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Database: PDB
Entry: 4IXR
LinkDB: 4IXR
Original site: 4IXR 
HEADER    PHOTOSYNTHESIS                          27-JAN-13   4IXR              
TITLE     RT FS X-RAY DIFFRACTION OF PHOTOSYSTEM II, FIRST ILLUMINATED STATE    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOTOSYSTEM Q(B) PROTEIN 1;                                
COMPND   3 CHAIN: A, a;                                                         
COMPND   4 SYNONYM: 32 KDA THYLAKOID MEMBRANE PROTEIN 1, PHOTOSYSTEM II PROTEIN 
COMPND   5 D1 1;                                                                
COMPND   6 EC: 1.10.3.9;                                                        
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PHOTOSYSTEM II CORE LIGHT HARVESTING PROTEIN;              
COMPND   9 CHAIN: B, b;                                                         
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: PHOTOSYSTEM II CP43 PROTEIN;                               
COMPND  12 CHAIN: C, c;                                                         
COMPND  13 MOL_ID: 4;                                                           
COMPND  14 MOLECULE: PHOTOSYSTEM II D2 PROTEIN;                                 
COMPND  15 CHAIN: D, d;                                                         
COMPND  16 SYNONYM: PSII D2 PROTEIN, PHOTOSYSTEM Q(A) PROTEIN;                  
COMPND  17 EC: 1.10.3.9;                                                        
COMPND  18 MOL_ID: 5;                                                           
COMPND  19 MOLECULE: CYTOCHROME B559 SUBUNIT ALPHA;                             
COMPND  20 CHAIN: E, e;                                                         
COMPND  21 SYNONYM: PSII REACTION CENTER SUBUNIT V;                             
COMPND  22 MOL_ID: 6;                                                           
COMPND  23 MOLECULE: CYTOCHROME B559 SUBUNIT BETA;                              
COMPND  24 CHAIN: F, f;                                                         
COMPND  25 SYNONYM: PSII REACTION CENTER SUBUNIT VI;                            
COMPND  26 MOL_ID: 7;                                                           
COMPND  27 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN H;                  
COMPND  28 CHAIN: H, h;                                                         
COMPND  29 SYNONYM: PSII-H;                                                     
COMPND  30 MOL_ID: 8;                                                           
COMPND  31 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN I;                  
COMPND  32 CHAIN: I, i;                                                         
COMPND  33 SYNONYM: PSII-I, PSII 4.4 KDA PROTEIN;                               
COMPND  34 MOL_ID: 9;                                                           
COMPND  35 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN J;                  
COMPND  36 CHAIN: J, j;                                                         
COMPND  37 SYNONYM: PSII-J;                                                     
COMPND  38 MOL_ID: 10;                                                          
COMPND  39 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN K;                  
COMPND  40 CHAIN: K, k;                                                         
COMPND  41 SYNONYM: PSII-K;                                                     
COMPND  42 MOL_ID: 11;                                                          
COMPND  43 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN L;                  
COMPND  44 CHAIN: L, l;                                                         
COMPND  45 SYNONYM: PSII-L, PSII 5 KDA PROTEIN;                                 
COMPND  46 MOL_ID: 12;                                                          
COMPND  47 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN M;                  
COMPND  48 CHAIN: M, m;                                                         
COMPND  49 SYNONYM: PSII-M;                                                     
COMPND  50 MOL_ID: 13;                                                          
COMPND  51 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;          
COMPND  52 CHAIN: O, o;                                                         
COMPND  53 SYNONYM: MSP;                                                        
COMPND  54 MOL_ID: 14;                                                          
COMPND  55 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN T;                  
COMPND  56 CHAIN: T, t;                                                         
COMPND  57 SYNONYM: PSII-T, PSII-TC;                                            
COMPND  58 MOL_ID: 15;                                                          
COMPND  59 MOLECULE: PHOTOSYSTEM II 12 KDA EXTRINSIC PROTEIN;                   
COMPND  60 CHAIN: U, u;                                                         
COMPND  61 SYNONYM: PS II COMPLEX 12 KDA EXTRINSIC PROTEIN, PSII-U;             
COMPND  62 MOL_ID: 16;                                                          
COMPND  63 MOLECULE: CYTOCHROME C-550;                                          
COMPND  64 CHAIN: V, v;                                                         
COMPND  65 SYNONYM: CYTOCHROME C-549, CYTOCHROME C550, LOW-POTENTIAL CYTOCHROME 
COMPND  66 C;                                                                   
COMPND  67 MOL_ID: 17;                                                          
COMPND  68 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN YCF12;              
COMPND  69 CHAIN: y, g;                                                         
COMPND  70 MOL_ID: 18;                                                          
COMPND  71 MOLECULE: PHOTOSYSTEM II REACTION CENTER X PROTEIN;                  
COMPND  72 CHAIN: X, x;                                                         
COMPND  73 MOL_ID: 19;                                                          
COMPND  74 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Z;                  
COMPND  75 CHAIN: Z, z;                                                         
COMPND  76 SYNONYM: PSII-Z;                                                     
COMPND  77 MOL_ID: 20;                                                          
COMPND  78 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Y;                  
COMPND  79 CHAIN: G, Y;                                                         
COMPND  80 FRAGMENT: SEE REMARK 999                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE   3 ORGANISM_TAXID: 146786;                                              
SOURCE   4 STRAIN: BP-1;                                                        
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE   7 ORGANISM_TAXID: 146786;                                              
SOURCE   8 STRAIN: BP-1;                                                        
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  11 ORGANISM_TAXID: 146786;                                              
SOURCE  12 STRAIN: BP-1;                                                        
SOURCE  13 MOL_ID: 4;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  15 ORGANISM_TAXID: 146786;                                              
SOURCE  16 STRAIN: BP-1;                                                        
SOURCE  17 MOL_ID: 5;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  19 ORGANISM_TAXID: 146786;                                              
SOURCE  20 STRAIN: BP-1;                                                        
SOURCE  21 MOL_ID: 6;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  23 ORGANISM_TAXID: 146786;                                              
SOURCE  24 STRAIN: BP-1;                                                        
SOURCE  25 MOL_ID: 7;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  27 ORGANISM_TAXID: 146786;                                              
SOURCE  28 STRAIN: BP-1;                                                        
SOURCE  29 MOL_ID: 8;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  31 ORGANISM_TAXID: 146786;                                              
SOURCE  32 STRAIN: BP-1;                                                        
SOURCE  33 MOL_ID: 9;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  35 ORGANISM_TAXID: 146786;                                              
SOURCE  36 STRAIN: BP-1;                                                        
SOURCE  37 MOL_ID: 10;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  39 ORGANISM_TAXID: 146786;                                              
SOURCE  40 STRAIN: BP-1;                                                        
SOURCE  41 MOL_ID: 11;                                                          
SOURCE  42 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  43 ORGANISM_TAXID: 146786;                                              
SOURCE  44 STRAIN: BP-1;                                                        
SOURCE  45 MOL_ID: 12;                                                          
SOURCE  46 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  47 ORGANISM_TAXID: 146786;                                              
SOURCE  48 STRAIN: BP-1;                                                        
SOURCE  49 MOL_ID: 13;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  51 ORGANISM_TAXID: 146786;                                              
SOURCE  52 STRAIN: BP-1;                                                        
SOURCE  53 MOL_ID: 14;                                                          
SOURCE  54 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  55 ORGANISM_TAXID: 146786;                                              
SOURCE  56 STRAIN: BP-1;                                                        
SOURCE  57 MOL_ID: 15;                                                          
SOURCE  58 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  59 ORGANISM_TAXID: 146786;                                              
SOURCE  60 STRAIN: BP-1;                                                        
SOURCE  61 MOL_ID: 16;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  63 ORGANISM_TAXID: 146786;                                              
SOURCE  64 STRAIN: BP-1;                                                        
SOURCE  65 MOL_ID: 17;                                                          
SOURCE  66 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  67 ORGANISM_TAXID: 146786;                                              
SOURCE  68 STRAIN: BP-1;                                                        
SOURCE  69 MOL_ID: 18;                                                          
SOURCE  70 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  71 ORGANISM_TAXID: 146786;                                              
SOURCE  72 STRAIN: BP-1;                                                        
SOURCE  73 MOL_ID: 19;                                                          
SOURCE  74 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  75 ORGANISM_TAXID: 146786;                                              
SOURCE  76 STRAIN: BP-1;                                                        
SOURCE  77 MOL_ID: 20;                                                          
SOURCE  78 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  79 ORGANISM_TAXID: 146786;                                              
SOURCE  80 STRAIN: BP-1                                                         
KEYWDS    IRON, MANGANESE, PS II, PS2, TRANSMEMBRANE ALPHA-HELIX, ELECTRON      
KEYWDS   2 TRANSPORT, REACTION CENTER, WATER OXIDATION, MEMBRANE COMPLEX,       
KEYWDS   3 THYLAKOID MEMBRANE, PHOTOSYNTHESIS                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.KERN,R.ALONSO-MORI,R.TRAN,J.HATTNE,R.J.GILDEA,N.ECHOLS,C.GLOECKNER, 
AUTHOR   2 J.HELLMICH,H.LAKSMONO,R.G.SIERRA,B.LASSALLE-KAISER,S.KOROIDOV,       
AUTHOR   3 A.LAMPE,G.HAN,S.GUL,D.DIFIORE,D.MILATHIANAKI,A.R.FRY,A.MIAHNAHRI,    
AUTHOR   4 D.W.SCHAFER,M.MESSERSCHMIDT,M.M.SEIBERT,J.E.KOGLIN,D.SOKARAS,T.-     
AUTHOR   5 C.WENG,J.SELLBERG,M.J.LATIMER,R.W.GROSSE-KUNSTLEVE,P.H.ZWART,        
AUTHOR   6 W.E.WHITE,P.GLATZEL,P.D.ADAMS,M.J.BOGAN,G.J.WILLIAMS,S.BOUTET,       
AUTHOR   7 J.MESSINGER,A.ZOUNI,N.K.SAUTER,V.K.YACHANDRA,U.BERGMANN,J.YANO       
REVDAT   3   08-MAY-13 4IXR    1       JRNL                                     
REVDAT   2   27-FEB-13 4IXR    1       JRNL                                     
REVDAT   1   20-FEB-13 4IXR    0                                                
JRNL        AUTH   J.KERN,R.ALONSO-MORI,R.TRAN,J.HATTNE,R.J.GILDEA,N.ECHOLS,    
JRNL        AUTH 2 C.GLOCKNER,J.HELLMICH,H.LAKSMONO,R.G.SIERRA,                 
JRNL        AUTH 3 B.LASSALLE-KAISER,S.KOROIDOV,A.LAMPE,G.HAN,S.GUL,D.DIFIORE,  
JRNL        AUTH 4 D.MILATHIANAKI,A.R.FRY,A.MIAHNAHRI,D.W.SCHAFER,              
JRNL        AUTH 5 M.MESSERSCHMIDT,M.M.SEIBERT,J.E.KOGLIN,D.SOKARAS,T.C.WENG,   
JRNL        AUTH 6 J.SELLBERG,M.J.LATIMER,R.W.GROSSE-KUNSTLEVE,P.H.ZWART,       
JRNL        AUTH 7 W.E.WHITE,P.GLATZEL,P.D.ADAMS,M.J.BOGAN,G.J.WILLIAMS,        
JRNL        AUTH 8 S.BOUTET,J.MESSINGER,A.ZOUNI,N.K.SAUTER,V.K.YACHANDRA,       
JRNL        AUTH 9 U.BERGMANN,J.YANO                                            
JRNL        TITL   SIMULTANEOUS FEMTOSECOND X-RAY SPECTROSCOPY AND DIFFRACTION  
JRNL        TITL 2 OF PHOTOSYSTEM II AT ROOM TEMPERATURE.                       
JRNL        REF    SCIENCE                       V. 340   491 2013              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   23413188                                                     
JRNL        DOI    10.1126/SCIENCE.1234273                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    5.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_1265)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 5.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 82.97                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.400                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 24668                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.286                           
REMARK   3   R VALUE            (WORKING SET) : 0.285                           
REMARK   3   FREE R VALUE                     : 0.313                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.860                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1200                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 82.9785 - 12.2613    1.00     2827   130  0.3373 0.3108        
REMARK   3     2 12.2613 -  9.7370    1.00     2691   140  0.2773 0.2964        
REMARK   3     3  9.7370 -  8.5076    1.00     2646   135  0.2487 0.2931        
REMARK   3     4  8.5076 -  7.7304    1.00     2623   137  0.2510 0.2633        
REMARK   3     5  7.7304 -  7.1766    1.00     2633   140  0.2625 0.3398        
REMARK   3     6  7.1766 -  6.7537    1.00     2616   129  0.2723 0.3099        
REMARK   3     7  6.7537 -  6.4156    0.99     2567   135  0.2937 0.3243        
REMARK   3     8  6.4156 -  6.1364    0.99     2578   132  0.3009 0.3452        
REMARK   3     9  6.1364 -  5.9000    0.88     2287   122  0.3047 0.3887        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.920            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.520           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005          52048                                  
REMARK   3   ANGLE     :  1.025          71500                                  
REMARK   3   CHIRALITY :  0.052           7286                                  
REMARK   3   PLANARITY :  0.005           8770                                  
REMARK   3   DIHEDRAL  : 18.513          18416                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4IXR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB077342.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-DEC-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1848                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : FREE ELECTRON LASER                
REMARK 200  BEAMLINE                       : CXI                                
REMARK 200  X-RAY GENERATOR MODEL          : SLAC LCLS BEAMLINE CXI             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2967, 1.7547                     
REMARK 200  MONOCHROMATOR                  : NO MONOCHROMATOR, FEL BEAM WITH    
REMARK 200                                   20-30 EV BANDWIDTH                 
REMARK 200  OPTICS                         : KB MIRRORS                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : CORNELL-SLAC PIXEL ARRAY           
REMARK 200                                   DETECTOR (CSPAD)                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CCTBX.XFEL                         
REMARK 200  DATA SCALING SOFTWARE          : CCTBX.XFEL                         
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24671                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 5.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 83.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 4.200                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 22.900                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 5.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 6.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3BZ1                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 4% PEG2000, 5 MM CALCIUM CHLORIDE, 100   
REMARK 280  MM PIPES, 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       65.98800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      153.49700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      113.78400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      153.49700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       65.98800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      113.78400            
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: 40-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, I, J,            
REMARK 350                    AND CHAINS: K, L, M, O, T, U, V, y, X,            
REMARK 350                    AND CHAINS: Z, G, a, b, c, d, e, f, h,            
REMARK 350                    AND CHAINS: i, j, k, l, m, o, t, u, v,            
REMARK 350                    AND CHAINS: g, x, z, Y                            
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     SER A   345                                                      
REMARK 465     ALA A   346                                                      
REMARK 465     GLU A   347                                                      
REMARK 465     SER A   348                                                      
REMARK 465     ALA A   349                                                      
REMARK 465     PRO A   350                                                      
REMARK 465     VAL A   351                                                      
REMARK 465     ALA A   352                                                      
REMARK 465     MET A   353                                                      
REMARK 465     ILE A   354                                                      
REMARK 465     ALA A   355                                                      
REMARK 465     PRO A   356                                                      
REMARK 465     SER A   357                                                      
REMARK 465     ILE A   358                                                      
REMARK 465     ASN A   359                                                      
REMARK 465     GLY A   360                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B   492                                                      
REMARK 465     TRP B   493                                                      
REMARK 465     GLY B   494                                                      
REMARK 465     PHE B   495                                                      
REMARK 465     TYR B   496                                                      
REMARK 465     GLN B   497                                                      
REMARK 465     LYS B   498                                                      
REMARK 465     VAL B   499                                                      
REMARK 465     GLY B   500                                                      
REMARK 465     ASP B   501                                                      
REMARK 465     VAL B   502                                                      
REMARK 465     THR B   503                                                      
REMARK 465     THR B   504                                                      
REMARK 465     ARG B   505                                                      
REMARK 465     ARG B   506                                                      
REMARK 465     LYS B   507                                                      
REMARK 465     GLU B   508                                                      
REMARK 465     ALA B   509                                                      
REMARK 465     VAL B   510                                                      
REMARK 465     MET C    13                                                      
REMARK 465     VAL C    14                                                      
REMARK 465     THR C    15                                                      
REMARK 465     LEU C    16                                                      
REMARK 465     SER C    17                                                      
REMARK 465     SER C    18                                                      
REMARK 465     ASN C    19                                                      
REMARK 465     SER C    20                                                      
REMARK 465     ILE C    21                                                      
REMARK 465     PHE C    22                                                      
REMARK 465     ALA C    23                                                      
REMARK 465     THR C    24                                                      
REMARK 465     ASN C    25                                                      
REMARK 465     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     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     MET K     1                                                      
REMARK 465     ILE K     2                                                      
REMARK 465     ASP K     3                                                      
REMARK 465     ALA K     4                                                      
REMARK 465     LEU K     5                                                      
REMARK 465     VAL K     6                                                      
REMARK 465     LEU K     7                                                      
REMARK 465     VAL K     8                                                      
REMARK 465     ALA K     9                                                      
REMARK 465     SER M    35                                                      
REMARK 465     SER M    36                                                      
REMARK 465     MET O     1                                                      
REMARK 465     LYS O     2                                                      
REMARK 465     TYR O     3                                                      
REMARK 465     ARG O     4                                                      
REMARK 465     ILE O     5                                                      
REMARK 465     LEU O     6                                                      
REMARK 465     MET O     7                                                      
REMARK 465     ALA O     8                                                      
REMARK 465     THR O     9                                                      
REMARK 465     LEU O    10                                                      
REMARK 465     LEU O    11                                                      
REMARK 465     ALA O    12                                                      
REMARK 465     VAL O    13                                                      
REMARK 465     CYS O    14                                                      
REMARK 465     LEU O    15                                                      
REMARK 465     GLY O    16                                                      
REMARK 465     ILE O    17                                                      
REMARK 465     PHE O    18                                                      
REMARK 465     SER O    19                                                      
REMARK 465     LEU O    20                                                      
REMARK 465     SER O    21                                                      
REMARK 465     ALA O    22                                                      
REMARK 465     PRO O    23                                                      
REMARK 465     ALA O    24                                                      
REMARK 465     PHE O    25                                                      
REMARK 465     ALA O    26                                                      
REMARK 465     ALA O    27                                                      
REMARK 465     LYS O    28                                                      
REMARK 465     GLN O    29                                                      
REMARK 465     MET U     1                                                      
REMARK 465     GLN U     2                                                      
REMARK 465     ARG U     3                                                      
REMARK 465     LEU U     4                                                      
REMARK 465     GLY U     5                                                      
REMARK 465     ARG U     6                                                      
REMARK 465     TRP U     7                                                      
REMARK 465     LEU U     8                                                      
REMARK 465     ALA U     9                                                      
REMARK 465     LEU U    10                                                      
REMARK 465     ALA U    11                                                      
REMARK 465     TYR U    12                                                      
REMARK 465     PHE U    13                                                      
REMARK 465     VAL U    14                                                      
REMARK 465     GLY U    15                                                      
REMARK 465     VAL U    16                                                      
REMARK 465     SER U    17                                                      
REMARK 465     LEU U    18                                                      
REMARK 465     LEU U    19                                                      
REMARK 465     GLY U    20                                                      
REMARK 465     TRP U    21                                                      
REMARK 465     ILE U    22                                                      
REMARK 465     ASN U    23                                                      
REMARK 465     TRP U    24                                                      
REMARK 465     SER U    25                                                      
REMARK 465     ALA U    26                                                      
REMARK 465     PRO U    27                                                      
REMARK 465     THR U    28                                                      
REMARK 465     LEU U    29                                                      
REMARK 465     ALA U    30                                                      
REMARK 465     ALA U    31                                                      
REMARK 465     THR U    32                                                      
REMARK 465     ALA U    33                                                      
REMARK 465     SER U    34                                                      
REMARK 465     THR U    35                                                      
REMARK 465     GLU U    36                                                      
REMARK 465     GLU U    37                                                      
REMARK 465     MET V     1                                                      
REMARK 465     LEU V     2                                                      
REMARK 465     LYS V     3                                                      
REMARK 465     LYS V     4                                                      
REMARK 465     CYS V     5                                                      
REMARK 465     VAL V     6                                                      
REMARK 465     TRP V     7                                                      
REMARK 465     LEU V     8                                                      
REMARK 465     ALA V     9                                                      
REMARK 465     VAL V    10                                                      
REMARK 465     ALA V    11                                                      
REMARK 465     LEU V    12                                                      
REMARK 465     CYS V    13                                                      
REMARK 465     LEU V    14                                                      
REMARK 465     CYS V    15                                                      
REMARK 465     LEU V    16                                                      
REMARK 465     TRP V    17                                                      
REMARK 465     GLN V    18                                                      
REMARK 465     PHE V    19                                                      
REMARK 465     THR V    20                                                      
REMARK 465     MET V    21                                                      
REMARK 465     GLY V    22                                                      
REMARK 465     THR V    23                                                      
REMARK 465     ALA V    24                                                      
REMARK 465     LEU V    25                                                      
REMARK 465     ALA V    26                                                      
REMARK 465     MET y     1                                                      
REMARK 465     GLY y     2                                                      
REMARK 465     ILE y     3                                                      
REMARK 465     PHE y     4                                                      
REMARK 465     ASN y     5                                                      
REMARK 465     GLY y     6                                                      
REMARK 465     ILE y     7                                                      
REMARK 465     ILE y     8                                                      
REMARK 465     GLU y     9                                                      
REMARK 465     PHE y    10                                                      
REMARK 465     LEU y    11                                                      
REMARK 465     SER y    12                                                      
REMARK 465     ASN y    13                                                      
REMARK 465     ILE y    14                                                      
REMARK 465     ASN y    15                                                      
REMARK 465     PHE y    16                                                      
REMARK 465     GLU y    17                                                      
REMARK 465     VAL y    18                                                      
REMARK 465     MET X    10                                                      
REMARK 465     ARG X    48                                                      
REMARK 465     SER X    49                                                      
REMARK 465     LEU X    50                                                      
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     SER a   345                                                      
REMARK 465     ALA a   346                                                      
REMARK 465     GLU a   347                                                      
REMARK 465     SER a   348                                                      
REMARK 465     ALA a   349                                                      
REMARK 465     PRO a   350                                                      
REMARK 465     VAL a   351                                                      
REMARK 465     ALA a   352                                                      
REMARK 465     MET a   353                                                      
REMARK 465     ILE a   354                                                      
REMARK 465     ALA a   355                                                      
REMARK 465     PRO a   356                                                      
REMARK 465     SER a   357                                                      
REMARK 465     ILE a   358                                                      
REMARK 465     ASN a   359                                                      
REMARK 465     GLY a   360                                                      
REMARK 465     MET b     1                                                      
REMARK 465     GLU b   492                                                      
REMARK 465     TRP b   493                                                      
REMARK 465     GLY b   494                                                      
REMARK 465     PHE b   495                                                      
REMARK 465     TYR b   496                                                      
REMARK 465     GLN b   497                                                      
REMARK 465     LYS b   498                                                      
REMARK 465     VAL b   499                                                      
REMARK 465     GLY b   500                                                      
REMARK 465     ASP b   501                                                      
REMARK 465     VAL b   502                                                      
REMARK 465     THR b   503                                                      
REMARK 465     THR b   504                                                      
REMARK 465     ARG b   505                                                      
REMARK 465     ARG b   506                                                      
