                                  
REMARK 470     PRO b5488    CG   CD                                             
REMARK 470     GLU b5489    CG   CD   OE1  OE2                                  
REMARK 470     GLN c5028    CG   CD   OE1  NE2                                  
REMARK 470     GLU c5104    CG   CD   OE1  OE2                                  
REMARK 470     ARG c5135    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU c5141    CG   CD   OE1  OE2                                  
REMARK 470     TYR c5143    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER c5144    OG                                                  
REMARK 470     LYS c5156    CG   CD   CE   NZ                                   
REMARK 470     GLU c5462    CG   CD   OE1  OE2                                  
REMARK 470     ARG d5024    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN d5239    CG   CD   OE1  NE2                                  
REMARK 470     ARG e5008    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP e5012    CG   OD1  OD2                                       
REMARK 470     ARG e5061    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS e5084    CG   CD   CE   NZ                                   
REMARK 470     SER f5012    OG                                                  
REMARK 470     ILE f5015    CG1  CG2  CD1                                       
REMARK 470     ARG h5004    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS h5020    CG   CD   CE   NZ                                   
REMARK 470     SER h5061    OG                                                  
REMARK 470     LEU h5065    CG   CD1  CD2                                       
REMARK 470     ARG j5007    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU j5010    CG   CD1  CD2                                       
REMARK 470     LYS k5010    CG   CD   CE   NZ                                   
REMARK 470     MET l5001    CG   SD   CE                                        
REMARK 470     LYS m5034    CG   CD   CE   NZ                                   
REMARK 470     LEU o5031    CG   CD1  CD2                                       
REMARK 470     ASP o5049    CG   OD1  OD2                                       
REMARK 470     ARG o5053    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE o5058    CG1  CG2  CD1                                       
REMARK 470     SER o5061    OG                                                  
REMARK 470     GLN o5062    CG   CD   OE1  NE2                                  
REMARK 470     LYS o5079    CG   CD   CE   NZ                                   
REMARK 470     GLU o5080    CG   CD   OE1  OE2                                  
REMARK 470     LYS o5083    CG   CD   CE   NZ                                   
REMARK 470     ASN o5084    CG   OD1  ND2                                       
REMARK 470     LYS o5085    CG   CD   CE   NZ                                   
REMARK 470     ARG o5086    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN o5087    CG   CD   OE1  NE2                                  
REMARK 470     GLU o5088    CG   CD   OE1  OE2                                  
REMARK 470     GLU o5090    CG   CD   OE1  OE2                                  
REMARK 470     LYS o5095    CG   CD   CE   NZ                                   
REMARK 470     GLU o5124    CG   CD   OE1  OE2                                  
REMARK 470     VAL o5159    CG1  CG2                                            
REMARK 470     SER o5161    OG                                                  
REMARK 470     SER o5165    OG                                                  
REMARK 470     GLN o5222    CG   CD   OE1  NE2                                  
REMARK 470     ASN o5226    CG   OD1  ND2                                       
REMARK 470     LYS o5229    CG   CD   CE   NZ                                   
REMARK 470     ARG o5233    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER o5247    OG                                                  
REMARK 470     THR t5030    OG1  CG2                                            
REMARK 470     GLU u5037    CG   CD   OE1  OE2                                  
REMARK 470     GLU u5099    CG   CD   OE1  OE2                                  
REMARK 470     GLN z5031    CG   CD   OE1  NE2                                  
REMARK 470     ASP z5032    CG   OD1  OD2                                       
REMARK 470     TRP z5033    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP z5033    CZ3  CH2                                            
REMARK 470     ASP z5034    CG   OD1  OD2                                       
REMARK 470     ARG z5035    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER z5036    OG                                                  
REMARK 470     LYS z5037    CG   CD   CE   NZ                                   
REMARK 470     GLN z5038    CG   CD   OE1  NE2                                  
REMARK 470     VAL z5062    CG1  CG2                                            
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   O    GLY v  5159     N    VAL v  5161              2.08            
REMARK 500   O    GLY V   159     N    VAL V   161              2.08            
REMARK 500   OE1  GLN M    28     OXT  SER m  5036              2.16            
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 C 298   C   -  N   -  CA  ANGL. DEV. =  10.7 DEGREES          
REMARK 500    PRO O  46   C   -  N   -  CA  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    PRO O 271   CA  -  C   -  O   ANGL. DEV. =  17.2 DEGREES          
REMARK 500    PRO U  73   C   -  N   -  CD  ANGL. DEV. = -14.7 DEGREES          
REMARK 500    PRO a5340   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    PRO c5298   C   -  N   -  CA  ANGL. DEV. =  11.4 DEGREES          
REMARK 500    PRO o5046   C   -  N   -  CA  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    PRO u5073   C   -  N   -  CD  ANGL. DEV. = -13.8 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    ALA A  11       42.02    172.21                                   
REMARK 500    ASN A  12      105.68     52.02                                   
REMARK 500    ARG A  27      -56.19    -25.32                                   
REMARK 500    ALA A  55      120.50    165.27                                   
REMARK 500    ASP A  59       72.97    -63.13                                   
REMARK 500    ASP A  61     -175.90    -64.95                                   
REMARK 500    ILE A  63     -149.17    -52.67                                   
REMARK 500    GLU A  65       75.46   -119.27                                   
REMARK 500    LEU A  72        1.28    -61.67                                   
REMARK 500    TYR A  94       75.76   -109.99                                   
REMARK 500    GLN A 130       18.35    -63.28                                   
REMARK 500    TRP A 131      -53.08   -128.97                                   
REMARK 500    PRO A 141     -108.12    -69.78                                   
REMARK 500    TRP A 142      -12.48     26.64                                   
REMARK 500    MET A 172      123.60    -21.70                                   
REMARK 500    SER A 217      -76.26    -61.04                                   
REMARK 500    GLU A 226       27.59   -147.68                                   
REMARK 500    THR A 230       55.90   -104.15                                   
REMARK 500    GLU A 231      132.99   -177.34                                   
REMARK 500    SER A 232      144.46    -34.28                                   
REMARK 500    GLU A 242      -79.40    -44.17                                   
REMARK 500    ILE A 259      -70.21   -103.20                                   
REMARK 500    PHE A 260      133.89    173.50                                   
REMARK 500    GLN A 261      -69.19    -17.84                                   
REMARK 500    ALA A 263       34.15    -90.73                                   
REMARK 500    ASN A 266       -4.24   -174.08                                   
REMARK 500    SER A 305     -151.78    -97.82                                   
REMARK 500    VAL A 306       65.97     23.62                                   
REMARK 500    ASN A 315      125.34     54.46                                   
REMARK 500    LEU A 343       40.69   -102.94                                   
REMARK 500    VAL B  11       10.76    -57.49                                   
REMARK 500    ILE B  13       -8.87    -59.74                                   
REMARK 500    ASN B  14       43.12   -152.03                                   
REMARK 500    PRO B  16      -23.91    -35.38                                   
REMARK 500    THR B  44       -5.29   -140.53                                   
REMARK 500    ASP B  87       93.37   -162.11                                   
REMARK 500    TRP B  91       67.63    -64.76                                   
REMARK 500    ALA B 132      148.93   -171.58                                   
REMARK 500    HIS B 157      -80.83    -72.93                                   
REMARK 500    PHE B 162       81.07   -154.90                                   
REMARK 500    ALA B 228      -78.40    -42.10                                   
REMARK 500    ARG B 230       59.77      4.50                                   
REMARK 500    MET B 231     -174.39    -57.52                                   
REMARK 500    GLU B 235        9.22    -66.27                                   
REMARK 500    SER B 260      135.13    144.70                                   
REMARK 500    THR B 297      151.93    -49.63                                   
REMARK 500    ASP B 313       41.49    -89.95                                   
REMARK 500    ALA B 361      101.54    -54.34                                   
REMARK 500    PHE B 362      -40.27    168.56                                   
REMARK 500    ASP B 372     -158.46    -75.72                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     588 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 B 273         0.07    SIDE CHAIN                              
REMARK 500    TYR b5273         0.07    SIDE CHAIN                              
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     CLA A  563                                                       
REMARK 610     PQ9 A  564                                                       
REMARK 610     LHG A  567                                                       
REMARK 610     SQD A 5212                                                       
REMARK 610     CLA B  511                                                       
REMARK 610     CLA B  524                                                       
REMARK 610     CLA C  492                                                       
REMARK 610     CLA C  494                                                       
REMARK 610     CLA C  499                                                       
REMARK 610     CLA C  502                                                       
REMARK 610     CLA C  503                                                       
REMARK 610     DGD C  507                                                       
REMARK 610     DGD C  508                                                       
REMARK 610     DGD C  509                                                       
REMARK 610     CLA D  355                                                       
REMARK 610     PQ9 D  356                                                       
REMARK 610     MGE D  358                                                       
REMARK 610     MGE D  359                                                       
REMARK 610     DGD H  208                                                       
REMARK 610     SQD L 5213                                                       
REMARK 610     SQD a  212                                                       
REMARK 610     CLA a 5563                                                       
REMARK 610     PQ9 a 5564                                                       
REMARK 610     LHG a 5567                                                       
REMARK 610     CLA b 5511                                                       
REMARK 610     CLA b 5524                                                       
REMARK 610     CLA c 5492                                                       
REMARK 610     CLA c 5494                                                       
REMARK 610     CLA c 5499                                                       
REMARK 610     CLA c 5502                                                       
REMARK 610     CLA c 5503                                                       
REMARK 610     DGD c 5507                                                       
REMARK 610     DGD c 5508                                                       
REMARK 610     DGD c 5509                                                       
REMARK 610     CLA d 5355                                                       
REMARK 610     PQ9 d 5356                                                       
REMARK 610     MGE d 5359                                                       
REMARK 610     MGE d 5360                                                       
REMARK 610     DGD h 5208                                                       
REMARK 610     SQD t  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                             HEM F  51  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  23   NE2                                                    
REMARK 620 2 HEM F  51   NA   87.1                                              
REMARK 620 3 HEM F  51   NB   92.1  88.2                                        
REMARK 620 4 HEM F  51   NC   94.0 177.5  89.6                                  
REMARK 620 5 HEM F  51   ND   91.3  90.4 176.3  91.8                            
REMARK 620 6 HIS F  24   NE2 157.6  75.9  73.2 102.5 103.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM V 552  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS V  67   NE2                                                    
REMARK 620 2 HEM V 552   NA   88.9                                              
REMARK 620 3 HEM V 552   NB   81.9  89.8                                        
REMARK 620 4 HEM V 552   NC   93.5 176.8  88.5                                  
REMARK 620 5 HEM V 552   ND  102.2  92.0 175.6  89.5                            
REMARK 620 6 HIS V 118   NE2 163.5  85.3  82.7  91.7  93.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 A 557  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 215   NE2                                                    
REMARK 620 2 HIS A 272   NE2  95.9                                              
REMARK 620 3 HIS D 214   NE2 114.4  92.0                                        
REMARK 620 4 HIS D 268   NE2  88.2 166.0  98.5                                  
REMARK 620 5 BCT D 353   O3  155.3  91.2  88.9  79.9                            
REMARK 620 6 BCT D 353   O2   98.7  80.5 146.8  85.7  59.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM f5051  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS e5023   NE2                                                    
REMARK 620 2 HEM f5051   NA   85.5                                              
REMARK 620 3 HEM f5051   NB   91.0  87.3                                        
REMARK 620 4 HEM f5051   NC   92.8 177.2  90.6                                  
REMARK 620 5 HEM f5051   ND   89.2  90.6 177.8  91.6                            
REMARK 620 6 HIS f5024   NE2 156.3  75.9  73.8 105.2 105.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM v5552  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS v5067   NE2                                                    
REMARK 620 2 HEM v5552   NA   88.3                                              
REMARK 620 3 HEM v5552   NB   80.7  89.9                                        
REMARK 620 4 HEM v5552   NC   93.8 177.0  88.4                                  
REMARK 620 5 HEM v5552   ND  102.4  92.0 176.4  89.6                            
REMARK 620 6 HIS v5118   NE2 161.5  83.1  82.9  94.3  94.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 a5557  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS a5215   NE2                                                    
REMARK 620 2 HIS a5272   NE2  95.8                                              
REMARK 620 3 HIS d5214   NE2 113.3  93.6                                        
REMARK 620 4 HIS d5268   NE2  86.8 165.0  98.9                                  
REMARK 620 5 BCT d5353   O3  155.9  88.9  89.9  83.0                            
REMARK 620 6 BCT d5353   O2   98.3  78.8 148.1  86.2  59.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC A 565  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 189   OE1                                                    
REMARK 620 2 ALA A 344   O   136.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC A 565  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 189   OE2                                                    
REMARK 620 2 ASP A 342   OD2  82.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A 558  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 198   NE2                                                    
REMARK 620 2 CLA A 558   NA   88.3                                              
REMARK 620 3 CLA A 558   NB  109.7  90.0                                        
REMARK 620 4 CLA A 558   NC  108.8 161.9  89.5                                  
REMARK 620 5 CLA A 558   ND   87.6  88.5 162.6  86.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC A 565  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 333   OE1                                                    
REMARK 620 2 GLU C 354   OE2  95.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC A 565  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 342   OD1                                                    
REMARK 620 2 ALA A 344   OXT 107.0                                              
