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Database: PDB
Entry: 4FBY
LinkDB: 4FBY
Original site: 4FBY 
HEADER    PHOTOSYNTHESIS                          23-MAY-12   4FBY              
TITLE     FS X-RAY DIFFRACTION OF PHOTOSYSTEM II                                
CAVEAT     4FBY    CHIRALITY ERRORS ON THE CHIRAL CENTERS OF SOME OF THE DGD    
CAVEAT   2 4FBY    AND LMG LIGANDS                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOTOSYSTEM Q(B) PROTEIN 1;                                
COMPND   3 CHAIN: A, G;                                                         
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, N;                                                         
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: PHOTOSYSTEM II CP43 PROTEIN;                               
COMPND  12 CHAIN: C, P;                                                         
COMPND  13 MOL_ID: 4;                                                           
COMPND  14 MOLECULE: PHOTOSYSTEM II D2 PROTEIN;                                 
COMPND  15 CHAIN: D, Q;                                                         
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, R;                                                         
COMPND  21 SYNONYM: PSII REACTION CENTER SUBUNIT V;                             
COMPND  22 MOL_ID: 6;                                                           
COMPND  23 MOLECULE: CYTOCHROME B559 SUBUNIT BETA;                              
COMPND  24 CHAIN: F, S;                                                         
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, W;                                                         
COMPND  29 SYNONYM: PSII-H;                                                     
COMPND  30 MOL_ID: 8;                                                           
COMPND  31 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN I;                  
COMPND  32 CHAIN: I, a;                                                         
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, b;                                                         
COMPND  37 SYNONYM: PSII-J;                                                     
COMPND  38 MOL_ID: 10;                                                          
COMPND  39 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN K;                  
COMPND  40 CHAIN: K, c;                                                         
COMPND  41 SYNONYM: PSII-K;                                                     
COMPND  42 MOL_ID: 11;                                                          
COMPND  43 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN L;                  
COMPND  44 CHAIN: L, d;                                                         
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, e;                                                         
COMPND  49 SYNONYM: PSII-M;                                                     
COMPND  50 MOL_ID: 13;                                                          
COMPND  51 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;          
COMPND  52 CHAIN: O, f;                                                         
COMPND  53 SYNONYM: MSP;                                                        
COMPND  54 MOL_ID: 14;                                                          
COMPND  55 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN T;                  
COMPND  56 CHAIN: T, g;                                                         
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, h;                                                         
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, i;                                                         
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, m;                                                         
COMPND  70 MOL_ID: 18;                                                          
COMPND  71 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN X;                  
COMPND  72 CHAIN: X, j;                                                         
COMPND  73 MOL_ID: 19;                                                          
COMPND  74 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Y;                  
COMPND  75 CHAIN: Y, k;                                                         
COMPND  76 MOL_ID: 20;                                                          
COMPND  77 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Z;                  
COMPND  78 CHAIN: Z, l;                                                         
COMPND  79 SYNONYM: PSII-Z                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE   3 ORGANISM_TAXID: 197221;                                              
SOURCE   4 STRAIN: BP-1;                                                        
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE   7 ORGANISM_TAXID: 197221;                                              
SOURCE   8 STRAIN: BP-1;                                                        
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  11 ORGANISM_TAXID: 197221;                                              
SOURCE  12 STRAIN: BP-1;                                                        
SOURCE  13 MOL_ID: 4;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  15 ORGANISM_TAXID: 197221;                                              
SOURCE  16 STRAIN: BP-1;                                                        
SOURCE  17 MOL_ID: 5;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  19 ORGANISM_TAXID: 197221;                                              
SOURCE  20 STRAIN: BP-1;                                                        
SOURCE  21 MOL_ID: 6;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  23 ORGANISM_TAXID: 197221;                                              
SOURCE  24 STRAIN: BP-1;                                                        