REMARK 465     LYS b   507                                                      
REMARK 465     GLU b   508                                                      
REMARK 465     ALA b   509                                                      
REMARK 465     VAL b   510                                                      
REMARK 465     MET c    13                                                      
REMARK 465     VAL c    14                                                      
REMARK 465     THR c    15                                                      
REMARK 465     LEU c    16                                                      
REMARK 465     SER c    17                                                      
REMARK 465     SER c    18                                                      
REMARK 465     ASN c    19                                                      
REMARK 465     SER c    20                                                      
REMARK 465     ILE c    21                                                      
REMARK 465     PHE c    22                                                      
REMARK 465     ALA c    23                                                      
REMARK 465     THR c    24                                                      
REMARK 465     ASN c    25                                                      
REMARK 465     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     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     MET k     1                                                      
REMARK 465     ILE k     2                                                      
REMARK 465     ASP k     3                                                      
REMARK 465     ALA k     4                                                      
REMARK 465     LEU k     5                                                      
REMARK 465     VAL k     6                                                      
REMARK 465     LEU k     7                                                      
REMARK 465     VAL k     8                                                      
REMARK 465     ALA k     9                                                      
REMARK 465     SER m    35                                                      
REMARK 465     SER m    36                                                      
REMARK 465     MET o     1                                                      
REMARK 465     LYS o     2                                                      
REMARK 465     TYR o     3                                                      
REMARK 465     ARG o     4                                                      
REMARK 465     ILE o     5                                                      
REMARK 465     LEU o     6                                                      
REMARK 465     MET o     7                                                      
REMARK 465     ALA o     8                                                      
REMARK 465     THR o     9                                                      
REMARK 465     LEU o    10                                                      
REMARK 465     LEU o    11                                                      
REMARK 465     ALA o    12                                                      
REMARK 465     VAL o    13                                                      
REMARK 465     CYS o    14                                                      
REMARK 465     LEU o    15                                                      
REMARK 465     GLY o    16                                                      
REMARK 465     ILE o    17                                                      
REMARK 465     PHE o    18                                                      
REMARK 465     SER o    19                                                      
REMARK 465     LEU o    20                                                      
REMARK 465     SER o    21                                                      
REMARK 465     ALA o    22                                                      
REMARK 465     PRO o    23                                                      
REMARK 465     ALA o    24                                                      
REMARK 465     PHE o    25                                                      
REMARK 465     ALA o    26                                                      
REMARK 465     ALA o    27                                                      
REMARK 465     LYS o    28                                                      
REMARK 465     GLN o    29                                                      
REMARK 465     MET u     1                                                      
REMARK 465     GLN u     2                                                      
REMARK 465     ARG u     3                                                      
REMARK 465     LEU u     4                                                      
REMARK 465     GLY u     5                                                      
REMARK 465     ARG u     6                                                      
REMARK 465     TRP u     7                                                      
REMARK 465     LEU u     8                                                      
REMARK 465     ALA u     9                                                      
REMARK 465     LEU u    10                                                      
REMARK 465     ALA u    11                                                      
REMARK 465     TYR u    12                                                      
REMARK 465     PHE u    13                                                      
REMARK 465     VAL u    14                                                      
REMARK 465     GLY u    15                                                      
REMARK 465     VAL u    16                                                      
REMARK 465     SER u    17                                                      
REMARK 465     LEU u    18                                                      
REMARK 465     LEU u    19                                                      
REMARK 465     GLY u    20                                                      
REMARK 465     TRP u    21                                                      
REMARK 465     ILE u    22                                                      
REMARK 465     ASN u    23                                                      
REMARK 465     TRP u    24                                                      
REMARK 465     SER u    25                                                      
REMARK 465     ALA u    26                                                      
REMARK 465     PRO u    27                                                      
REMARK 465     THR u    28                                                      
REMARK 465     LEU u    29                                                      
REMARK 465     ALA u    30                                                      
REMARK 465     ALA u    31                                                      
REMARK 465     THR u    32                                                      
REMARK 465     ALA u    33                                                      
REMARK 465     SER u    34                                                      
REMARK 465     THR u    35                                                      
REMARK 465     GLU u    36                                                      
REMARK 465     GLU u    37                                                      
REMARK 465     MET v     1                                                      
REMARK 465     LEU v     2                                                      
REMARK 465     LYS v     3                                                      
REMARK 465     LYS v     4                                                      
REMARK 465     CYS v     5                                                      
REMARK 465     VAL v     6                                                      
REMARK 465     TRP v     7                                                      
REMARK 465     LEU v     8                                                      
REMARK 465     ALA v     9                                                      
REMARK 465     VAL v    10                                                      
REMARK 465     ALA v    11                                                      
REMARK 465     LEU v    12                                                      
REMARK 465     CYS v    13                                                      
REMARK 465     LEU v    14                                                      
REMARK 465     CYS v    15                                                      
REMARK 465     LEU v    16                                                      
REMARK 465     TRP v    17                                                      
REMARK 465     GLN v    18                                                      
REMARK 465     PHE v    19                                                      
REMARK 465     THR v    20                                                      
REMARK 465     MET v    21                                                      
REMARK 465     GLY v    22                                                      
REMARK 465     THR v    23                                                      
REMARK 465     ALA v    24                                                      
REMARK 465     LEU v    25                                                      
REMARK 465     ALA v    26                                                      
REMARK 465     MET g     1                                                      
REMARK 465     GLY g     2                                                      
REMARK 465     ILE g     3                                                      
REMARK 465     PHE g     4                                                      
REMARK 465     ASN g     5                                                      
REMARK 465     GLY g     6                                                      
REMARK 465     ILE g     7                                                      
REMARK 465     ILE g     8                                                      
REMARK 465     GLU g     9                                                      
REMARK 465     PHE g    10                                                      
REMARK 465     LEU g    11                                                      
REMARK 465     SER g    12                                                      
REMARK 465     ASN g    13                                                      
REMARK 465     ILE g    14                                                      
REMARK 465     ASN g    15                                                      
REMARK 465     PHE g    16                                                      
REMARK 465     GLU g    17                                                      
REMARK 465     VAL g    18                                                      
REMARK 465     MET x    10                                                      
REMARK 465     ARG x    48                                                      
REMARK 465     SER x    49                                                      
REMARK 465     LEU x    50                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     TYR C 143    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU C 462    CG   CD   OE1  OE2                                  
REMARK 470     LYS H  20    CG   CD   CE   NZ                                   
REMARK 470     ARG O  53    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU O  80    CG   CD   OE1  OE2                                  
REMARK 470     LYS O  85    CG   CD   CE   NZ                                   
REMARK 470     ARG O 233    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU V  41    CG   CD   OE1  OE2                                  
REMARK 470     ARG y  43    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR c 143    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU c 462    CG   CD   OE1  OE2                                  
REMARK 470     LYS h  20    CG   CD   CE   NZ                                   
REMARK 470     ARG o  53    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU o  80    CG   CD   OE1  OE2                                  
REMARK 470     LYS o  85    CG   CD   CE   NZ                                   
REMARK 470     ARG o 233    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU v  41    CG   CD   OE1  OE2                                  
REMARK 470     ARG g  43    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    TRP C   250     OG1  THR C   254              2.03            
REMARK 500   O    TRP C   291     OG1  THR C   305              2.05            
REMARK 500   O    TRP c   250     OG1  THR c   254              2.07            
REMARK 500   OD2  ASP u    56     OG1  THR u   115              2.16            
REMARK 500   O    TYR c   297     NH2  ARG c   423              2.18            
REMARK 500   OG   SER M    31     O    GLN m    28              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B 484   C   -  N   -  CA  ANGL. DEV. =  13.5 DEGREES          
REMARK 500    PRO b 484   C   -  N   -  CA  ANGL. DEV. =  14.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  12      110.38    138.24                                   
REMARK 500    PRO A 141     -128.15    -74.58                                   
REMARK 500    TRP A 142      -12.07     56.33                                   
REMARK 500    LEU A 159      -52.80   -130.69                                   
REMARK 500    ILE A 176      -72.31    -59.41                                   
REMARK 500    GLU A 226       12.08   -146.23                                   
REMARK 500    ILE A 259      -85.65   -103.84                                   
REMARK 500    SER A 305      -70.32    -77.35                                   
REMARK 500    ARG A 334      -73.22    -27.96                                   
REMARK 500    LEU A 343       44.29   -108.69                                   
REMARK 500    ASP B 119       56.01    -91.23                                   
REMARK 500    ARG B 127      -72.38    -61.53                                   
REMARK 500    PRO B 183      175.33    -58.08                                   
REMARK 500    LEU B 218      -69.67   -100.76                                   
REMARK 500    ARG B 230       52.39     27.20                                   
REMARK 500    ASP B 313       43.02    -91.26                                   
REMARK 500    SER B 480      -14.01     71.33                                   
REMARK 500    ILE B 482     -169.41   -117.24                                   
REMARK 500    PRO B 484     -158.98      3.49                                   
REMARK 500    GLU B 485      164.99     65.78                                   
REMARK 500    LEU B 486       70.86   -154.07                                   
REMARK 500    PRO B 488     -110.33      6.37                                   
REMARK 500    GLU B 489       57.71    -62.36                                   
REMARK 500    GLN B 490      109.04   -168.25                                   
REMARK 500    GLU C  29     -149.96   -148.63                                   
REMARK 500    SER C  46      -50.34    -27.40                                   
REMARK 500    ARG C 135      -63.67   -121.63                                   
REMARK 500    SER C 144      113.63    171.12                                   
REMARK 500    ASN C 201       61.53   -167.84                                   
REMARK 500    ILE C 209      -70.98    -50.63                                   
REMARK 500    TRP C 223     -145.06     60.98                                   
REMARK 500    PHE C 257     -147.53    -69.68                                   
REMARK 500    ARG C 320      -71.23    -59.77                                   
REMARK 500    LEU C 375      112.64    -29.24                                   
REMARK 500    ASN C 382       12.15   -159.40                                   
REMARK 500    HIS C 398       34.86   -140.33                                   
REMARK 500    SER C 406       65.33     61.43                                   
REMARK 500    ALA C 411      -17.70    -48.82                                   
REMARK 500    SER C 416      -62.52    176.84                                   
REMARK 500    ALA C 452      -70.44    -52.52                                   
REMARK 500    PHE C 455       23.97   -147.79                                   
REMARK 500    GLU C 462      -79.28    -67.29                                   
REMARK 500    ARG D  26     -165.99   -103.73                                   
REMARK 500    VAL D  30      -83.03    -90.10                                   
REMARK 500    LEU D  37      -70.90    -56.55                                   
REMARK 500    PRO D 140       38.24    -85.38                                   
REMARK 500    LEU D 158      -67.19   -128.24                                   
REMARK 500    ALA D 234       24.43    -72.90                                   
REMARK 500    GLN D 239     -116.54     22.74                                   
REMARK 500    ALA D 240     -138.64     65.04                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     250 RAMACHANDRAN OUTLIERS.                        
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     PL9 A  408                                                       
REMARK 610     OEC A  409                                                       
REMARK 610     DGD A  411                                                       
REMARK 610     LHG A  412                                                       
REMARK 610     SQD A  413                                                       
REMARK 610     LMG A  414                                                       
REMARK 610     LHG A  415                                                       
REMARK 610     LMG A  418                                                       
REMARK 610     DGD B  621                                                       
REMARK 610     LMG B  622                                                       
REMARK 610     LMG B  623                                                       
REMARK 610     SQD B  626                                                       
REMARK 610     DGD B  627                                                       
REMARK 610     DGD C  517                                                       
REMARK 610     DGD C  518                                                       
REMARK 610     LMG C  520                                                       
REMARK 610     LMG C  521                                                       
REMARK 610     LMG D  406                                                       
REMARK 610     LMG D  407                                                       
REMARK 610     SQD D  408                                                       
REMARK 610     DGD D  409                                                       
REMARK 610     LMT D  410                                                       
REMARK 610     LMG E  101                                                       
REMARK 610     SQD F  102                                                       
REMARK 610     LMG I  101                                                       
REMARK 610     PL9 J  101                                                       
REMARK 610     LMG M  101                                                       
REMARK 610     LMG a  402                                                       
REMARK 610     PL9 a  410                                                       
REMARK 610     OEC a  411                                                       
REMARK 610     DGD a  413                                                       
REMARK 610     LHG a  414                                                       
REMARK 610     SQD a  415                                                       
REMARK 610     LMG a  416                                                       
REMARK 610     LHG a  417                                                       
REMARK 610     SQD b  601                                                       
REMARK 610     DGD b  602                                                       
REMARK 610     DGD b  623                                                       
REMARK 610     LMG b  624                                                       
REMARK 610     LMG b  625                                                       
REMARK 610     DGD c  516                                                       
REMARK 610     DGD c  517                                                       
REMARK 610     LMG c  519                                                       
REMARK 610     LMG d  406                                                       
REMARK 610     LMG d  407                                                       
REMARK 610     SQD d  408                                                       
REMARK 610     DGD d  409                                                       
REMARK 610     LMT d  410                                                       
REMARK 610     LMG e  101                                                       
REMARK 610     SQD f  102                                                       
REMARK 610     LMG i  101                                                       
REMARK 610     PL9 j  101                                                       
REMARK 610     LMG k  103                                                       
REMARK 610     LMG m  102                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC A 409  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 189   OE2                                                    
REMARK 620 2 HIS A 332   NE2 113.4                                              
REMARK 620 3 ASP A 342   OD2  81.4  82.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC a 411  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 189   OE2                                                    
REMARK 620 2 HIS a 332   NE2  96.0                                              
REMARK 620 3 ASP a 342   OD2  69.7  78.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC a 411  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 333   OE1                                                    
REMARK 620 2 GLU c 354   OE2  83.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC A 409  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 333   OE1                                                    
REMARK 620 2 GLU C 354   OE2  84.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC a 411  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 170   OD2                                                    
REMARK 620 2 GLU a 333   OE2 159.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC a 411  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 342   OD1                                                    
REMARK 620 2 ALA a 344   O   118.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC A 409  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 342   OD1                                                    
REMARK 620 2 ALA A 344   O   113.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC A 409  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 170   OD2                                                    
REMARK 620 2 GLU A 333   OE2 154.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC A 409  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 189   OE1                                                    
REMARK 620 2 ASP A 170   OD1 159.3                                              
REMARK 620 3 ALA A 344   O   113.9  71.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 A 401  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 215   NE2                                                    
REMARK 620 2 HIS D 214   NE2 136.3                                              
REMARK 620 3 HIS A 272   NE2 108.6 100.7                                        
REMARK 620 4 HIS D 268   NE2  78.5  89.4 153.8                                  
REMARK 620 5 BCT A 402   O2   78.4 139.3  80.6  76.1                            
REMARK 620 6 BCT A 402   O3  127.3  87.3  82.8  73.5  52.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC a 411  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 189   OE1                                                    
REMARK 620 2 ASP a 170   OD1 164.0                                              
REMARK 620 3 ALA a 344   O   114.2  68.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 a 403  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS a 215   NE2                                                    
REMARK 620 2 HIS d 214   NE2 132.7                                              
REMARK 620 3 HIS d 268   NE2  82.8  87.3                                        
REMARK 620 4 BCT d 401   O2   79.6 143.0  78.7                                  
REMARK 620 5 HIS a 272   NE2 105.1 101.4 157.6  82.1                            
REMARK 620 6 BCT d 401   O3  130.0  90.3  73.9  53.0  85.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM V 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS V  67   NE2                                                    
REMARK 620 2 HEM V 201   NA   88.7                                              
REMARK 620 3 HEM V 201   NB   91.2  89.0                                        
REMARK 620 4 HEM V 201   NC   91.3 179.1  90.0                                  
REMARK 620 5 HEM V 201   ND   88.6  89.1 178.1  91.8                            
REMARK 620 6 HIS V 118   NE2 173.6  84.9  89.0  95.1  90.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM v 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS v  67   NE2                                                    
REMARK 620 2 HEM v 201   NA   87.4                                              
REMARK 620 3 HEM v 201   NB   89.8  87.2                                        
REMARK 620 4 HEM v 201   NC   92.4 177.9  90.8                                  
REMARK 620 5 HEM v 201   ND   89.9  91.2 178.4  90.9                            
REMARK 620 6 HIS v 118   NE2 170.3  83.3  86.9  96.8  93.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA k 101  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP k  19   OD2                                                    
REMARK 620 2 ASP k  23   OD2 124.7                                              
REMARK 620 3 ASP k  23   OD1 128.5  42.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM F 101  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  24   NE2                                                    
REMARK 620 2 HEM F 101   NA   72.9                                              
REMARK 620 3 HEM F 101   NB   75.9  88.6                                        
REMARK 620 4 HEM F 101   NC  106.8 178.4  89.8                                  
REMARK 620 5 HEM F 101   ND  104.0  91.0 179.6  90.6                            
REMARK 620 6 HIS E  23   NE2 154.3  81.4 103.3  98.9  76.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM f 101  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS e  23   NE2                                                    
REMARK 620 2 HEM f 101   NA   82.0                                              
REMARK 620 3 HEM f 101   NB  104.0  88.4                                        
REMARK 620 4 HEM f 101   NC   98.0 179.2  90.8                                  
REMARK 620 5 HEM f 101   ND   75.7  90.5 178.9  90.3                            
REMARK 620 6 HIS f  24   NE2 153.8  71.9  77.9 108.1 101.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA K 101  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP K  19   OD2                                                    
REMARK 620 2 ASP K  23   OD2 125.0                                              
REMARK 620 3 ASP K  23   OD1 126.3  43.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 511  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C  39   OD1                                                    
REMARK 620 2 CLA C 511   NA   94.9                                              
REMARK 620 3 CLA C 511   NB   73.5  92.2                                        
REMARK 620 4 CLA C 511   NC   85.5 176.6  91.2                                  
REMARK 620 5 CLA C 511   ND  105.9  91.0 176.8  85.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OEC A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR A 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD A 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG A 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD A 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG A 414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG A 415                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 416                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD A 417                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG A 418                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD B 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG B 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG B 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD B 626                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD B 627                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 628                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 629                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR C 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR C 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR C 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG C 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG C 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 D 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR D 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG D 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG D 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD D 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD D 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT D 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG E 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM F 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD F 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR H 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG I 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT I 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 J 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR J 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA K 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG M 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT M 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA O 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR T 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR T 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM V 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR y 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD a 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG a 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 a 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO a 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO a 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 a 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OEC a 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR a 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD a 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG a 414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD a 415                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG a 416                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG a 417                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL a 418                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD b 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD b 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT b 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT b 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR b 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR b 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD b 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG b 624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG b 625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT b 626                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT b 627                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR c 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR c 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD c 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD c 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD c 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG c 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT d 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA d 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA d 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 d 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR d 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG d 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG d 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD d 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD d 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT d 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG e 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM f 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD f 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR h 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG i 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT i 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 j 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR j 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA k 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR k 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG k 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT m 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG m 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA o 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM v 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR z 101                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4IXQ   RELATED DB: PDB                                   
REMARK 900 RT FS X-RAY DIFFRACTION OF PHOTOSYSTEM II, DARK STATE                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE OF CHAINS Y AND G IS KNOWN BUT WAS                      
REMARK 999 MODELED AS POLYALANINE DUE TO POOR DENSITY.                          