REMARK 620 3 GLU C 354   OE1  86.1  66.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 524  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B   9   NE2                                                    
REMARK 620 2 CLA B 524   NA   90.0                                              
REMARK 620 3 CLA B 524   NB   84.3  88.8                                        
REMARK 620 4 CLA B 524   NC  106.7 163.0  89.5                                  
REMARK 620 5 CLA B 524   ND  113.2  89.0 162.4  87.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 512  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 201   ND1                                                    
REMARK 620 2 CLA B 512   NA   99.3                                              
REMARK 620 3 CLA B 512   NB   99.8  89.7                                        
REMARK 620 4 CLA B 512   NC   97.8 162.9  88.1                                  
REMARK 620 5 CLA B 512   ND   97.7  90.0 162.3  87.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 513  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 202   NE2                                                    
REMARK 620 2 CLA B 513   NA   87.1                                              
REMARK 620 3 CLA B 513   NB  100.9  90.9                                        
REMARK 620 4 CLA B 513   NC  110.5 162.2  88.2                                  
REMARK 620 5 CLA B 513   ND   96.6  88.3 162.4  87.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 514  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 455   NE2                                                    
REMARK 620 2 CLA B 514   NA  101.3                                              
REMARK 620 3 CLA B 514   NB  108.4  89.6                                        
REMARK 620 4 CLA B 514   NC   96.7 161.4  89.2                                  
REMARK 620 5 CLA B 514   ND   89.3  89.3 162.1  86.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 518  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 466   NE2                                                    
REMARK 620 2 CLA B 518   NA   95.4                                              
REMARK 620 3 CLA B 518   NB  111.8  89.5                                        
REMARK 620 4 CLA B 518   NC  100.8 162.9  89.3                                  
REMARK 620 5 CLA B 518   ND   85.1  88.8 163.1  87.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 521  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 469   NE2                                                    
REMARK 620 2 CLA B 521   NA   82.9                                              
REMARK 620 3 CLA B 521   NB  102.1  90.5                                        
REMARK 620 4 CLA B 521   NC  114.2 162.7  88.5                                  
REMARK 620 5 CLA B 521   ND   94.8  88.9 162.9  87.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C  39   OD1                                                    
REMARK 620 2 CLA C 501   NA  108.8                                              
REMARK 620 3 CLA C 501   NB   92.9  90.1                                        
REMARK 620 4 CLA C 501   NC   87.7 163.5  89.1                                  
REMARK 620 5 CLA C 501   ND  102.9  89.1 163.6  87.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 493  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 118   NE2                                                    
REMARK 620 2 CLA C 493   NA   99.5                                              
REMARK 620 3 CLA C 493   NB  104.1  90.8                                        
REMARK 620 4 CLA C 493   NC   97.6 162.4  88.5                                  
REMARK 620 5 CLA C 493   ND   92.1  89.1 163.6  86.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 503  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 132   NE2                                                    
REMARK 620 2 CLA C 503   NA   83.0                                              
REMARK 620 3 CLA C 503   NB  107.9  89.7                                        
REMARK 620 4 CLA C 503   NC  113.4 162.9  89.6                                  
REMARK 620 5 CLA C 503   ND   89.4  88.6 162.3  86.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 491  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 237   NE2                                                    
REMARK 620 2 CLA C 491   NA  101.6                                              
REMARK 620 3 CLA C 491   NB  101.7  90.2                                        
REMARK 620 4 CLA C 491   NC   94.4 163.8  88.8                                  
REMARK 620 5 CLA C 491   ND   94.1  90.1 163.8  86.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 496  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 251   NE2                                                    
REMARK 620 2 CLA C 496   NA  100.1                                              
REMARK 620 3 CLA C 496   NB   84.5  89.8                                        
REMARK 620 4 CLA C 496   NC   97.5 162.0  88.1                                  
REMARK 620 5 CLA C 496   ND  113.8  88.7 161.6  87.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 492  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 430   NE2                                                    
REMARK 620 2 CLA C 492   NA   84.2                                              
REMARK 620 3 CLA C 492   NB  114.5  89.4                                        
REMARK 620 4 CLA C 492   NC  110.2 164.8  88.9                                  
REMARK 620 5 CLA C 492   ND   81.5  91.2 164.0  86.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 498  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 444   NE2                                                    
REMARK 620 2 CLA C 498   NA   85.6                                              
REMARK 620 3 CLA C 498   NB   96.6  88.1                                        
REMARK 620 4 CLA C 498   NC  112.0 162.4  89.9                                  
REMARK 620 5 CLA C 498   ND  101.4  89.9 161.7  86.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA D 354  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 197   NE2                                                    
REMARK 620 2 CLA D 354   NA  108.3                                              
REMARK 620 3 CLA D 354   NB   97.2  90.2                                        
REMARK 620 4 CLA D 354   NC   90.1 161.5  88.5                                  
REMARK 620 5 CLA D 354   ND  101.6  89.2 160.4  85.9                            
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   OD1                                                    
REMARK 620 2 ASP K  23   OD2  62.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC a5565  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a5189   OE1                                                    
REMARK 620 2 ALA a5344   O   130.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC a5565  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a5189   OE2                                                    
REMARK 620 2 ASP a5342   OD2  77.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA a5558  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS a5198   NE2                                                    
REMARK 620 2 CLA a5558   NA   89.6                                              
REMARK 620 3 CLA a5558   NB  110.6  89.5                                        
REMARK 620 4 CLA a5558   NC  107.5 162.1  89.3                                  
REMARK 620 5 CLA a5558   ND   86.6  89.3 162.8  86.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC a5565  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a5333   OE1                                                    
REMARK 620 2 GLU c5354   OE2  98.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC a5565  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a5342   OD1                                                    
REMARK 620 2 ALA a5344   OXT 110.6                                              
REMARK 620 3 GLU c5354   OE1  88.9  69.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b5524  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS b5009   NE2                                                    
REMARK 620 2 CLA b5524   NA   92.6                                              
REMARK 620 3 CLA b5524   NB   84.9  89.0                                        
REMARK 620 4 CLA b5524   NC  104.8 162.2  88.9                                  
REMARK 620 5 CLA b5524   ND  112.5  89.4 162.6  87.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b5512  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS b5201   ND1                                                    
REMARK 620 2 CLA b5512   NA   98.6                                              
REMARK 620 3 CLA b5512   NB   99.9  90.7                                        
REMARK 620 4 CLA b5512   NC   98.3 163.0  88.3                                  
REMARK 620 5 CLA b5512   ND   97.6  89.4 162.3  86.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b5513  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS b5202   NE2                                                    
REMARK 620 2 CLA b5513   NA   88.7                                              
REMARK 620 3 CLA b5513   NB   99.9  90.9                                        
REMARK 620 4 CLA b5513   NC  108.3 162.8  88.1                                  
REMARK 620 5 CLA b5513   ND   96.7  88.6 163.3  87.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b5514  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS b5455   NE2                                                    
REMARK 620 2 CLA b5514   NA  100.5                                              
REMARK 620 3 CLA b5514   NB  108.4  89.2                                        
REMARK 620 4 CLA b5514   NC   97.5 161.5  89.2                                  
REMARK 620 5 CLA b5514   ND   89.4  89.6 162.1  86.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b5518  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS b5466   NE2                                                    
REMARK 620 2 CLA b5518   NA   94.6                                              
REMARK 620 3 CLA b5518   NB  112.3  89.2                                        
REMARK 620 4 CLA b5518   NC  101.5 162.9  89.8                                  
REMARK 620 5 CLA b5518   ND   84.2  89.0 163.5  87.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b5521  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS b5469   NE2                                                    
REMARK 620 2 CLA b5521   NA   83.1                                              
REMARK 620 3 CLA b5521   NB  101.2  89.7                                        
REMARK 620 4 CLA b5521   NC  113.3 163.6  88.1                                  
REMARK 620 5 CLA b5521   ND   95.0  90.8 163.7  86.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c5501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN c5039   OD1                                                    
REMARK 620 2 CLA c5501   NA  109.7                                              
REMARK 620 3 CLA c5501   NB   94.9  89.6                                        
REMARK 620 4 CLA c5501   NC   87.1 163.2  89.0                                  
REMARK 620 5 CLA c5501   ND  101.3  89.8 163.0  86.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c5493  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS c5118   NE2                                                    
REMARK 620 2 CLA c5493   NA   99.5                                              
REMARK 620 3 CLA c5493   NB  104.5  90.7                                        
REMARK 620 4 CLA c5493   NC   97.9 162.3  88.6                                  
REMARK 620 5 CLA c5493   ND   92.0  89.1 163.3  86.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c5503  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS c5132   NE2                                                    
REMARK 620 2 CLA c5503   NA   82.8                                              
REMARK 620 3 CLA c5503   NB  107.0  90.5                                        
REMARK 620 4 CLA c5503   NC  112.8 163.7  89.1                                  
REMARK 620 5 CLA c5503   ND   89.4  88.1 163.3  87.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c5491  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS c5237   NE2                                                    
REMARK 620 2 CLA c5491   NA  100.5                                              
REMARK 620 3 CLA c5491   NB  104.4  89.3                                        
REMARK 620 4 CLA c5491   NC   96.9 162.3  89.2                                  
REMARK 620 5 CLA c5491   ND   92.7  89.0 162.8  87.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c5492  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS c5430   NE2                                                    
REMARK 620 2 CLA c5492   NA   85.1                                              
REMARK 620 3 CLA c5492   NB  114.9  89.4                                        
REMARK 620 4 CLA c5492   NC  109.4 164.5  89.2                                  
REMARK 620 5 CLA c5492   ND   80.9  91.1 164.2  86.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c5498  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS c5444   NE2                                                    
REMARK 620 2 CLA c5498   NA   85.7                                              
REMARK 620 3 CLA c5498   NB   96.1  88.1                                        
REMARK 620 4 CLA c5498   NC  112.4 161.9  89.6                                  
REMARK 620 5 CLA c5498   ND  102.1  89.5 161.4  87.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA d5354  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS d5197   NE2                                                    
REMARK 620 2 CLA d5354   NA  107.1                                              
REMARK 620 3 CLA d5354   NB   96.7  90.1                                        
REMARK 620 4 CLA d5354   NC   89.8 163.1  88.9                                  
REMARK 620 5 CLA d5354   ND  101.0  89.2 161.6  86.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA k5056  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP k5019   OD1                                                    
REMARK 620 2 ASP k5019   OD2  49.3                                              
REMARK 620 3 ASP k5023   OD2  66.2  68.6                                        
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 CA K 56                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 557                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT D 353                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA k 5056                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 a 5557                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT d 5353                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 558                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA D 354                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 559                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 560                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO A 561                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO A 562                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 563                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA D 355                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 522                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 523                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 524                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 525                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 526                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 491                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 492                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 493                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 494                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 495                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 496                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 497                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 498                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM F 51                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM V 552                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PQ9 D 356                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PQ9 A 564                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OEC A 565                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR A 566                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 527                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR t 104                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 528                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 529                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR H 107                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR D 357                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR X 130                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR C 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE I 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG A 567                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD A 568                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE D 358                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD H 208                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE D 359                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE L 210                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE D 360                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD a 212                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD t 