SOURCE  25 MOL_ID: 7;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  27 ORGANISM_TAXID: 197221;                                              
SOURCE  28 STRAIN: BP-1;                                                        
SOURCE  29 MOL_ID: 8;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  31 ORGANISM_TAXID: 197221;                                              
SOURCE  32 STRAIN: BP-1;                                                        
SOURCE  33 MOL_ID: 9;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  35 ORGANISM_TAXID: 197221;                                              
SOURCE  36 STRAIN: BP-1;                                                        
SOURCE  37 MOL_ID: 10;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  39 ORGANISM_TAXID: 197221;                                              
SOURCE  40 STRAIN: BP-1;                                                        
SOURCE  41 MOL_ID: 11;                                                          
SOURCE  42 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  43 ORGANISM_TAXID: 197221;                                              
SOURCE  44 STRAIN: BP-1;                                                        
SOURCE  45 MOL_ID: 12;                                                          
SOURCE  46 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  47 ORGANISM_TAXID: 197221;                                              
SOURCE  48 STRAIN: BP-1;                                                        
SOURCE  49 MOL_ID: 13;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  51 ORGANISM_TAXID: 197221;                                              
SOURCE  52 STRAIN: BP-1;                                                        
SOURCE  53 MOL_ID: 14;                                                          
SOURCE  54 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  55 ORGANISM_TAXID: 197221;                                              
SOURCE  56 STRAIN: BP-1;                                                        
SOURCE  57 MOL_ID: 15;                                                          
SOURCE  58 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  59 ORGANISM_TAXID: 197221;                                              
SOURCE  60 STRAIN: BP-1;                                                        
SOURCE  61 MOL_ID: 16;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  63 ORGANISM_TAXID: 197221;                                              
SOURCE  64 STRAIN: BP-1;                                                        
SOURCE  65 MOL_ID: 17;                                                          
SOURCE  66 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  67 ORGANISM_TAXID: 197221;                                              
SOURCE  68 STRAIN: BP-1;                                                        
SOURCE  69 MOL_ID: 18;                                                          
SOURCE  70 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  71 ORGANISM_TAXID: 197221;                                              
SOURCE  72 STRAIN: BP-1;                                                        
SOURCE  73 MOL_ID: 19;                                                          
SOURCE  74 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  75 ORGANISM_TAXID: 197221;                                              
SOURCE  76 STRAIN: BP-1;                                                        
SOURCE  77 MOL_ID: 20;                                                          
SOURCE  78 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  79 ORGANISM_TAXID: 197221;                                              
SOURCE  80 STRAIN: BP-1                                                         
KEYWDS    PHOTOSYSTEM, PS II, PS2, MEMBRANE COMPLEX, TRANSMEMBRANE ALPHA-HELIX, 
KEYWDS   2 PHOTOSYNTHESIS, X-RAY FREE ELECTRON LASER, PHOTOSYSTEM II, REACTION  
KEYWDS   3 CENTER, IRON, MANGANESE, LIGHT HARVESTING, ELECTRON TRANSPORT, WATER 
KEYWDS   4 OXIDATION, THYLAKOID MEMBRANE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.KERN,R.ALONSO-MORI,J.HELLMICH,R.TRAN,J.HATTNE,H.LAKSMONO,           
AUTHOR   2 C.GLOECKNER,N.ECHOLS,R.G.SIERRA,J.SELLBERG,B.LASSALLE-KAISER,        
AUTHOR   3 R.J.GILDEA,P.GLATZEL,R.W.GROSSE-KUNSTLEVE,M.J.LATIMER,T.A.MCQUEEN,   
AUTHOR   4 D.DIFIORE,A.R.FRY,M.M.MESSERSCHMIDT,A.MIAHNAHRI,D.W.SCHAFER,         
AUTHOR   5 M.M.SEIBERT,D.SOKARAS,T.-C.WENG,P.H.ZWART,W.E.WHITE,P.D.ADAMS,       
AUTHOR   6 M.J.BOGAN,S.BOUTET,G.J.WILLIAMS,J.MESSINGER,N.K.SAUTER,A.ZOUNI,      
AUTHOR   7 U.BERGMANN,J.YANO,V.K.YACHANDRA                                      
REVDAT   7   14-FEB-18 4FBY    1       REMARK                                   
REVDAT   6   29-NOV-17 4FBY    1       REMARK                                   
REVDAT   5   15-NOV-17 4FBY    1       REMARK                                   
REVDAT   4   21-DEC-16 4FBY    1       REMARK                                   
REVDAT   3   09-JAN-13 4FBY    1       JRNL                                     
REVDAT   2   25-JUL-12 4FBY    1       HET                                      
REVDAT   1   20-JUN-12 4FBY    0                                                
JRNL        AUTH   J.KERN,R.ALONSO-MORI,J.HELLMICH,R.TRAN,J.HATTNE,H.LAKSMONO,  
JRNL        AUTH 2 C.GLOCKNER,N.ECHOLS,R.G.SIERRA,J.SELLBERG,B.LASSALLE-KAISER, 
JRNL        AUTH 3 R.J.GILDEA,P.GLATZEL,R.W.GROSSE-KUNSTLEVE,M.J.LATIMER,       
JRNL        AUTH 4 T.A.MCQUEEN,D.DIFIORE,A.R.FRY,M.MESSERSCHMIDT,A.MIAHNAHRI,   
JRNL        AUTH 5 D.W.SCHAFER,M.M.SEIBERT,D.SOKARAS,T.C.WENG,P.H.ZWART,        
JRNL        AUTH 6 W.E.WHITE,P.D.ADAMS,M.J.BOGAN,S.BOUTET,G.J.WILLIAMS,         
JRNL        AUTH 7 J.MESSINGER,N.K.SAUTER,A.ZOUNI,U.BERGMANN,J.YANO,            
JRNL        AUTH 8 V.K.YACHANDRA                                                
JRNL        TITL   ROOM TEMPERATURE FEMTOSECOND X-RAY DIFFRACTION OF            
JRNL        TITL 2 PHOTOSYSTEM II MICROCRYSTALS.                                