REMARK 999 THE ACTUAL SEQUENCE MATCHES UNIPROT REFERENCE Q8DKM3:                
REMARK 999 MET ASP TRP ARG VAL LEU VAL VAL LEU LEU PRO VAL LEU                  
REMARK 999 LEU ALA ALA GLY TRP ALA VAL ARG ASN ILE LEU PRO TYR                  
REMARK 999 ALA VAL LYS GLN VAL GLN LYS LEU LEU GLN LYS ALA LYS                  
REMARK 999 ALA ALA                                                              
DBREF  4IXR A    1   360  UNP    P0A444   PSBA1_THEEB      1    360             
DBREF  4IXR B    1   510  UNP    Q8DIQ1   Q8DIQ1_THEEB     1    510             
DBREF  4IXR C   13   473  UNP    Q8DIF8   Q8DIF8_THEEB     1    461             
DBREF  4IXR D    1   352  UNP    Q8CM25   PSBD_THEEB       1    352             
DBREF  4IXR E    1    84  UNP    Q8DIP0   PSBE_THEEB       1     84             
DBREF  4IXR F    1    45  UNP    Q8DIN9   PSBF_THEEB       1     45             
DBREF  4IXR H    1    66  UNP    Q8DJ43   PSBH_THEEB       1     66             
DBREF  4IXR I    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  4IXR J    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  4IXR K    1    46  UNP    Q9F1K9   PSBK_THEEB       1     46             
DBREF  4IXR L    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  4IXR M    1    36  UNP    Q8DHA7   PSBM_THEEB       1     36             
DBREF  4IXR O    1   272  UNP    P0A431   PSBO_THEEB       1    272             
DBREF  4IXR T    1    32  UNP    Q8DIQ0   PSBT_THEEB       1     32             
DBREF  4IXR U    1   134  UNP    Q9F1L5   PSBU_THEEB       1    134             
DBREF  4IXR V    1   163  UNP    P0A386   CY550_THEEB      1    163             
DBREF  4IXR y    1    46  UNP    Q8DJI1   YCF12_THEEB      1     46             
DBREF  4IXR X   10    50  UNP    Q9F1R6   PSBX_THEEB       1     41             
DBREF  4IXR Z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
DBREF  4IXR a    1   360  UNP    P0A444   PSBA1_THEEB      1    360             
DBREF  4IXR b    1   510  UNP    Q8DIQ1   Q8DIQ1_THEEB     1    510             
DBREF  4IXR c   13   473  UNP    Q8DIF8   Q8DIF8_THEEB     1    461             
DBREF  4IXR d    1   352  UNP    Q8CM25   PSBD_THEEB       1    352             
DBREF  4IXR e    1    84  UNP    Q8DIP0   PSBE_THEEB       1     84             
DBREF  4IXR f    1    45  UNP    Q8DIN9   PSBF_THEEB       1     45             
DBREF  4IXR h    1    66  UNP    Q8DJ43   PSBH_THEEB       1     66             
DBREF  4IXR i    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  4IXR j    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  4IXR k    1    46  UNP    Q9F1K9   PSBK_THEEB       1     46             
DBREF  4IXR l    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  4IXR m    1    36  UNP    Q8DHA7   PSBM_THEEB       1     36             
DBREF  4IXR o    1   272  UNP    P0A431   PSBO_THEEB       1    272             
DBREF  4IXR t    1    32  UNP    Q8DIQ0   PSBT_THEEB       1     32             
DBREF  4IXR u    1   134  UNP    Q9F1L5   PSBU_THEEB       1    134             
DBREF  4IXR v    1   163  UNP    P0A386   CY550_THEEB      1    163             
DBREF  4IXR g    1    46  UNP    Q8DJI1   YCF12_THEEB      1     46             
DBREF  4IXR x   10    50  UNP    Q9F1R6   PSBX_THEEB       1     41             
DBREF  4IXR z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
DBREF  4IXR G    1    28  PDB    4IXR     4IXR             1     28             
DBREF  4IXR Y    1    28  PDB    4IXR     4IXR             1     28             
SEQRES   1 A  360  MET THR THR THR LEU GLN ARG ARG GLU SER ALA ASN LEU          
SEQRES   2 A  360  TRP GLU ARG PHE CYS ASN TRP VAL THR SER THR ASP ASN          
SEQRES   3 A  360  ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE MET ILE PRO          
SEQRES   4 A  360  THR LEU LEU ALA ALA THR ILE CYS PHE VAL ILE ALA PHE          
SEQRES   5 A  360  ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY ILE ARG GLU          
SEQRES   6 A  360  PRO VAL SER GLY SER LEU LEU TYR GLY ASN ASN ILE ILE          
SEQRES   7 A  360  THR GLY ALA VAL VAL PRO SER SER ASN ALA ILE GLY LEU          
SEQRES   8 A  360  HIS PHE TYR PRO ILE TRP GLU ALA ALA SER LEU ASP GLU          
SEQRES   9 A  360  TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU ILE ILE PHE          
SEQRES  10 A  360  HIS PHE LEU LEU GLY ALA SER CYS TYR MET GLY ARG GLN          
SEQRES  11 A  360  TRP GLU LEU SER TYR ARG LEU GLY MET ARG PRO TRP ILE          
SEQRES  12 A  360  CYS VAL ALA TYR SER ALA PRO LEU ALA SER ALA PHE ALA          
SEQRES  13 A  360  VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY SER PHE SER          
SEQRES  14 A  360  ASP GLY MET PRO LEU GLY ILE SER GLY THR PHE ASN PHE          
SEQRES  15 A  360  MET ILE VAL PHE GLN ALA GLU HIS ASN ILE LEU MET HIS          
SEQRES  16 A  360  PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL PHE GLY GLY          
SEQRES  17 A  360  ALA LEU PHE CYS ALA MET HIS GLY SER LEU VAL THR SER          
SEQRES  18 A  360  SER LEU ILE ARG GLU THR THR GLU THR GLU SER ALA ASN          
SEQRES  19 A  360  TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU THR TYR ASN          
SEQRES  20 A  360  ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG LEU ILE PHE          
SEQRES  21 A  360  GLN TYR ALA SER PHE ASN ASN SER ARG SER LEU HIS PHE          
SEQRES  22 A  360  PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL TRP PHE THR          
SEQRES  23 A  360  ALA LEU GLY ILE SER THR MET ALA PHE ASN LEU ASN GLY          
SEQRES  24 A  360  PHE ASN PHE ASN HIS SER VAL ILE ASP ALA LYS GLY ASN          
SEQRES  25 A  360  VAL ILE ASN THR TRP ALA ASP ILE ILE ASN ARG ALA ASN          
SEQRES  26 A  360  LEU GLY MET GLU VAL MET HIS GLU ARG ASN ALA HIS ASN          
SEQRES  27 A  360  PHE PRO LEU ASP LEU ALA SER ALA GLU SER ALA PRO VAL          
SEQRES  28 A  360  ALA MET ILE ALA PRO SER ILE ASN GLY                          
SEQRES   1 B  510  MET GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE          
SEQRES   2 B  510  ASN ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS          
SEQRES   3 B  510  THR ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU          
SEQRES   4 B  510  TYR GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU          
SEQRES   5 B  510  ASN PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE          
SEQRES   6 B  510  MET ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP          
SEQRES   7 B  510  SER ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP          
SEQRES   8 B  510  SER PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER          
SEQRES   9 B  510  GLY LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR          
SEQRES  10 B  510  TRP ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU          
SEQRES  11 B  510  PRO ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU          
SEQRES  12 B  510  PHE LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE          
SEQRES  13 B  510  HIS LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER          
SEQRES  14 B  510  ASP PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA          
SEQRES  15 B  510  PRO GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO          
SEQRES  16 B  510  GLY GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL          
SEQRES  17 B  510  GLY ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO          
SEQRES  18 B  510  PRO GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE          
SEQRES  19 B  510  GLU THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE          
SEQRES  20 B  510  ALA ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER          
SEQRES  21 B  510  ALA THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR          
SEQRES  22 B  510  GLN TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG          
SEQRES  23 B  510  ARG VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU          
SEQRES  24 B  510  GLU ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR          
SEQRES  25 B  510  ASP TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE          
SEQRES  26 B  510  ARG THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN          
SEQRES  27 B  510  ALA TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY          
SEQRES  28 B  510  GLU GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU          
SEQRES  29 B  510  SER PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL          
SEQRES  30 B  510  LYS ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR          
SEQRES  31 B  510  SER PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY          
SEQRES  32 B  510  GLY GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR          
SEQRES  33 B  510  VAL LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE          
SEQRES  34 B  510  PHE GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE          
SEQRES  35 B  510  PHE ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS          
SEQRES  36 B  510  ALA VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP          
SEQRES  37 B  510  HIS GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY          
SEQRES  38 B  510  ILE ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY          
SEQRES  39 B  510  PHE TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG LYS          
SEQRES  40 B  510  GLU ALA VAL                                                  
SEQRES   1 C  461  MET VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN          
SEQRES   2 C  461  ARG ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY          
SEQRES   3 C  461  ASN ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY          
SEQRES   4 C  461  ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA          
SEQRES   5 C  461  GLY ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO          
SEQRES   6 C  461  GLU LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO          
SEQRES   7 C  461  HIS ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY          
SEQRES   8 C  461  GLU VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL          
SEQRES   9 C  461  VAL HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY          
SEQRES  10 C  461  VAL TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU          
SEQRES  11 C  461  TYR SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN          
SEQRES  12 C  461  LYS MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU          
SEQRES  13 C  461  GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE          
SEQRES  14 C  461  PHE GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY          
SEQRES  15 C  461  ASP VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG          
SEQRES  16 C  461  VAL ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY          
SEQRES  17 C  461  GLU GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL          
SEQRES  18 C  461  VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA          
SEQRES  19 C  461  GLY GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP          
SEQRES  20 C  461  ALA ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU          
SEQRES  21 C  461  SER TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE          
SEQRES  22 C  461  ALA THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO          
SEQRES  23 C  461  SER GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN          
SEQRES  24 C  461  ALA GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU          
SEQRES  25 C  461  GLY ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU          
SEQRES  26 C  461  GLY LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE          
SEQRES  27 C  461  PHE GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY          
SEQRES  28 C  461  PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP          
SEQRES  29 C  461  LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU          
SEQRES  30 C  461  ARG ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY          
SEQRES  31 C  461  SER LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN          
SEQRES  32 C  461  SER VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR          
SEQRES  33 C  461  SER HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS          
SEQRES  34 C  461  LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY          
SEQRES  35 C  461  PHE GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU          
SEQRES  36 C  461  SER MET PRO SER LEU ASP                                      
SEQRES   1 D  352  MET THR ILE ALA ILE GLY ARG ALA PRO ALA GLU ARG GLY          
SEQRES   2 D  352  TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS ARG ASP ARG          
SEQRES   3 D  352  PHE VAL PHE VAL GLY TRP SER GLY ILE LEU LEU PHE PRO          
SEQRES   4 D  352  CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU THR GLY THR          
SEQRES   5 D  352  THR PHE VAL THR SER TRP TYR THR HIS GLY LEU ALA SER          
SEQRES   6 D  352  SER TYR LEU GLU GLY CYS ASN PHE LEU THR VAL ALA VAL          
SEQRES   7 D  352  SER THR PRO ALA ASN SER MET GLY HIS SER LEU LEU LEU          
SEQRES   8 D  352  LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE THR ARG TRP          
SEQRES   9 D  352  CYS GLN LEU GLY GLY LEU TRP THR PHE ILE ALA LEU HIS          
SEQRES  10 D  352  GLY ALA PHE GLY LEU ILE GLY PHE MET LEU ARG GLN PHE          
SEQRES  11 D  352  GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO TYR ASN ALA          
SEQRES  12 D  352  ILE ALA PHE SER ALA PRO ILE ALA VAL PHE VAL SER VAL          
SEQRES  13 D  352  PHE LEU ILE TYR PRO LEU GLY GLN SER SER TRP PHE PHE          
SEQRES  14 D  352  ALA PRO SER PHE GLY VAL ALA ALA ILE PHE ARG PHE LEU          
SEQRES  15 D  352  LEU PHE PHE GLN GLY PHE HIS ASN TRP THR LEU ASN PRO          
SEQRES  16 D  352  PHE HIS MET MET GLY VAL ALA GLY VAL LEU GLY GLY ALA          
SEQRES  17 D  352  LEU LEU CYS ALA ILE HIS GLY ALA THR VAL GLU ASN THR          
SEQRES  18 D  352  LEU PHE GLN ASP GLY GLU GLY ALA SER THR PHE ARG ALA          
SEQRES  19 D  352  PHE ASN PRO THR GLN ALA GLU GLU THR TYR SER MET VAL          
SEQRES  20 D  352  THR ALA ASN ARG PHE TRP SER GLN ILE PHE GLY ILE ALA          
SEQRES  21 D  352  PHE SER ASN LYS ARG TRP LEU HIS PHE PHE MET LEU PHE          
SEQRES  22 D  352  VAL PRO VAL THR GLY LEU TRP MET SER ALA ILE GLY VAL          
SEQRES  23 D  352  VAL GLY LEU ALA LEU ASN LEU ARG SER TYR ASP PHE ILE          
SEQRES  24 D  352  SER GLN GLU ILE ARG ALA ALA GLU ASP PRO GLU PHE GLU          
SEQRES  25 D  352  THR PHE TYR THR LYS ASN LEU LEU LEU ASN GLU GLY ILE          
SEQRES  26 D  352  ARG ALA TRP MET ALA PRO GLN ASP GLN PRO HIS GLU ASN          
SEQRES  27 D  352  PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG GLY ASN ALA          
SEQRES  28 D  352  LEU                                                          
SEQRES   1 E   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   46  MET ILE ASP ALA LEU VAL LEU VAL ALA LYS LEU PRO GLU          
SEQRES   2 K   46  ALA TYR ALA ILE PHE ASP PRO LEU VAL ASP VAL LEU PRO          
SEQRES   3 K   46  VAL ILE PRO VAL LEU PHE LEU ALA LEU ALA PHE VAL TRP          
SEQRES   4 K   46  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  272  MET LYS TYR ARG ILE LEU MET ALA THR LEU LEU ALA VAL          
SEQRES   2 O  272  CYS LEU GLY ILE PHE SER LEU SER ALA PRO ALA PHE ALA          
SEQRES   3 O  272  ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY THR          
SEQRES   4 O  272  GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR ALA          
SEQRES   5 O  272  ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR ARG          
SEQRES   6 O  272  ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU VAL          
SEQRES   7 O  272  LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE          
SEQRES   8 O  272  VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER LEU          
SEQRES   9 O  272  ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP GLY          
SEQRES  10 O  272  SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN          
SEQRES  11 O  272  PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE PRO          
SEQRES  12 O  272  LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR GLN          
SEQRES  13 O  272  PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE LYS          
SEQRES  14 O  272  GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN PHE          
SEQRES  15 O  272  LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR ASP          
SEQRES  16 O  272  SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU          
SEQRES  17 O  272  ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS GLY          
SEQRES  18 O  272  GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG THR          
SEQRES  19 O  272  GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU SER          
SEQRES  20 O  272  ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL LYS          
SEQRES  21 O  272  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  134  MET GLN ARG LEU GLY ARG TRP LEU ALA LEU ALA TYR PHE          
SEQRES   2 U  134  VAL GLY VAL SER LEU LEU GLY TRP ILE ASN TRP SER ALA          
SEQRES   3 U  134  PRO THR LEU ALA ALA THR ALA SER THR GLU GLU GLU LEU          
SEQRES   4 U  134  VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA TYR GLY          
SEQRES   5 U  134  GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA ALA PHE          
SEQRES   6 U  134  ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA LYS LEU          
SEQRES   7 U  134  ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU ASP VAL          
SEQRES   8 U  134  LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS GLN ILE          
SEQRES   9 U  134  LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR GLU VAL          
SEQRES  10 U  134  GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR ASN ASN          
SEQRES  11 U  134  GLY LEU TYR LYS                                              
SEQRES   1 V  163  MET LEU LYS LYS CYS VAL TRP LEU ALA VAL ALA LEU CYS          
SEQRES   2 V  163  LEU CYS LEU TRP GLN PHE THR MET GLY THR ALA LEU ALA          
SEQRES   3 V  163  ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN          
SEQRES   4 V  163  SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR          
SEQRES   5 V  163  LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER          
SEQRES   6 V  163  CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU          
SEQRES   7 V  163  ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO          
SEQRES   8 V  163  ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN          
SEQRES   9 V  163  PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL          
SEQRES  10 V  163  HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET          
SEQRES  11 V  163  ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY          
SEQRES  12 V  163  HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP          
SEQRES  13 V  163  GLY GLY GLY LYS VAL TYR TYR                                  
SEQRES   1 y   46  MET GLY ILE PHE ASN GLY ILE ILE GLU PHE LEU SER ASN          
SEQRES   2 y   46  ILE ASN PHE GLU VAL ILE ALA GLN LEU THR MET ILE ALA          
SEQRES   3 y   46  MET ILE GLY ILE ALA GLY PRO MET ILE ILE PHE LEU LEU          
SEQRES   4 y   46  ALA VAL ARG ARG GLY ASN LEU                                  
SEQRES   1 X   41  MET THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY          
SEQRES   2 X   41  LEU LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA          
SEQRES   3 X   41  VAL LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG          
SEQRES   4 X   41  SER LEU                                                      
SEQRES   1 Z   62  MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL          
SEQRES   2 Z   62  ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA          
SEQRES   3 Z   62  TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU          
SEQRES   4 Z   62  ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU          
SEQRES   5 Z   62  VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL                      
SEQRES   1 G   28  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 G   28  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   3 G   28  UNK UNK                                                      
SEQRES   1 a  360  MET THR THR THR LEU GLN ARG ARG GLU SER ALA ASN LEU          
SEQRES   2 a  360  TRP GLU ARG PHE CYS ASN TRP VAL THR SER THR ASP ASN          
SEQRES   3 a  360  ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE MET ILE PRO          
SEQRES   4 a  360  THR LEU LEU ALA ALA THR ILE CYS PHE VAL ILE ALA PHE          
SEQRES   5 a  360  ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY ILE ARG GLU          
SEQRES   6 a  360  PRO VAL SER GLY SER LEU LEU TYR GLY ASN ASN ILE ILE          
SEQRES   7 a  360  THR GLY ALA VAL VAL PRO SER SER ASN ALA ILE GLY LEU          
SEQRES   8 a  360  HIS PHE TYR PRO ILE TRP GLU ALA ALA SER LEU ASP GLU          
SEQRES   9 a  360  TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU ILE ILE PHE          
SEQRES  10 a  360  HIS PHE LEU LEU GLY ALA SER CYS TYR MET GLY ARG GLN          
SEQRES  11 a  360  TRP GLU LEU SER TYR ARG LEU GLY MET ARG PRO TRP ILE          
SEQRES  12 a  360  CYS VAL ALA TYR SER ALA PRO LEU ALA SER ALA PHE ALA          
SEQRES  13 a  360  VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY SER PHE SER          
SEQRES  14 a  360  ASP GLY MET PRO LEU GLY ILE SER GLY THR PHE ASN PHE          
SEQRES  15 a  360  MET ILE VAL PHE GLN ALA GLU HIS ASN ILE LEU MET HIS          
SEQRES  16 a  360  PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL PHE GLY GLY          
SEQRES  17 a  360  ALA LEU PHE CYS ALA MET HIS GLY SER LEU VAL THR SER          
SEQRES  18 a  360  SER LEU ILE ARG GLU THR THR GLU THR GLU SER ALA ASN          
SEQRES  19 a  360  TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU THR TYR ASN          
SEQRES  20 a  360  ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG LEU ILE PHE          
SEQRES  21 a  360  GLN TYR ALA SER PHE ASN ASN SER ARG SER LEU HIS PHE          
SEQRES  22 a  360  PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL TRP PHE THR          
SEQRES  23 a  360  ALA LEU GLY ILE SER THR MET ALA PHE ASN LEU ASN GLY          
SEQRES  24 a  360  PHE ASN PHE ASN HIS SER VAL ILE ASP ALA LYS GLY ASN          
SEQRES  25 a  360  VAL ILE ASN THR TRP ALA ASP ILE ILE ASN ARG ALA ASN          
SEQRES  26 a  360  LEU GLY MET GLU VAL MET HIS GLU ARG ASN ALA HIS ASN          
SEQRES  27 a  360  PHE PRO LEU ASP LEU ALA SER ALA GLU SER ALA PRO VAL          
SEQRES  28 a  360  ALA MET ILE ALA PRO SER ILE ASN GLY                          
SEQRES   1 b  510  MET GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE          