213                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE B 530                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT A 569                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT m 216                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT T 217                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 5558                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA d 5354                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 5559                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 5560                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO a 5561                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO a 5562                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 5563                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA d 5355                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5511                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5512                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5513                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5514                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5515                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5516                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5517                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5518                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5519                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5520                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5521                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5522                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5523                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5524                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5525                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 5526                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5491                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5492                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5493                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5494                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5495                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5496                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5497                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5498                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5499                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5500                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5502                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 5503                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM f 5051                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM v 5552                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PQ9 d 5356                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PQ9 a 5564                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OEC a 5565                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR a 5566                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR b 5527                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR T 5104                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR b 5528                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR b 5529                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR h 5107                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR d 5357                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR x 5130                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR c 5504                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR c 5505                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR c 5506                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE i 5201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD c 5507                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG a 5567                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD d 5358                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD c 5508                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD c 5509                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE d 5359                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD h 5208                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE d 5360                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE l 5210                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE d 5361                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD A 5212                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD L 5213                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGE b 5530                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT a 5568                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT M 5216                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT t 5217                
DBREF  2AXT A    1   344  UNP    P0A445   PSBA1_SYNEN      1    344             
DBREF  2AXT B    1   510  GB     11761354 BAB19261         1    510             
DBREF  2AXT C    1   473  GB     22295356 BAC09183         1    473             
DBREF  2AXT D    1   352  GB     22295355 BAC09182         1    352             
DBREF  2AXT E    1    84  UNP    Q8DIP0   PSBE_SYNEL       0     83             
DBREF  2AXT F    1    45  UNP    Q8DIN9   PSBF_SYNEL       1     45             
DBREF  2AXT H    1    66  UNP    Q8DJ43   PSBH_SYNEL       1     66             
DBREF  2AXT I    1    38  UNP    Q8DJZ6   PSBI_SYNEL       1     38             
DBREF  2AXT J    1    40  UNP    P59087   PSBJ_SYNEL       1     40             
DBREF  2AXT K   10    46  UNP    Q9F1K9   PSBK_SYNEL      10     46             
DBREF  2AXT L    1    37  UNP    Q8DIN8   PSBL_SYNEL       1     37             
DBREF  2AXT M    1    36  UNP    Q8DHA7   PSBM_SYNEL       1     36             
DBREF  2AXT O   26   272  UNP    P0A431   PSBO_SYNEL      26    272             
DBREF  2AXT T    1    32  UNP    Q8DIQ0   PSBT_SYNEL       1     32             
DBREF  2AXT U   31   134  UNP    Q9F1L5   PSBU_SYNEL      31    134             
DBREF  2AXT V   27   163  UNP    P0A386   CY550_SYNEL     27    163             
DBREF  2AXT Z    1    62  UNP    Q8DHJ2   PSBZ_SYNEL       1     62             
DBREF  2AXT a 5001  5344  UNP    P0A445   PSBA1_SYNEN      1    344             
DBREF  2AXT b 5001  5510  GB     11761354 BAB19261         1    510             
DBREF  2AXT c 5001  5473  GB     22295356 BAC09183         1    473             
DBREF  2AXT d 5001  5352  GB     22295355 BAC09182         1    352             
DBREF  2AXT e 5001  5084  UNP    Q8DIP0   PSBE_SYNEL       0     83             
DBREF  2AXT f 5001  5045  UNP    Q8DIN9   PSBF_SYNEL       1     45             
DBREF  2AXT h 5001  5066  UNP    Q8DJ43   PSBH_SYNEL       1     66             
DBREF  2AXT i 5001  5038  UNP    Q8DJZ6   PSBI_SYNEL       1     38             
DBREF  2AXT j 5001  5040  UNP    P59087   PSBJ_SYNEL       1     40             
DBREF  2AXT k 5010  5046  UNP    Q9F1K9   PSBK_SYNEL      10     46             
DBREF  2AXT l 5001  5037  UNP    Q8DIN8   PSBL_SYNEL       1     37             
DBREF  2AXT m 5001  5036  UNP    Q8DHA7   PSBM_SYNEL       1     36             
DBREF  2AXT o 5026  5272  UNP    P0A431   PSBO_SYNEL      26    272             
DBREF  2AXT t 5001  5032  UNP    Q8DIQ0   PSBT_SYNEL       1     32             
DBREF  2AXT u 5031  5134  UNP    Q9F1L5   PSBU_SYNEL      31    134             
DBREF  2AXT v 5027  5163  UNP    P0A386   CY550_SYNEL     27    163             
DBREF  2AXT z 5001  5062  UNP    Q8DHJ2   PSBZ_SYNEL       1     62             
DBREF  2AXT X    1   129  PDB    2AXT     2AXT             1    129             
DBREF  2AXT x 5001  5129  PDB    2AXT     2AXT          5001   5129             
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  473  MET LYS THR LEU SER SER GLN LYS ARG TYR SER PRO VAL          
SEQRES   2 C  473  VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN ARG          
SEQRES   3 C  473  ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY ASN          
SEQRES   4 C  473  ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY ALA          
SEQRES   5 C  473  HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA GLY          
SEQRES   6 C  473  ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO GLU          
SEQRES   7 C  473  LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO HIS          
SEQRES   8 C  473  ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY GLU          
SEQRES   9 C  473  VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL VAL          
SEQRES  10 C  473  HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY VAL          
SEQRES  11 C  473  TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU TYR          
SEQRES  12 C  473  SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN LYS          
SEQRES  13 C  473  MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU GLY          
SEQRES  14 C  473  ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE PHE          
SEQRES  15 C  473  GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY ASP          
SEQRES  16 C  473  VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG VAL          
SEQRES  17 C  473  ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY GLU          
SEQRES  18 C  473  GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL VAL          
SEQRES  19 C  473  GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA GLY          
SEQRES  20 C  473  GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP ALA          
SEQRES  21 C  473  ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU SER          
SEQRES  22 C  473  TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE ALA          
SEQRES  23 C  473  THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO SER          
SEQRES  24 C  473  GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN ALA          
SEQRES  25 C  473  GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU GLY          
SEQRES  26 C  473  ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU GLY          
SEQRES  27 C  473  LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE PHE          
SEQRES  28 C  473  GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY PRO          
SEQRES  29 C  473  TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP LEU          
SEQRES  30 C  473  ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU ARG          
SEQRES  31 C  473  ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY SER          
SEQRES  32 C  473  LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN SER          
SEQRES  33 C  473  VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR SER          
SEQRES  34 C  473  HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS LEU          
SEQRES  35 C  473  TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY PHE          
SEQRES  36 C  473  GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU SER          
SEQRES  37 C  473  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   84  MET ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE          
SEQRES   2 E   84  ILE THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR          
SEQRES   3 E   84  ILE PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER          
SEQRES   4 E   84  THR GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO          
SEQRES   5 E   84  ASP SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU          
SEQRES   6 E   84  VAL THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR          
SEQRES   7 E   84  PHE LEU GLU GLN LEU LYS                                      
SEQRES   1 F   45  MET THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR          
SEQRES   2 F   45  PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU          
SEQRES   3 F   45  ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA          
SEQRES   4 F   45  MET GLN PHE ILE GLN ARG                                      
SEQRES   1 H   66  MET ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO          
SEQRES   2 H   66  LEU ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY          
SEQRES   3 H   66  THR THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU          
SEQRES   4 H   66  VAL PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR          
SEQRES   5 H   66  LEU ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU          
SEQRES   6 H   66  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  247  ALA ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY          
SEQRES   2 O  247  THR GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR          
SEQRES   3 O  247  ALA ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR          
SEQRES   4 O  247  ARG ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU          
SEQRES   5 O  247  VAL LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU          
SEQRES   6 O  247  PHE VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER          
SEQRES   7 O  247  LEU ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP          
SEQRES   8 O  247  GLY SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE          
SEQRES   9 O  247  GLN PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE          
SEQRES  10 O  247  PRO LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR          
SEQRES  11 O  247  GLN PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE          
SEQRES  12 O  247  LYS GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN          
SEQRES  13 O  247  PHE LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR          
SEQRES  14 O  247  ASP SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU          
SEQRES  15 O  247  LEU ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS          
SEQRES  16 O  247  GLY GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG          
SEQRES  17 O  247  THR GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU          
SEQRES  18 O  247  SER ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL          
SEQRES  19 O  247  LYS 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 X  129  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 X  129  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   3 X  129  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   4 X  129  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   5 X  129  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   6 X  129  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   7 X  129  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   8 X  129  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   9 X  129  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES  10 X  129  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK              
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                      
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  473  MET LYS THR LEU SER SER GLN LYS ARG TYR SER PRO VAL          
SEQRES   2 c  473  VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN ARG          
SEQRES   3 c  473  ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY ASN          
SEQRES   4 c  473  ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY ALA          
SEQRES   5 c  473  HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA GLY          
SEQRES   6 c  473  ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO GLU          
SEQRES   7 c  473  LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO HIS          
SEQRES   8 c  473  ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY GLU          
SEQRES   9 c  473  VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL VAL          
SEQRES  10 c  473  HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY VAL          
SEQRES  11 c  473  TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU TYR          
SEQRES  12 c  473  SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN LYS          
SEQRES  13 c  473  MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU GLY          
SEQRES  14 c  473  ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE PHE          
SEQRES  15 c  473  GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY ASP          
SEQRES  16 c  473  VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG VAL          
SEQRES  17 c  473  ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY GLU          
SEQRES  18 c  473  GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL VAL          
SEQRES  19 c  473  GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA GLY          
SEQRES  20 c  473  GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP ALA          
SEQRES  21 c  473  ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU SER          
SEQRES  22 c  473  TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE ALA          
SEQRES  23 c  473  THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO SER          
SEQRES  24 c  473  GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN ALA          
SEQRES  25 c  473  GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU GLY          
SEQRES  26 c  473  ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU GLY          
SEQRES  27 c  473  LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE PHE          
SEQRES  28 c  473  GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY PRO          
SEQRES  29 c  473  TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP LEU          
SEQRES  30 c  473  ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU ARG          
SEQRES  31 c  473  ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY SER          