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 109  9721 2012              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   22665786                                                     
JRNL        DOI    10.1073/PNAS.1204598109                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    6.56 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.7.3                                         
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 6.56                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 85.89                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.480                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 17914                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.367                           
REMARK   3   R VALUE            (WORKING SET) : 0.366                           
REMARK   3   FREE R VALUE                     : 0.385                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 895                             
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 85.8920 - 11.9035    1.00     3031   160  0.3942 0.3855        
REMARK   3     2 11.9035 -  9.4520    1.00     2923   152  0.3181 0.3419        
REMARK   3     3  9.4520 -  8.2583    1.00     2884   153  0.3270 0.3471        
REMARK   3     4  8.2583 -  7.5037    1.00     2866   149  0.3526 0.3996        
REMARK   3     5  7.5037 -  6.9662    1.00     2835   150  0.3913 0.4193        
REMARK   3     6  6.9662 -  6.5556    0.88     2480   131  0.4272 0.4568        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.73                                          
REMARK   3   K_SOL              : 0.29                                          
REMARK   3   B_SOL              : 73.83                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 1.360            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 40.290           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 10.83                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 150.1                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.95850                                             
REMARK   3    B22 (A**2) : 43.00520                                             
REMARK   3    B33 (A**2) : -39.04670                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  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      :  0.007          52048                                  
REMARK   3   ANGLE     :  1.483          71500                                  
REMARK   3   CHIRALITY :  0.095           7242                                  
REMARK   3   PLANARITY :  0.008           7548                                  
REMARK   3   DIHEDRAL  : 16.095          19968                                  
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 4FBY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000072709.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-SEP-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2984                               
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) : 1.323                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : KB MIRRORS                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : CS-PAD                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CCTBX.XFEL                         
REMARK 200  DATA SCALING SOFTWARE          : CCTBX.XFEL                         
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17962                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 6.556                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 85.890                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 6.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 6.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.84                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.740                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3BZ1                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 4% PEG 2000, 5 MM CACL2, 100 MM PIPES,   
REMARK 280  PH 7.0, BATCH, TEMPERATURE 298K                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       65.39150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      154.31500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      113.88200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      154.31500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       65.39150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      113.88200            
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYMMETRIC UNIT               
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 40-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, I, J, K,         
REMARK 350                    AND CHAINS: L, M, O, T, U, V, y, X, Y,            
REMARK 350                    AND CHAINS: Z, G, N, P, Q, R, S, W, a, b,         
REMARK 350                    AND CHAINS: c, d, e, f, g, h, i, m, j,            
REMARK 350                    AND CHAINS: k, l                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     ARG A     7                                                      
REMARK 465     ARG A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     MET B     1                                                      
REMARK 465     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     ALA E     2                                                      
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     ASP I    36                                                      
REMARK 465     LEU I    37                                                      
REMARK 465     GLU I    38                                                      
REMARK 465     MET J     2                                                      
REMARK 465     SER J     3                                                      
REMARK 465     GLU J     4                                                      
REMARK 465     GLY J     5                                                      
REMARK 465     GLY J     6                                                      
REMARK 465     SER M    35                                                      
REMARK 465     SER M    36                                                      
REMARK 465     ALA O    27                                                      
REMARK 465     LYS O    28                                                      
REMARK 465     GLN O    29                                                      
REMARK 465     ALA U    31                                                      
REMARK 465     THR U    32                                                      
REMARK 465     ALA U    33                                                      
REMARK 465     SER U    34                                                      
REMARK 465     THR U    35                                                      
REMARK 465     GLU U    36                                                      
REMARK 465     GLU U    37                                                      
REMARK 465     MET y     1                                                      
REMARK 465     GLY y     2                                                      
REMARK 465     ILE y     3                                                      
REMARK 465     PHE y     4                                                      
REMARK 465     ASN y     5                                                      
REMARK 465     GLY y     6                                                      
REMARK 465     ILE y     7                                                      
REMARK 465     ILE y     8                                                      
REMARK 465     GLU y     9                                                      
REMARK 465     PHE y    10                                                      
REMARK 465     LEU y    11                                                      
REMARK 465     SER y    12                                                      
REMARK 465     ASN y    13                                                      