SEQRES   2 b  510  ASN ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS          
SEQRES   3 b  510  THR ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU          
SEQRES   4 b  510  TYR GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU          
SEQRES   5 b  510  ASN PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE          
SEQRES   6 b  510  MET ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP          
SEQRES   7 b  510  SER ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP          
SEQRES   8 b  510  SER PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER          
SEQRES   9 b  510  GLY LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR          
SEQRES  10 b  510  TRP ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU          
SEQRES  11 b  510  PRO ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU          
SEQRES  12 b  510  PHE LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE          
SEQRES  13 b  510  HIS LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER          
SEQRES  14 b  510  ASP PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA          
SEQRES  15 b  510  PRO GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO          
SEQRES  16 b  510  GLY GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL          
SEQRES  17 b  510  GLY ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO          
SEQRES  18 b  510  PRO GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE          
SEQRES  19 b  510  GLU THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE          
SEQRES  20 b  510  ALA ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER          
SEQRES  21 b  510  ALA THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR          
SEQRES  22 b  510  GLN TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG          
SEQRES  23 b  510  ARG VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU          
SEQRES  24 b  510  GLU ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR          
SEQRES  25 b  510  ASP TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE          
SEQRES  26 b  510  ARG THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN          
SEQRES  27 b  510  ALA TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY          
SEQRES  28 b  510  GLU GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU          
SEQRES  29 b  510  SER PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL          
SEQRES  30 b  510  LYS ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR          
SEQRES  31 b  510  SER PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY          
SEQRES  32 b  510  GLY GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR          
SEQRES  33 b  510  VAL LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE          
SEQRES  34 b  510  PHE GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE          
SEQRES  35 b  510  PHE ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS          
SEQRES  36 b  510  ALA VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP          
SEQRES  37 b  510  HIS GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY          
SEQRES  38 b  510  ILE ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY          
SEQRES  39 b  510  PHE TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG LYS          
SEQRES  40 b  510  GLU ALA VAL                                                  
SEQRES   1 c  461  MET VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN          
SEQRES   2 c  461  ARG ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY          
SEQRES   3 c  461  ASN ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY          
SEQRES   4 c  461  ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA          
SEQRES   5 c  461  GLY ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO          
SEQRES   6 c  461  GLU LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO          
SEQRES   7 c  461  HIS ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY          
SEQRES   8 c  461  GLU VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL          
SEQRES   9 c  461  VAL HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY          
SEQRES  10 c  461  VAL TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU          
SEQRES  11 c  461  TYR SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN          
SEQRES  12 c  461  LYS MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU          
SEQRES  13 c  461  GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE          
SEQRES  14 c  461  PHE GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY          
SEQRES  15 c  461  ASP VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG          
SEQRES  16 c  461  VAL ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY          
SEQRES  17 c  461  GLU GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL          
SEQRES  18 c  461  VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA          
SEQRES  19 c  461  GLY GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP          
SEQRES  20 c  461  ALA ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU          
SEQRES  21 c  461  SER TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE          
SEQRES  22 c  461  ALA THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO          
SEQRES  23 c  461  SER GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN          
SEQRES  24 c  461  ALA GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU          
SEQRES  25 c  461  GLY ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU          
SEQRES  26 c  461  GLY LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE          
SEQRES  27 c  461  PHE GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY          
SEQRES  28 c  461  PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP          
SEQRES  29 c  461  LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU          
SEQRES  30 c  461  ARG ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY          
SEQRES  31 c  461  SER LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN          
SEQRES  32 c  461  SER VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR          
SEQRES  33 c  461  SER HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS          
SEQRES  34 c  461  LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY          
SEQRES  35 c  461  PHE GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU          
SEQRES  36 c  461  SER MET PRO SER LEU ASP                                      
SEQRES   1 d  352  MET THR ILE ALA ILE GLY ARG ALA PRO ALA GLU ARG GLY          
SEQRES   2 d  352  TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS ARG ASP ARG          
SEQRES   3 d  352  PHE VAL PHE VAL GLY TRP SER GLY ILE LEU LEU PHE PRO          
SEQRES   4 d  352  CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU THR GLY THR          
SEQRES   5 d  352  THR PHE VAL THR SER TRP TYR THR HIS GLY LEU ALA SER          
SEQRES   6 d  352  SER TYR LEU GLU GLY CYS ASN PHE LEU THR VAL ALA VAL          
SEQRES   7 d  352  SER THR PRO ALA ASN SER MET GLY HIS SER LEU LEU LEU          
SEQRES   8 d  352  LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE THR ARG TRP          
SEQRES   9 d  352  CYS GLN LEU GLY GLY LEU TRP THR PHE ILE ALA LEU HIS          
SEQRES  10 d  352  GLY ALA PHE GLY LEU ILE GLY PHE MET LEU ARG GLN PHE          
SEQRES  11 d  352  GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO TYR ASN ALA          
SEQRES  12 d  352  ILE ALA PHE SER ALA PRO ILE ALA VAL PHE VAL SER VAL          
SEQRES  13 d  352  PHE LEU ILE TYR PRO LEU GLY GLN SER SER TRP PHE PHE          
SEQRES  14 d  352  ALA PRO SER PHE GLY VAL ALA ALA ILE PHE ARG PHE LEU          
SEQRES  15 d  352  LEU PHE PHE GLN GLY PHE HIS ASN TRP THR LEU ASN PRO          
SEQRES  16 d  352  PHE HIS MET MET GLY VAL ALA GLY VAL LEU GLY GLY ALA          
SEQRES  17 d  352  LEU LEU CYS ALA ILE HIS GLY ALA THR VAL GLU ASN THR          
SEQRES  18 d  352  LEU PHE GLN ASP GLY GLU GLY ALA SER THR PHE ARG ALA          
SEQRES  19 d  352  PHE ASN PRO THR GLN ALA GLU GLU THR TYR SER MET VAL          
SEQRES  20 d  352  THR ALA ASN ARG PHE TRP SER GLN ILE PHE GLY ILE ALA          
SEQRES  21 d  352  PHE SER ASN LYS ARG TRP LEU HIS PHE PHE MET LEU PHE          
SEQRES  22 d  352  VAL PRO VAL THR GLY LEU TRP MET SER ALA ILE GLY VAL          
SEQRES  23 d  352  VAL GLY LEU ALA LEU ASN LEU ARG SER TYR ASP PHE ILE          
SEQRES  24 d  352  SER GLN GLU ILE ARG ALA ALA GLU ASP PRO GLU PHE GLU          
SEQRES  25 d  352  THR PHE TYR THR LYS ASN LEU LEU LEU ASN GLU GLY ILE          
SEQRES  26 d  352  ARG ALA TRP MET ALA PRO GLN ASP GLN PRO HIS GLU ASN          
SEQRES  27 d  352  PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG GLY ASN ALA          
SEQRES  28 d  352  LEU                                                          
SEQRES   1 e   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   46  MET ILE ASP ALA LEU VAL LEU VAL ALA LYS LEU PRO GLU          
SEQRES   2 k   46  ALA TYR ALA ILE PHE ASP PRO LEU VAL ASP VAL LEU PRO          
SEQRES   3 k   46  VAL ILE PRO VAL LEU PHE LEU ALA LEU ALA PHE VAL TRP          
SEQRES   4 k   46  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  272  MET LYS TYR ARG ILE LEU MET ALA THR LEU LEU ALA VAL          
SEQRES   2 o  272  CYS LEU GLY ILE PHE SER LEU SER ALA PRO ALA PHE ALA          
SEQRES   3 o  272  ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY THR          
SEQRES   4 o  272  GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR ALA          
SEQRES   5 o  272  ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR ARG          
SEQRES   6 o  272  ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU VAL          
SEQRES   7 o  272  LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE          
SEQRES   8 o  272  VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER LEU          
SEQRES   9 o  272  ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP GLY          
SEQRES  10 o  272  SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN          
SEQRES  11 o  272  PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE PRO          
SEQRES  12 o  272  LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR GLN          
SEQRES  13 o  272  PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE LYS          
SEQRES  14 o  272  GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN PHE          
SEQRES  15 o  272  LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR ASP          
SEQRES  16 o  272  SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU          
SEQRES  17 o  272  ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS GLY          
SEQRES  18 o  272  GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG THR          
SEQRES  19 o  272  GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU SER          
SEQRES  20 o  272  ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL LYS          
SEQRES  21 o  272  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  134  MET GLN ARG LEU GLY ARG TRP LEU ALA LEU ALA TYR PHE          
SEQRES   2 u  134  VAL GLY VAL SER LEU LEU GLY TRP ILE ASN TRP SER ALA          
SEQRES   3 u  134  PRO THR LEU ALA ALA THR ALA SER THR GLU GLU GLU LEU          
SEQRES   4 u  134  VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA TYR GLY          
SEQRES   5 u  134  GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA ALA PHE          
SEQRES   6 u  134  ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA LYS LEU          
SEQRES   7 u  134  ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU ASP VAL          
SEQRES   8 u  134  LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS GLN ILE          
SEQRES   9 u  134  LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR GLU VAL          
SEQRES  10 u  134  GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR ASN ASN          
SEQRES  11 u  134  GLY LEU TYR LYS                                              
SEQRES   1 v  163  MET LEU LYS LYS CYS VAL TRP LEU ALA VAL ALA LEU CYS          
SEQRES   2 v  163  LEU CYS LEU TRP GLN PHE THR MET GLY THR ALA LEU ALA          
SEQRES   3 v  163  ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN          
SEQRES   4 v  163  SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR          
SEQRES   5 v  163  LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER          
SEQRES   6 v  163  CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU          
SEQRES   7 v  163  ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO          
SEQRES   8 v  163  ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN          
SEQRES   9 v  163  PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL          
SEQRES  10 v  163  HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET          
SEQRES  11 v  163  ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY          
SEQRES  12 v  163  HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP          
SEQRES  13 v  163  GLY GLY GLY LYS VAL TYR TYR                                  
SEQRES   1 g   46  MET GLY ILE PHE ASN GLY ILE ILE GLU PHE LEU SER ASN          
SEQRES   2 g   46  ILE ASN PHE GLU VAL ILE ALA GLN LEU THR MET ILE ALA          
SEQRES   3 g   46  MET ILE GLY ILE ALA GLY PRO MET ILE ILE PHE LEU LEU          
SEQRES   4 g   46  ALA VAL ARG ARG GLY ASN LEU                                  
SEQRES   1 x   41  MET THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY          
SEQRES   2 x   41  LEU LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA          
SEQRES   3 x   41  VAL LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG          
SEQRES   4 x   41  SER LEU                                                      
SEQRES   1 z   62  MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL          
SEQRES   2 z   62  ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA          
SEQRES   3 z   62  TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU          
SEQRES   4 z   62  ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU          
SEQRES   5 z   62  VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL                      
SEQRES   1 Y   28  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 Y   28  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   3 Y   28  UNK UNK                                                      
HET    FE2  A 401       1                                                       
HET    BCT  A 402       4                                                       
HET    CLA  A 403      65                                                       
HET    CLA  A 404      65                                                       
HET    CLA  A 405      65                                                       
HET    PHO  A 406      64                                                       
HET    CLA  A 407      65                                                       
HET    PL9  A 408      45                                                       
HET    OEC  A 409       5                                                       
HET    BCR  A 410      40                                                       
HET    DGD  A 411      56                                                       
HET    LHG  A 412      39                                                       
HET    SQD  A 413      51                                                       
HET    LMG  A 414      51                                                       
HET    LHG  A 415      37                                                       
HET     CL  A 416       1                                                       
HET    SQD  A 417      54                                                       
HET    LMG  A 418      42                                                       
HET    CLA  B 601      65                                                       
HET    CLA  B 602      65                                                       
HET    CLA  B 603      65                                                       
HET    CLA  B 604      65                                                       
HET    CLA  B 605      65                                                       
HET    CLA  B 606      65                                                       
HET    CLA  B 607      65                                                       
HET    CLA  B 608      65                                                       
HET    CLA  B 609      65                                                       
HET    CLA  B 610      65                                                       
HET    CLA  B 611      65                                                       
HET    CLA  B 612      65                                                       
HET    CLA  B 613      65                                                       
HET    CLA  B 614      65                                                       
HET    CLA  B 615      65                                                       
HET    CLA  B 616      65                                                       
HET    BCR  B 617      40                                                       
HET    BCR  B 618      40                                                       
HET    BCR  B 619      40                                                       
HET    BCR  B 620      40                                                       
HET    DGD  B 621      58                                                       
HET    LMG  B 622      49                                                       
HET    LMG  B 623      49                                                       
HET    LMT  B 624      35                                                       
HET    LMT  B 625      35                                                       
HET    SQD  B 626      47                                                       
HET    DGD  B 627      52                                                       
HET    LMT  B 628      35                                                       
HET    LMT  B 629      35                                                       
HET    CLA  C 501      65                                                       
HET    CLA  C 502      65                                                       
HET    CLA  C 503      65                                                       
HET    CLA  C 504      65                                                       
HET    CLA  C 505      65                                                       
HET    CLA  C 506      65                                                       
HET    CLA  C 507      65                                                       
HET    CLA  C 508      65                                                       
HET    CLA  C 509      65                                                       
HET    CLA  C 510      65                                                       
HET    CLA  C 511      65                                                       
HET    CLA  C 512      65                                                       
HET    CLA  C 513      65                                                       
HET    BCR  C 514      40                                                       
HET    BCR  C 515      40                                                       
HET    BCR  C 516      40                                                       
HET    DGD  C 517      53                                                       
HET    DGD  C 518      62                                                       
HET    DGD  C 519      66                                                       
HET    LMG  C 520      48                                                       
HET    LMG  C 521      45                                                       
HET    CLA  D 401      65                                                       
HET    PHO  D 402      64                                                       
HET    CLA  D 403      65                                                       
HET    PL9  D 404      55                                                       
HET    BCR  D 405      40                                                       
HET    LMG  D 406      46                                                       
HET    LMG  D 407      48                                                       
HET    SQD  D 408      43                                                       
HET    DGD  D 409      63                                                       
HET    LMT  D 410      31                                                       
HET    LMG  E 101      44                                                       
HET    HEM  F 101      43                                                       
HET    SQD  F 102      45                                                       
HET    BCR  H 101      40                                                       
HET    LMG  I 101      43                                                       
HET    LMT  I 102      35                                                       
HET    PL9  J 101      35                                                       
HET    BCR  J 102      40                                                       
HET     CA  K 101       1                                                       
HET    LMG  M 101      42                                                       
HET    LMT  M 102      35                                                       
HET     CA  O 301       1                                                       
HET    BCR  T 101      40                                                       
HET    BCR  T 102      40                                                       
HET    HEM  V 201      43                                                       
HET    BCR  y 101      40                                                       
HET    SQD  a 401      54                                                       
HET    LMG  a 402      42                                                       
HET    FE2  a 403       1                                                       
HET    CLA  a 404      65                                                       
HET    CLA  a 405      65                                                       
HET    CLA  a 406      65                                                       
HET    PHO  a 407      64                                                       
HET    PHO  a 408      64                                                       
HET    CLA  a 409      65                                                       
HET    PL9  a 410      45                                                       
HET    OEC  a 411       5                                                       
HET    BCR  a 412      40                                                       