SEQRES  32 c  473  LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN SER          
SEQRES  33 c  473  VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR SER          
SEQRES  34 c  473  HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS LEU          
SEQRES  35 c  473  TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY PHE          
SEQRES  36 c  473  GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU SER          
SEQRES  37 c  473  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   84  MET ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE          
SEQRES   2 e   84  ILE THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR          
SEQRES   3 e   84  ILE PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER          
SEQRES   4 e   84  THR GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO          
SEQRES   5 e   84  ASP SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU          
SEQRES   6 e   84  VAL THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR          
SEQRES   7 e   84  PHE LEU GLU GLN LEU LYS                                      
SEQRES   1 f   45  MET THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR          
SEQRES   2 f   45  PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU          
SEQRES   3 f   45  ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA          
SEQRES   4 f   45  MET GLN PHE ILE GLN ARG                                      
SEQRES   1 h   66  MET ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO          
SEQRES   2 h   66  LEU ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY          
SEQRES   3 h   66  THR THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU          
SEQRES   4 h   66  VAL PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR          
SEQRES   5 h   66  LEU ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU          
SEQRES   6 h   66  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  247  ALA ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY          
SEQRES   2 o  247  THR GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR          
SEQRES   3 o  247  ALA ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR          
SEQRES   4 o  247  ARG ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU          
SEQRES   5 o  247  VAL LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU          
SEQRES   6 o  247  PHE VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER          
SEQRES   7 o  247  LEU ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP          
SEQRES   8 o  247  GLY SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE          
SEQRES   9 o  247  GLN PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE          
SEQRES  10 o  247  PRO LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR          
SEQRES  11 o  247  GLN PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE          
SEQRES  12 o  247  LYS GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN          
SEQRES  13 o  247  PHE LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR          
SEQRES  14 o  247  ASP SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU          
SEQRES  15 o  247  LEU ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS          
SEQRES  16 o  247  GLY GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG          
SEQRES  17 o  247  THR GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU          
SEQRES  18 o  247  SER ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL          
SEQRES  19 o  247  LYS 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 x  129  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 x  129  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   3 x  129  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   4 x  129  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   5 x  129  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   6 x  129  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   7 x  129  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   8 x  129  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   9 x  129  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES  10 x  129  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK              
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 557       1                                                       
HET    CLA  A 558      65                                                       
HET    CLA  A 559      65                                                       
HET    CLA  A 560      65                                                       
HET    PHO  A 561      64                                                       
HET    PHO  A 562      64                                                       
HET    CLA  A 563      55                                                       
HET    PQ9  A 564      30                                                       
HET    OEC  A 565       5                                                       
HET    BCR  A 566      40                                                       
HET    LHG  A 567      39                                                       
HET    SQD  A 568      54                                                       
HET    LMT  A 569      35                                                       
HET    SQD  A5212      26                                                       
HET    CLA  B 511      41                                                       
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      56                                                       
HET    CLA  B 525      65                                                       
HET    CLA  B 526      65                                                       
HET    BCR  B 527      40                                                       
HET    BCR  B 528      40                                                       
HET    BCR  B 529      40                                                       
HET    MGE  B 530      48                                                       
HET    CLA  C 491      65                                                       
HET    CLA  C 492      60                                                       
HET    CLA  C 493      65                                                       
HET    CLA  C 494      46                                                       
HET    CLA  C 495      65                                                       
HET    CLA  C 496      65                                                       
HET    CLA  C 497      65                                                       
HET    CLA  C 498      65                                                       
HET    CLA  C 499      47                                                       
HET    CLA  C 500      65                                                       
HET    CLA  C 501      65                                                       
HET    CLA  C 502      51                                                       
HET    CLA  C 503      50                                                       
HET    BCR  C 504      40                                                       
HET    BCR  C 505      40                                                       
HET    BCR  C 506      40                                                       
HET    DGD  C 507      53                                                       
HET    DGD  C 508      47                                                       
HET    DGD  C 509      57                                                       
HET    BCT  D 353       4                                                       
HET    CLA  D 354      65                                                       
HET    CLA  D 355      50                                                       
HET    PQ9  D 356      30                                                       
HET    BCR  D 357      40                                                       
HET    MGE  D 358      47                                                       
HET    MGE  D 359      41                                                       
HET    MGE  D 360      48                                                       
HET    HEM  F  51      43                                                       
HET    BCR  H 107      40                                                       
HET    DGD  H 208      54                                                       
HET    MGE  I 201      48                                                       
HET     CA  K  56       1                                                       
HET    MGE  L 210      48                                                       
HET    SQD  L5213      47                                                       
HET    LMT  M5216      35                                                       
HET    LMT  T 217      35                                                       
HET    BCR  T5104      40                                                       
HET    HEM  V 552      43                                                       
HET    BCR  X 130      40                                                       
HET    FE2  a5557       1                                                       
HET    SQD  a 212      26                                                       
HET    CLA  a5558      65                                                       
HET    CLA  a5559      65                                                       
HET    CLA  a5560      65                                                       
HET    PHO  a5561      64                                                       
HET    PHO  a5562      64                                                       
HET    CLA  a5563      55                                                       
HET    PQ9  a5564      30                                                       
HET    OEC  a5565       5                                                       
HET    BCR  a5566      40                                                       
HET    LHG  a5567      39                                                       
HET    LMT  a5568      35                                                       
HET    CLA  b5511      41                                                       
HET    CLA  b5512      65                                                       
HET    CLA  b5513      65                                                       
HET    CLA  b5514      65                                                       
HET    CLA  b5515      65                                                       
HET    CLA  b5516      65                                                       
HET    CLA  b5517      65                                                       
HET    CLA  b5518      65                                                       
HET    CLA  b5519      65                                                       
HET    CLA  b5520      65                                                       
HET    CLA  b5521      65                                                       
HET    CLA  b5522      65                                                       
HET    CLA  b5523      65                                                       
HET    CLA  b5524      56                                                       
HET    CLA  b5525      65                                                       
HET    CLA  b5526      65                                                       
HET    BCR  b5527      40                                                       
HET    BCR  b5528      40                                                       
HET    BCR  b5529      40                                                       
HET    MGE  b5530      48                                                       
HET    CLA  c5491      65                                                       
HET    CLA  c5492      60                                                       
HET    CLA  c5493      65                                                       
HET    CLA  c5494      46                                                       
HET    CLA  c5495      65                                                       
HET    CLA  c5496      65                                                       
HET    CLA  c5497      65                                                       
HET    CLA  c5498      65                                                       
HET    CLA  c5499      47                                                       
HET    CLA  c5500      65                                                       
HET    CLA  c5501      65                                                       
HET    CLA  c5502      51                                                       
HET    CLA  c5503      50                                                       
HET    BCR  c5504      40                                                       
HET    BCR  c5505      40                                                       
HET    BCR  c5506      40                                                       
HET    DGD  c5507      53                                                       
HET    DGD  c5508      47                                                       
HET    DGD  c5509      57                                                       
HET    BCT  d5353       4                                                       
HET    CLA  d5354      65                                                       
HET    CLA  d5355      50                                                       
HET    PQ9  d5356      30                                                       
HET    BCR  d5357      40                                                       
HET    SQD  d5358      54                                                       
HET    MGE  d5359      47                                                       
HET    MGE  d5360      41                                                       
HET    MGE  d5361      48                                                       
HET    HEM  f5051      43                                                       
HET    BCR  h5107      40                                                       
HET    DGD  h5208      54                                                       
HET    MGE  i5201      48                                                       
HET     CA  k5056       1                                                       
HET    MGE  l5210      48                                                       
HET    LMT  m 216      35                                                       
HET    BCR  t 104      40                                                       
HET    SQD  t 213      47                                                       
HET    LMT  t5217      35                                                       
HET    HEM  v5552      43                                                       
HET    BCR  x5130      40                                                       
HETNAM     FE2 FE (II) ION                                                      
HETNAM     CLA CHLOROPHYLL A                                                    
HETNAM     PHO PHEOPHYTIN A                                                     
HETNAM     PQ9 5-[(2E,6E,10E,14E,18E,22E)-3,7,11,15,19,23,27-                   
HETNAM   2 PQ9  HEPTAMETHYLOCTACOSA-2,6,10,14,18,22,26-HEPTAENYL]-2,3-          
HETNAM   3 PQ9  DIMETHYLBENZO-1,4-QUINONE                                       
HETNAM     OEC OXYGEN EVOLVING SYSTEM                                           
HETNAM     BCR BETA-CAROTENE                                                    
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     LMT DODECYL-BETA-D-MALTOSIDE                                         
HETNAM     MGE (1S)-2-(ALPHA-L-ALLOPYRANOSYLOXY)-1-[(TRIDECANOYLOXY)            
HETNAM   2 MGE  METHYL]ETHYL PALMITATE                                          
HETNAM     DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)                              
HETNAM     BCT BICARBONATE ION                                                  
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM      CA CALCIUM ION                                                      
HETSYN     SQD SULFOQUINOVOSYLDIACYLGLYCEROL                                    
HETSYN     MGE MONOGALACTOSYL-DIACYLGLYCEROL                                    
HETSYN     HEM HEME                                                             
FORMUL  37  FE2    2(FE 2+)                                                     
FORMUL  38  CLA    70(C55 H72 MG N4 O5 2+)                                      
FORMUL  41  PHO    4(C55 H74 N4 O5)                                             
FORMUL  44  PQ9    4(C43 H64 O2)                                                
FORMUL  45  OEC    2(CA MN4 O4)                                                 
FORMUL  46  BCR    22(C40 H56)                                                  
FORMUL  47  LHG    2(C38 H75 O10 P)                                             
FORMUL  48  SQD    6(C41 H78 O12 S)                                             
FORMUL  49  LMT    6(C24 H46 O11)                                               
FORMUL  70  MGE    12(C38 H72 O10)                                              
FORMUL  04  DGD    8(C51 H96 O15)                                               
FORMUL  07  BCT    2(C H O3 1-)                                                 
FORMUL  15  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL  19   CA    2(CA 2+)                                                     
HELIX    1   1 ASN A   12  THR A   22  1                                  11    
HELIX    2   2 PHE A   33  ALA A   54  1                                  22    
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 GLY A  175  ASN A  191  1                                  17    
HELIX   11  11 ILE A  192  MET A  194  5                                   3    
HELIX   12  12 HIS A  195  SER A  222  1                                  28    
HELIX   13  13 ALA A  233  TYR A  237  5                                   5    