REMARK 465     ILE y    14                                                      
REMARK 465     ASN y    15                                                      
REMARK 465     PHE y    16                                                      
REMARK 465     GLU y    17                                                      
REMARK 465     VAL y    18                                                      
REMARK 465     ARG X    48                                                      
REMARK 465     SER X    49                                                      
REMARK 465     LEU X    50                                                      
REMARK 465     MET G     1                                                      
REMARK 465     THR G     2                                                      
REMARK 465     THR G     3                                                      
REMARK 465     THR G     4                                                      
REMARK 465     LEU G     5                                                      
REMARK 465     GLN G     6                                                      
REMARK 465     ARG G     7                                                      
REMARK 465     ARG G     8                                                      
REMARK 465     GLU G     9                                                      
REMARK 465     MET N     1                                                      
REMARK 465     GLU N   492                                                      
REMARK 465     TRP N   493                                                      
REMARK 465     GLY N   494                                                      
REMARK 465     PHE N   495                                                      
REMARK 465     TYR N   496                                                      
REMARK 465     GLN N   497                                                      
REMARK 465     LYS N   498                                                      
REMARK 465     VAL N   499                                                      
REMARK 465     GLY N   500                                                      
REMARK 465     ASP N   501                                                      
REMARK 465     VAL N   502                                                      
REMARK 465     THR N   503                                                      
REMARK 465     THR N   504                                                      
REMARK 465     ARG N   505                                                      
REMARK 465     ARG N   506                                                      
REMARK 465     LYS N   507                                                      
REMARK 465     GLU N   508                                                      
REMARK 465     ALA N   509                                                      
REMARK 465     VAL N   510                                                      
REMARK 465     MET P    13                                                      
REMARK 465     VAL P    14                                                      
REMARK 465     THR P    15                                                      
REMARK 465     LEU P    16                                                      
REMARK 465     SER P    17                                                      
REMARK 465     SER P    18                                                      
REMARK 465     ASN P    19                                                      
REMARK 465     SER P    20                                                      
REMARK 465     ILE P    21                                                      
REMARK 465     PHE P    22                                                      
REMARK 465     ALA P    23                                                      
REMARK 465     THR P    24                                                      
REMARK 465     ASN P    25                                                      
REMARK 465     ARG P    26                                                      
REMARK 465     MET Q     1                                                      
REMARK 465     THR Q     2                                                      
REMARK 465     ILE Q     3                                                      
REMARK 465     ALA Q     4                                                      
REMARK 465     ILE Q     5                                                      
REMARK 465     GLY Q     6                                                      
REMARK 465     ARG Q     7                                                      
REMARK 465     ALA Q     8                                                      
REMARK 465     PRO Q     9                                                      
REMARK 465     ALA Q    10                                                      
REMARK 465     GLU Q    11                                                      
REMARK 465     ARG Q    12                                                      
REMARK 465     ALA R     2                                                      
REMARK 465     THR S     2                                                      
REMARK 465     SER S     3                                                      
REMARK 465     ASN S     4                                                      
REMARK 465     THR S     5                                                      
REMARK 465     PRO S     6                                                      
REMARK 465     ASN S     7                                                      
REMARK 465     GLN S     8                                                      
REMARK 465     GLU S     9                                                      
REMARK 465     PRO S    10                                                      
REMARK 465     ASP a    36                                                      
REMARK 465     LEU a    37                                                      
REMARK 465     GLU a    38                                                      
REMARK 465     MET b     2                                                      
REMARK 465     SER b     3                                                      
REMARK 465     GLU b     4                                                      
REMARK 465     GLY b     5                                                      
REMARK 465     GLY b     6                                                      
REMARK 465     SER e    35                                                      
REMARK 465     SER e    36                                                      
REMARK 465     ALA f    27                                                      
REMARK 465     LYS f    28                                                      
REMARK 465     GLN f    29                                                      
REMARK 465     ALA h    31                                                      
REMARK 465     THR h    32                                                      
REMARK 465     ALA h    33                                                      
REMARK 465     SER h    34                                                      
REMARK 465     THR h    35                                                      
REMARK 465     GLU h    36                                                      
REMARK 465     GLU h    37                                                      
REMARK 465     MET m     1                                                      
REMARK 465     GLY m     2                                                      
REMARK 465     ILE m     3                                                      
REMARK 465     PHE m     4                                                      
REMARK 465     ASN m     5                                                      
REMARK 465     GLY m     6                                                      
REMARK 465     ILE m     7                                                      
REMARK 465     ILE m     8                                                      
REMARK 465     GLU m     9                                                      