HET    DGD  a 413      56                                                       
HET    LHG  a 414      39                                                       
HET    SQD  a 415      51                                                       
HET    LMG  a 416      51                                                       
HET    LHG  a 417      37                                                       
HET     CL  a 418       1                                                       
HET    SQD  b 601      47                                                       
HET    DGD  b 602      52                                                       
HET    LMT  b 603      35                                                       
HET    LMT  b 604      35                                                       
HET    CLA  b 605      65                                                       
HET    CLA  b 606      65                                                       
HET    CLA  b 607      65                                                       
HET    CLA  b 608      65                                                       
HET    CLA  b 609      65                                                       
HET    CLA  b 610      65                                                       
HET    CLA  b 611      65                                                       
HET    CLA  b 612      65                                                       
HET    CLA  b 613      65                                                       
HET    CLA  b 614      65                                                       
HET    CLA  b 615      65                                                       
HET    CLA  b 616      65                                                       
HET    CLA  b 617      65                                                       
HET    CLA  b 618      65                                                       
HET    CLA  b 619      65                                                       
HET    CLA  b 620      65                                                       
HET    BCR  b 621      40                                                       
HET    BCR  b 622      40                                                       
HET    DGD  b 623      58                                                       
HET    LMG  b 624      49                                                       
HET    LMG  b 625      49                                                       
HET    LMT  b 626      35                                                       
HET    LMT  b 627      35                                                       
HET    CLA  c 501      65                                                       
HET    CLA  c 502      65                                                       
HET    CLA  c 503      65                                                       
HET    CLA  c 504      65                                                       
HET    CLA  c 505      65                                                       
HET    CLA  c 506      65                                                       
HET    CLA  c 507      65                                                       
HET    CLA  c 508      65                                                       
HET    CLA  c 509      65                                                       
HET    CLA  c 510      65                                                       
HET    CLA  c 511      65                                                       
HET    CLA  c 512      65                                                       
HET    CLA  c 513      65                                                       
HET    BCR  c 514      40                                                       
HET    BCR  c 515      40                                                       
HET    DGD  c 516      53                                                       
HET    DGD  c 517      62                                                       
HET    DGD  c 518      66                                                       
HET    LMG  c 519      45                                                       
HET    BCT  d 401       4                                                       
HET    CLA  d 402      65                                                       
HET    CLA  d 403      65                                                       
HET    PL9  d 404      55                                                       
HET    BCR  d 405      40                                                       
HET    LMG  d 406      46                                                       
HET    LMG  d 407      48                                                       
HET    SQD  d 408      43                                                       
HET    DGD  d 409      63                                                       
HET    LMT  d 410      31                                                       
HET    LMG  e 101      44                                                       
HET    HEM  f 101      43                                                       
HET    SQD  f 102      45                                                       
HET    BCR  h 101      40                                                       
HET    LMG  i 101      43                                                       
HET    LMT  i 102      35                                                       
HET    PL9  j 101      35                                                       
HET    BCR  j 102      40                                                       
HET     CA  k 101       1                                                       
HET    BCR  k 102      40                                                       
HET    LMG  k 103      48                                                       
HET    LMT  m 101      35                                                       
HET    LMG  m 102      42                                                       
HET     CA  o 301       1                                                       
HET    HEM  v 201      43                                                       
HET    BCR  z 101      40                                                       
HETNAM     FE2 FE (II) ION                                                      
HETNAM     BCT BICARBONATE ION                                                  
HETNAM     CLA CHLOROPHYLL A                                                    
HETNAM     PHO PHEOPHYTIN A                                                     
HETNAM     PL9 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,           
HETNAM   2 PL9  6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-               
HETNAM   3 PL9  CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-          
HETNAM   4 PL9  BENZOQUINONE                                                    
HETNAM     OEC OXYGEN EVOLVING SYSTEM                                           
HETNAM     BCR BETA-CAROTENE                                                    
HETNAM     DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)                              
HETNAM     LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE                           
HETNAM     SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-                      
HETNAM   2 SQD  GLUCOPYRANOSYL]-SN-GLYCEROL                                     
HETNAM     LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE                        
HETNAM      CL CHLORIDE ION                                                     
HETNAM     LMT DODECYL-BETA-D-MALTOSIDE                                         
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM      CA CALCIUM ION                                                      
HETSYN     PL9 PLASTOQUINONE 9                                                  
HETSYN     SQD SULFOQUINOVOSYLDIACYLGLYCEROL                                    
HETSYN     HEM HEME                                                             
FORMUL  41  FE2    2(FE 2+)                                                     
FORMUL  42  BCT    2(C H O3 1-)                                                 
FORMUL  43  CLA    70(C55 H72 MG N4 O5 2+)                                      
FORMUL  46  PHO    4(C55 H74 N4 O5)                                             
FORMUL  48  PL9    6(C53 H80 O2)                                                
FORMUL  49  OEC    2(CA MN4 O4)                                                 
FORMUL  50  BCR    24(C40 H56)                                                  
FORMUL  51  DGD    14(C51 H96 O15)                                              
FORMUL  52  LHG    4(C38 H75 O10 P)                                             
FORMUL  53  SQD    10(C41 H78 O12 S)                                            
FORMUL  54  LMG    22(C45 H86 O10)                                              
FORMUL  56   CL    2(CL 1-)                                                     
FORMUL  82  LMT    14(C24 H46 O11)                                              
FORMUL  20  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL  27   CA    4(CA 2+)                                                     
HELIX    1   1 ASN A   12  THR A   22  1                                  11    
HELIX    2   2 PHE A   33  ALA A   55  1                                  23    
HELIX    3   3 SER A   70  GLY A   74  5                                   5    
HELIX    4   4 PRO A   95  ALA A   99  5                                   5    
HELIX    5   5 SER A  101  ASN A  108  1                                   8    
HELIX    6   6 GLY A  109  LEU A  137  1                                  29    
HELIX    7   7 TRP A  142  TYR A  147  1                                   6    
HELIX    8   8 TYR A  147  LEU A  159  1                                  13    
HELIX    9   9 LEU A  159  GLY A  166  1                                   8    
HELIX   10  10 SER A  167  GLY A  171  5                                   5    
HELIX   11  11 ILE A  176  ASN A  191  1                                  16    
HELIX   12  12 ILE A  192  MET A  194  5                                   3    
HELIX   13  13 HIS A  195  SER A  222  1                                  28    
HELIX   14  14 SER A  232  TYR A  237  5                                   6    
HELIX   15  15 ASN A  247  ILE A  259  1                                  13    
HELIX   16  16 PHE A  260  SER A  264  5                                   5    
HELIX   17  17 ASN A  267  MET A  293  1                                  27    
HELIX   18  18 THR A  316  HIS A  332  1                                  17    
HELIX   19  19 GLU A  333  HIS A  337  5                                   5    
HELIX   20  20 PRO B    4  ILE B   13  5                                  10    
HELIX   21  21 ASP B   15  ALA B   43  1                                  29    
HELIX   22  22 PRO B   54  GLN B   58  5                                   5    
HELIX   23  23 VAL B   62  ARG B   68  1                                   7    
HELIX   24  24 SER B   92  TYR B  117  1                                  26    
HELIX   25  25 LEU B  120  ARG B  124  5                                   5    
HELIX   26  26 ASP B  134  PHE B  156  1                                  23    
HELIX   27  27 GLY B  186  ASN B  191  5                                   6    
HELIX   28  28 ASN B  194  VAL B  219  1                                  26    
HELIX   29  29 PRO B  222  LEU B  229  1                                   8    
HELIX   30  30 ILE B  234  TYR B  258  1                                  25    
HELIX   31  31 PRO B  264  GLY B  269  1                                   6    
HELIX   32  32 THR B  271  SER B  277  1                                   7    
HELIX   33  33 SER B  278  SER B  294  1                                  17    
HELIX   34  34 THR B  297  ILE B  305  1                                   9    
HELIX   35  35 PRO B  306  TYR B  312  1                                   7    
HELIX   36  36 ASP B  313  ASN B  318  5                                   6    
HELIX   37  37 PRO B  329  GLY B  333  5                                   5    
HELIX   38  38 SER B  391  GLY B  396  1                                   6    
HELIX   39  39 ASP B  413  ILE B  425  1                                  13    
HELIX   40  40 SER B  446  PHE B  475  1                                  30    
HELIX   41  41 ALA C   34  ILE C   43  5                                  10    
HELIX   42  42 LEU C   45  PHE C   75  1                                  31    
HELIX   43  43 PRO C   80  GLN C   84  5                                   5    
HELIX   44  44 LEU C   88  LEU C   95  1                                   8    
HELIX   45  45 GLY C  100  GLU C  104  5                                   5    
HELIX   46  46 THR C  108  ARG C  135  1                                  28    
HELIX   47  47 ASP C  153  PHE C  181  1                                  29    
HELIX   48  48 ASP C  205  PHE C  210  1                                   6    
HELIX   49  49 GLY C  211  LYS C  215  5                                   5    
HELIX   50  50 GLY C  222  VAL C  227  5                                   6    
HELIX   51  51 ASN C  229  LEU C  253  1                                  25    
HELIX   52  52 GLY C  258  PHE C  264  1                                   7    
HELIX   53  53 SER C  267  ASN C  293  1                                  27    
HELIX   54  54 THR C  305  LEU C  324  1                                  20    
HELIX   55  55 ASN C  327  ALA C  331  5                                   5    
HELIX   56  56 GLY C  353  TRP C  359  5                                   7    
HELIX   57  57 LEU C  366  PRO C  368  5                                   3    
HELIX   58  58 ASP C  376  ASP C  383  1                                   8    
HELIX   59  59 GLN C  385  THR C  397  1                                  13    
HELIX   60  60 SER C  421  GLY C  454  1                                  34    
HELIX   61  61 GLU C  464  MET C  469  5                                   6    
HELIX   62  62 TRP D   14  LYS D   23  1                                  10    
HELIX   63  63 VAL D   30  PHE D   54  1                                  25    
HELIX   64  64 SER D   57  GLY D   62  1                                   6    
HELIX   65  65 SER D   66  GLY D   70  5                                   5    
HELIX   66  66 ALA D   82  GLY D   86  5                                   5    
HELIX   67  67 ASP D  100  LEU D  107  1                                   8    
HELIX   68  68 GLY D  108  GLY D  137  1                                  30    
HELIX   69  69 PRO D  140  PHE D  146  1                                   7    
HELIX   70  70 PHE D  146  LEU D  158  1                                  13    
HELIX   71  71 LEU D  158  GLN D  164  1                                   7    
HELIX   72  72 SER D  166  ALA D  170  5                                   5    
HELIX   73  73 GLY D  174  PHE D  188  1                                  15    
HELIX   74  74 ASN D  190  LEU D  193  5                                   4    
HELIX   75  75 ASN D  194  ASN D  220  1                                  27    
HELIX   76  76 SER D  245  PHE D  257  1                                  13    
HELIX   77  77 ASN D  263  LEU D  291  1                                  29    
HELIX   78  78 PHE D  298  ASP D  308  1                                  11    
HELIX   79  79 THR D  313  GLN D  334  1                                  22    
HELIX   80  80 PRO D  335  ASN D  338  5                                   4    
HELIX   81  81 PRO D  342  LEU D  346  5                                   5    
HELIX   82  82 PRO E    9  SER E   16  1                                   8    
HELIX   83  83 SER E   16  THR E   40  1                                  25    
HELIX   84  84 GLY E   41  PHE E   47  1                                   7    
HELIX   85  85 GLU E   71  GLN E   82  1                                  12    
HELIX   86  86 THR F   17  GLN F   41  1                                  25    
HELIX   87  87 THR H    5  ARG H   12  1                                   8    
HELIX   88  88 THR H   27  ASN H   50  1                                  24    
HELIX   89  89 GLU I    2  SER I   25  1                                  24    
HELIX   90  90 PRO J    9  ALA J   32  1                                  24    
HELIX   91  91 ALA K   14  ILE K   17  5                                   4    
HELIX   92  92 PHE K   18  ASP K   23  1                                   6    
HELIX   93  93 VAL K   24  PRO K   26  5                                   3    
HELIX   94  94 VAL K   27  VAL K   43  1                                  17    
HELIX   95  95 ASN L   13  ASN L   37  1                                  25    
HELIX   96  96 LEU M    6  SER M   31  1                                  26    
HELIX   97  97 GLY O   40  LYS O   44  5                                   5    
HELIX   98  98 LEU O  208  VAL O  213  1                                   6    
HELIX   99  99 GLU T    2  PHE T   23  1                                  22    
HELIX  100 100 ASN U   41  LEU U   47  1                                   7    
HELIX  101 101 ASN U   61  TYR U   68  5                                   8    
HELIX  102 102 TYR U   72  ASN U   82  1                                  11    
HELIX  103 103 SER U   87  ILE U   94  5                                   8    
HELIX  104 104 THR U   98  LEU U  109  1                                  12    
HELIX  105 105 GLU U  118  GLU U  123  1                                   6    
HELIX  106 106 GLY U  124  ASP U  126  5                                   3    
HELIX  107 107 THR V   48  CYS V   63  1                                  16    
HELIX  108 108 CYS V   63  VAL V   68  1                                   6    
HELIX  109 109 GLY V   69  ILE V   71  5                                   3    
HELIX  110 110 ARG V   81  LEU V   87  1                                   7    
HELIX  111 111 ASN V   94  MET V  102  1                                   9    
HELIX  112 112 SER V  120  ALA V  124  5                                   5    
HELIX  113 113 PRO V  128  LEU V  133  1                                   6    
HELIX  114 114 THR V  134  GLY V  153  1                                  20    
HELIX  115 115 GLY V  153  GLY V  158  1                                   6    
HELIX  116 116 GLY V  159  TYR V  163  5                                   5    
HELIX  117 117 GLN y   21  ARG y   42  1                                  22    
HELIX  118 118 THR X   13  GLN X   42  1                                  30    
HELIX  119 119 THR Z    2  SER Z   29  1                                  28    
HELIX  120 120 ARG Z   35  VAL Z   62  1                                  28    
HELIX  121 121 UNK G    2  UNK G   13  1                                  12    
HELIX  122 122 UNK G   14  UNK G   25  1                                  12    
HELIX  123 123 ASN a   12  THR a   22  1                                  11    
HELIX  124 124 PHE a   33  ALA a   55  1                                  23    
HELIX  125 125 SER a   70  GLY a   74  5                                   5    
HELIX  126 126 PRO a   95  ALA a   99  5                                   5    
HELIX  127 127 SER a  101  ASN a  108  1                                   8    
HELIX  128 128 GLY a  109  LEU a  137  1                                  29    
HELIX  129 129 TRP a  142  LEU a  159  1                                  18    
HELIX  130 130 LEU a  159  GLY a  166  1                                   8    
HELIX  131 131 SER a  167  GLY a  171  5                                   5    
HELIX  132 132 ILE a  176  ASN a  191  1                                  16    
HELIX  133 133 ILE a  192  MET a  194  5                                   3    
HELIX  134 134 HIS a  195  SER a  222  1                                  28    
HELIX  135 135 SER a  232  TYR a  237  5                                   6    
HELIX  136 136 ASN a  247  ILE a  259  1                                  13    
HELIX  137 137 PHE a  260  SER a  264  5                                   5    
HELIX  138 138 ASN a  267  MET a  293  1                                  27    
HELIX  139 139 THR a  316  HIS a  332  1                                  17    
HELIX  140 140 GLU a  333  HIS a  337  5                                   5    
HELIX  141 141 PRO b    4  ILE b   13  5                                  10    
HELIX  142 142 ASP b   15  ALA b   43  1                                  29    
HELIX  143 143 PRO b   54  GLN b   58  5                                   5    
HELIX  144 144 VAL b   62  ARG b   68  1                                   7    
HELIX  145 145 SER b   92  TYR b  117  1                                  26    
HELIX  146 146 LEU b  120  ARG b  124  5                                   5    
HELIX  147 147 ASP b  134  PHE b  156  1                                  23    
HELIX  148 148 GLY b  186  ASN b  191  5                                   6    
HELIX  149 149 PRO b  195  VAL b  219  1                                  25    
HELIX  150 150 PRO b  222  LEU b  229  1                                   8    
HELIX  151 151 ASN b  233  GLU b  235  5                                   3    
HELIX  152 152 THR b  236  TYR b  258  1                                  23    
HELIX  153 153 PRO b  264  GLY b  269  1                                   6    
HELIX  154 154 THR b  271  SER b  277  1                                   7    
HELIX  155 155 SER b  278  SER b  294  1                                  17    
HELIX  156 156 THR b  297  ALA b  304  1                                   8    
HELIX  157 157 PRO b  306  TYR b  312  1                                   7    
HELIX  158 158 ASP b  313  ASN b  318  5                                   6    
HELIX  159 159 PRO b  329  GLY b  333  5                                   5    
HELIX  160 160 SER b  391  GLY b  396  1                                   6    
HELIX  161 161 ASP b  413  ILE b  425  1                                  13    
HELIX  162 162 SER b  446  PHE b  475  1                                  30    
HELIX  163 163 ALA c   34  ILE c   43  5                                  10    
HELIX  164 164 LEU c   45  PHE c   75  1                                  31    
HELIX  165 165 PRO c   80  GLN c   84  5                                   5    
HELIX  166 166 LEU c   88  LEU c   95  1                                   8    
HELIX  167 167 GLY c  100  GLU c  104  5                                   5    
HELIX  168 168 THR c  108  ARG c  135  1                                  28    
HELIX  169 169 ASP c  153  PHE c  181  1                                  29    