HELIX   14  14 ASN A  247  ILE A  259  1                                  13    
HELIX   15  15 ASN A  267  MET A  293  1                                  27    
HELIX   16  16 THR A  316  HIS A  332  1                                  17    
HELIX   17  17 PRO B    4  VAL B   11  5                                   8    
HELIX   18  18 ASP B   15  ALA B   43  1                                  29    
HELIX   19  19 PRO B   54  GLY B   59  5                                   6    
HELIX   20  20 VAL B   62  LEU B   69  1                                   8    
HELIX   21  21 SER B   92  TYR B  117  1                                  26    
HELIX   22  22 LEU B  120  ARG B  124  5                                   5    
HELIX   23  23 ASP B  134  HIS B  157  1                                  24    
HELIX   24  24 GLY B  186  ASN B  191  5                                   6    
HELIX   25  25 ASN B  194  VAL B  219  1                                  26    
HELIX   26  26 PRO B  222  LEU B  229  1                                   8    
HELIX   27  27 ILE B  234  TYR B  258  1                                  25    
HELIX   28  28 ARG B  272  SER B  277  1                                   6    
HELIX   29  29 SER B  278  SER B  294  1                                  17    
HELIX   30  30 THR B  297  SER B  303  1                                   7    
HELIX   31  31 PRO B  306  ASP B  313  1                                   8    
HELIX   32  32 TYR B  314  ASN B  318  5                                   5    
HELIX   33  33 PRO B  329  GLY B  333  5                                   5    
HELIX   34  34 ARG B  384  SER B  388  5                                   5    
HELIX   35  35 ASP B  413  ILE B  425  1                                  13    
HELIX   36  36 SER B  446  LEU B  474  1                                  29    
HELIX   37  37 PHE B  475  PHE B  479  5                                   5    
HELIX   38  38 ALA C   34  ARG C   41  5                                   8    
HELIX   39  39 LEU C   45  PHE C   75  1                                  31    
HELIX   40  40 MET C   81  GLY C   85  5                                   5    
HELIX   41  41 LEU C   88  LEU C   95  1                                   8    
HELIX   42  42 GLY C  100  GLU C  104  5                                   5    
HELIX   43  43 THR C  108  ALA C  133  1                                  26    
HELIX   44  44 ASN C  155  PHE C  181  1                                  27    
HELIX   45  45 ASP C  205  TYR C  212  1                                   8    
HELIX   46  46 LEU C  213  LYS C  215  5                                   3    
HELIX   47  47 ASN C  229  LEU C  253  1                                  25    
HELIX   48  48 PHE C  257  ARG C  262  1                                   6    
HELIX   49  49 SER C  267  ASN C  293  1                                  27    
HELIX   50  50 THR C  305  LYS C  323  1                                  19    
HELIX   51  51 GLY C  353  TRP C  359  5                                   7    
HELIX   52  52 LEU C  366  ARG C  370  5                                   5    
HELIX   53  53 ASP C  376  ASP C  383  1                                   8    
HELIX   54  54 GLN C  385  THR C  397  1                                  13    
HELIX   55  55 SER C  421  ALA C  452  1                                  32    
HELIX   56  56 ASP C  460  MET C  469  5                                  10    
HELIX   57  57 TRP D   14  LYS D   23  1                                  10    
HELIX   58  58 SER D   33  PHE D   54  1                                  22    
HELIX   59  59 ALA D   82  GLY D   86  5                                   5    
HELIX   60  60 ASP D  100  GLY D  108  1                                   9    
HELIX   61  61 GLY D  108  GLY D  137  1                                  30    
HELIX   62  62 PHE D  146  PHE D  157  1                                  12    
HELIX   63  63 LEU D  158  GLN D  164  1                                   7    
HELIX   64  64 SER D  166  ALA D  170  5                                   5    
HELIX   65  65 VAL D  175  HIS D  189  1                                  15    
HELIX   66  66 ASN D  190  LEU D  193  5                                   4    
HELIX   67  67 ASN D  194  ASN D  220  1                                  27    
HELIX   68  68 SER D  245  PHE D  257  1                                  13    
HELIX   69  69 ASN D  263  ALA D  290  1                                  28    
HELIX   70  70 PHE D  298  ASP D  308  1                                  11    
HELIX   71  71 THR D  313  GLN D  334  1                                  22    
HELIX   72  72 PRO D  335  ASN D  338  5                                   4    
HELIX   73  73 PRO E    9  SER E   16  1                                   8    
HELIX   74  74 SER E   16  THR E   40  1                                  25    
HELIX   75  75 GLY E   41  PHE E   47  1                                   7    
HELIX   76  76 GLU E   71  LEU E   83  1                                  13    
HELIX   77  77 THR F   17  GLN F   41  1                                  25    
HELIX   78  78 THR H    5  ARG H   12  1                                   8    
HELIX   79  79 THR H   27  ASN H   50  1                                  24    
HELIX   80  80 GLU I    2  SER I   25  1                                  24    
HELIX   81  81 PRO J    9  ALA J   32  1                                  24    
HELIX   82  82 PRO K   12  ILE K   17  5                                   6    
HELIX   83  83 PHE K   18  LEU K   25  1                                   8    
HELIX   84  84 VAL K   27  VAL K   43  1                                  17    
HELIX   85  85 ASN L   13  ASN L   37  1                                  25    
HELIX   86  86 LEU M    6  SER M   31  1                                  26    
HELIX   87  87 GLN M   32  LYS M   34  5                                   3    
HELIX   88  88 THR O   32  VAL O   37  1                                   6    
HELIX   89  89 GLU O  205  GLU O  207  5                                   3    
HELIX   90  90 LEU O  208  VAL O  213  1                                   6    
HELIX   91  91 MET T    1  PHE T   23  1                                  23    
HELIX   92  92 ASN U   41  LEU U   47  1                                   7    
HELIX   93  93 ASN U   61  ILE U   66  5                                   6    
HELIX   94  94 TYR U   72  ASN U   82  1                                  11    
HELIX   95  95 SER U   87  ILE U   94  5                                   8    
HELIX   96  96 ARG U  100  LEU U  109  1                                  10    
HELIX   97  97 GLU U  118  GLU U  123  1                                   6    
HELIX   98  98 GLY U  124  ASP U  126  5                                   3    
HELIX   99  99 THR V   48  CYS V   63  1                                  16    
HELIX  100 100 CYS V   63  VAL V   68  1                                   6    
HELIX  101 101 GLY V   69  ILE V   71  5                                   3    
HELIX  102 102 ARG V   81  LEU V   87  1                                   7    
HELIX  103 103 ASN V   94  ASN V  104  1                                  11    
HELIX  104 104 SER V  120  ALA V  124  5                                   5    
HELIX  105 105 PRO V  128  LEU V  133  1                                   6    
HELIX  106 106 THR V  134  GLY V  153  1                                  20    
HELIX  107 107 GLY V  153  GLY V  158  1                                   6    
HELIX  108 108 GLY V  159  TYR V  163  5                                   5    
HELIX  109 109 UNK X    4  UNK X   27  1                                  24    
HELIX  110 110 UNK X   54  UNK X   85  1                                  32    
HELIX  111 111 UNK X  100  UNK X  111  1                                  12    
HELIX  112 112 UNK X  113  UNK X  123  1                                  11    
HELIX  113 113 MET Z    1  SER Z   29  1                                  29    
HELIX  114 114 ASP Z   34  VAL Z   62  1                                  29    
HELIX  115 115 ASN a 5012  THR a 5022  1                                  11    
HELIX  116 116 PHE a 5033  ALA a 5054  1                                  22    
HELIX  117 117 SER a 5070  GLY a 5074  5                                   5    
HELIX  118 118 PRO a 5095  ALA a 5099  5                                   5    
HELIX  119 119 SER a 5101  ASN a 5108  1                                   8    
HELIX  120 120 GLY a 5109  LEU a 5137  1                                  29    
HELIX  121 121 TRP a 5142  TYR a 5147  1                                   6    
HELIX  122 122 TYR a 5147  LEU a 5159  1                                  13    
HELIX  123 123 LEU a 5159  GLY a 5166  1                                   8    
HELIX  124 124 ILE a 5176  ASN a 5191  1                                  16    
HELIX  125 125 ILE a 5192  MET a 5194  5                                   3    
HELIX  126 126 HIS a 5195  SER a 5222  1                                  28    
HELIX  127 127 SER a 5232  TYR a 5237  5                                   6    
HELIX  128 128 ASN a 5247  PHE a 5260  1                                  14    
HELIX  129 129 ASN a 5267  MET a 5293  1                                  27    
HELIX  130 130 THR a 5316  HIS a 5332  1                                  17    
HELIX  131 131 PRO b 5004  ILE b 5013  5                                  10    
HELIX  132 132 ASP b 5015  ALA b 5043  1                                  29    
HELIX  133 133 PRO b 5054  GLY b 5059  5                                   6    
HELIX  134 134 VAL b 5062  LEU b 5069  1                                   8    
HELIX  135 135 SER b 5092  TYR b 5117  1                                  26    
HELIX  136 136 LEU b 5120  ARG b 5124  5                                   5    
HELIX  137 137 ASP b 5134  HIS b 5157  1                                  24    
HELIX  138 138 GLY b 5186  ASN b 5191  5                                   6    
HELIX  139 139 ASN b 5194  VAL b 5219  1                                  26    
HELIX  140 140 PRO b 5222  LEU b 5229  1                                   8    
HELIX  141 141 ASN b 5233  GLU b 5235  5                                   3    
HELIX  142 142 THR b 5236  TYR b 5258  1                                  23    
HELIX  143 143 THR b 5271  SER b 5277  1                                   7    
HELIX  144 144 SER b 5278  SER b 5294  1                                  17    
HELIX  145 145 THR b 5297  SER b 5303  1                                   7    
HELIX  146 146 PRO b 5306  ASP b 5313  1                                   8    
HELIX  147 147 TYR b 5314  ASN b 5318  5                                   5    
HELIX  148 148 PRO b 5329  ASP b 5334  1                                   6    
HELIX  149 149 ARG b 5384  SER b 5388  5                                   5    
HELIX  150 150 ASP b 5413  ILE b 5425  1                                  13    
HELIX  151 151 SER b 5446  LEU b 5474  1                                  29    
HELIX  152 152 PHE b 5475  PHE b 5479  5                                   5    
HELIX  153 153 ALA c 5034  ARG c 5041  5                                   8    
HELIX  154 154 LEU c 5045  ALA c 5073  1                                  29    
HELIX  155 155 MET c 5081  GLY c 5085  5                                   5    
HELIX  156 156 LEU c 5088  LEU c 5095  1                                   8    
HELIX  157 157 GLY c 5100  GLU c 5104  5                                   5    
HELIX  158 158 THR c 5108  ALA c 5133  1                                  26    
HELIX  159 159 ASN c 5155  PHE c 5181  1                                  27    
HELIX  160 160 ASP c 5205  TYR c 5212  1                                   8    
HELIX  161 161 LEU c 5213  LYS c 5215  5                                   3    
HELIX  162 162 ASN c 5229  LEU c 5253  1                                  25    
HELIX  163 163 PHE c 5257  ARG c 5262  1                                   6    
HELIX  164 164 SER c 5267  ASN c 5293  1                                  27    
HELIX  165 165 THR c 5305  LYS c 5323  1                                  19    
HELIX  166 166 GLY c 5353  TRP c 5359  5                                   7    
HELIX  167 167 LEU c 5366  ARG c 5370  5                                   5    
HELIX  168 168 ASP c 5376  ASP c 5383  1                                   8    
HELIX  169 169 GLN c 5385  THR c 5397  1                                  13    
HELIX  170 170 SER c 5421  ALA c 5452  1                                  32    
HELIX  171 171 ASP c 5460  MET c 5469  5                                  10    
HELIX  172 172 TRP d 5014  LYS d 5023  1                                  10    
HELIX  173 173 SER d 5033  PHE d 5054  1                                  22    
HELIX  174 174 ALA d 5082  GLY d 5086  5                                   5    
HELIX  175 175 ASP d 5100  GLY d 5108  1                                   9    
HELIX  176 176 GLY d 5108  GLY d 5137  1                                  30    
HELIX  177 177 PHE d 5146  PHE d 5157  1                                  12    
HELIX  178 178 LEU d 5158  GLN d 5164  1                                   7    
HELIX  179 179 SER d 5166  ALA d 5170  5                                   5    
HELIX  180 180 VAL d 5175  HIS d 5189  1                                  15    
HELIX  181 181 ASN d 5190  LEU d 5193  5                                   4    
HELIX  182 182 ASN d 5194  ASN d 5220  1                                  27    
HELIX  183 183 SER d 5245  PHE d 5257  1                                  13    
HELIX  184 184 ASN d 5263  ALA d 5290  1                                  28    
HELIX  185 185 PHE d 5298  ASP d 5308  1                                  11    
HELIX  186 186 THR d 5313  GLN d 5334  1                                  22    
HELIX  187 187 PRO d 5335  ASN d 5338  5                                   4    
HELIX  188 188 PRO e 5009  SER e 5016  1                                   8    
HELIX  189 189 SER e 5016  THR e 5040  1                                  25    
HELIX  190 190 GLY e 5041  PHE e 5047  1                                   7    
HELIX  191 191 GLU e 5071  LEU e 5083  1                                  13    
HELIX  192 192 THR f 5017  GLN f 5041  1                                  25    
HELIX  193 193 THR h 5005  ARG h 5012  1                                   8    
HELIX  194 194 THR h 5027  ASN h 5050  1                                  24    
HELIX  195 195 GLU i 5002  SER i 5025  1                                  24    
HELIX  196 196 PRO j 5009  ALA j 5032  1                                  24    
HELIX  197 197 PRO k 5012  ILE k 5017  5                                   6    
HELIX  198 198 PHE k 5018  LEU k 5025  1                                   8    
HELIX  199 199 VAL k 5027  VAL k 5043  1                                  17    
HELIX  200 200 ASN l 5013  ASN l 5037  1                                  25    
HELIX  201 201 LEU m 5006  SER m 5031  1                                  26    
HELIX  202 202 GLN m 5032  LYS m 5034  5                                   3    
HELIX  203 203 THR o 5032  VAL o 5037  1                                   6    
HELIX  204 204 GLU o 5205  GLU o 5207  5                                   3    
HELIX  205 205 LEU o 5208  VAL o 5213  1                                   6    
HELIX  206 206 MET t 5001  PHE t 5023  1                                  23    
HELIX  207 207 ASN u 5041  LEU u 5047  1                                   7    
HELIX  208 208 ASN u 5061  ILE u 5066  5                                   6    
HELIX  209 209 TYR u 5072  ASN u 5082  1                                  11    
HELIX  210 210 SER u 5087  ILE u 5094  5                                   8    
HELIX  211 211 ARG u 5100  LEU u 5109  1                                  10    
HELIX  212 212 GLU u 5118  GLU u 5123  1                                   6    
HELIX  213 213 GLY u 5124  ASP u 5126  5                                   3    
HELIX  214 214 THR v 5048  CYS v 5063  1                                  16    
HELIX  215 215 CYS v 5063  VAL v 5068  1                                   6    
HELIX  216 216 GLY v 5069  ILE v 5071  5                                   3    
HELIX  217 217 ARG v 5081  LEU v 5087  1                                   7    
HELIX  218 218 ASN v 5094  ASN v 5104  1                                  11    
HELIX  219 219 SER v 5120  ALA v 5124  5                                   5    
HELIX  220 220 PRO v 5128  LEU v 5133  1                                   6    
HELIX  221 221 THR v 5134  GLY v 5153  1                                  20    
HELIX  222 222 GLY v 5153  GLY v 5158  1                                   6    
HELIX  223 223 GLY v 5159  TYR v 5163  5                                   5    
HELIX  224 224 UNK x 5004  UNK x 5027  1                                  24    
HELIX  225 225 UNK x 5054  UNK x 5085  1                                  32    
HELIX  226 226 UNK x 5100  UNK x 5111  1                                  12    
HELIX  227 227 UNK x 5113  UNK x 5123  1                                  11    
HELIX  228 228 MET z 5001  SER z 5029  1                                  29    
HELIX  229 229 ASP z 5034  VAL z 5062  1                                  29    
SHEET    1   A 2 LEU A 297  ASN A 298  0                                        
SHEET    2   A 2 GLY C 402  SER C 403  1  O  GLY C 402   N  ASN A 298           
SHEET    1   B 2 MET B 166  VAL B 168  0                                        
SHEET    2   B 2 SER B 177  GLN B 179 -1  O  SER B 177   N  VAL B 168           
SHEET    1   C 2 ILE B 336  TRP B 340  0                                        
SHEET    2   C 2 PHE B 430  ASP B 433 -1  O  ASP B 433   N  ILE B 336           
SHEET    1   D 6 VAL B 377  ASP B 380  0                                        
SHEET    2   D 6 ILE B 369  THR B 371 -1  N  LEU B 370   O  ALA B 379           
SHEET    3   D 6 GLU B 353  VAL B 356 -1  N  PHE B 355   O  THR B 371           
SHEET    4   D 6 HIS B 343  ARG B 347 -1  N  PHE B 346   O  LEU B 354           
SHEET    5   D 6 THR B 398  TYR B 402 -1  O  TYR B 402   N  HIS B 343           