REMARK 465     PHE m    10                                                      
REMARK 465     LEU m    11                                                      
REMARK 465     SER m    12                                                      
REMARK 465     ASN m    13                                                      
REMARK 465     ILE m    14                                                      
REMARK 465     ASN m    15                                                      
REMARK 465     PHE m    16                                                      
REMARK 465     GLU m    17                                                      
REMARK 465     VAL m    18                                                      
REMARK 465     ARG j    48                                                      
REMARK 465     SER j    49                                                      
REMARK 465     LEU j    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 P 143    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU P 462    CG   CD   OE1  OE2                                  
REMARK 470     LYS W  20    CG   CD   CE   NZ                                   
REMARK 470     ARG f  53    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU f  80    CG   CD   OE1  OE2                                  
REMARK 470     LYS f  85    CG   CD   CE   NZ                                   
REMARK 470     ARG f 233    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU i  41    CG   CD   OE1  OE2                                  
REMARK 470     ARG m  43    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    PHE Z    60     OG   SER f   115     3755     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B 484   C   -  N   -  CA  ANGL. DEV. =  11.3 DEGREES          
REMARK 500    LEU B 486   CA  -  CB  -  CG  ANGL. DEV. =  16.2 DEGREES          
REMARK 500    PRO N 484   C   -  N   -  CA  ANGL. DEV. =  11.5 DEGREES          
REMARK 500    LEU N 486   CA  -  CB  -  CG  ANGL. DEV. =  15.6 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      106.61    128.67                                   
REMARK 500    GLN A 130       -7.13    -56.20                                   
REMARK 500    PRO A 141     -119.24    -71.51                                   
REMARK 500    TRP A 142      -17.50     47.07                                   
REMARK 500    LEU A 159      -46.53   -137.26                                   
REMARK 500    ILE A 176      -71.85    -56.70                                   
REMARK 500    GLU A 226        9.02   -151.35                                   
REMARK 500    GLU A 242      -60.62    -90.58                                   
REMARK 500    ILE A 259      -80.60   -101.73                                   
REMARK 500    PHE A 260      137.21   -178.21                                   
REMARK 500    GLN A 261      -65.00    -27.16                                   
REMARK 500    PHE A 302       34.02    -96.36                                   
REMARK 500    ARG A 334      -69.30    -26.23                                   
REMARK 500    LEU A 343       58.74   -108.20                                   
REMARK 500    VAL B  11        1.83    -61.99                                   
REMARK 500    ILE B  13      -27.06    -38.87                                   
REMARK 500    ASN B  14       62.99   -151.66                                   
REMARK 500    PRO B  16      -35.47    -34.16                                   
REMARK 500    ASP B 119       52.38    -93.70                                   
REMARK 500    ARG B 127      -78.05    -58.11                                   
REMARK 500    SER B 177     -179.56    178.41                                   
REMARK 500    PRO B 183     -179.82    -51.48                                   
REMARK 500    GLU B 184      101.34   -167.29                                   
REMARK 500    ASP B 188       -1.24    -59.73                                   
REMARK 500    LEU B 218      -69.07   -103.94                                   
REMARK 500    LEU B 229       38.92    -81.19                                   
REMARK 500    ARG B 230       48.71     17.96                                   
REMARK 500    MET B 231      178.45    -57.36                                   
REMARK 500    GLU B 235       15.91    -68.87                                   
REMARK 500    SER B 294       29.55    -75.91                                   
REMARK 500    ASP B 313       40.21    -93.35                                   
REMARK 500    LYS B 349      -48.09    -22.44                                   
REMARK 500    PRO B 414      -62.91    -19.16                                   
REMARK 500    GLU B 435      -75.77    -59.21                                   
REMARK 500    THR B 436      -73.88    -22.40                                   
REMARK 500    SER B 480      -18.09     73.93                                   
REMARK 500    ILE B 482     -162.54   -117.97                                   
REMARK 500    PRO B 484     -177.23     17.56                                   
REMARK 500    GLU B 485      172.31     67.66                                   
REMARK 500    LEU B 486       67.99   -160.19                                   
REMARK 500    PRO B 488     -103.47     22.80                                   
REMARK 500    GLN B 490      101.92   -166.02                                   
REMARK 500    GLU C  29     -155.52   -148.94                                   
REMARK 500    TRP C  36        3.15    -67.69                                   
REMARK 500    LEU C  45       54.76   -141.83                                   
REMARK 500    SER C  46      -54.81    -19.19                                   
REMARK 500    LYS C  79      134.99   -170.24                                   
REMARK 500    ILE C  87       -3.29   -142.96                                   
REMARK 500    ARG C 135      -67.02   -124.86                                   
REMARK 500    GLU C 141      -42.73    -28.72                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     386 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    HIS B  23         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PL9 A  406                                                       
REMARK 610     DGD A  407                                                       
REMARK 610     LHG A  408                                                       
REMARK 610     SQD A  409                                                       
REMARK 610     LMG A  410                                                       
REMARK 610     LHG A  411                                                       
REMARK 610     DGD B  621                                                       
REMARK 610     LMG B  622                                                       
REMARK 610     LMG B  623                                                       
REMARK 610     SQD B  624                                                       
REMARK 610     SQD B  627                                                       
REMARK 610     DGD B  628                                                       
REMARK 610     DGD C  516                                                       
REMARK 610     DGD C  517                                                       
REMARK 610     LMG C  519                                                       
REMARK 610     LMG C  520                                                       
REMARK 610     LMG D  406                                                       
REMARK 610     LMG D  407                                                       
REMARK 610     DGD D  408                                                       
REMARK 610     LMT D  409                                                       
REMARK 610     LMG D  412                                                       
REMARK 610     LMG E  102                                                       
REMARK 610     SQD F  101                                                       
REMARK 610     LMG I  102                                                       
REMARK 610     PL9 J  101                                                       