HELIX  170 170 ASP c  205  PHE c  210  1                                   6    
HELIX  171 171 GLY c  211  LYS c  215  5                                   5    
HELIX  172 172 GLY c  222  VAL c  227  5                                   6    
HELIX  173 173 ASN c  229  LEU c  253  1                                  25    
HELIX  174 174 GLY c  258  PHE c  264  1                                   7    
HELIX  175 175 SER c  267  ASN c  293  1                                  27    
HELIX  176 176 THR c  305  LEU c  324  1                                  20    
HELIX  177 177 ASN c  327  ALA c  331  5                                   5    
HELIX  178 178 GLY c  353  TRP c  359  5                                   7    
HELIX  179 179 LEU c  366  PRO c  368  5                                   3    
HELIX  180 180 ASP c  376  ASP c  383  1                                   8    
HELIX  181 181 GLN c  385  THR c  397  1                                  13    
HELIX  182 182 SER c  421  GLY c  454  1                                  34    
HELIX  183 183 GLU c  464  MET c  469  5                                   6    
HELIX  184 184 TRP d   14  LYS d   23  1                                  10    
HELIX  185 185 VAL d   30  PHE d   54  1                                  25    
HELIX  186 186 SER d   57  GLY d   62  1                                   6    
HELIX  187 187 ALA d   82  GLY d   86  5                                   5    
HELIX  188 188 ASP d  100  LEU d  107  1                                   8    
HELIX  189 189 GLY d  108  GLY d  137  1                                  30    
HELIX  190 190 PRO d  140  PHE d  146  1                                   7    
HELIX  191 191 PHE d  146  LEU d  158  1                                  13    
HELIX  192 192 LEU d  158  GLN d  164  1                                   7    
HELIX  193 193 SER d  166  ALA d  170  5                                   5    
HELIX  194 194 VAL d  175  PHE d  188  1                                  14    
HELIX  195 195 ASN d  190  LEU d  193  5                                   4    
HELIX  196 196 ASN d  194  ASN d  220  1                                  27    
HELIX  197 197 SER d  245  PHE d  257  1                                  13    
HELIX  198 198 ASN d  263  LEU d  291  1                                  29    
HELIX  199 199 PHE d  298  ASP d  308  1                                  11    
HELIX  200 200 THR d  313  GLN d  334  1                                  22    
HELIX  201 201 PRO d  335  ASN d  338  5                                   4    
HELIX  202 202 PRO d  342  LEU d  346  5                                   5    
HELIX  203 203 PRO e    9  SER e   16  1                                   8    
HELIX  204 204 SER e   16  THR e   40  1                                  25    
HELIX  205 205 GLY e   41  PHE e   47  1                                   7    
HELIX  206 206 GLU e   71  GLN e   82  1                                  12    
HELIX  207 207 THR f   17  GLN f   41  1                                  25    
HELIX  208 208 THR h    5  ARG h   12  1                                   8    
HELIX  209 209 THR h   27  ASN h   50  1                                  24    
HELIX  210 210 GLU i    2  SER i   25  1                                  24    
HELIX  211 211 PRO j    9  ALA j   32  1                                  24    
HELIX  212 212 PRO k   12  ILE k   17  5                                   6    
HELIX  213 213 PHE k   18  ASP k   23  1                                   6    
HELIX  214 214 VAL k   24  PRO k   26  5                                   3    
HELIX  215 215 VAL k   27  VAL k   43  1                                  17    
HELIX  216 216 ASN l   13  ASN l   37  1                                  25    
HELIX  217 217 LEU m    6  SER m   31  1                                  26    
HELIX  218 218 GLY o   40  LYS o   44  5                                   5    
HELIX  219 219 LEU o  208  VAL o  213  1                                   6    
HELIX  220 220 GLU t    2  PHE t   23  1                                  22    
HELIX  221 221 ASN u   41  LEU u   47  1                                   7    
HELIX  222 222 ASN u   61  TYR u   68  5                                   8    
HELIX  223 223 TYR u   72  ASN u   82  1                                  11    
HELIX  224 224 SER u   87  ILE u   94  5                                   8    
HELIX  225 225 THR u   98  LEU u  109  1                                  12    
HELIX  226 226 GLU u  118  GLU u  123  1                                   6    
HELIX  227 227 GLY u  124  ASP u  126  5                                   3    
HELIX  228 228 THR v   48  CYS v   63  1                                  16    
HELIX  229 229 CYS v   63  VAL v   68  1                                   6    
HELIX  230 230 GLY v   69  ILE v   71  5                                   3    
HELIX  231 231 ARG v   81  LEU v   87  1                                   7    
HELIX  232 232 ASN v   94  MET v  102  1                                   9    
HELIX  233 233 SER v  120  ALA v  124  5                                   5    
HELIX  234 234 PRO v  128  LEU v  133  1                                   6    
HELIX  235 235 THR v  134  GLY v  153  1                                  20    
HELIX  236 236 GLY v  153  GLY v  158  1                                   6    
HELIX  237 237 GLN g   21  ARG g   42  1                                  22    
HELIX  238 238 THR x   13  GLN x   42  1                                  30    
HELIX  239 239 THR z    2  SER z   29  1                                  28    
HELIX  240 240 ARG z   35  VAL z   62  1                                  28    
HELIX  241 241 UNK Y    2  UNK Y   13  1                                  12    
HELIX  242 242 UNK Y   14  UNK Y   25  1                                  12    
SHEET    1   A 2 ALA A  81  VAL A  82  0                                        
SHEET    2   A 2 LEU A 174  GLY A 175 -1  O  LEU A 174   N  VAL A  82           
SHEET    1   B 2 LEU A 297  ASN A 298  0                                        
SHEET    2   B 2 GLY C 402  SER C 403  1  O  GLY C 402   N  ASN A 298           
SHEET    1   C 2 MET B 166  VAL B 168  0                                        
SHEET    2   C 2 SER B 177  GLN B 179 -1  O  SER B 177   N  VAL B 168           
SHEET    1   D 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 ILE B 336  ARG B 347 -1  N  PHE B 346   O  LEU B 354           
SHEET    5   D 6 THR B 398  TYR B 402 -1  O  SER B 400   N  VAL B 345           
SHEET    6   D 6 THR B 410  PHE B 411 -1  O  PHE B 411   N  VAL B 399           
SHEET    1   E 5 VAL B 377  ASP B 380  0                                        
SHEET    2   E 5 ILE B 369  THR B 371 -1  N  LEU B 370   O  ALA B 379           
SHEET    3   E 5 GLU B 353  VAL B 356 -1  N  PHE B 355   O  THR B 371           
SHEET    4   E 5 ILE B 336  ARG B 347 -1  N  PHE B 346   O  LEU B 354           
SHEET    5   E 5 ILE B 429  ASP B 433 -1  O  GLU B 431   N  GLN B 338           
SHEET    1   F 2 LEU C 185  ASP C 187  0                                        
SHEET    2   F 2 ASP C 195  ARG C 197 -1  O  ARG C 197   N  LEU C 185           
SHEET    1   G 2 LEU C 341  ARG C 343  0                                        
SHEET    2   G 2 ILE C 349  PHE C 351 -1  O  ILE C 350   N  MET C 342           
SHEET    1   H 2 ARG C 370  GLY C 371  0                                        
SHEET    2   H 2 GLY C 374  LEU C 375 -1  O  GLY C 374   N  GLY C 371           
SHEET    1   I 2 TYR O  56  PRO O  57  0                                        
SHEET    2   I 2 SER O 161  ILE O 162 -1  O  ILE O 162   N  TYR O  56           
SHEET    1   J10 PHE O  91  PRO O  93  0                                        
SHEET    2   J10 ARG O  65  LYS O  79 -1  N  VAL O  78   O  VAL O  92           
SHEET    3   J10 GLU O 258  GLU O 270 -1  O  LYS O 260   N  LEU O  77           
SHEET    4   J10 GLU O 236  LEU O 246 -1  N  SER O 243   O  ILE O 261           
SHEET    5   J10 LEU O 218  LYS O 229 -1  N  ALA O 228   O  ALA O 238           
SHEET    6   J10 PHE O 168  PRO O 175 -1  N  VAL O 174   O  THR O 219           
SHEET    7   J10 LYS O 149  SER O 154 -1  N  LYS O 149   O  ASN O 173           
SHEET    8   J10 LEU O 119  ILE O 127 -1  N  GLU O 123   O  LEU O 151           
SHEET    9   J10 LEU O 104  VAL O 113 -1  N  GLN O 108   O  GLU O 124           
SHEET   10   J10 ARG O  65  LYS O  79 -1  N  LEU O  71   O  LEU O 104           
SHEET    1   K 3 LYS O  95  LEU O  96  0                                        
SHEET    2   K 3 PHE O 129  GLN O 135 -1  O  GLN O 135   N  LYS O  95           
SHEET    3   K 3 ARG O 141  THR O 147 -1  O  ILE O 142   N  VAL O 134           
SHEET    1   L 2 ILE U  55  ASP U  56  0                                        
SHEET    2   L 2 PHE U 112  THR U 113  1  O  THR U 113   N  ILE U  55           
SHEET    1   M 2 THR V  35  PRO V  37  0                                        
SHEET    2   M 2 THR V  44  THR V  46 -1  O  ILE V  45   N  VAL V  36           
SHEET    1   N 2 ALA a  81  VAL a  82  0                                        
SHEET    2   N 2 LEU a 174  GLY a 175 -1  O  LEU a 174   N  VAL a  82           
SHEET    1   O 2 LEU a 297  ASN a 298  0                                        
SHEET    2   O 2 GLY c 402  SER c 403  1  O  GLY c 402   N  ASN a 298           
SHEET    1   P 2 MET b 166  VAL b 168  0                                        
SHEET    2   P 2 SER b 177  GLN b 179 -1  O  SER b 177   N  VAL b 168           
SHEET    1   Q 6 VAL b 377  ASP b 380  0                                        
SHEET    2   Q 6 ILE b 369  THR b 371 -1  N  LEU b 370   O  ALA b 379           
SHEET    3   Q 6 GLU b 353  VAL b 356 -1  N  PHE b 355   O  THR b 371           
SHEET    4   Q 6 ILE b 336  ARG b 347 -1  N  PHE b 346   O  LEU b 354           
SHEET    5   Q 6 THR b 398  TYR b 402 -1  O  THR b 398   N  ARG b 347           
SHEET    6   Q 6 THR b 410  PHE b 411 -1  O  PHE b 411   N  VAL b 399           
SHEET    1   R 5 VAL b 377  ASP b 380  0                                        
SHEET    2   R 5 ILE b 369  THR b 371 -1  N  LEU b 370   O  ALA b 379           
SHEET    3   R 5 GLU b 353  VAL b 356 -1  N  PHE b 355   O  THR b 371           
SHEET    4   R 5 ILE b 336  ARG b 347 -1  N  PHE b 346   O  LEU b 354           
SHEET    5   R 5 ILE b 429  ASP b 433 -1  O  GLU b 431   N  GLN b 338           
SHEET    1   S 2 LEU c 185  ASP c 187  0                                        
SHEET    2   S 2 ASP c 195  ARG c 197 -1  O  ARG c 197   N  LEU c 185           
SHEET    1   T 2 LEU c 341  ARG c 343  0                                        
SHEET    2   T 2 ILE c 349  PHE c 351 -1  O  ILE c 350   N  MET c 342           
SHEET    1   U 2 ARG c 370  GLY c 371  0                                        
SHEET    2   U 2 GLY c 374  LEU c 375 -1  O  GLY c 374   N  GLY c 371           
SHEET    1   V 2 ALA d  77  VAL d  78  0                                        
SHEET    2   V 2 PHE d 173  GLY d 174 -1  O  PHE d 173   N  VAL d  78           
SHEET    1   W 2 TYR o  56  PRO o  57  0                                        
SHEET    2   W 2 SER o 161  ILE o 162 -1  O  ILE o 162   N  TYR o  56           
SHEET    1   X10 PHE o  91  PRO o  93  0                                        
SHEET    2   X10 ARG o  65  LYS o  79 -1  N  VAL o  78   O  VAL o  92           
SHEET    3   X10 GLU o 258  GLU o 270 -1  O  LYS o 260   N  LEU o  77           
SHEET    4   X10 GLU o 236  LEU o 246 -1  N  ILE o 237   O  ALA o 267           
SHEET    5   X10 LEU o 218  LYS o 229 -1  N  GLN o 222   O  GLU o 244           
SHEET    6   X10 PHE o 168  PRO o 175 -1  N  VAL o 174   O  THR o 219           
SHEET    7   X10 LYS o 149  SER o 154 -1  N  LYS o 149   O  ASN o 173           
SHEET    8   X10 LEU o 119  ILE o 127 -1  N  PHE o 121   O  ALA o 153           
SHEET    9   X10 LEU o 104  VAL o 113 -1  N  GLN o 108   O  GLU o 124           
SHEET   10   X10 ARG o  65  LYS o  79 -1  N  LEU o  71   O  LEU o 104           
SHEET    1   Y 3 LYS o  95  LEU o  96  0                                        
SHEET    2   Y 3 PHE o 129  GLN o 135 -1  O  GLN o 135   N  LYS o  95           
SHEET    3   Y 3 ARG o 141  THR o 147 -1  O  ILE o 142   N  VAL o 134           
SHEET    1   Z 2 ILE u  55  ASP u  56  0                                        
SHEET    2   Z 2 PHE u 112  THR u 113  1  O  THR u 113   N  ILE u  55           
SHEET    1  AA 2 THR v  35  PRO v  37  0                                        
SHEET    2  AA 2 THR v  44  THR v  46 -1  O  ILE v  45   N  VAL v  36           
SSBOND   1 CYS O   45    CYS O   70                          1555   1555  2.03  
SSBOND   2 CYS o   45    CYS o   70                          1555   1555  2.03  
LINK         OE2 GLU A 189                MN1  OEC A 409     1555   1555  1.76  
LINK         OE2 GLU a 189                MN1  OEC a 411     1555   1555  1.77  
LINK         OE1 GLU a 333                MN3  OEC a 411     1555   1555  2.21  
LINK         OE1 GLU A 333                MN3  OEC A 409     1555   1555  2.21  
LINK         OE2 GLU c 354                MN3  OEC a 411     1555   1555  2.25  
LINK         OE2 GLU C 354                MN3  OEC A 409     1555   1555  2.27  
LINK         OD2 ASP a 170                MN4  OEC a 411     1555   1555  2.29  
LINK         OD1 ASP a 342                MN2  OEC a 411     1555   1555  2.29  
LINK         OD1 ASP A 342                MN2  OEC A 409     1555   1555  2.29  
LINK         OD2 ASP A 170                MN4  OEC A 409     1555   1555  2.31  
LINK         OE1 GLU A 189                CA1  OEC A 409     1555   1555  2.33  
LINK         NE2 HIS A 332                MN1  OEC A 409     1555   1555  2.33  
LINK         OE2 GLU A 333                MN4  OEC A 409     1555   1555  2.35  
LINK         NE2 HIS A 215                FE   FE2 A 401     1555   1555  2.36  
LINK         OE1 GLU a 189                CA1  OEC a 411     1555   1555  2.36  
LINK         NE2 HIS a 215                FE   FE2 a 403     1555   1555  2.41  
LINK         NE2 HIS V  67                FE   HEM V 201     1555   1555  2.42  
LINK         OE2 GLU a 333                MN4  OEC a 411     1555   1555  2.42  
LINK         NE2 HIS D 214                FE   FE2 A 401     1555   1555  2.46  
LINK         OE1 GLU o 140                CA    CA o 301     1555   1555  2.47  
LINK         NE2 HIS v  67                FE   HEM v 201     1555   1555  2.50  
LINK         NE2 HIS a 332                MN1  OEC a 411     1555   1555  2.50  
LINK         NE2 HIS d 214                FE   FE2 a 403     1555   1555  2.51  
LINK         NE2 HIS A 272                FE   FE2 A 401     1555   1555  2.52  
LINK         NE2 HIS d 268                FE   FE2 a 403     1555   1555  2.55  
LINK         NE2 HIS V 118                FE   HEM V 201     1555   1555  2.56  
LINK         OD2 ASP A 342                MN1  OEC A 409     1555   1555  2.57  
LINK        FE   FE2 a 403                 O2  BCT d 401     1555   1555  2.57  
LINK         OD2 ASP k  19                CA    CA k 101     1555   1555  2.58  
LINK         NE2 HIS a 272                FE   FE2 a 403     1555   1555  2.59  
LINK         O   ALA a 344                MN2  OEC a 411     1555   1555  2.60  
LINK         OE1 GLU O 140                CA    CA O 301     1555   1555  2.61  
LINK         OD2 ASP a 342                MN1  OEC a 411     1555   1555  2.62  
LINK         NE2 HIS D 268                FE   FE2 A 401     1555   1555  2.62  
LINK         O   ALA A 344                MN2  OEC A 409     1555   1555  2.62  
LINK         NE2 HIS F  24                FE   HEM F 101     1555   1555  2.64  
LINK        FE   FE2 A 401                 O2  BCT A 402     1555   1555  2.65  
LINK         NE2 HIS v 118                FE   HEM v 201     1555   1555  2.66  
LINK         NE2 HIS e  23                FE   HEM f 101     1555   1555  2.67  
LINK         NE2 HIS E  23                FE   HEM F 101     1555   1555  2.69  
LINK        FE   FE2 a 403                 O3  BCT d 401     1555   1555  2.71  
LINK        FE   FE2 A 401                 O3  BCT A 402     1555   1555  2.72  
LINK         OD2 ASP K  19                CA    CA K 101     1555   1555  2.73  
LINK         NE2 HIS f  24                FE   HEM f 101     1555   1555  2.74  
LINK         OD2 ASP K  23                CA    CA K 101     1555   1555  2.82  
LINK         OD1 ASP A 170                CA1  OEC A 409     1555   1555  2.92  
LINK         OD1 ASP a 170                CA1  OEC a 411     1555   1555  2.93  
LINK         OD1 ASN C  39                MG   CLA C 511     1555   1555  2.94  
LINK         OD2 ASP k  23                CA    CA k 101     1555   1555  2.97  
LINK         O   ALA a 344                CA1  OEC a 411     1555   1555  3.06  
LINK         O   ALA A 344                CA1  OEC A 409     1555   1555  3.07  
LINK         OD1 ASP K  23                CA    CA K 101     1555   1555  3.08  
LINK         OD1 ASP k  23                CA    CA k 101     1555   1555  3.14  
CISPEP   1 THR V   89    PRO V   90          0        -1.67                     
CISPEP   2 THR v   89    PRO v   90          0        -1.29                     
SITE     1 AC1  5 HIS A 215  HIS A 272  BCT A 402  HIS D 214                    
SITE     2 AC1  5 HIS D 268                                                     
SITE     1 AC2  9 HIS A 215  GLU A 244  TYR A 246  HIS A 272                    
SITE     2 AC2  9 FE2 A 401  HIS D 214  TYR D 244  LYS D 264                    
SITE     3 AC2  9 HIS D 268                                                     
SITE     1 AC3 25 PHE A 119  TYR A 147  PRO A 150  SER A 153                    
SITE     2 AC3 25 VAL A 157  MET A 183  ILE A 184  PHE A 186                    
SITE     3 AC3 25 GLN A 187  ILE A 192  LEU A 193  HIS A 198                    
SITE     4 AC3 25 GLY A 201  VAL A 205  PHE A 206  VAL A 283                    
SITE     5 AC3 25 THR A 286  ILE A 290  CLA A 404  CLA A 405                    
SITE     6 AC3 25 LEU D 182  LEU D 205  CLA D 401  PHO D 402                    
SITE     7 AC3 25 PHE T  17                                                     
SITE     1 AC4 13 THR A  45  PHE A 158  MET A 172  ILE A 176                    
SITE     2 AC4 13 THR A 179  MET A 183  CLA A 403  MET D 198                    
SITE     3 AC4 13 VAL D 201  ALA D 202  CLA D 401  PHO D 402                    
SITE     4 AC4 13 PL9 D 404                                                     
SITE     1 AC5 14 GLN A 199  VAL A 202  ALA A 203  TRP A 278                    
SITE     2 AC5 14 CLA A 403  PHO A 406  PHE D 157  VAL D 175                    
SITE     3 AC5 14 ILE D 178  PHE D 179  PHE D 181  LEU D 182                    
SITE     4 AC5 14 CLA D 401  PL9 J 101                                          
SITE     1 AC6 20 PHE A 206  ALA A 209  LEU A 210  MET A 214                    
SITE     2 AC6 20 LEU A 258  CLA A 405  PL9 A 408  ALA D  41                    
SITE     3 AC6 20 TRP D  48  PHE D 125  GLN D 129  ASN D 142                    
SITE     4 AC6 20 ALA D 145  PHE D 146  ALA D 148  PHE D 153                    
SITE     5 AC6 20 PHE D 173  PRO D 275  LEU D 279  CLA D 401                    
SITE     1 AC7 15 ILE A  36  PRO A  39  THR A  40  PHE A  93                    
SITE     2 AC7 15 PRO A  95  ILE A  96  TRP A  97  LEU A 114                    
SITE     3 AC7 15 HIS A 118  LEU A 121  BCR A 410  DGD A 411                    
SITE     4 AC7 15 SQD A 417  TYR I   9  PHE I  15                               
SITE     1 AC8 17 PHE A 211  HIS A 215  LEU A 218  HIS A 252                    
SITE     2 AC8 17 PHE A 255  SER A 264  PHE A 265  LEU A 271                    
SITE     3 AC8 17 PHE A 274  PHO A 406  PHE D  38  ALA D  41                    
SITE     4 AC8 17 TYR D  42  LEU D  45  ALA F  22  THR F  25                    
SITE     5 AC8 17 PL9 J 101                                                     
SITE     1 AC9  7 ASP A 170  GLU A 189  HIS A 332  GLU A 333                    
SITE     2 AC9  7 ASP A 342  ALA A 344  GLU C 354                               
SITE     1 BC1  6 VAL A  35  ILE A  38  ALA A  43  CLA A 407                    
SITE     2 BC1  6 SQD A 417  LMT b 604                                          
SITE     1 BC2 14 PHE A  93  TRP A  97  GLU A  98  CLA A 407                    
SITE     2 BC2 14 LEU C 214  LYS C 215  SER C 216  PRO C 217                    
SITE     3 BC2 14 TRP C 223  PHE C 284  DGD C 517  LYS I   5                    
SITE     4 BC2 14 TYR I   9  GLY O  38                                          
SITE     1 BC3 15 ARG A 140  TRP A 142  PHE A 273  SQD A 413                    
SITE     2 BC3 15 TRP C  36  PHE C 436  TRP C 443  ARG C 447                    
SITE     3 BC3 15 CLA C 508  CLA C 510  ASN D 220  ALA D 229                    
SITE     4 BC3 15 SER D 230  THR D 231  PHE D 232                               
SITE     1 BC4 13 ASN A 267  SER A 270  PHE A 273  PHE A 274                    
SITE     2 BC4 13 LHG A 412  LHG A 415  TRP C  36  DGD C 518                    
SITE     3 BC4 13 DGD C 519  PHE D 232  ARG D 233  PL9 J 101                    
SITE     4 BC4 13 PHE K  37                                                     
SITE     1 BC5 17 SER A 232  ASN A 234  TRP B   5  TYR B   6                    
SITE     2 BC5 17 CLA B 611  LMG B 622  TRP D 266  PHE D 269                    
SITE     3 BC5 17 PHE D 270  PHE D 273  PL9 D 404  LMG D 407                    
SITE     4 BC5 17 GLU L  11  ASN L  13  SER L  16  GLY L  20                    
SITE     5 BC5 17 VAL L  26                                                     
SITE     1 BC6  9 TYR A 262  SER A 264  ASN A 266  SQD A 413                    
SITE     2 BC6  9 TRP C  35  DGD C 518  LMG E 101  BCR J 102                    
SITE     3 BC6  9 PHE K  45                                                     
SITE     1 BC7  2 ASN A 181  LYS D 317                                          
SITE     1 BC8 14 TRP A  20  ASN A  26  ARG A  27  LEU A  28                    
SITE     2 BC8 14 LEU A  41  LEU A  42  CLA A 407  BCR A 410                    
SITE     3 BC8 14 BCR T 102  TRP b 113  TYR b 117  CLA b 610                    
SITE     4 BC8 14 CLA b 620  BCR b 622                                          
SITE     1 BC9 11 LEU A  72  TYR A  73  LEU A 102  ASP A 103                    
SITE     2 BC9 11 LEU A 106  ARG D 304  GLY O 138  ALA b  43                    
SITE     3 BC9 11 TRP b  75  SER b  76  LEU b  98                               
SITE     1 CC1  8 TRP B 185  PRO B 187  PHE B 190  ILE B 207                    
SITE     2 CC1  8 CLA B 602  PHE H  41  ILE H  44  BCR H 101                    
SITE     1 CC2 16 GLU B 184  GLY B 189  GLY B 197  HIS B 201                    
SITE     2 CC2 16 ALA B 204  ALA B 205  VAL B 208  PHE B 247                    
SITE     3 CC2 16 CLA B 601  CLA B 603  DGD B 621  VAL D 154                    