SHEET    6   D 6 THR B 410  PHE B 411 -1  O  PHE B 411   N  VAL B 399           
SHEET    1   E 2 LEU C 341  ARG C 343  0                                        
SHEET    2   E 2 ILE C 349  PHE C 351 -1  O  ILE C 350   N  MET C 342           
SHEET    1   F 6 ASP O 125  ILE O 127  0                                        
SHEET    2   F 6 LEU O 104  VAL O 113 -1  N  ASP O 105   O  ILE O 127           
SHEET    3   F 6 TYR O  64  LYS O  79 -1  N  LEU O  71   O  LEU O 104           
SHEET    4   F 6 PHE O  91  LEU O  96 -1  O  VAL O  92   N  VAL O  78           
SHEET    5   F 6 PHE O 129  MET O 136 -1  O  GLN O 135   N  LYS O  95           
SHEET    6   F 6 ARG O 141  THR O 147 -1  O  ILE O 142   N  VAL O 134           
SHEET    1   G12 ASP O 125  ILE O 127  0                                        
SHEET    2   G12 LEU O 104  VAL O 113 -1  N  ASP O 105   O  ILE O 127           
SHEET    3   G12 LEU O 119  VAL O 122 -1  O  THR O 120   N  LYS O 112           
SHEET    4   G12 LYS O 149  THR O 155 -1  O  ALA O 153   N  PHE O 121           
SHEET    5   G12 ASP O 167  VAL O 174 -1  O  LYS O 169   N  SER O 154           
SHEET    6   G12 THR O 219  LYS O 229 -1  O  THR O 219   N  VAL O 174           
SHEET    7   G12 GLU O 236  LEU O 246 -1  O  ALA O 238   N  ALA O 228           
SHEET    8   G12 GLU O 258  GLU O 270 -1  O  ILE O 261   N  SER O 243           
SHEET    9   G12 TYR O  64  LYS O  79 -1  N  ARG O  65   O  GLU O 270           
SHEET   10   G12 PHE O  91  LEU O  96 -1  O  VAL O  92   N  VAL O  78           
SHEET   11   G12 PHE O 129  MET O 136 -1  O  GLN O 135   N  LYS O  95           
SHEET   12   G12 ARG O 141  THR O 147 -1  O  ILE O 142   N  VAL O 134           
SHEET    1   H 2 ILE U  55  ASP U  56  0                                        
SHEET    2   H 2 PHE U 112  THR U 113  1  O  THR U 113   N  ILE U  55           
SHEET    1   I 2 THR V  35  PRO V  37  0                                        
SHEET    2   I 2 THR V  44  THR V  46 -1  O  ILE V  45   N  VAL V  36           
SHEET    1   J 2 ALA a5081  VAL a5082  0                                        
SHEET    2   J 2 LEU a5174  GLY a5175 -1  O  LEU a5174   N  VAL a5082           
SHEET    1   K 2 LEU a5297  ASN a5298  0                                        
SHEET    2   K 2 GLY c5402  SER c5403  1  O  GLY c5402   N  ASN a5298           
SHEET    1   L 2 MET b5166  VAL b5168  0                                        
SHEET    2   L 2 SER b5177  GLN b5179 -1  O  SER b5177   N  VAL b5168           
SHEET    1   M 2 ILE b5336  TRP b5340  0                                        
SHEET    2   M 2 PHE b5430  ASP b5433 -1  O  GLU b5431   N  GLN b5338           
SHEET    1   N 6 VAL b5377  ASP b5380  0                                        
SHEET    2   N 6 ILE b5369  THR b5371 -1  N  LEU b5370   O  ALA b5379           
SHEET    3   N 6 GLU b5353  VAL b5356 -1  N  PHE b5355   O  THR b5371           
SHEET    4   N 6 HIS b5343  ARG b5347 -1  N  PHE b5346   O  LEU b5354           
SHEET    5   N 6 THR b5398  TYR b5402 -1  O  TYR b5402   N  HIS b5343           
SHEET    6   N 6 THR b5410  PHE b5411 -1  O  PHE b5411   N  VAL b5399           
SHEET    1   O 2 LEU c5341  ARG c5343  0                                        
SHEET    2   O 2 ILE c5349  PHE c5351 -1  O  ILE c5350   N  MET c5342           
SHEET    1   P 6 ASP o5125  ILE o5127  0                                        
SHEET    2   P 6 LEU o5104  VAL o5113 -1  N  ASP o5105   O  ILE o5127           
SHEET    3   P 6 TYR o5064  LYS o5079 -1  N  LEU o5071   O  LEU o5104           
SHEET    4   P 6 PHE o5091  LEU o5096 -1  O  VAL o5092   N  VAL o5078           
SHEET    5   P 6 PHE o5129  MET o5136 -1  O  GLN o5135   N  LYS o5095           
SHEET    6   P 6 ARG o5141  THR o5147 -1  O  ILE o5142   N  VAL o5134           
SHEET    1   Q12 ASP o5125  ILE o5127  0                                        
SHEET    2   Q12 LEU o5104  VAL o5113 -1  N  ASP o5105   O  ILE o5127           
SHEET    3   Q12 LEU o5119  VAL o5122 -1  O  THR o5120   N  LYS o5112           
SHEET    4   Q12 LYS o5149  SER o5154 -1  O  ALA o5153   N  PHE o5121           
SHEET    5   Q12 ASP o5167  VAL o5174 -1  O  LYS o5169   N  SER o5154           
SHEET    6   Q12 THR o5219  LYS o5229 -1  O  THR o5219   N  VAL o5174           
SHEET    7   Q12 GLU o5236  LEU o5246 -1  O  ALA o5238   N  ALA o5228           
SHEET    8   Q12 GLU o5258  GLU o5270 -1  O  ILE o5261   N  SER o5243           
SHEET    9   Q12 TYR o5064  LYS o5079 -1  N  GLN o5072   O  VAL o5264           
SHEET   10   Q12 PHE o5091  LEU o5096 -1  O  VAL o5092   N  VAL o5078           
SHEET   11   Q12 PHE o5129  MET o5136 -1  O  GLN o5135   N  LYS o5095           
SHEET   12   Q12 ARG o5141  THR o5147 -1  O  ILE o5142   N  VAL o5134           
SHEET    1   R 2 ILE u5055  ASP u5056  0                                        
SHEET    2   R 2 PHE u5112  THR u5113  1  O  THR u5113   N  ILE u5055           
SHEET    1   S 2 THR v5035  PRO v5037  0                                        
SHEET    2   S 2 THR v5044  THR v5046 -1  O  ILE v5045   N  VAL v5036           
SSBOND   1 CYS O   45    CYS O   70                          1555   1555  2.05  
SSBOND   2 CYS o 5045    CYS o 5070                          1555   1555  2.07  
LINK        FE   HEM F  51                 NE2 HIS E  23     1555   1555  1.99  
LINK        FE   HEM F  51                 NE2 HIS F  24     1555   1555  2.41  
LINK        FE   HEM V 552                 NE2 HIS V  67     1555   1555  2.06  
LINK        FE   HEM V 552                 NE2 HIS V 118     1555   1555  2.15  
LINK        FE   FE2 A 557                 NE2 HIS A 215     1555   1555  1.87  
LINK        FE   FE2 A 557                 NE2 HIS A 272     1555   1555  2.39  
LINK        FE   HEM f5051                 NE2 HIS e5023     1555   1555  2.07  
LINK        FE   HEM f5051                 NE2 HIS f5024     1555   1555  2.34  
LINK        FE   HEM v5552                 NE2 HIS v5067     1555   1555  2.10  
LINK        FE   HEM v5552                 NE2 HIS v5118     1555   1555  2.16  
LINK        FE   FE2 a5557                 NE2 HIS a5215     1555   1555  1.91  
LINK        FE   FE2 a5557                 NE2 HIS a5272     1555   1555  2.39  
LINK         OD1 ASP A 170                MN4  OEC A 565     1555   1555  2.39  
LINK         OE1 GLU A 189                CA1  OEC A 565     1555   1555  2.52  
LINK         OE2 GLU A 189                MN1  OEC A 565     1555   1555  1.81  
LINK         NE2 HIS A 198                MG   CLA A 558     1555   1555  2.25  
LINK         OE1 GLU A 333                MN3  OEC A 565     1555   1555  2.31  
LINK         OD1 ASP A 342                MN2  OEC A 565     1555   1555  2.18  
LINK         OD2 ASP A 342                MN1  OEC A 565     1555   1555  2.42  
LINK         O   ALA A 344                CA1  OEC A 565     1555   1555  2.61  
LINK         OXT ALA A 344                MN2  OEC A 565     1555   1555  1.77  
LINK         NE2 HIS B   9                MG   CLA B 524     1555   1555  2.24  
LINK         ND1 HIS B 201                MG   CLA B 512     1555   1555  2.13  
LINK         NE2 HIS B 202                MG   CLA B 513     1555   1555  2.12  
LINK         NE2 HIS B 455                MG   CLA B 514     1555   1555  2.17  
LINK         NE2 HIS B 466                MG   CLA B 518     1555   1555  2.34  
LINK         NE2 HIS B 469                MG   CLA B 521     1555   1555  2.24  
LINK         OD1 ASN C  39                MG   CLA C 501     1555   1555  2.21  
LINK         NE2 HIS C 118                MG   CLA C 493     1555   1555  2.35  
LINK         NE2 HIS C 132                MG   CLA C 503     1555   1555  2.38  
LINK         NE2 HIS C 237                MG   CLA C 491     1555   1555  2.18  
LINK         NE2 HIS C 251                MG   CLA C 496     1555   1555  2.50  
LINK         OE1 GLU C 354                MN2  OEC A 565     1555   1555  2.48  
LINK         OE2 GLU C 354                MN3  OEC A 565     1555   1555  2.12  
LINK         NE2 HIS C 430                MG   CLA C 492     1555   1555  2.50  
LINK         NE2 HIS C 444                MG   CLA C 498     1555   1555  2.39  
LINK         NE2 HIS D 197                MG   CLA D 354     1555   1555  2.16  
LINK         NE2 HIS D 214                FE   FE2 A 557     1555   1555  2.23  
LINK         NE2 HIS D 268                FE   FE2 A 557     1555   1555  2.29  
LINK         OD1 ASP K  19                CA    CA K  56     1555   1555  2.84  
LINK         OD2 ASP K  23                CA    CA K  56     1555   1555  2.86  
LINK         OE1 GLU a5189                CA1  OEC a5565     1555   1555  2.74  
LINK         OE2 GLU a5189                MN1  OEC a5565     1555   1555  1.84  
LINK         NE2 HIS a5198                MG   CLA a5558     1555   1555  2.24  
LINK         OE1 GLU a5333                MN3  OEC a5565     1555   1555  2.20  
LINK         OE2 GLU a5333                MN4  OEC a5565     1555   1555  2.17  
LINK         OD1 ASP a5342                MN2  OEC a5565     1555   1555  2.14  
LINK         OD2 ASP a5342                MN1  OEC a5565     1555   1555  2.49  
LINK         O   ALA a5344                CA1  OEC a5565     1555   1555  2.53  
LINK         OXT ALA a5344                MN2  OEC a5565     1555   1555  1.69  
LINK         NE2 HIS b5009                MG   CLA b5524     1555   1555  2.20  
LINK         ND1 HIS b5201                MG   CLA b5512     1555   1555  2.15  
LINK         NE2 HIS b5202                MG   CLA b5513     1555   1555  2.15  
LINK         NE2 HIS b5455                MG   CLA b5514     1555   1555  2.21  
LINK         NE2 HIS b5466                MG   CLA b5518     1555   1555  2.35  
LINK         NE2 HIS b5469                MG   CLA b5521     1555   1555  2.28  
LINK         OD1 ASN c5039                MG   CLA c5501     1555   1555  2.18  
LINK         NE2 HIS c5118                MG   CLA c5493     1555   1555  2.33  
LINK         NE2 HIS c5132                MG   CLA c5503     1555   1555  2.40  
LINK         NE2 HIS c5237                MG   CLA c5491     1555   1555  2.13  
LINK         OE1 GLU c5354                MN2  OEC a5565     1555   1555  2.32  
LINK         OE2 GLU c5354                MN3  OEC a5565     1555   1555  2.12  
LINK         NE2 HIS c5430                MG   CLA c5492     1555   1555  2.46  
LINK         NE2 HIS c5444                MG   CLA c5498     1555   1555  2.33  
LINK         NE2 HIS d5197                MG   CLA d5354     1555   1555  2.22  
LINK         NE2 HIS d5214                FE   FE2 a5557     1555   1555  2.18  
LINK         NE2 HIS d5268                FE   FE2 a5557     1555   1555  2.27  
LINK         OD1 ASP k5019                CA    CA k5056     1555   1555  2.59  
LINK         OD2 ASP k5019                CA    CA k5056     1555   1555  2.73  
LINK         OD2 ASP k5023                CA    CA k5056     1555   1555  2.78  
LINK        FE   FE2 A 557                 O3  BCT D 353     1555   1555  2.34  
LINK        FE   FE2 A 557                 O2  BCT D 353     1555   1555  2.31  
LINK        FE   FE2 a5557                 O3  BCT d5353     1555   1555  2.31  
LINK        FE   FE2 a5557                 O2  BCT d5353     1555   1555  2.34  
CISPEP   1 THR V   89    PRO V   90          0        -0.27                     
CISPEP   2 THR v 5089    PRO v 5090          0        -0.07                     
SITE     1 AC1  3 ASP K  19  ASP K  23  UNK X   2                               
SITE     1 AC2  5 HIS A 215  HIS A 272  HIS D 214  HIS D 268                    
SITE     2 AC2  5 BCT D 353                                                     
SITE     1 AC3  9 HIS A 215  GLU A 244  TYR A 246  HIS A 272                    
SITE     2 AC3  9 FE2 A 557  HIS D 214  TYR D 244  LYS D 264                    
SITE     3 AC3  9 HIS D 268                                                     
SITE     1 AC4  3 ASP k5019  ASP k5023  UNK x5002                               
SITE     1 AC5  5 HIS a5215  HIS a5272  HIS d5214  HIS d5268                    
SITE     2 AC5  5 BCT d5353                                                     
SITE     1 AC6  9 HIS a5215  GLU a5244  TYR a5246  HIS a5272                    
SITE     2 AC6  9 FE2 a5557  HIS d5214  TYR d5244  LYS d5264                    
SITE     3 AC6  9 HIS d5268                                                     
SITE     1 AC7 20 PHE A 119  TYR A 147  PRO A 150  SER A 153                    
SITE     2 AC7 20 VAL A 157  MET A 183  ILE A 184  PHE A 186                    
SITE     3 AC7 20 GLN A 187  LEU A 193  HIS A 198  GLY A 201                    
SITE     4 AC7 20 VAL A 205  THR A 286  ILE A 290  CLA A 559                    
SITE     5 AC7 20 CLA A 560  PHO A 561  CLA D 354  MGE D 360                    
SITE     1 AC8 23 MET A 183  PHE A 206  CLA A 558  CLA A 559                    
SITE     2 AC8 23 CLA A 560  PHO A 562  VAL D 152  VAL D 156                    
SITE     3 AC8 23 PHE D 181  LEU D 182  PHE D 185  GLN D 186                    
SITE     4 AC8 23 TRP D 191  THR D 192  HIS D 197  GLY D 200                    
SITE     5 AC8 23 VAL D 201  VAL D 204  LEU D 279  SER D 282                    
SITE     6 AC8 23 ALA D 283  VAL D 286  MGE D 358                               
SITE     1 AC9 18 THR A  45  VAL A 157  PHE A 158  MET A 172                    
SITE     2 AC9 18 ILE A 176  THR A 179  PHE A 180  MET A 183                    
SITE     3 AC9 18 CLA A 558  PHO A 561  UNK C 474  MET D 198                    
SITE     4 AC9 18 VAL D 201  ALA D 202  GLY D 206  LEU D 209                    
SITE     5 AC9 18 CLA D 354  MGE L 210                                          
SITE     1 BC1 14 GLN A 199  VAL A 202  ALA A 203  GLY A 207                    
SITE     2 BC1 14 LEU A 210  TRP A 278  CLA A 558  PHO A 562                    
SITE     3 BC1 14 DGD C 509  PHE D 157  VAL D 175  PHE D 179                    
SITE     4 BC1 14 LEU D 182  CLA D 354                                          
SITE     1 BC2 21 LEU A  41  ALA A  44  THR A  45  ILE A 115                    
SITE     2 BC2 21 PHE A 119  TYR A 126  GLN A 130  TYR A 147                    
SITE     3 BC2 21 PRO A 150  PHE A 158  LEU A 174  PRO A 279                    
SITE     4 BC2 21 VAL A 283  CLA A 558  CLA A 559  LEU D 205                    
SITE     5 BC2 21 ALA D 208  LEU D 209  ILE D 213  TRP D 253                    
SITE     6 BC2 21 PHE D 257                                                     
SITE     1 BC3 21 PHE A 206  ALA A 209  LEU A 210  ALA A 213                    
SITE     2 BC3 21 MET A 214  LEU A 258  CLA A 560  LEU D  37                    
SITE     3 BC3 21 ALA D  41  LEU D  45  TRP D  48  LEU D 122                    
SITE     4 BC3 21 PHE D 125  GLN D 129  ASN D 142  PHE D 146                    
SITE     5 BC3 21 PRO D 149  PHE D 153  PRO D 275  LEU D 279                    
SITE     6 BC3 21 CLA D 354                                                     
SITE     1 BC4 14 ILE A  36  PRO A  39  PHE A  93  PRO A  95                    
SITE     2 BC4 14 ILE A  96  TRP A  97  LEU A 114  PHE A 117                    
SITE     3 BC4 14 HIS A 118  TYR I   9  VAL I  12  THR I  13                    
SITE     4 BC4 14 PHE I  15  MGE I 201                                          
SITE     1 BC5 17 UNK C 480  LEU D  36  PRO D  39  LEU D  43                    
SITE     2 BC5 17 LEU D  89  LEU D  90  LEU D  91  LEU D  92                    
SITE     3 BC5 17 TRP D  93  THR D 112  PHE D 113  HIS D 117                    
SITE     4 BC5 17 PHE D 120  BCR D 357  UNK X  63  UNK X  64                    
SITE     5 BC5 17 UNK X  67                                                     
SITE     1 BC6  5 TRP B 185  PHE B 190  CLA B 512  PHE H  41                    
SITE     2 BC6  5 BCR H 107                                                     
SITE     1 BC7 19 GLY B 189  PHE B 190  GLY B 197  ALA B 200                    
SITE     2 BC7 19 HIS B 201  ALA B 204  ALA B 205  VAL B 208                    
SITE     3 BC7 19 PHE B 247  PHE B 250  CLA B 511  CLA B 513                    
SITE     4 BC7 19 CLA B 518  LEU D 158  ILE D 159  PHE H  38                    
SITE     5 BC7 19 ILE H  45  LEU H  46  TYR H  49                               
SITE     1 BC8 18 ARG B  68  LEU B  69  ALA B 146  LEU B 149                    
SITE     2 BC8 18 CYS B 150  PHE B 153  LEU B 158  HIS B 201                    
SITE     3 BC8 18 HIS B 202  PHE B 247  VAL B 252  THR B 262                    
SITE     4 BC8 18 CLA B 512  CLA B 514  CLA B 515  CLA B 516                    
SITE     5 BC8 18 PHE H  38  LEU H  39                                          
SITE     1 BC9 19 TRP B  33  PHE B  61  PHE B  65  ARG B  68                    
SITE     2 BC9 19 LEU B 149  VAL B 245  ALA B 248  ALA B 249                    
SITE     3 BC9 19 VAL B 252  PHE B 451  HIS B 455  PHE B 458                    
SITE     4 BC9 19 PHE B 462  CLA B 513  CLA B 515  CLA B 517                    
SITE     5 BC9 19 CLA B 522  CLA B 523  CLA B 525                               
SITE     1 CC1 18 THR B  27  VAL B  30  ALA B  31  TRP B  33                    
SITE     2 CC1 18 ALA B  34  VAL B  62  PHE B  65  MET B  66                    
SITE     3 CC1 18 ARG B  68  LEU B  69  VAL B  96  HIS B 100                    
SITE     4 CC1 18 GLY B 147  ALA B 205  CLA B 513  CLA B 514                    
SITE     5 CC1 18 CLA B 516  CLA B 520                                          
SITE     1 CC2 16 LEU B  69  GLY B  70  TRP B  91  ALA B  99                    
SITE     2 CC2 16 HIS B 100  LEU B 103  GLY B 152  PHE B 153                    
SITE     3 CC2 16 PHE B 156  HIS B 157  PHE B 162  GLY B 163                    
SITE     4 CC2 16 PRO B 164  CLA B 513  CLA B 515  BCR B 529                    
SITE     1 CC3 20 TRP B  33  TYR B  40  GLN B  58  GLY B  59                    
SITE     2 CC3 20 PHE B  61  LEU B 324  PHE B 325  THR B 327                    
SITE     3 CC3 20 GLY B 328  PRO B 329  TRP B 450  PHE B 451                    
SITE     4 CC3 20 HIS B 455  CLA B 514  MGE B 530  PHE D 196                    
SITE     5 CC3 20 MET D 281  LEU L  27  PHE M  14  BCR t 104                    
SITE     1 CC4 18 THR B 236  SER B 239  ALA B 243  PHE B 246                    
SITE     2 CC4 18 PHE B 463  HIS B 466  LEU B 474  CLA B 512                    