REMARK 610     LMG M  101                                                       
REMARK 610     PL9 G  407                                                       
REMARK 610     DGD G  408                                                       
REMARK 610     SQD G  410                                                       
REMARK 610     LHG G  409                                                       
REMARK 610     LMG G  411                                                       
REMARK 610     LHG G  412                                                       
REMARK 610     SQD N  601                                                       
REMARK 610     DGD N  602                                                       
REMARK 610     LMG N  623                                                       
REMARK 610     LMG N  622                                                       
REMARK 610     DGD P  517                                                       
REMARK 610     DGD P  518                                                       
REMARK 610     LMG P  520                                                       
REMARK 610     LMG P  521                                                       
REMARK 610     LMG Q  401                                                       
REMARK 610     LMG Q  407                                                       
REMARK 610     SQD Q  408                                                       
REMARK 610     DGD Q  409                                                       
REMARK 610     LMG Q  406                                                       
REMARK 610     LMT Q  410                                                       
REMARK 610     LMG R  102                                                       
REMARK 610     SQD S  102                                                       
REMARK 610     DGD W  102                                                       
REMARK 610     LMG a  102                                                       
REMARK 610     PL9 b  101                                                       
REMARK 610     LMG e  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                             FE2 A 413  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 215   NE2                                                    
REMARK 620 2 HIS D 214   NE2 129.1                                              
REMARK 620 3 HIS A 272   NE2 103.5 103.6                                        
REMARK 620 4 BCT D 410   O3  136.4  85.4  90.2                                  
REMARK 620 5 BCT D 410   O2   85.2 141.3  80.9  56.0                            
REMARK 620 6 HIS D 268   NE2  78.3  91.4 157.8  74.7  77.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 G 414  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS Q 214   NE2                                                    
REMARK 620 2 HIS G 215   NE2 128.6                                              
REMARK 620 3 HIS G 272   NE2 101.5 103.9                                        
REMARK 620 4 BCT Q 411   O3   89.5 133.7  90.4                                  
REMARK 620 5 BCT Q 411   O2  145.0  80.7  86.3  56.1                            
REMARK 620 6 HIS Q 268   NE2  92.9  79.3 157.8  72.7  72.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM R 101  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS R  23   NE2                                                    
REMARK 620 2 HEM R 101   NA   81.0                                              
REMARK 620 3 HEM R 101   NB  100.8  89.2                                        
REMARK 620 4 HEM R 101   NC   99.0 178.8  89.6                                  
REMARK 620 5 HEM R 101   ND   78.9  90.0 179.1  91.2                            
REMARK 620 6 HIS S  24   NE2 155.9  74.9  79.0 105.1 101.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM E 101  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  23   NE2                                                    
REMARK 620 2 HEM E 101   NA   79.1                                              
REMARK 620 3 HEM E 101   NB  100.7  89.5                                        
REMARK 620 4 HEM E 101   NC  100.8 179.1  89.6                                  
REMARK 620 5 HEM E 101   ND   78.8  89.4 178.8  91.5                            
REMARK 620 6 HIS F  24   NE2 153.2  74.1  80.7 106.0  99.2                      
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   90.1                                              
REMARK 620 3 HEM V 201   NB   92.6  87.0                                        
REMARK 620 4 HEM V 201   NC   89.9 179.0  92.1                                  
REMARK 620 5 HEM V 201   ND   87.3  91.2 178.2  89.8                            
REMARK 620 6 HIS V 118   NE2 168.5  78.9  90.0 101.1  89.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC A 412  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 342   OD1                                                    
REMARK 620 2 ALA A 344   OXT  80.6                                              
REMARK 620 3 ASP A 342   OD2  48.9 128.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM i 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS i 118   NE2                                                    
REMARK 620 2 HEM i 201   NA   80.0                                              
REMARK 620 3 HEM i 201   NB   89.4  86.3                                        
REMARK 620 4 HEM i 201   NC   99.9 178.2  91.8                                  
REMARK 620 5 HEM i 201   ND   90.4  92.1 178.4  89.7                            
REMARK 620 6 HIS i  67   NE2 168.9  88.8  89.7  91.2  90.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC A 412  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 354   OE2                                                    
REMARK 620 2 GLU A 333   OE1  65.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC G 413  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA G 344   OXT                                                    
REMARK 620 2 ASP G 342   OD1  75.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC A 412  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 333   OE2                                                    
REMARK 620 2 ASP A 170   OD2 164.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC G 413  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 333   OE2                                                    
REMARK 620 2 ASP G 170   OD2 141.2                                              
REMARK 620 N                    1                                               
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   95.7                                              
REMARK 620 3 CLA C 511   NB   76.5  93.7                                        
REMARK 620 4 CLA C 511   NC   84.1 176.8  89.3                                  
REMARK 620 5 CLA C 511   ND  102.3  90.9 175.3  86.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA P 511  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN P  39   OD1                                                    
REMARK 620 2 CLA P 511   NA   95.3                                              
REMARK 620 3 CLA P 511   NB   78.1  93.6                                        
REMARK 620 4 CLA P 511   NC   84.6 176.8  89.6                                  
REMARK 620 5 CLA P 511   ND  100.9  90.9 175.5  85.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC G 413  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 189   OE1                                                    
REMARK 620 2 ASP G 170   OD1 139.9                                              
REMARK 620 3 ASP G 170   OD2 157.5  41.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC A 412  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 189   OE1                                                    
REMARK 620 2 ASP A 170   OD1 136.8                                              