SITE     4 CC2 16 PHE H  38  PHE H  41  ILE H  45  TYR H  49                    
SITE     1 CC3 18 ARG B  68  LEU B  69  ALA B 146  LEU B 149                    
SITE     2 CC3 18 CYS B 150  PHE B 153  HIS B 201  HIS B 202                    
SITE     3 CC3 18 PHE B 247  ALA B 248  VAL B 252  THR B 262                    
SITE     4 CC3 18 CLA B 602  CLA B 604  CLA B 605  CLA B 606                    
SITE     5 CC3 18 PHE H  38  LEU H  42                                          
SITE     1 CC4 19 TRP B  33  PHE B  61  PHE B  65  ARG B  68                    
SITE     2 CC4 19 LEU B 149  VAL B 245  ALA B 248  ALA B 249                    
SITE     3 CC4 19 VAL B 252  PHE B 451  HIS B 455  PHE B 458                    
SITE     4 CC4 19 ALA B 459  PHE B 462  CLA B 603  CLA B 605                    
SITE     5 CC4 19 CLA B 607  CLA B 612  CLA B 615                               
SITE     1 CC5 17 THR B  27  VAL B  30  ALA B  31  VAL B  62                    
SITE     2 CC5 17 PHE B  65  MET B  66  ARG B  68  LEU B  69                    
SITE     3 CC5 17 VAL B  96  HIS B 100  LEU B 103  ALA B 205                    
SITE     4 CC5 17 CLA B 603  CLA B 604  CLA B 606  CLA B 610                    
SITE     5 CC5 17 CLA B 612                                                     
SITE     1 CC6 15 LEU B  69  TRP B  91  LEU B 103  LEU B 106                    
SITE     2 CC6 15 GLY B 152  PHE B 153  PHE B 156  HIS B 157                    
SITE     3 CC6 15 PHE B 162  PRO B 164  CLA B 603  CLA B 605                    
SITE     4 CC6 15 BCR B 620  LMT B 624  SQD a 401                               
SITE     1 CC7 17 TRP B  33  MET B  37  TYR B  40  GLN B  58                    
SITE     2 CC7 17 GLY B  59  PHE B  61  THR B 327  GLY B 328                    
SITE     3 CC7 17 PRO B 329  TRP B 450  ALA B 454  CLA B 604                    
SITE     4 CC7 17 BCR B 618  LMG B 623  MET D 281  LEU L  27                    
SITE     5 CC7 17 PHE M  14                                                     
SITE     1 CC8 17 THR B 236  SER B 239  SER B 240  ALA B 243                    
SITE     2 CC8 17 PHE B 246  PHE B 463  HIS B 466  LEU B 474                    
SITE     3 CC8 17 CLA B 609  CLA B 610  PHE D 120  ILE D 123                    
SITE     4 CC8 17 MET D 126  LEU D 127  PHE D 130  CLA D 403                    
SITE     5 CC8 17 SQD D 408                                                     
SITE     1 CC9 15 PHE B 139  ALA B 212  PHE B 215  HIS B 216                    
SITE     2 CC9 15 PRO B 221  PRO B 222  LEU B 229  CLA B 608                    
SITE     3 CC9 15 CLA B 610  THR H  27  THR H  28  MET H  31                    
SITE     4 CC9 15 PHE H  34  MET H  35  BCR H 101                               
SITE     1 DC1 13 LEU B 135  PHE B 139  HIS B 142  LEU B 143                    
SITE     2 DC1 13 ALA B 146  VAL B 237  SER B 240  CLA B 605                    
SITE     3 DC1 13 CLA B 608  CLA B 609  CLA B 612  CLA B 615                    
SITE     4 DC1 13 BCR H 101                                                     
SITE     1 DC2 17 LMG A 414  TRP B   5  TYR B   6  ARG B   7                    
SITE     2 DC2 17 VAL B   8  HIS B   9  LEU B 238  PHE B 462                    
SITE     3 DC2 17 PHE B 464  GLY B 465  TRP B 468  HIS B 469                    
SITE     4 DC2 17 ARG B 472  CLA B 612  CLA B 613  CLA B 614                    
SITE     5 DC2 17 LMG B 622                                                     
SITE     1 DC3 18 HIS B   9  LEU B  12  LEU B  19  HIS B  23                    
SITE     2 DC3 18 HIS B  26  THR B  27  ILE B 234  VAL B 237                    
SITE     3 DC3 18 LEU B 238  SER B 241  VAL B 245  CLA B 604                    
SITE     4 DC3 18 CLA B 605  CLA B 610  CLA B 611  CLA B 613                    
SITE     5 DC3 18 CLA B 614  CLA B 615                                          
SITE     1 DC4  8 HIS B   9  HIS B  26  VAL B  30  PHE B 462                    
SITE     2 DC4  8 CLA B 611  CLA B 612  CLA B 614  BCR B 619                    
SITE     1 DC5 15 VAL B   8  HIS B   9  VAL B  11  LEU B  12                    
SITE     2 DC5 15 LEU B  29  TRP B 115  CLA B 611  CLA B 612                    
SITE     3 DC5 15 CLA B 613  BCR B 617  LMG B 623  SQD B 626                    
SITE     4 DC5 15 VAL L  10  LMG m 102  PHE t   8                               
SITE     1 DC6 12 HIS B  23  MET B 138  ILE B 141  HIS B 142                    
SITE     2 DC6 12 LEU B 145  CLA B 604  CLA B 610  CLA B 612                    
SITE     3 DC6 12 CLA B 616  BCR B 620  LEU H  14  ASN H  15                    
SITE     1 DC7  7 LEU B  24  ALA B 110  TRP B 113  HIS B 114                    
SITE     2 DC7  7 CLA B 615  THR H   5  LEU H   7                               
SITE     1 DC8  9 MET B  25  LEU B  29  CYS B 112  TRP B 115                    
SITE     2 DC8  9 CLA B 614  BCR B 618  SQD B 626  LMT M 102                    
SITE     3 DC8  9 PHE t  19                                                     
SITE     1 DC9 13 TRP B  33  SER B  36  MET B  37  CLA B 607                    
SITE     2 DC9 13 BCR B 617  BCR B 619  LMT B 628  LMG d 407                    
SITE     3 DC9 13 ILE t   4  PHE t   8  ALA t  11  ILE t  14                    
SITE     4 DC9 13 PHE t  18                                                     
SITE     1 EC1  7 LEU B  29  GLY B  32  TRP B  33  GLY B 105                    
SITE     2 EC1  7 CLA B 613  BCR B 618  DGD B 627                               
SITE     1 EC2  9 LEU B 109  ALA B 110  CYS B 112  TYR B 117                    
SITE     2 EC2  9 CLA B 606  CLA B 615  LMT B 624  SQD a 401                    
SITE     3 EC2  9 PHE t  22                                                     
SITE     1 EC3 13 TYR B 193  PHE B 250  TYR B 258  TYR B 273                    
SITE     2 EC3 13 SER B 277  PHE B 463  CLA B 602  HIS D  87                    
SITE     3 EC3 13 TYR H  49  ASN H  50  VAL H  60  SER H  61                    
SITE     4 EC3 13 TRP H  62                                                     
SITE     1 EC4 11 ASN A 234  LMG A 414  TRP B   5  TYR B   6                    
SITE     2 EC4 11 ARG B   7  PHE B 464  TRP B 468  CLA B 611                    
SITE     3 EC4 11 ARG D 139  TYR D 141  PHE D 269                               
SITE     1 EC5 11 THR B 327  GLY B 328  PRO B 329  LYS B 332                    
SITE     2 EC5 11 CLA B 607  CLA B 614  ILE D 284  PHE L  35                    
SITE     3 EC5 11 ASN M   4  LEU M   6  LMT M 102                               
SITE     1 EC6  5 TRP B  91  PHE B 162  CLA B 606  BCR B 620                    
SITE     2 EC6  5 DGD B 627                                                     
SITE     1 EC7  7 ARG B 224  LYS B 227  ASP D  16  ASP D  19                    
SITE     2 EC7  7 SQD D 408  ALA H  32  MET H  35                               
SITE     1 EC8 11 ARG B  18  SER B 104  TRP B 115  CLA B 614                    
SITE     2 EC8 11 BCR B 617  ASN L   4  ARG l  14  TYR l  18                    
SITE     3 EC8 11 TYR m  26  PHE t  19  PHE t  23                               
SITE     1 EC9 12 TRP B  75  ASP B  87  GLY B  89  PHE B  90                    
SITE     2 EC9 12 TRP B  91  LEU B  98  VAL B 102  BCR B 619                    
SITE     3 EC9 12 LMT B 624  LMT B 629  ILE a  46  LMG i 101                    
SITE     1 FC1  5 SER B  36  ALA B  43  LEU B 437  BCR B 618                    
SITE     2 FC1  5 VAL t   7                                                     
SITE     1 FC2  8 GLY B  85  ASP B  87  DGD B 627  ALA a 100                    
SITE     2 FC2  8 MET i   1  LEU i   4  LMG i 101  LYS o  95                    
SITE     1 FC3 18 LEU C  95  LEU C 168  GLY C 171  ALA C 172                    
SITE     2 FC3 18 LEU C 185  ILE C 224  VAL C 233  HIS C 237                    
SITE     3 FC3 18 ILE C 240  ALA C 278  MET C 282  PHE C 289                    
SITE     4 FC3 18 VAL C 296  TYR C 297  CLA C 502  CLA C 503                    
SITE     5 FC3 18 CLA C 507  BCR C 516                                          
SITE     1 FC4 18 TRP C  63  HIS C  91  TRP C  97  GLY C 171                    
SITE     2 FC4 18 LEU C 174  LYS C 178  PHE C 182  LEU C 279                    
SITE     3 FC4 18 MET C 282  ALA C 286  TYR C 297  HIS C 430                    
SITE     4 FC4 18 LEU C 433  PHE C 437  CLA C 501  CLA C 503                    
SITE     5 FC4 18 CLA C 509  CLA C 510                                          
SITE     1 FC5 14 ILE C  60  VAL C  61  ALA C  64  THR C  68                    
SITE     2 FC5 14 LEU C  88  HIS C  91  ILE C  92  VAL C 114                    
SITE     3 FC5 14 HIS C 118  CLA C 501  CLA C 502  CLA C 510                    
SITE     4 FC5 14 CLA C 512  LMG C 521                                          
SITE     1 FC6 15 PHE A 285  TRP C  63  MET C  67  PHE C  70                    
SITE     2 FC6 15 GLN C  84  GLY C  85  ILE C  87  TRP C 425                    
SITE     3 FC6 15 SER C 429  CLA C 508  DGD C 518  DGD C 519                    
SITE     4 FC6 15 LMG C 520  PRO K  26  VAL K  30                               
SITE     1 FC7 18 PHE A  33  MET A 127  GLY A 128  TRP A 131                    
SITE     2 FC7 18 PHE C 264  ILE C 265  SER C 273  TYR C 274                    
SITE     3 FC7 18 GLY C 277  ALA C 278  MET C 281  HIS C 441                    
SITE     4 FC7 18 LEU C 442  ALA C 445  ARG C 449  CLA C 507                    
SITE     5 FC7 18 BCR C 516  PHE I  23                                          
SITE     1 FC8 13 LEU C 165  ILE C 243  GLY C 247  TRP C 250                    
SITE     2 FC8 13 HIS C 251  THR C 255  PRO C 256  PHE C 257                    
SITE     3 FC8 13 TRP C 259  ALA C 260  PHE C 264  CLA C 507                    
SITE     4 FC8 13 BCR C 516                                                     
SITE     1 FC9 16 MET C 157  LEU C 161  HIS C 164  ILE C 240                    
SITE     2 FC9 16 PHE C 264  TRP C 266  TYR C 271  TYR C 274                    
SITE     3 FC9 16 SER C 275  LEU C 279  MET C 282  CLA C 501                    
SITE     4 FC9 16 CLA C 505  CLA C 506  CLA C 509  BCR C 516                    
SITE     1 GC1 17 LHG A 412  TRP C  36  ALA C  37  ASN C  39                    
SITE     2 GC1 17 ALA C  40  GLU C 269  LEU C 276  PHE C 436                    
SITE     3 GC1 17 PHE C 437  GLY C 440  TRP C 443  HIS C 444                    
SITE     4 GC1 17 ARG C 447  CLA C 504  CLA C 509  CLA C 510                    
SITE     5 GC1 17 VAL K  30                                                     
SITE     1 GC2 19 ASN C  39  LEU C  42  LEU C  49  ALA C  52                    
SITE     2 GC2 19 HIS C  53  HIS C  56  TYR C 149  ILE C 160                    
SITE     3 GC2 19 GLY C 268  GLU C 269  TYR C 271  LEU C 272                    
SITE     4 GC2 19 SER C 275  CLA C 502  CLA C 507  CLA C 508                    
SITE     5 GC2 19 CLA C 510  CLA C 511  CLA C 512                               
SITE     1 GC3 17 LHG A 412  ASN C  39  HIS C  56  LEU C  59                    
SITE     2 GC3 17 ILE C  60  TRP C  63  LEU C 279  PHE C 436                    
SITE     3 GC3 17 PHE C 437  CLA C 502  CLA C 503  CLA C 508                    
SITE     4 GC3 17 CLA C 509  CLA C 511  PRO K  29  VAL K  30                    
SITE     5 GC3 17 LEU K  33                                                     
SITE     1 GC4 19 GLN C  28  TRP C  35  GLY C  38  ASN C  39                    
SITE     2 GC4 19 ARG C  41  LEU C  42  LYS C  48  PHE C 127                    
SITE     3 GC4 19 ILE C 134  CLA C 509  CLA C 510  BCR C 514                    
SITE     4 GC4 19 TRP K  39  GLN K  40  MET Z  19  VAL Z  20                    
SITE     5 GC4 19 PRO Z  24  ILE y  35  LEU y  46                               
SITE     1 GC5 12 HIS C  53  ALA C  57  PHE C 147  PHE C 163                    
SITE     2 GC5 12 HIS C 164  VAL C 167  LEU C 168  LEU C 174                    
SITE     3 GC5 12 CLA C 503  CLA C 509  CLA C 513  BCR C 515                    
SITE     1 GC6 10 LEU C  50  VAL C 124  GLY C 128  TYR C 131                    
SITE     2 GC6 10 HIS C 132  PRO C 137  LEU C 140  PHE C 147                    
SITE     3 GC6 10 CLA C 512  BCR C 515                                          
SITE     1 GC7 12 ALA C  55  LEU C  59  VAL C 116  LEU C 119                    
SITE     2 GC7 12 ILE C 120  SER C 122  ALA C 123  GLY C 126                    
SITE     3 GC7 12 CLA C 511  PHE K  32  VAL Z  13  BCR y 101                    
SITE     1 GC8  8 VAL C 116  SER C 121  VAL C 124  CLA C 512                    
SITE     2 GC8  8 CLA C 513  TYR K  15  GLY Z  55  ASN Z  58                    
SITE     1 GC9 13 ILE C 209  TYR C 212  LEU C 213  VAL C 227                    
SITE     2 GC9 13 ASP C 232  VAL C 233  ILE C 240  PHE C 264                    
SITE     3 GC9 13 CLA C 501  CLA C 505  CLA C 506  CLA C 507                    
SITE     4 GC9 13 VAL I  20                                                     
SITE     1 HC1 17 LEU A  91  PHE A 155  ILE A 163  DGD A 411                    
SITE     2 HC1 17 PRO C 217  PHE C 218  GLY C 219  GLY C 220                    
SITE     3 HC1 17 GLY C 222  VAL C 225  SER C 226  PHE C 284                    
SITE     4 HC1 17 CYS C 288  PHE C 292  ASN C 294  PHE C 361                    
SITE     5 HC1 17 ARG C 362                                                     
SITE     1 HC2 18 SQD A 413  LHG A 415  TYR C  82  GLU C  83                    
SITE     2 HC2 18 GLN C  84  GLY C  85  LEU C 404  SER C 406                    
SITE     3 HC2 18 ASN C 418  PHE C 419  VAL C 420  TRP C 425                    
SITE     4 HC2 18 SER C 429  CLA C 504  DGD C 519  LMG C 520                    
SITE     5 HC2 18 TYR J  33  BCR J 102                                          
SITE     1 HC3 19 LEU A 200  TRP A 278  PHE A 300  ASN A 301                    
SITE     2 HC3 19 SER A 305  SQD A 413  ASN C 405  ASN C 415                    
SITE     3 HC3 19 SER C 416  ASN C 418  CLA C 504  DGD C 518                    
SITE     4 HC3 19 LMG D 406  ALA J  32  TYR J  33  GLY J  37                    
SITE     5 HC3 19 SER J  38  SER J  39  GLN V  60                               
SITE     1 HC4  7 HIS C  74  CLA C 504  DGD C 518  BCR J 102                    
SITE     2 HC4  7 ASP K  23  VAL K  27  ILE y  25                               
SITE     1 HC5  6 TRP C  97  PHE C 109  VAL C 117  HIS C 118                    
SITE     2 HC5  6 CLA C 503  PHE Z  59                                          
SITE     1 HC6 24 PHE A 206  CLA A 403  CLA A 404  CLA A 405                    
SITE     2 HC6 24 PHO A 406  TRP D  48  LEU D 122  VAL D 152                    
SITE     3 HC6 24 PHE D 153  SER D 155  VAL D 156  LEU D 182                    
SITE     4 HC6 24 PHE D 185  GLN D 186  TRP D 191  THR D 192                    
SITE     5 HC6 24 HIS D 197  GLY D 200  VAL D 201  VAL D 204                    
SITE     6 HC6 24 LEU D 279  SER D 282  ALA D 283  VAL D 286                    
SITE     1 HC7 18 LEU A  41  ALA A  44  THR A  45  ILE A 115                    
SITE     2 HC7 18 TYR A 126  GLN A 130  ALA A 146  TYR A 147                    
SITE     3 HC7 18 GLY A 175  VAL A 283  CLA A 403  CLA A 404                    
SITE     4 HC7 18 LEU D 205  ALA D 208  LEU D 209  ILE D 213                    
SITE     5 HC7 18 TRP D 253  PHE D 257                                          
SITE     1 HC8 15 CLA B 608  LEU D  43  LEU D  89  LEU D  90                    
SITE     2 HC8 15 LEU D  91  LEU D  92  TRP D  93  THR D 112                    
SITE     3 HC8 15 PHE D 113  HIS D 117  PHE D 120  LMT D 410                    
SITE     4 HC8 15 GLY X  22  LEU X  23  GLY X  26                               
SITE     1 HC9 20 PHE A  52  ILE A  77  CLA A 404  LMG A 414                    
SITE     2 HC9 20 MET D 199  ILE D 213  HIS D 214  THR D 217                    
SITE     3 HC9 20 TRP D 253  ILE D 259  ALA D 260  PHE D 261                    
SITE     4 HC9 20 LEU D 267  PHE D 273  VAL D 274  GLY D 278                    
SITE     5 HC9 20 LMG D 407  LEU L  23  VAL L  26  PHE T  10                    
SITE     1 IC1 10 TYR D  42  GLY D  46  LEU D  49  THR D  50                    
SITE     2 IC1 10 LMG D 406  DGD D 409  PRO F  29  PHE F  33                    
SITE     3 IC1 10 VAL J  21  VAL J  25                                          
SITE     1 IC2 12 DGD C 519  TYR D  67  GLY D  70  ASN D  72                    
SITE     2 IC2 12 PHE D  73  BCR D 405  MET F  40  GLN F  41                    
SITE     3 IC2 12 PHE J  28  GLY J  31  ALA J  32  GLY J  37                    
SITE     1 IC3 14 LMG A 414  PHE D 257  ALA D 260  PHE D 261                    
SITE     2 IC3 14 SER D 262  ASN D 263  TRP D 266  PL9 D 404                    
SITE     3 IC3 14 THR L  15  TYR L  18  LEU L  19  PHE T  17                    
SITE     4 IC3 14 ALA T  20  BCR T 102                                          
SITE     1 IC4 10 LYS B 227  ALA B 228  ARG B 230  LEU B 474                    
SITE     2 IC4 10 CLA B 608  LMT B 625  LYS D  23  TRP D  32                    
SITE     3 IC4 10 ARG D 134  LEU D 135                                          
SITE     1 IC5  8 ASP D 100  PHE D 101  THR D 102  BCR D 405                    
SITE     2 IC5  8 LMT D 410  LEU E  42  ASP E  45  VAL E  46                    
SITE     1 IC6  8 LEU D  92  TRP D  93  GLY D  99  CLA D 403                    
SITE     2 IC6  8 DGD D 409  ILE X  21  SER X  25  GLY X  26                    
SITE     1 IC7  7 TYR A 262  LHG A 415  PHE D  27  PRO E   9                    
SITE     2 IC7  7 PHE E  10  SER E  11  PL9 J 101                               
SITE     1 IC8 15 ARG E   8  PHE E  10  ILE E  13  ILE E  14                    
SITE     2 IC8 15 ARG E  18  TYR E  19  HIS E  23  THR E  26                    
SITE     3 IC8 15 LEU E  30  ILE F  15  ARG F  19  TRP F  20                    
SITE     4 IC8 15 HIS F  24  ALA F  27  ILE F  31                               
SITE     1 IC9 10 TRP D  21  ARG D  24  ARG D  26  GLU E   7                    
SITE     2 IC9 10 PHE F  16  THR F  17  VAL F  18  THR X  33                    
SITE     3 IC9 10 VAL X  36  ASP X  44                                          
SITE     1 JC1 10 CLA B 601  CLA B 609  CLA B 610  MET H  35                    
SITE     2 JC1 10 LEU H  37  PHE H  38  PHE H  41  ILE H  44                    
SITE     3 JC1 10 THR X  11  LEU X  16                                          
SITE     1 JC2  6 MET I   1  THR I   3  LEU I   4  LMT I 102                    
SITE     2 JC2  6 DGD b 602  LMT b 604                                          
SITE     1 JC3  3 THR I   3  ILE I   6  LMG I 101                               
SITE     1 JC4  5 CLA A 405  PL9 A 408  SQD A 413  LMG E 101                    
SITE     2 JC4  5 VAL J  16                                                     
SITE     1 JC5  6 LHG A 415  DGD C 518  LMG C 520  ILE J  22                    
SITE     2 JC5  6 PHE J  29  TYR J  33                                          
SITE     1 JC6  2 ASP K  19  ASP K  23                                          
SITE     1 JC7 11 VAL M  27  GLU M  30  SER M  31  CLA b 618                    
SITE     2 JC7 11 PRO l   9  VAL l  10  PHE m  21  ILE m  24                    
SITE     3 JC7 11 LEU m  25  GLN m  28  GLN m  32                               
SITE     1 JC8  8 TYR B  40  BCR B 617  LMG B 623  GLN M   5                    
SITE     2 JC8  8 MET m   1  GLU m   2  MET t   1  ILE t   4                    
SITE     1 JC9  3 GLU O  81  GLU O 140  HIS O 257                               
SITE     1 KC1 11 PHE T  19  BCR T 102  MET b  25  LEU b  29                    
SITE     2 KC1 11 TRP b 115  SQD b 601  CLA b 618  BCR b 621                    
SITE     3 KC1 11 ALA m  10  LEU m  13  LMT m 101                               
SITE     1 KC2 14 SQD A 417  LMG D 407  ILE T   4  PHE T   8                    
SITE     2 KC2 14 ALA T  11  PHE T  18  ILE T  21  BCR T 101                    
SITE     3 KC2 14 TRP b  33  SER b  36  MET b  37  LMT b 603                    
SITE     4 KC2 14 CLA b 611  BCR b 621                                          
SITE     1 KC3 13 ALA V  62  CYS V  63  CYS V  66  HIS V  67                    
SITE     2 KC3 13 THR V  74  ASN V  75  LEU V  78  ASP V  79                    
SITE     3 KC3 13 THR V  84  TYR V 101  TYR V 108  HIS V 118                    
SITE     4 KC3 13 PRO V 119                                                     
SITE     1 KC4 16 BCR C 514  ALA J  14  THR J  15  MET J  19                    
SITE     2 KC4 16 LEU K  21  ILE K  28  LEU K  31  ALA K  34                    
SITE     3 KC4 16 PHE K  37  VAL K  38  ALA K  41  SER Z  16                    
SITE     4 KC4 16 PHE Z  17  ILE y  28  GLY y  29  GLY y  32                    
SITE     1 KC5 11 TRP B 113  TYR B 117  CLA B 606  BCR B 620                    
SITE     2 KC5 11 TRP a  20  ASN a  26  ARG a  27  LEU a  28                    
SITE     3 KC5 11 LEU a  41  CLA a 409  BCR a 412                               
SITE     1 KC6 10 ALA B  43  TRP B  75  SER B  76  LEU B  98                    
SITE     2 KC6 10 LEU a  72  TYR a  73  LEU a 102  ASP a 103                    
SITE     3 KC6 10 ARG d 304  GLY o 138                                          
SITE     1 KC7  5 HIS a 215  HIS a 272  HIS d 214  HIS d 268                    
SITE     2 KC7  5 BCT d 401                                                     
SITE     1 KC8 24 PHE a 119  TYR a 147  PRO a 150  SER a 153                    
SITE     2 KC8 24 VAL a 157  MET a 183  ILE a 184  PHE a 186                    
SITE     3 KC8 24 GLN a 187  LEU a 193  HIS a 198  GLY a 201                    
SITE     4 KC8 24 VAL a 205  PHE a 206  VAL a 283  THR a 286                    
SITE     5 KC8 24 ILE a 290  CLA a 405  CLA a 406  PHO a 407                    
SITE     6 KC8 24 LEU d 182  LEU d 205  CLA d 402  LMG d 407                    
SITE     1 KC9 14 THR a  45  VAL a 157  PHE a 158  MET a 172                    
SITE     2 KC9 14 ILE a 176  THR a 179  PHE a 180  MET a 183                    
SITE     3 KC9 14 CLA a 404  PHO a 407  MET d 198  VAL d 201                    
SITE     4 KC9 14 CLA d 402  PL9 d 404                                          
SITE     1 LC1 15 GLN a 199  VAL a 202  ALA a 203  TRP a 278                    
SITE     2 LC1 15 CLA a 404  PHO a 408  PL9 a 410  PHE d 157                    
SITE     3 LC1 15 VAL d 175  ILE d 178  PHE d 179  PHE d 181                    
SITE     4 LC1 15 LEU d 182  CLA d 402  PL9 j 101                               
SITE     1 LC2 19 LEU a  41  ALA a  44  THR a  45  ILE a 115                    
SITE     2 LC2 19 TYR a 126  GLN a 130  ALA a 146  TYR a 147                    
SITE     3 LC2 19 PRO a 150  LEU a 174  VAL a 283  CLA a 404                    
SITE     4 LC2 19 CLA a 405  LEU d 205  ALA d 208  LEU d 209                    
SITE     5 LC2 19 ILE d 213  TRP d 253  PHE d 257                               