SITE     3 CC4 18 CLA B 519  CLA B 520  UNK C 481  UNK C 482                    
SITE     4 CC4 18 ILE D 123  MET D 126  LEU D 127  PHE D 130                    
SITE     5 CC4 18 LEU H  43  LEU H  46                                          
SITE     1 CC5 13 PHE B 139  ALA B 212  PHE B 215  HIS B 216                    
SITE     2 CC5 13 PRO B 221  LEU B 229  CLA B 518  CLA B 520                    
SITE     3 CC5 13 THR H  27  THR H  28  MET H  31  PHE H  34                    
SITE     4 CC5 13 BCR H 107                                                     
SITE     1 CC6 13 LEU B 135  PRO B 136  PHE B 139  HIS B 142                    
SITE     2 CC6 13 MET B 231  VAL B 237  SER B 240  SER B 241                    
SITE     3 CC6 13 CLA B 515  CLA B 518  CLA B 519  CLA B 522                    
SITE     4 CC6 13 CLA B 525                                                     
SITE     1 CC7 19 TRP B   5  TYR B   6  ARG B   7  VAL B   8                    
SITE     2 CC7 19 HIS B   9  LEU B 238  ILE B 242  LEU B 461                    
SITE     3 CC7 19 PHE B 462  PHE B 464  GLY B 465  TRP B 468                    
SITE     4 CC7 19 HIS B 469  ARG B 472  PHE B 479  CLA B 522                    
SITE     5 CC7 19 CLA B 523  CLA B 524  MGE D 359                               
SITE     1 CC8 16 HIS B   9  LEU B  12  LEU B  19  ALA B  22                    
SITE     2 CC8 16 HIS B  23  HIS B  26  THR B  27  VAL B 237                    
SITE     3 CC8 16 LEU B 238  SER B 241  VAL B 245  CLA B 514                    
SITE     4 CC8 16 CLA B 520  CLA B 521  CLA B 523  CLA B 525                    
SITE     1 CC9 11 HIS B   9  HIS B  26  VAL B  30  PHE B 462                    
SITE     2 CC9 11 CLA B 514  CLA B 521  CLA B 522  CLA B 524                    
SITE     3 CC9 11 BCR B 527  BCR B 528  MGE D 359                               
SITE     1 DC1 15 VAL B   8  HIS B   9  LEU B  12  ALA B  22                    
SITE     2 DC1 15 MET B  25  LEU B  29  TRP B 115  CLA B 521                    
SITE     3 DC1 15 CLA B 523  BCR B 527  ARG L   7  VAL L  10                    
SITE     4 DC1 15 MGE L 210  UNK c5475  UNK c5476                               
SITE     1 DC2 11 ILE B  20  HIS B  23  MET B 138  ILE B 141                    
SITE     2 DC2 11 HIS B 142  LEU B 145  CLA B 514  CLA B 520                    
SITE     3 DC2 11 CLA B 522  CLA B 526  LEU H  14                               
SITE     1 DC3  9 ILE B  20  LEU B  24  ALA B 110  TRP B 113                    
SITE     2 DC3  9 HIS B 114  LEU B 120  CLA B 525  THR H   5                    
SITE     3 DC3  9 LEU H   7                                                     
SITE     1 DC4 16 LEU C  95  LEU C 168  GLY C 171  ALA C 172                    
SITE     2 DC4 16 ILE C 224  VAL C 233  HIS C 237  ILE C 240                    
SITE     3 DC4 16 ALA C 278  MET C 281  MET C 282  VAL C 296                    
SITE     4 DC4 16 TYR C 297  CLA C 492  CLA C 493  BCR C 506                    
SITE     1 DC5 14 TRP C  63  HIS C  91  GLY C 171  LEU C 175                    
SITE     2 DC5 14 LYS C 178  ALA C 286  TYR C 297  HIS C 430                    
SITE     3 DC5 14 LEU C 433  PHE C 437  CLA C 491  CLA C 493                    
SITE     4 DC5 14 CLA C 494  CLA C 500                                          
SITE     1 DC6 16 ILE C  60  VAL C  61  ALA C  64  THR C  68                    
SITE     2 DC6 16 LEU C  88  HIS C  91  ILE C  92  LEU C  95                    
SITE     3 DC6 16 VAL C 114  HIS C 118  LEU C 279  UNK C 477                    
SITE     4 DC6 16 CLA C 491  CLA C 492  CLA C 500  CLA C 502                    
SITE     1 DC7 14 TRP C  63  MET C  67  PHE C  70  GLY C  85                    
SITE     2 DC7 14 ILE C  87  SER C 406  TRP C 425  SER C 429                    
SITE     3 DC7 14 HIS C 430  UNK C 478  CLA C 492  CLA C 500                    
SITE     4 DC7 14 DGD C 508  PRO K  26                                          
SITE     1 DC8 15 ILE A  36  SER A 124  MET A 127  TRP A 131                    
SITE     2 DC8 15 ILE C 265  TYR C 274  GLY C 277  ALA C 278                    
SITE     3 DC8 15 LEU C 438  HIS C 441  LEU C 442  ALA C 445                    
SITE     4 DC8 15 ARG C 449  CLA C 497  PHE I  23                               
SITE     1 DC9 12 LEU C 165  ILE C 243  GLY C 247  TRP C 250                    
SITE     2 DC9 12 HIS C 251  PRO C 256  PHE C 257  TRP C 259                    
SITE     3 DC9 12 PHE C 264  CLA C 497  BCR C 506  LEU I  24                    
SITE     1 EC1 14 MET C 157  LEU C 161  HIS C 164  LEU C 168                    
SITE     2 EC1 14 PHE C 264  TRP C 266  TYR C 271  TYR C 274                    
SITE     3 EC1 14 SER C 275  LEU C 279  MET C 282  CLA C 495                    
SITE     4 EC1 14 CLA C 496  CLA C 499                                          
SITE     1 EC2 15 LHG A 567  TRP C  36  ALA C  37  ASN C  39                    
SITE     2 EC2 15 ALA C  40  GLU C 269  LEU C 276  PHE C 436                    
SITE     3 EC2 15 PHE C 437  GLY C 440  TRP C 443  HIS C 444                    
SITE     4 EC2 15 ARG C 447  CLA C 499  CLA C 500                               
SITE     1 EC3 11 ASN C  39  LEU C  49  ALA C  52  HIS C  53                    
SITE     2 EC3 11 HIS C  56  GLY C 268  GLU C 269  SER C 275                    
SITE     3 EC3 11 CLA C 497  CLA C 498  CLA C 500                               
SITE     1 EC4 15 ASN C  39  HIS C  56  LEU C  59  LEU C 279                    
SITE     2 EC4 15 PHE C 436  PHE C 437  CLA C 492  CLA C 493                    
SITE     3 EC4 15 CLA C 494  CLA C 498  CLA C 499  CLA C 501                    
SITE     4 EC4 15 PRO K  29  VAL K  30  LEU K  33                               
SITE     1 EC5 19 ASP C  27  TRP C  35  GLY C  38  ASN C  39                    
SITE     2 EC5 19 ARG C  41  LEU C  42  LEU C  45  LYS C  48                    
SITE     3 EC5 19 ALA C  52  PHE C 127  ALA C 133  ILE C 134                    
SITE     4 EC5 19 CLA C 500  BCR C 504  TRP K  39  GLN K  40                    
SITE     5 EC5 19 UNK X  31  VAL Z  20  PRO Z  24                               
SITE     1 EC6 10 HIS C  53  PHE C 147  PHE C 163  HIS C 164                    
SITE     2 EC6 10 VAL C 167  LEU C 168  GLY C 171  CLA C 493                    
SITE     3 EC6 10 CLA C 503  BCR C 505                                          
SITE     1 EC7  9 LEU C  50  GLY C 128  TYR C 131  HIS C 132                    
SITE     2 EC7  9 PRO C 137  LEU C 140  PHE C 147  CLA C 502                    
SITE     3 EC7  9 BCR C 505                                                     
SITE     1 EC8 12 ILE E  13  ARG E  18  TYR E  19  HIS E  23                    
SITE     2 EC8 12 THR E  26  ILE E  27  ARG F  19  TRP F  20                    
SITE     3 EC8 12 HIS F  24  ALA F  27  ILE F  31  UNK X 116                    
SITE     1 EC9 12 ALA V  62  CYS V  63  CYS V  66  HIS V  67                    
SITE     2 EC9 12 THR V  74  LEU V  78  ASP V  79  LEU V  80                    
SITE     3 EC9 12 THR V  84  TYR V 101  TYR V 108  HIS V 118                    
SITE     1 FC1 12 UNK C 474  LEU D 209  LEU D 210  HIS D 214                    
SITE     2 FC1 12 THR D 217  ASN D 250  TRP D 253  ALA D 260                    
SITE     3 FC1 12 PHE D 261  LEU D 267  PHE D 270  VAL D 274                    
SITE     1 FC2  9 HIS A 215  LEU A 218  ALA A 251  HIS A 252                    
SITE     2 FC2  9 PHE A 255  SER A 264  PHE A 265  LEU A 271                    
SITE     3 FC2  9 PHE A 274                                                     
SITE     1 FC3  7 ASP A 170  GLU A 189  HIS A 332  GLU A 333                    
SITE     2 FC3  7 ASP A 342  ALA A 344  GLU C 354                               
SITE     1 FC4  6 ILE A  38  ALA A  43  ALA A  51  ALA A  54                    
SITE     2 FC4  6 TRP A 105  PHE I  15                                          
SITE     1 FC5 10 MET B  25  LEU B  29  TRP B 115  CLA B 523                    
SITE     2 FC5 10 CLA B 524  BCR B 528  MGE B 530  ALA M  10                    
SITE     3 FC5 10 BCR t 104  PHE t5019                                          
SITE     1 FC6 13 TRP B  33  SER B  36  MET B  37  LEU B 109                    
SITE     2 FC6 13 CLA B 517  BCR B 527  BCR B 528  SQD a 212                    
SITE     3 FC6 13 ILE t5004  PHE t5008  ALA t5011  PHE t5018                    
SITE     4 FC6 13 PHE t5022                                                     
SITE     1 FC7  9 LEU B  29  GLY B  32  TRP B  33  SER B  36                    
SITE     2 FC7  9 ILE B 101  VAL B 102  CLA B 523  BCR B 527                    
SITE     3 FC7  9 BCR t 104                                                     
SITE     1 FC8  6 LEU B 106  CYS B 112  VAL B 116  TYR B 117                    
SITE     2 FC8  6 CLA B 516  SQD a 212                                          
SITE     1 FC9  7 CLA B 511  CLA B 519  MET H  35  PHE H  38                    
SITE     2 FC9  7 PHE H  41  UNK X  52  UNK X  57                               
SITE     1 GC1 14 TYR D  42  LEU D  43  GLY D  46  GLY D  47                    
SITE     2 GC1 14 LEU D  49  THR D  50  PHE D 113  CLA D 355                    
SITE     3 GC1 14 PRO F  29  THR F  30  PHE F  33  ILE F  37                    
SITE     4 GC1 14 VAL J  21  VAL J  25                                          
SITE     1 GC2 14 BCR C 504  ALA J  14  THR J  15  GLY J  18                    
SITE     2 GC2 14 MET J  19  LEU K  21  LEU K  31  ALA K  34                    
SITE     3 GC2 14 PHE K  37  VAL K  38  UNK X  13  UNK X  14                    
SITE     4 GC2 14 UNK X  17  VAL Z  13                                          
SITE     1 GC3 15 ALA C  55  GLY C  58  LEU C  59  VAL C 116                    
SITE     2 GC3 15 LEU C 119  SER C 122  ALA C 123  GLY C 126                    
SITE     3 GC3 15 CLA C 501  BCR C 505  TYR K  15  PHE K  18                    
SITE     4 GC3 15 PHE K  32  ALA K  36  BCR X 130                               
SITE     1 GC4 11 PHE C 112  VAL C 116  ILE C 120  SER C 121                    
SITE     2 GC4 11 VAL C 124  LEU C 125  CLA C 502  CLA C 503                    
SITE     3 GC4 11 BCR C 504  TYR K  15  GLY Z  55                               
SITE     1 GC5 14 ILE C 209  TYR C 212  LEU C 213  ILE C 224                    
SITE     2 GC5 14 VAL C 227  ASP C 232  VAL C 233  HIS C 237                    
SITE     3 GC5 14 PHE C 264  CLA C 491  CLA C 496  VAL I  20                    
SITE     4 GC5 14 PHE I  23  LEU I  24                                          
SITE     1 GC6 11 PHE A  93  TRP A  97  LEU A 121  CLA A 563                    
SITE     2 GC6 11 SER C 216  PHE C 218  TRP C 223  MET C 281                    
SITE     3 GC6 11 PHE C 284  LYS I   5  TYR I   9                               
SITE     1 GC7 17 PHE A 155  ILE A 160  ILE A 163  PRO C 217                    
SITE     2 GC7 17 PHE C 218  GLY C 219  GLY C 220  GLY C 222                    
SITE     3 GC7 17 VAL C 225  SER C 226  ASN C 228  PHE C 284                    
SITE     4 GC7 17 CYS C 288  PHE C 292  ASN C 294  ARG C 362                    
SITE     5 GC7 17 LEU C 438                                                     
SITE     1 GC8 15 ARG A 140  TRP A 142  PHE A 273  SQD A 568                    
SITE     2 GC8 15 TRP C  36  PHE C 436  TRP C 443  ARG C 447                    
SITE     3 GC8 15 CLA C 498  GLU D 219  ASN D 220  ALA D 229                    
SITE     4 GC8 15 SER D 230  THR D 231  PHE D 232                               
SITE     1 GC9 10 ASN A 267  SER A 270  PHE A 273  PHE A 274                    
SITE     2 GC9 10 LHG A 567  GLU C  29  TRP C  36  SER D 230                    
SITE     3 GC9 10 PHE D 232  ARG D 233                                          
SITE     1 HC1 14 PHE A 197  GLU C  83  GLN C  84  GLY C  85                    
SITE     2 HC1 14 SER C 406  ASN C 418  PHE C 419  VAL C 420                    
SITE     3 HC1 14 TRP C 425  THR C 428  UNK C 479  CLA C 494                    
SITE     4 HC1 14 DGD C 509  TYR J  33                                          
SITE     1 HC2 20 GLN A 199  LEU A 200  PHE A 300  ASN A 301                    
SITE     2 HC2 20 PHE A 302  SER A 305  CLA A 560  ASN C 405                    
SITE     3 HC2 20 ASN C 415  SER C 416  ASN C 418  DGD C 508                    
SITE     4 HC2 20 MGE D 358  PHE J  29  ALA J  32  TYR J  33                    
SITE     5 HC2 20 GLY J  37  SER J  38  SER J  39  GLN V  60                    
SITE     1 HC3 12 DGD C 509  TYR D  67  GLY D  70  CYS D  71                    
SITE     2 HC3 12 CLA D 354  THR F  30  MET F  40  GLN F  41                    
SITE     3 HC3 12 GLY J  31  ALA J  32  GLY J  35  GLY J  37                    
SITE     1 HC4 14 TYR B 193  PHE B 250  TYR B 258  TYR B 273                    
SITE     2 HC4 14 SER B 277  PHE B 463  HIS D  87  ILE D 123                    
SITE     3 HC4 14 LEU D 162  SER D 165  TYR H  49  VAL H  60                    
SITE     4 HC4 14 SER H  61  TRP H  62                                          
SITE     1 HC5 13 ASN A 234  TRP B   5  TYR B   6  ARG B   7                    
SITE     2 HC5 13 PHE B 464  TRP B 468  CLA B 521  CLA B 523                    
SITE     3 HC5 13 ARG D 139  TYR D 141  PHE D 269  PHE D 273                    
SITE     4 HC5 13 MGE L 210                                                     
SITE     1 HC6 14 SER A 232  ASN A 234  CLA A 559  TRP B   5                    
SITE     2 HC6 14 TYR B   6  CLA B 524  UNK C 474  TRP D 266                    
SITE     3 HC6 14 PHE D 270  PHE D 273  MGE D 359  GLU L  11                    
SITE     4 HC6 14 SER L  16  GLY L  20                                          
SITE     1 HC7 14 CLA A 558  ILE D 259  ALA D 260  PHE D 261                    
SITE     2 HC7 14 SER D 262  ASN D 263  TRP D 266  PHE D 270                    
SITE     3 HC7 14 THR L  15  TYR L  18  LEU L  19  PHE T  10                    
SITE     4 HC7 14 PHE T  17  ALA T  20                                          
SITE     1 HC8  8 TRP B 113  TYR B 117  BCR B 529  TRP a5020                    
SITE     2 HC8  8 ASN a5026  ARG a5027  LEU a5028  BCR t 104                    
SITE     1 HC9  7 ARG B  18  LEU B  29  SER B 104  ARG l5014                    
SITE     2 HC9  7 TYR l5018  PHE t5019  PHE t5023                               
SITE     1 IC1 10 THR B 327  GLY B 328  PRO B 329  PHE B 453                    
SITE     2 IC1 10 CLA B 517  BCR B 527  PHE L  35  ASN M   4                    
SITE     3 IC1 10 LEU M   6  LMT M5216                                          
SITE     1 IC2 11 ILE A  50  LEU A  72  TYR A  73  UNK C 488                    
SITE     2 IC2 11 UNK C 489  ARG D 304  GLY O 139  GLU O 140                    
SITE     3 IC2 11 LMT T 217  ALA b5043  LEU b5098                               
SITE     1 IC3  9 MET M   1  LMT M5216  MET T   1  ILE T   4                    
SITE     2 IC3  9 LMT T 217  TYR b5040  MGE b5530  GLN m5005                    
SITE     3 IC3  9 LEU m5006                                                     
SITE     1 IC4 11 LEU A  72  LMT A 569  MET T   1  ILE T   4                    
SITE     2 IC4 11 ALA T  11  ILE T  14  TYR b5040  ALA b5043                    
SITE     3 IC4 11 THR b5044  BCR b5528  LMT m 216                               
SITE     1 IC5 21 PHE a5119  TYR a5147  PRO a5150  SER a5153                    
SITE     2 IC5 21 VAL a5157  MET a5183  ILE a5184  PHE a5186                    
SITE     3 IC5 21 GLN a5187  LEU a5193  HIS a5198  GLY a5201                    
SITE     4 IC5 21 VAL a5205  THR a5286  ILE a5290  CLA a5559                    
SITE     5 IC5 21 CLA a5560  PHO a5561  LEU d5182  CLA d5354                    
SITE     6 IC5 21 MGE d5361                                                     
SITE     1 IC6 23 MET a5183  PHE a5206  CLA a5558  CLA a5559                    
SITE     2 IC6 23 CLA a5560  PHO a5562  VAL d5152  VAL d5156                    
SITE     3 IC6 23 PHE d5181  LEU d5182  PHE d5185  GLN d5186                    
SITE     4 IC6 23 TRP d5191  THR d5192  HIS d5197  GLY d5200                    
SITE     5 IC6 23 VAL d5201  VAL d5204  LEU d5279  SER d5282                    
SITE     6 IC6 23 ALA d5283  VAL d5286  MGE d5359                               
SITE     1 IC7 18 THR a5045  VAL a5157  PHE a5158  MET a5172                    
SITE     2 IC7 18 ILE a5176  THR a5179  PHE a5180  MET a5183                    
SITE     3 IC7 18 CLA a5558  UNK c5474  MET d5198  VAL d5201                    
SITE     4 IC7 18 ALA d5202  GLY d5206  LEU d5209  CLA d5354                    
SITE     5 IC7 18 MGE d5361  MGE l5210                                          
SITE     1 IC8 15 GLN a5199  VAL a5202  ALA a5203  GLY a5207                    
SITE     2 IC8 15 LEU a5210  TRP a5278  CLA a5558  PHO a5562                    
SITE     3 IC8 15 DGD c5509  PHE d5157  VAL d5175  PHE d5179                    
SITE     4 IC8 15 LEU d5182  CLA d5354  MGE d5359                               
SITE     1 IC9 20 LEU a5041  ALA a5044  THR a5045  ILE a5115                    
SITE     2 IC9 20 PHE a5119  TYR a5126  GLN a5130  TYR a5147                    
SITE     3 IC9 20 PRO a5150  PHE a5158  LEU a5174  PRO a5279                    
SITE     4 IC9 20 VAL a5283  CLA a5558  LEU d5205  ALA d5208                    
SITE     5 IC9 20 LEU d5209  ILE d5213  TRP d5253  PHE d5257                    
SITE     1 JC1 22 PHE a5206  ALA a5209  LEU a5210  ALA a5213                    
SITE     2 JC1 22 MET a5214  LEU a5258  CLA a5560  LEU d5037                    
SITE     3 JC1 22 ALA d5041  LEU d5045  TRP d5048  GLY d5118                    
SITE     4 JC1 22 LEU d5122  PHE d5125  GLN d5129  ASN d5142                    
SITE     5 JC1 22 PHE d5146  PRO d5149  PHE d5153  PRO d5275                    
SITE     6 JC1 22 LEU d5279  CLA d5354                                          
SITE     1 JC2 15 ILE a5036  PRO a5039  THR a5040  PHE a5093                    
SITE     2 JC2 15 PRO a5095  ILE a5096  TRP a5097  LEU a5114                    
SITE     3 JC2 15 PHE a5117  HIS a5118  LEU a5121  TYR i5009                    
SITE     4 JC2 15 THR i5013  PHE i5015  MGE i5201                               
SITE     1 JC3 16 UNK c5480  LEU d5036  PRO d5039  LEU d5043                    