REMARK 620 3 ASP A 170   OD2 154.6  41.6                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 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 PHO 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 PL9 A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG A 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG A 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OEC A 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD A 414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD B 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG B 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG B 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD B 624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 626                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD B 627                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD B 628                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 629                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 630                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR C 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR C 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG C 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG C 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 D 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR D 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG D 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG D 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD D 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT D 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT D 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 411                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG D 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM E 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG E 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD F 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR H 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR I 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG I 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT I 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 J 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR J 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR K 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG M 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT M 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA O 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR T 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR T 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR T 103                 
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 Z 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD G 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA G 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA G 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA G 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO G 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA G 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 G 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD G 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG G 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD G 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG G 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG G 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OEC G 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 G 414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 415                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD N 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD N 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT N 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT N 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA N 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR N 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG N 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG N 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT N 624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT N 625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA P 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR P 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR P 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR P 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD P 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD P 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD P 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG P 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG P 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG Q 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA Q 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO Q 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA Q 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 Q 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG Q 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG Q 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD Q 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD Q 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT Q 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT Q 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM R 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG R 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR S 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD S 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR W 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD W 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR a 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG a 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT a 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 b 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR b 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR c 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT e 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG e 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA f 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM i 201                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3BZ1   RELATED DB: PDB                                   
REMARK 900 SYNCHROTRON STRUCTURE USING IDENTICAL CRYSTALLIZATION PROTOCOL       
REMARK 900 RELATED ID: 3BZ2   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 CHAIN "Y" AND "K":THE DEPOSITORS KNOW THE SEQUENCE                   
REMARK 999 (UNIPROT ID Q8DKM3) BUT DUE TO POOR DENSITY CAN'T                    
REMARK 999 ASIGN IT WITH CERTAINTY TO THE DENSITY. INSTEAD CHAIN                
REMARK 999 Y WAS MODELED AS POLY-ALA.                                           
REMARK 999 MET ASP TRP ARG VAL LEU VAL VAL LEU LEU PRO VAL LEU LEU ALA          
REMARK 999 ALA GLY TRP ALA VAL ARG ASN ILE LEU PRO TYR ALA VAL LYS GLN          
REMARK 999 VAL GLN LYS LEU LEU GLN LYS ALA LYS ALA ALA                          
REMARK 999 THE SEQUENCE MATCHES TO UNIPROT REFERENCE Q8DKM3                     
DBREF  4FBY A    1   344  UNP    P0A444   PSBA1_THEEB      1    344             
DBREF  4FBY B    1   510  UNP    Q8DIQ1   Q8DIQ1_THEEB     1    510             
DBREF  4FBY C   13   473  UNP    Q8DIF8   Q8DIF8_THEEB     1    461             
DBREF  4FBY D    1   352  UNP    Q8CM25   PSBD_THEEB       1    352             
DBREF  4FBY E    2    84  UNP    Q8DIP0   PSBE_THEEB       2     84             
DBREF  4FBY F    2    45  UNP    Q8DIN9   PSBF_THEEB       2     45             
DBREF  4FBY H    2    66  UNP    Q8DJ43   PSBH_THEEB       2     66             
DBREF  4FBY I    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  4FBY J    2    40  UNP    P59087   PSBJ_THEEB       2     40             
DBREF  4FBY K   10    46  UNP    Q9F1K9   PSBK_THEEB      10     46             
DBREF  4FBY L    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  4FBY M    1    36  UNP    Q8DHA7   PSBM_THEEB       1     36             
DBREF  4FBY O   27   272  UNP    P0A431   PSBO_THEEB      27    272             
DBREF  4FBY T    1    32  UNP    Q8DIQ0   PSBT_THEEB       1     32             
DBREF  4FBY U   31   134  UNP    Q9F1L5   PSBU_THEEB      31    134             
DBREF  4FBY V   27   163  UNP    P0A386   CY550_THEEB     27    163             