SITE     1 LC3 20 PHE a 206  ALA a 209  LEU a 210  MET a 214                    
SITE     2 LC3 20 LEU a 258  CLA a 406  ALA d  41  TRP d  48                    
SITE     3 LC3 20 GLY d 118  LEU d 122  PHE d 125  GLN d 129                    
SITE     4 LC3 20 ASN d 142  ALA d 145  PHE d 146  ALA d 148                    
SITE     5 LC3 20 PHE d 153  PRO d 275  LEU d 279  CLA d 402                    
SITE     1 LC4 15 ILE a  36  THR a  40  PHE a  93  PRO a  95                    
SITE     2 LC4 15 ILE a  96  TRP a  97  LEU a 114  HIS a 118                    
SITE     3 LC4 15 SQD a 401  BCR a 412  DGD a 413  TYR i   9                    
SITE     4 LC4 15 VAL i  12  PHE i  15  LMG i 101                               
SITE     1 LC5 15 HIS a 215  LEU a 218  HIS a 252  PHE a 255                    
SITE     2 LC5 15 SER a 264  PHE a 265  LEU a 271  PHE a 274                    
SITE     3 LC5 15 CLA a 406  PHE d  38  ALA d  41  TYR d  42                    
SITE     4 LC5 15 ALA f  22  THR f  25  PL9 j 101                               
SITE     1 LC6  7 ASP a 170  GLU a 189  HIS a 332  GLU a 333                    
SITE     2 LC6  7 ASP a 342  ALA a 344  GLU c 354                               
SITE     1 LC7  7 VAL a  35  ILE a  38  LEU a  42  ALA a  43                    
SITE     2 LC7  7 LEU a 106  SQD a 401  CLA a 409                               
SITE     1 LC8 15 PHE a  93  TRP a  97  GLU a  98  CLA a 409                    
SITE     2 LC8 15 LEU c 214  LYS c 215  SER c 216  PRO c 217                    
SITE     3 LC8 15 PHE c 218  TRP c 223  PHE c 284  DGD c 516                    
SITE     4 LC8 15 LYS i   5  TYR i   9  GLY o  38                               
SITE     1 LC9 15 ARG a 140  TRP a 142  VAL a 145  PHE a 273                    
SITE     2 LC9 15 SQD a 415  TRP c  36  TRP c 443  ARG c 447                    
SITE     3 LC9 15 CLA c 504  CLA c 508  ASN d 220  ALA d 229                    
SITE     4 LC9 15 SER d 230  THR d 231  PHE d 232                               
SITE     1 MC1 12 ASN a 267  SER a 270  PHE a 273  PHE a 274                    
SITE     2 MC1 12 LHG a 414  LHG a 417  TRP c  36  CLA c 508                    
SITE     3 MC1 12 DGD c 517  DGD c 518  PHE d 232  ARG d 233                    
SITE     1 MC2 16 SER a 232  ASN a 234  TRP b   5  TYR b   6                    
SITE     2 MC2 16 CLA b 618  LMG b 624  TRP d 266  PHE d 269                    
SITE     3 MC2 16 PHE d 270  PHE d 273  PL9 d 404  GLU l  11                    
SITE     4 MC2 16 ASN l  13  SER l  16  ILE l  24  VAL l  26                    
SITE     1 MC3  9 TYR a 262  SER a 264  ASN a 266  SQD a 415                    
SITE     2 MC3  9 TRP c  35  DGD c 517  LMG e 101  BCR j 102                    
SITE     3 MC3  9 PHE k  45                                                     
SITE     1 MC4  3 ASN a 181  GLU a 333  LYS d 317                               
SITE     1 MC5 10 TYR L  18  TYR M  26  PHE T  19  PHE T  23                    
SITE     2 MC5 10 BCR T 101  ARG b  18  SER b 104  TRP b 115                    
SITE     3 MC5 10 CLA b 618  ASN l   4                                          
SITE     1 MC6 12 ILE A  46  LMG I 101  TRP b  75  ASP b  87                    
SITE     2 MC6 12 GLY b  89  PHE b  90  TRP b  91  LEU b  98                    
SITE     3 MC6 12 VAL b 102  LMT b 604  BCR b 621  LMT b 626                    
SITE     1 MC7  5 VAL T   7  BCR T 102  SER b  36  ALA b  43                    
SITE     2 MC7  5 LEU b 437                                                     
SITE     1 MC8  6 BCR A 410  LMG I 101  LYS O  95  GLY b  85                    
SITE     2 MC8  6 ASP b  87  DGD b 602                                          
SITE     1 MC9  8 TRP b 185  PRO b 187  PHE b 190  ILE b 207                    
SITE     2 MC9  8 CLA b 606  PHE h  41  ILE h  44  BCR h 101                    
SITE     1 NC1 15 GLU b 184  GLY b 189  GLY b 197  HIS b 201                    
SITE     2 NC1 15 ALA b 204  ALA b 205  VAL b 208  PHE b 247                    
SITE     3 NC1 15 CLA b 605  CLA b 607  DGD b 623  PHE h  38                    
SITE     4 NC1 15 PHE h  41  ILE h  45  TYR h  49                               
SITE     1 NC2 20 ARG b  68  LEU b  69  ALA b 146  LEU b 149                    
SITE     2 NC2 20 CYS b 150  PHE b 153  VAL b 198  HIS b 201                    
SITE     3 NC2 20 HIS b 202  PHE b 247  ALA b 248  VAL b 252                    
SITE     4 NC2 20 THR b 262  CLA b 606  CLA b 608  CLA b 609                    
SITE     5 NC2 20 CLA b 610  CLA b 613  PHE h  38  LEU h  42                    
SITE     1 NC3 19 TRP b  33  PHE b  61  PHE b  65  ARG b  68                    
SITE     2 NC3 19 LEU b 149  VAL b 245  ALA b 248  ALA b 249                    
SITE     3 NC3 19 VAL b 252  PHE b 451  HIS b 455  PHE b 458                    
SITE     4 NC3 19 ALA b 459  CLA b 607  CLA b 609  CLA b 611                    
SITE     5 NC3 19 CLA b 616  CLA b 617  CLA b 619                               
SITE     1 NC4 19 THR b  27  VAL b  30  ALA b  31  ALA b  34                    
SITE     2 NC4 19 VAL b  62  PHE b  65  MET b  66  ARG b  68                    
SITE     3 NC4 19 VAL b  96  HIS b 100  LEU b 103  GLY b 147                    
SITE     4 NC4 19 ALA b 205  CLA b 607  CLA b 608  CLA b 610                    
SITE     5 NC4 19 CLA b 613  CLA b 614  CLA b 616                               
SITE     1 NC5 16 SQD A 417  LEU b  69  TRP b  91  LEU b 103                    
SITE     2 NC5 16 LEU b 106  LEU b 149  GLY b 152  PHE b 153                    
SITE     3 NC5 16 PHE b 156  HIS b 157  PHE b 162  PRO b 164                    
SITE     4 NC5 16 CLA b 607  CLA b 609  BCR b 622  LMT b 626                    
SITE     1 NC6 15 BCR T 102  TRP b  33  TYR b  40  GLN b  58                    
SITE     2 NC6 15 GLY b  59  PHE b  61  GLY b 328  PRO b 329                    
SITE     3 NC6 15 TRP b 450  ALA b 454  CLA b 608  LMG b 625                    
SITE     4 NC6 15 MET d 281  LEU l  27  PHE m  14                               
SITE     1 NC7 14 THR b 236  SER b 239  ALA b 243  PHE b 246                    
SITE     2 NC7 14 PHE b 463  HIS b 466  LEU b 474  CLA b 613                    
SITE     3 NC7 14 CLA b 614  PHE d 120  ILE d 123  MET d 126                    
SITE     4 NC7 14 LEU d 127  PHE d 130                                          
SITE     1 NC8 19 PHE b 139  LEU b 143  VAL b 208  ALA b 212                    
SITE     2 NC8 19 PHE b 215  HIS b 216  PRO b 221  PRO b 222                    
SITE     3 NC8 19 LEU b 229  CLA b 607  CLA b 609  CLA b 612                    
SITE     4 NC8 19 CLA b 614  THR h  27  THR h  28  MET h  31                    
SITE     5 NC8 19 PHE h  34  MET h  35  BCR h 101                               
SITE     1 NC9 13 LEU b 135  PHE b 139  HIS b 142  LEU b 143                    
SITE     2 NC9 13 VAL b 237  SER b 240  SER b 241  CLA b 609                    
SITE     3 NC9 13 CLA b 612  CLA b 613  CLA b 616  CLA b 619                    
SITE     4 NC9 13 BCR h 101                                                     
SITE     1 OC1 17 TRP b   5  TYR b   6  ARG b   7  VAL b   8                    
SITE     2 OC1 17 HIS b   9  LEU b 238  LEU b 461  PHE b 462                    
SITE     3 OC1 17 PHE b 464  GLY b 465  TRP b 468  HIS b 469                    
SITE     4 OC1 17 ARG b 472  CLA b 616  CLA b 617  CLA b 618                    
SITE     5 OC1 17 LMG b 624                                                     
SITE     1 OC2 17 HIS b   9  LEU b  19  HIS b  23  HIS b  26                    
SITE     2 OC2 17 THR b  27  ILE b 234  VAL b 237  LEU b 238                    
SITE     3 OC2 17 SER b 241  VAL b 245  CLA b 608  CLA b 609                    
SITE     4 OC2 17 CLA b 614  CLA b 615  CLA b 617  CLA b 618                    
SITE     5 OC2 17 CLA b 619                                                     
SITE     1 OC3  9 HIS b   9  HIS b  26  VAL b  30  PHE b 462                    
SITE     2 OC3  9 CLA b 608  CLA b 615  CLA b 616  CLA b 618                    
SITE     3 OC3  9 LMG b 624                                                     
SITE     1 OC4 14 LMG M 101  PHE T   8  BCR T 101  LMG a 416                    
SITE     2 OC4 14 VAL b   8  HIS b   9  VAL b  11  LEU b  29                    
SITE     3 OC4 14 TRP b 115  SQD b 601  CLA b 615  CLA b 616                    
SITE     4 OC4 14 CLA b 617  VAL l  10                                          
SITE     1 OC5 12 HIS b  23  LEU b 133  MET b 138  ILE b 141                    
SITE     2 OC5 12 HIS b 142  LEU b 145  CLA b 608  CLA b 614                    
SITE     3 OC5 12 CLA b 616  CLA b 620  BCR b 622  LEU h  14                    
SITE     1 OC6  9 SQD A 417  ILE b  20  LEU b  24  ALA b 110                    
SITE     2 OC6  9 TRP b 113  HIS b 114  LEU b 120  CLA b 619                    
SITE     3 OC6  9 THR h   5                                                     
SITE     1 OC7  8 BCR T 101  BCR T 102  LEU b  29  GLY b  32                    
SITE     2 OC7  8 TRP b  33  ILE b 101  GLY b 105  DGD b 602                    
SITE     1 OC8 10 SQD A 417  PHE T  22  LEU b 106  LEU b 109                    
SITE     2 OC8 10 ALA b 110  CYS b 112  TYR b 117  CLA b 610                    
SITE     3 OC8 10 CLA b 619  LMT b 626                                          
SITE     1 OC9 15 TYR b 193  PHE b 250  TYR b 258  TYR b 273                    
SITE     2 OC9 15 SER b 277  PHE b 463  CLA b 606  GLY d  86                    
SITE     3 OC9 15 HIS d  87  LEU d 162  TYR h  49  ASN h  50                    
SITE     4 OC9 15 VAL h  60  SER h  61  TRP h  62                               
SITE     1 PC1 13 ASN a 234  LMG a 416  TRP b   5  TYR b   6                    
SITE     2 PC1 13 ARG b   7  PHE b 464  TRP b 468  CLA b 615                    
SITE     3 PC1 13 CLA b 617  ARG d 139  TYR d 141  PHE d 269                    
SITE     4 PC1 13 PHE d 273                                                     
SITE     1 PC2 10 THR b 327  GLY b 328  PRO b 329  LYS b 332                    
SITE     2 PC2 10 CLA b 611  ILE d 284  PHE l  35  ASN m   4                    
SITE     3 PC2 10 LEU m   6  LMT m 101                                          
SITE     1 PC3  5 TRP b  91  PHE b 162  DGD b 602  CLA b 610                    
SITE     2 PC3  5 BCR b 622                                                     
SITE     1 PC4  7 ARG b 224  LEU b 225  LYS b 227  ASP d  16                    
SITE     2 PC4  7 ASP d  19  SQD d 408  ALA h  32                               
SITE     1 PC5 16 LEU c  95  LEU c 168  GLY c 171  ALA c 172                    
SITE     2 PC5 16 LEU c 175  ILE c 224  VAL c 233  HIS c 237                    
SITE     3 PC5 16 ILE c 240  MET c 282  VAL c 296  TYR c 297                    
SITE     4 PC5 16 CLA c 502  CLA c 503  CLA c 507  BCR c 515                    
SITE     1 PC6 17 TRP c  63  HIS c  91  TRP c  97  GLY c 171                    
SITE     2 PC6 17 LEU c 174  LYS c 178  PHE c 182  LEU c 279                    
SITE     3 PC6 17 MET c 282  ALA c 286  TYR c 297  HIS c 430                    
SITE     4 PC6 17 LEU c 433  PHE c 437  CLA c 501  CLA c 503                    
SITE     5 PC6 17 CLA c 509                                                     
SITE     1 PC7 14 ILE c  60  VAL c  61  ALA c  64  THR c  68                    
SITE     2 PC7 14 LEU c  88  HIS c  91  ILE c  92  VAL c 114                    
SITE     3 PC7 14 HIS c 118  MET c 282  CLA c 501  CLA c 502                    
SITE     4 PC7 14 CLA c 512  LMG c 519                                          
SITE     1 PC8 15 PHE a 285  LHG a 414  TRP c  63  MET c  67                    
SITE     2 PC8 15 PHE c  70  GLN c  84  GLY c  85  ILE c  87                    
SITE     3 PC8 15 TRP c 425  SER c 429  DGD c 517  DGD c 518                    
SITE     4 PC8 15 PRO k  26  VAL k  30  LMG k 103                               
SITE     1 PC9 17 PHE a  33  MET a 127  GLY a 128  TRP a 131                    
SITE     2 PC9 17 PHE c 264  ILE c 265  TYR c 274  GLY c 277                    
SITE     3 PC9 17 ALA c 278  MET c 281  HIS c 441  LEU c 442                    
SITE     4 PC9 17 ALA c 445  ARG c 449  CLA c 507  BCR c 515                    
SITE     5 PC9 17 PHE i  23                                                     
SITE     1 QC1 12 LEU c 165  ILE c 243  GLY c 247  TRP c 250                    
SITE     2 QC1 12 HIS c 251  THR c 255  PRO c 256  PHE c 257                    
SITE     3 QC1 12 TRP c 259  ALA c 260  PHE c 264  CLA c 507                    
SITE     1 QC2 13 MET c 157  LEU c 161  HIS c 164  PHE c 264                    
SITE     2 QC2 13 TRP c 266  TYR c 271  TYR c 274  SER c 275                    
SITE     3 QC2 13 LEU c 279  CLA c 501  CLA c 505  CLA c 506                    
SITE     4 QC2 13 CLA c 509                                                     
SITE     1 QC3 16 LHG a 414  SQD a 415  TRP c  36  ALA c  37                    
SITE     2 QC3 16 ASN c  39  ALA c  40  GLU c 269  LEU c 276                    
SITE     3 QC3 16 PHE c 436  PHE c 437  GLY c 440  TRP c 443                    
SITE     4 QC3 16 HIS c 444  ARG c 447  CLA c 509  CLA c 510                    
SITE     1 QC4 18 ASN c  39  LEU c  42  LEU c  49  ALA c  52                    
SITE     2 QC4 18 HIS c  53  HIS c  56  TYR c 149  TRP c 151                    
SITE     3 QC4 18 GLY c 268  TYR c 271  LEU c 272  SER c 275                    
SITE     4 QC4 18 CLA c 502  CLA c 507  CLA c 508  CLA c 510                    
SITE     5 QC4 18 CLA c 511  CLA c 512                                          
SITE     1 QC5 12 ASN c  39  HIS c  56  LEU c  59  ILE c  60                    
SITE     2 QC5 12 TRP c  63  LEU c 279  PHE c 436  PHE c 437                    
SITE     3 QC5 12 CLA c 508  CLA c 509  PRO k  29  LEU k  33                    
SITE     1 QC6 20 TRP c  35  GLY c  38  ASN c  39  ARG c  41                    
SITE     2 QC6 20 LEU c  42  LYS c  48  ALA c  52  PHE c 127                    
SITE     3 QC6 20 ILE c 134  CLA c 509  BCR c 514  ILE g  35                    
SITE     4 QC6 20 LEU g  46  PHE k  32  LEU k  33  TRP k  39                    
SITE     5 QC6 20 GLN k  40  MET z  19  VAL z  20  PRO z  24                    
SITE     1 QC7 14 HIS c  53  ALA c  57  PHE c 147  PHE c 163                    
SITE     2 QC7 14 HIS c 164  VAL c 167  LEU c 168  ILE c 170                    
SITE     3 QC7 14 GLY c 171  LEU c 174  CLA c 503  CLA c 509                    
SITE     4 QC7 14 CLA c 513  BCR z 101                                          
SITE     1 QC8 11 LEU c  50  VAL c  54  VAL c 124  GLY c 128                    
SITE     2 QC8 11 TYR c 131  HIS c 132  PRO c 137  LEU c 140                    
SITE     3 QC8 11 PHE c 147  CLA c 512  BCR z 101                               
SITE     1 QC9 13 ALA c  55  LEU c  59  VAL c 116  LEU c 119                    
SITE     2 QC9 13 ILE c 120  SER c 122  ALA c 123  GLY c 126                    
SITE     3 QC9 13 CLA c 511  PHE k  32  BCR k 102  VAL z  13                    
SITE     4 QC9 13 BCR z 101                                                     
SITE     1 RC1 11 ILE c 209  TYR c 212  LEU c 213  VAL c 227                    
SITE     2 RC1 11 ASP c 232  VAL c 233  ILE c 240  PHE c 264                    
SITE     3 RC1 11 CLA c 501  CLA c 505  VAL i  20                               
SITE     1 RC2 17 ILE a 163  DGD a 413  PRO c 217  PHE c 218                    
SITE     2 RC2 17 GLY c 220  GLY c 222  VAL c 225  SER c 226                    
SITE     3 RC2 17 PHE c 284  CYS c 288  PHE c 292  ASN c 294                    
SITE     4 RC2 17 THR c 305  PRO c 307  PHE c 361  ARG c 362                    
SITE     5 RC2 17 LEU c 438                                                     
SITE     1 RC3 19 PHE a 197  THR a 292  SQD a 415  LHG a 417                    
SITE     2 RC3 19 TYR c  82  GLU c  83  GLN c  84  GLY c  85                    
SITE     3 RC3 19 SER c 406  ASN c 418  PHE c 419  VAL c 420                    
SITE     4 RC3 19 TRP c 425  SER c 429  CLA c 504  DGD c 518                    
SITE     5 RC3 19 TYR j  33  BCR j 102  LMG k 103                               
SITE     1 RC4 19 LEU a 200  TRP a 278  PHE a 300  ASN a 301                    
SITE     2 RC4 19 SER a 305  SQD a 415  ASN c 405  ASN c 415                    
SITE     3 RC4 19 SER c 416  ASN c 418  CLA c 504  DGD c 517                    
SITE     4 RC4 19 LMG d 406  ALA j  32  TYR j  33  GLY j  37                    
SITE     5 RC4 19 SER j  38  SER j  39  GLN v  60                               
SITE     1 RC5  6 TRP c  97  PHE c 109  VAL c 117  HIS c 118                    
SITE     2 RC5  6 CLA c 503  PHE z  59                                          
SITE     1 RC6  8 HIS a 215  GLU a 244  TYR a 246  HIS a 272                    
SITE     2 RC6  8 FE2 a 403  TYR d 244  LYS d 264  HIS d 268                    
SITE     1 RC7 23 PHE a 206  CLA a 404  CLA a 405  CLA a 406                    
SITE     2 RC7 23 PHO a 408  LEU d  45  VAL d 152  PHE d 153                    
SITE     3 RC7 23 SER d 155  VAL d 156  LEU d 182  PHE d 185                    
SITE     4 RC7 23 GLN d 186  TRP d 191  THR d 192  HIS d 197                    
SITE     5 RC7 23 GLY d 200  VAL d 201  VAL d 204  LEU d 279                    
SITE     6 RC7 23 SER d 282  ALA d 283  VAL d 286                               
SITE     1 RC8 14 LEU d  43  LEU d  89  LEU d  90  LEU d  91                    
SITE     2 RC8 14 LEU d  92  TRP d  93  THR d 112  PHE d 113                    
SITE     3 RC8 14 HIS d 117  PHE d 120  LMT d 410  GLY x  22                    
SITE     4 RC8 14 LEU x  23  GLY x  26                                          
SITE     1 RC9 17 ILE a  77  CLA a 405  LMG a 416  MET d 199                    
SITE     2 RC9 17 ILE d 213  HIS d 214  THR d 217  TRP d 253                    
SITE     3 RC9 17 ILE d 259  ALA d 260  PHE d 261  LEU d 267                    
SITE     4 RC9 17 PHE d 273  VAL d 274  LEU l  23  VAL l  26                    
SITE     5 RC9 17 PHE t  10                                                     
SITE     1 SC1  8 GLY d  46  LEU d  49  THR d  50  LMG d 406                    
SITE     2 SC1  8 PRO f  29  PHE f  33  VAL j  21  VAL j  25                    
SITE     1 SC2 13 DGD c 518  TYR d  67  GLY d  70  ASN d  72                    
SITE     2 SC2 13 PHE d  73  BCR d 405  ILE f  37  MET f  40                    
SITE     3 SC2 13 GLN f  41  PHE j  28  GLY j  31  ALA j  32                    
SITE     4 SC2 13 GLY j  37                                                     
SITE     1 SC3 14 BCR B 618  CLA a 404  PHE d 257  ILE d 259                    
SITE     2 SC3 14 ALA d 260  PHE d 261  SER d 262  ASN d 263                    
SITE     3 SC3 14 TRP d 266  THR l  15  TYR l  18  LEU l  19                    
SITE     4 SC3 14 PHE t  17  ALA t  20                                          
SITE     1 SC4  8 ALA b 228  ARG b 230  LMT b 627  LYS d  23                    
SITE     2 SC4  8 TRP d  32  ARG d 134  LEU d 135  PHE x  34                    
SITE     1 SC5  7 ASP d 100  PHE d 101  THR d 102  LMT d 410                    
SITE     2 SC5  7 LEU e  42  ASP e  45  VAL e  46                               
SITE     1 SC6  8 LEU d  92  TRP d  93  GLY d  99  CLA d 403                    
SITE     2 SC6  8 DGD d 409  ILE x  21  SER x  25  GLY x  26                    
SITE     1 SC7  7 TYR a 262  LHG a 417  PHE d  27  PRO e   9                    
SITE     2 SC7  7 PHE e  10  SER e  11  PL9 j 101                               
SITE     1 SC8 15 ARG e   8  PHE e  10  ILE e  13  ILE e  14                    
SITE     2 SC8 15 ARG e  18  TYR e  19  HIS e  23  THR e  26                    
SITE     3 SC8 15 LEU e  30  ILE f  15  ARG f  19  TRP f  20                    
SITE     4 SC8 15 HIS f  24  ALA f  27  ILE f  31                               
SITE     1 SC9  8 TRP d  21  ARG d  24  ARG d  26  PHE f  16                    
SITE     2 SC9  8 THR f  17  VAL f  18  THR x  33  ASP x  44                    
SITE     1 TC1  9 CLA b 605  CLA b 613  CLA b 614  MET h  35                    
SITE     2 TC1  9 LEU h  37  PHE h  38  PHE h  41  THR x  11                    
SITE     3 TC1  9 LEU x  16                                                     
SITE     1 TC2  7 DGD B 627  LMT B 629  CLA a 409  MET i   1                    
SITE     2 TC2  7 THR i   3  LEU i   4  LMT i 102                               
SITE     1 TC3  5 THR i   3  ILE i   6  ILE i  10  PHE i  14                    
SITE     2 TC3  5 LMG i 101                                                     
SITE     1 TC4  3 CLA a 406  PL9 a 410  LMG e 101                               
SITE     1 TC5  7 LHG a 417  DGD c 517  ILE j  22  PHE j  29                    
SITE     2 TC5  7 TYR j  30  TYR j  33  LMG k 103                               
SITE     1 TC6  2 ASP k  19  ASP k  23                                          
SITE     1 TC7 14 BCR c 514  ILE g  28  GLY g  29  GLY g  32                    
SITE     2 TC7 14 ALA j  14  THR j  15  MET j  19  LEU k  21                    
SITE     3 TC7 14 LEU k  31  ALA k  34  PHE k  37  VAL k  38                    
SITE     4 TC7 14 SER z  16  PHE z  17                                          
SITE     1 TC8  7 HIS c  74  CLA c 504  DGD c 517  ILE g  25                    
SITE     2 TC8  7 BCR j 102  ASP k  23  VAL k  27                               
SITE     1 TC9  9 MET M   1  GLU M   2  ILE T   4  PHE T   8                    
SITE     2 TC9  9 BCR T 101  TYR b  40  LMG b 625  GLN m   5                    
SITE     3 TC9  9 LEU m   6                                                     
SITE     1 UC1 10 CLA B 614  PRO L   9  VAL L  10  PHE M  21                    
SITE     2 UC1 10 LEU M  25  GLN M  28  GLN M  32  VAL m  27                    
SITE     3 UC1 10 GLU m  30  SER m  31                                          
SITE     1 UC2  2 GLU o 140  HIS o 257                                          
SITE     1 UC3 14 ALA v  62  CYS v  63  CYS v  66  HIS v  67                    
SITE     2 UC3 14 THR v  74  ASN v  75  LEU v  78  ASP v  79                    
SITE     3 UC3 14 THR v  84  LEU v  85  TYR v 101  TYR v 108                    
SITE     4 UC3 14 HIS v 118  PRO v 119                                          
SITE     1 UC4  9 VAL c 116  SER c 121  VAL c 124  CLA c 512                    
SITE     2 UC4  9 CLA c 513  BCR c 514  TYR k  15  GLY z  55                    
SITE     3 UC4  9 ASN z  58                                                     
CRYST1  131.976  227.568  306.994  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      0.007577  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004394  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003257        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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