SITE     2 JC3 16 LEU d5089  LEU d5090  LEU d5091  LEU d5092                    
SITE     3 JC3 16 TRP d5093  THR d5112  PHE d5113  HIS d5117                    
SITE     4 JC3 16 PHE d5120  BCR d5357  UNK x5063  UNK x5064                    
SITE     1 JC4  5 TRP b5185  PHE b5190  CLA b5512  PHE h5041                    
SITE     2 JC4  5 BCR h5107                                                     
SITE     1 JC5 20 GLY b5189  PHE b5190  GLY b5197  ALA b5200                    
SITE     2 JC5 20 HIS b5201  ALA b5204  ALA b5205  VAL b5208                    
SITE     3 JC5 20 PHE b5247  PHE b5250  CLA b5511  CLA b5513                    
SITE     4 JC5 20 CLA b5518  LEU d5158  ILE d5159  PHE h5038                    
SITE     5 JC5 20 PHE h5041  ILE h5045  LEU h5046  TYR h5049                    
SITE     1 JC6 19 ARG b5068  LEU b5069  ALA b5146  LEU b5149                    
SITE     2 JC6 19 CYS b5150  PHE b5153  LEU b5158  HIS b5201                    
SITE     3 JC6 19 HIS b5202  PHE b5247  VAL b5252  THR b5262                    
SITE     4 JC6 19 CLA b5512  CLA b5514  CLA b5515  CLA b5516                    
SITE     5 JC6 19 CLA b5520  PHE h5038  LEU h5039                               
SITE     1 JC7 19 TRP b5033  PHE b5061  PHE b5065  ARG b5068                    
SITE     2 JC7 19 LEU b5148  VAL b5245  ALA b5248  ALA b5249                    
SITE     3 JC7 19 VAL b5252  PHE b5451  HIS b5455  PHE b5458                    
SITE     4 JC7 19 PHE b5462  CLA b5513  CLA b5515  CLA b5517                    
SITE     5 JC7 19 CLA b5522  CLA b5523  CLA b5525                               
SITE     1 JC8 17 THR b5027  VAL b5030  ALA b5031  TRP b5033                    
SITE     2 JC8 17 ALA b5034  VAL b5062  PHE b5065  MET b5066                    
SITE     3 JC8 17 ARG b5068  LEU b5069  HIS b5100  GLY b5147                    
SITE     4 JC8 17 ALA b5205  CLA b5513  CLA b5514  CLA b5516                    
SITE     5 JC8 17 CLA b5520                                                     
SITE     1 JC9 16 LEU b5069  GLY b5070  TRP b5091  ALA b5099                    
SITE     2 JC9 16 HIS b5100  LEU b5103  GLY b5152  PHE b5153                    
SITE     3 JC9 16 PHE b5156  HIS b5157  PHE b5162  GLY b5163                    
SITE     4 JC9 16 PRO b5164  CLA b5513  CLA b5515  BCR b5529                    
SITE     1 KC1 20 BCR T5104  TRP b5033  TYR b5040  GLN b5058                    
SITE     2 KC1 20 GLY b5059  PHE b5061  LEU b5324  PHE b5325                    
SITE     3 KC1 20 THR b5327  GLY b5328  PRO b5329  TRP b5450                    
SITE     4 KC1 20 PHE b5451  HIS b5455  CLA b5514  MGE b5530                    
SITE     5 KC1 20 PHE d5196  MET d5281  LEU l5027  PHE m5014                    
SITE     1 KC2 18 THR b5236  SER b5239  ALA b5243  PHE b5246                    
SITE     2 KC2 18 PHE b5463  HIS b5466  LEU b5474  CLA b5512                    
SITE     3 KC2 18 CLA b5519  CLA b5520  UNK c5481  UNK c5482                    
SITE     4 KC2 18 ILE d5123  MET d5126  LEU d5127  PHE d5130                    
SITE     5 KC2 18 LEU h5043  LEU h5046                                          
SITE     1 KC3 13 PHE b5139  ALA b5212  PHE b5215  HIS b5216                    
SITE     2 KC3 13 PRO b5221  LEU b5229  CLA b5518  CLA b5520                    
SITE     3 KC3 13 THR h5027  THR h5028  MET h5031  PHE h5034                    
SITE     4 KC3 13 BCR h5107                                                     
SITE     1 KC4 13 LEU b5135  PRO b5136  PHE b5139  HIS b5142                    
SITE     2 KC4 13 MET b5231  VAL b5237  SER b5240  CLA b5513                    
SITE     3 KC4 13 CLA b5515  CLA b5518  CLA b5519  CLA b5522                    
SITE     4 KC4 13 CLA b5525                                                     
SITE     1 KC5 19 TRP b5005  TYR b5006  ARG b5007  VAL b5008                    
SITE     2 KC5 19 HIS b5009  LEU b5238  ILE b5242  LEU b5461                    
SITE     3 KC5 19 PHE b5462  PHE b5464  GLY b5465  TRP b5468                    
SITE     4 KC5 19 HIS b5469  ARG b5472  PHE b5479  CLA b5522                    
SITE     5 KC5 19 CLA b5523  CLA b5524  MGE d5360                               
SITE     1 KC6 16 HIS b5009  LEU b5012  LEU b5019  ALA b5022                    
SITE     2 KC6 16 HIS b5023  HIS b5026  THR b5027  VAL b5237                    
SITE     3 KC6 16 LEU b5238  SER b5241  VAL b5245  CLA b5514                    
SITE     4 KC6 16 CLA b5520  CLA b5521  CLA b5523  CLA b5525                    
SITE     1 KC7 11 HIS b5009  HIS b5026  VAL b5030  PHE b5462                    
SITE     2 KC7 11 CLA b5514  CLA b5521  CLA b5522  CLA b5524                    
SITE     3 KC7 11 BCR b5527  BCR b5528  MGE d5360                               
SITE     1 KC8 15 UNK C 475  UNK C 476  VAL b5008  HIS b5009                    
SITE     2 KC8 15 LEU b5012  ALA b5022  LEU b5029  TRP b5115                    
SITE     3 KC8 15 CLA b5521  CLA b5523  BCR b5527  ARG l5007                    
SITE     4 KC8 15 VAL l5010  MGE l5210  PHE m5021                               
SITE     1 KC9 11 ILE b5020  HIS b5023  MET b5138  ILE b5141                    
SITE     2 KC9 11 HIS b5142  LEU b5145  CLA b5514  CLA b5520                    
SITE     3 KC9 11 CLA b5522  CLA b5526  LEU h5014                               
SITE     1 LC1  9 ILE b5020  LEU b5024  ALA b5110  TRP b5113                    
SITE     2 LC1  9 HIS b5114  LEU b5120  CLA b5525  THR h5005                    
SITE     3 LC1  9 LEU h5007                                                     
SITE     1 LC2 14 LEU c5095  LEU c5168  GLY c5171  ALA c5172                    
SITE     2 LC2 14 VAL c5233  HIS c5237  ILE c5240  ALA c5278                    
SITE     3 LC2 14 MET c5281  VAL c5296  TYR c5297  CLA c5492                    
SITE     4 LC2 14 CLA c5493  BCR c5506                                          
SITE     1 LC3 14 TRP c5063  HIS c5091  TRP c5097  GLY c5171                    
SITE     2 LC3 14 LYS c5178  ALA c5286  TYR c5297  HIS c5430                    
SITE     3 LC3 14 LEU c5433  PHE c5437  CLA c5491  CLA c5493                    
SITE     4 LC3 14 CLA c5494  CLA c5500                                          
SITE     1 LC4 16 ILE c5060  VAL c5061  ALA c5064  THR c5068                    
SITE     2 LC4 16 LEU c5088  HIS c5091  ILE c5092  LEU c5095                    
SITE     3 LC4 16 VAL c5114  HIS c5118  LEU c5279  UNK c5477                    
SITE     4 LC4 16 CLA c5491  CLA c5492  CLA c5500  CLA c5502                    
SITE     1 LC5 14 TRP c5063  MET c5067  PHE c5070  GLY c5085                    
SITE     2 LC5 14 ILE c5087  SER c5406  TRP c5425  SER c5429                    
SITE     3 LC5 14 HIS c5430  UNK c5478  CLA c5492  CLA c5500                    
SITE     4 LC5 14 DGD c5508  PRO k5026                                          
SITE     1 LC6 15 ILE a5036  SER a5124  MET a5127  TRP a5131                    
SITE     2 LC6 15 ILE c5265  TYR c5274  GLY c5277  ALA c5278                    
SITE     3 LC6 15 LEU c5438  HIS c5441  LEU c5442  ALA c5445                    
SITE     4 LC6 15 ARG c5449  CLA c5497  PHE i5023                               
SITE     1 LC7 12 LEU c5165  ILE c5243  GLY c5247  TRP c5250                    
SITE     2 LC7 12 HIS c5251  PRO c5256  PHE c5257  TRP c5259                    
SITE     3 LC7 12 PHE c5264  CLA c5497  BCR c5506  LEU i5024                    
SITE     1 LC8 14 MET c5157  LEU c5161  HIS c5164  LEU c5168                    
SITE     2 LC8 14 PHE c5264  TRP c5266  TYR c5271  TYR c5274                    
SITE     3 LC8 14 SER c5275  LEU c5279  MET c5282  CLA c5495                    
SITE     4 LC8 14 CLA c5496  CLA c5499                                          
SITE     1 LC9 16 LHG a5567  TRP c5036  ALA c5037  ASN c5039                    
SITE     2 LC9 16 ALA c5040  GLU c5269  LEU c5272  LEU c5276                    
SITE     3 LC9 16 PHE c5436  PHE c5437  GLY c5440  TRP c5443                    
SITE     4 LC9 16 HIS c5444  ARG c5447  CLA c5499  CLA c5500                    
SITE     1 MC1 11 ASN c5039  LEU c5049  ALA c5052  HIS c5053                    
SITE     2 MC1 11 HIS c5056  GLU c5269  LEU c5272  SER c5275                    
SITE     3 MC1 11 CLA c5497  CLA c5498  CLA c5500                               
SITE     1 MC2 14 ASN c5039  HIS c5056  LEU c5059  LEU c5279                    
SITE     2 MC2 14 PHE c5436  PHE c5437  CLA c5492  CLA c5493                    
SITE     3 MC2 14 CLA c5494  CLA c5498  CLA c5499  PRO k5029                    
SITE     4 MC2 14 VAL k5030  LEU k5033                                          
SITE     1 MC3 18 ASP c5027  TRP c5035  GLY c5038  ASN c5039                    
SITE     2 MC3 18 ARG c5041  LEU c5042  LEU c5045  LYS c5048                    
SITE     3 MC3 18 ALA c5052  PHE c5127  ALA c5133  ILE c5134                    
SITE     4 MC3 18 BCR c5504  TRP k5039  GLN k5040  UNK x5031                    
SITE     5 MC3 18 VAL z5020  PRO z5024                                          
SITE     1 MC4 10 HIS c5053  PHE c5147  PHE c5163  HIS c5164                    
SITE     2 MC4 10 VAL c5167  LEU c5168  GLY c5171  CLA c5493                    
SITE     3 MC4 10 CLA c5503  BCR c5505                                          
SITE     1 MC5 10 LEU c5050  VAL c5124  GLY c5128  TYR c5131                    
SITE     2 MC5 10 HIS c5132  PRO c5137  LEU c5140  PHE c5147                    
SITE     3 MC5 10 CLA c5502  BCR c5505                                          
SITE     1 MC6 12 ILE e5013  ARG e5018  TYR e5019  HIS e5023                    
SITE     2 MC6 12 THR e5026  ILE e5027  ARG f5019  TRP f5020                    
SITE     3 MC6 12 HIS f5024  ALA f5027  ILE f5031  UNK x5116                    
SITE     1 MC7 12 ALA v5062  CYS v5063  CYS v5066  HIS v5067                    
SITE     2 MC7 12 THR v5074  LEU v5078  ASP v5079  LEU v5080                    
SITE     3 MC7 12 THR v5084  TYR v5101  TYR v5108  HIS v5118                    
SITE     1 MC8 12 UNK c5474  LEU d5209  LEU d5210  HIS d5214                    
SITE     2 MC8 12 THR d5217  TRP d5253  ALA d5260  PHE d5261                    
SITE     3 MC8 12 LEU d5267  PHE d5270  VAL d5274  THR d5277                    
SITE     1 MC9  9 HIS a5215  LEU a5218  ALA a5251  HIS a5252                    
SITE     2 MC9  9 PHE a5255  SER a5264  PHE a5265  LEU a5271                    
SITE     3 MC9  9 PHE a5274                                                     
SITE     1 NC1  7 ASP a5170  GLU a5189  HIS a5332  GLU a5333                    
SITE     2 NC1  7 ASP a5342  ALA a5344  GLU c5354                               
SITE     1 NC2  6 ILE a5038  ALA a5043  ALA a5051  ALA a5054                    
SITE     2 NC2  6 TRP a5105  PHE i5015                                          
SITE     1 NC3  9 PHE T  19  BCR T5104  MET b5025  LEU b5029                    
SITE     2 NC3  9 TRP b5115  CLA b5523  CLA b5524  BCR b5528                    
SITE     3 NC3  9 MGE b5530                                                     
SITE     1 NC4 16 SQD A5212  ILE T   4  PHE T   8  ALA T  11                    
SITE     2 NC4 16 ALA T  15  PHE T  17  PHE T  18  ILE T  21                    
SITE     3 NC4 16 PHE T  22  TRP b5033  SER b5036  MET b5037                    
SITE     4 NC4 16 LEU b5109  CLA b5517  BCR b5527  BCR b5528                    
SITE     1 NC5 10 LMT T 217  BCR T5104  LEU b5029  GLY b5032                    
SITE     2 NC5 10 TRP b5033  SER b5036  ILE b5101  VAL b5102                    
SITE     3 NC5 10 CLA b5523  BCR b5527                                          
SITE     1 NC6  8 SQD A5212  PHE T  18  PHE T  22  LEU b5106                    
SITE     2 NC6  8 CYS b5112  VAL b5116  TYR b5117  CLA b5516                    
SITE     1 NC7  6 CLA b5511  CLA b5519  PHE h5038  PHE h5041                    
SITE     2 NC7  6 UNK x5052  UNK x5057                                          
SITE     1 NC8 15 TYR d5042  LEU d5043  GLY d5046  GLY d5047                    
SITE     2 NC8 15 LEU d5049  THR d5050  PHE d5101  PHE d5113                    
SITE     3 NC8 15 CLA d5355  PRO f5029  THR f5030  PHE f5033                    
SITE     4 NC8 15 ILE f5037  VAL j5021  VAL j5025                               
SITE     1 NC9 14 BCR c5504  ALA j5014  THR j5015  GLY j5018                    
SITE     2 NC9 14 MET j5019  LEU k5021  LEU k5031  ALA k5034                    
SITE     3 NC9 14 PHE k5037  VAL k5038  UNK x5013  UNK x5014                    
SITE     4 NC9 14 UNK x5017  VAL z5013                                          
SITE     1 OC1 14 ALA c5055  GLY c5058  LEU c5059  VAL c5116                    
SITE     2 OC1 14 LEU c5119  SER c5122  ALA c5123  CLA c5501                    
SITE     3 OC1 14 BCR c5505  TYR k5015  PHE k5018  PHE k5032                    
SITE     4 OC1 14 ALA k5036  BCR x5130                                          
SITE     1 OC2 11 PHE c5112  VAL c5116  ILE c5120  SER c5121                    
SITE     2 OC2 11 VAL c5124  LEU c5125  CLA c5502  CLA c5503                    
SITE     3 OC2 11 BCR c5504  TYR k5015  GLY z5055                               
SITE     1 OC3 12 ILE c5209  TYR c5212  ILE c5224  VAL c5227                    
SITE     2 OC3 12 ASP c5232  HIS c5237  PHE c5264  CLA c5491                    
SITE     3 OC3 12 CLA c5496  VAL i5020  PHE i5023  LEU i5024                    
SITE     1 OC4 11 PHE a5093  TRP a5097  LEU a5121  CLA a5563                    
SITE     2 OC4 11 SER c5216  PHE c5218  TRP c5223  MET c5281                    
SITE     3 OC4 11 PHE c5284  LYS i5005  TYR i5009                               
SITE     1 OC5 17 PHE a5155  ILE a5160  ILE a5163  PRO c5217                    
SITE     2 OC5 17 PHE c5218  GLY c5219  GLY c5220  GLY c5222                    
SITE     3 OC5 17 VAL c5225  SER c5226  ASN c5228  PHE c5284                    
SITE     4 OC5 17 CYS c5288  PHE c5292  ASN c5294  ARG c5362                    
SITE     5 OC5 17 LEU c5438                                                     
SITE     1 OC6 15 ARG a5140  TRP a5142  PHE a5273  TRP c5036                    
SITE     2 OC6 15 PHE c5436  TRP c5443  ARG c5447  CLA c5498                    
SITE     3 OC6 15 GLU d5219  ASN d5220  ALA d5229  SER d5230                    
SITE     4 OC6 15 THR d5231  PHE d5232  SQD d5358                               
SITE     1 OC7  9 ASN a5267  SER a5270  PHE a5274  LHG a5567                    
SITE     2 OC7  9 GLU c5029  TRP c5036  SER d5230  PHE d5232                    
SITE     3 OC7  9 ARG d5233                                                     
SITE     1 OC8 14 PHE a5197  GLU c5083  GLN c5084  GLY c5085                    
SITE     2 OC8 14 SER c5406  ASN c5418  PHE c5419  VAL c5420                    
SITE     3 OC8 14 TRP c5425  THR c5428  UNK c5479  CLA c5494                    
SITE     4 OC8 14 DGD c5509  TYR j5033                                          
SITE     1 OC9 20 GLN a5199  LEU a5200  PHE a5300  ASN a5301                    
SITE     2 OC9 20 SER a5305  CLA a5560  ASN c5405  VAL c5407                    
SITE     3 OC9 20 ASN c5415  SER c5416  ASN c5418  DGD c5508                    
SITE     4 OC9 20 MGE d5359  PHE j5029  ALA j5032  TYR j5033                    
SITE     5 OC9 20 GLY j5037  SER j5038  SER j5039  GLN v5060                    
SITE     1 PC1 12 CLA a5560  DGD c5509  TYR d5067  GLY d5070                    
SITE     2 PC1 12 CYS d5071  PHE d5073  CLA d5354  THR f5030                    
SITE     3 PC1 12 GLN f5041  GLY j5031  ALA j5032  GLY j5037                    
SITE     1 PC2 14 TYR b5193  PHE b5250  TYR b5258  TYR b5273                    
SITE     2 PC2 14 SER b5277  PHE b5463  HIS d5087  ILE d5123                    
SITE     3 PC2 14 LEU d5162  SER d5165  TYR h5049  VAL h5060                    
SITE     4 PC2 14 SER h5061  TRP h5062                                          
SITE     1 PC3 12 TRP b5005  TYR b5006  ARG b5007  PHE b5464                    
SITE     2 PC3 12 TRP b5468  CLA b5521  CLA b5523  ARG d5139                    
SITE     3 PC3 12 TYR d5141  PHE d5269  PHE d5273  MGE l5210                    
SITE     1 PC4 14 SER a5232  ASN a5234  CLA a5559  TRP b5005                    
SITE     2 PC4 14 TYR b5006  CLA b5524  UNK c5474  TRP d5266                    
SITE     3 PC4 14 PHE d5270  PHE d5273  MGE d5360  GLU l5011                    
SITE     4 PC4 14 SER l5016  GLY l5020                                          
SITE     1 PC5 16 CLA a5558  CLA a5559  ILE d5259  ALA d5260                    
SITE     2 PC5 16 PHE d5261  SER d5262  ASN d5263  TRP d5266                    
SITE     3 PC5 16 PHE d5270  ASN l5013  THR l5015  TYR l5018                    
SITE     4 PC5 16 LEU l5019  PHE t5010  PHE t5017  ALA t5020                    
SITE     1 PC6  8 TRP A  20  ASN A  26  ARG A  27  LEU A  28                    
SITE     2 PC6  8 BCR T5104  TRP b5113  TYR b5117  BCR b5529                    
SITE     1 PC7  8 ARG L  14  TYR L  18  LEU L  21  PHE T  19                    
SITE     2 PC7  8 PHE T  23  ARG b5018  LEU b5029  SER b5104                    
SITE     1 PC8 11 THR b5327  GLY b5328  PRO b5329  LYS b5332                    
SITE     2 PC8 11 PHE b5453  CLA b5517  BCR b5527  PHE l5035                    
SITE     3 PC8 11 LMT m 216  ASN m5004  LEU m5006                               
SITE     1 PC9 11 ALA B  43  LEU B  98  ILE a5050  LEU a5072                    
SITE     2 PC9 11 TYR a5073  UNK c5488  UNK c5489  ARG d5304                    
SITE     3 PC9 11 GLY o5139  GLU o5140  LMT t5217                               
SITE     1 QC1  9 TYR B  40  MGE B 530  GLN M   5  LEU M   6                    
SITE     2 QC1  9 LMT m 216  MET m5001  MET t5001  ILE t5004                    
SITE     3 QC1  9 LMT t5217                                                     
SITE     1 QC2  8 TYR B  40  ALA B  43  THR B  44  LMT M5216                    
SITE     2 QC2  8 LEU a5072  LMT a5568  MET t5001  ILE t5004                    
CRYST1  127.692  225.403  306.106  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007831  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004436  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003267        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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