DBREF  4FBY y    1    46  UNP    Q8DJI1   YCF12_THEEB      1     46             
DBREF  4FBY X   11    50  UNP    Q9F1R6   PSBX_THEEB       2     41             
DBREF  4FBY Y    1    28  PDB    4FBY     4FBY             1     28             
DBREF  4FBY Z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
DBREF  4FBY G    1   344  UNP    P0A444   PSBA1_THEEB      1    344             
DBREF  4FBY N    1   510  UNP    Q8DIQ1   Q8DIQ1_THEEB     1    510             
DBREF  4FBY P   13   473  UNP    Q8DIF8   Q8DIF8_THEEB     1    461             
DBREF  4FBY Q    1   352  UNP    Q8CM25   PSBD_THEEB       1    352             
DBREF  4FBY R    2    84  UNP    Q8DIP0   PSBE_THEEB       2     84             
DBREF  4FBY S    2    45  UNP    Q8DIN9   PSBF_THEEB       2     45             
DBREF  4FBY W    2    66  UNP    Q8DJ43   PSBH_THEEB       2     66             
DBREF  4FBY a    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  4FBY b    2    40  UNP    P59087   PSBJ_THEEB       2     40             
DBREF  4FBY c   10    46  UNP    Q9F1K9   PSBK_THEEB      10     46             
DBREF  4FBY d    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  4FBY e    1    36  UNP    Q8DHA7   PSBM_THEEB       1     36             
DBREF  4FBY f   27   272  UNP    P0A431   PSBO_THEEB      27    272             
DBREF  4FBY g    1    32  UNP    Q8DIQ0   PSBT_THEEB       1     32             
DBREF  4FBY h   31   134  UNP    Q9F1L5   PSBU_THEEB      31    134             
DBREF  4FBY i   27   163  UNP    P0A386   CY550_THEEB     27    163             
DBREF  4FBY m    1    46  UNP    Q8DJI1   YCF12_THEEB      1     46             
DBREF  4FBY j   11    50  UNP    Q9F1R6   PSBX_THEEB       2     41             
DBREF  4FBY k    1    28  PDB    4FBY     4FBY             1     28             
DBREF  4FBY l    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
SEQRES   1 A  344  MET THR THR THR LEU GLN ARG ARG GLU SER ALA ASN LEU          
SEQRES   2 A  344  TRP GLU ARG PHE CYS ASN TRP VAL THR SER THR ASP ASN          
SEQRES   3 A  344  ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE MET ILE PRO          
SEQRES   4 A  344  THR LEU LEU ALA ALA THR ILE CYS PHE VAL ILE ALA PHE          
SEQRES   5 A  344  ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY ILE ARG GLU          
SEQRES   6 A  344  PRO VAL SER GLY SER LEU LEU TYR GLY ASN ASN ILE ILE          
SEQRES   7 A  344  THR GLY ALA VAL VAL PRO SER SER ASN ALA ILE GLY LEU          
SEQRES   8 A  344  HIS PHE TYR PRO ILE TRP GLU ALA ALA SER LEU ASP GLU          
SEQRES   9 A  344  TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU ILE ILE PHE          
SEQRES  10 A  344  HIS PHE LEU LEU GLY ALA SER CYS TYR MET GLY ARG GLN          
SEQRES  11 A  344  TRP GLU LEU SER TYR ARG LEU GLY MET ARG PRO TRP ILE          
SEQRES  12 A  344  CYS VAL ALA TYR SER ALA PRO LEU ALA SER ALA PHE ALA          
SEQRES  13 A  344  VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY SER PHE SER          
SEQRES  14 A  344  ASP GLY MET PRO LEU GLY ILE SER GLY THR PHE ASN PHE          
SEQRES  15 A  344  MET ILE VAL PHE GLN ALA GLU HIS ASN ILE LEU MET HIS          
SEQRES  16 A  344  PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL PHE GLY GLY          
SEQRES  17 A  344  ALA LEU PHE CYS ALA MET HIS GLY SER LEU VAL THR SER          
SEQRES  18 A  344  SER LEU ILE ARG GLU THR THR GLU THR GLU SER ALA ASN          
SEQRES  19 A  344  TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU THR TYR ASN          
SEQRES  20 A  344  ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG LEU ILE PHE          
SEQRES  21 A  344  GLN TYR ALA SER PHE ASN ASN SER ARG SER LEU HIS PHE          
SEQRES  22 A  344  PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL TRP PHE THR          
SEQRES  23 A  344  ALA LEU GLY ILE SER THR MET ALA PHE ASN LEU ASN GLY          
SEQRES  24 A  344  PHE ASN PHE ASN HIS SER VAL ILE ASP ALA LYS GLY ASN          
SEQRES  25 A  344  VAL ILE ASN THR TRP ALA ASP ILE ILE ASN ARG ALA ASN          
SEQRES  26 A  344  LEU GLY MET GLU VAL MET HIS GLU ARG ASN ALA HIS ASN          
SEQRES  27 A  344  PHE PRO LEU ASP LEU ALA                                      
SEQRES   1 B  510  MET GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE          
SEQRES   2 B  510  ASN ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS          
SEQRES   3 B  510  THR ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU          
SEQRES   4 B  510  TYR GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU          
SEQRES   5 B  510  ASN PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE          
SEQRES   6 B  510  MET ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP          
SEQRES   7 B  510  SER ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP          
SEQRES   8 B  510  SER PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER          
SEQRES   9 B  510  GLY LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR          
SEQRES  10 B  510  TRP ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU          
SEQRES  11 B  510  PRO ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU          
SEQRES  12 B  510  PHE LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE          
SEQRES  13 B  510  HIS LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER          
SEQRES  14 B  510  ASP PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA          
SEQRES  15 B  510  PRO GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO          
SEQRES  16 B  510  GLY GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL          
SEQRES  17 B  510  GLY ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO          
SEQRES  18 B  510  PRO GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE          
SEQRES  19 B  510  GLU THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE          
SEQRES  20 B  510  ALA ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER          
SEQRES  21 B  510  ALA THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR          
SEQRES  22 B  510  GLN TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG          
SEQRES  23 B  510  ARG VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU          
SEQRES  24 B  510  GLU ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR          
SEQRES  25 B  510  ASP TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE          
SEQRES  26 B  510  ARG THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN          
SEQRES  27 B  510  ALA TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY          
SEQRES  28 B  510  GLU GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU          
SEQRES  29 B  510  SER PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL          
SEQRES  30 B  510  LYS ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR          
SEQRES  31 B  510  SER PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY          
SEQRES  32 B  510  GLY GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR          
SEQRES  33 B  510  VAL LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE          
SEQRES  34 B  510  PHE GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE          
SEQRES  35 B  510  PHE ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS          
SEQRES  36 B  510  ALA VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP          
SEQRES  37 B  510  HIS GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY          
SEQRES  38 B  510  ILE ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY          
SEQRES  39 B  510  PHE TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG LYS          
SEQRES  40 B  510  GLU ALA VAL                                                  
SEQRES   1 C  461  MET VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN          
SEQRES   2 C  461  ARG ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY          
SEQRES   3 C  461  ASN ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY          
SEQRES   4 C  461  ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA          
SEQRES   5 C  461  GLY ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO          
SEQRES   6 C  461  GLU LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO          
SEQRES   7 C  461  HIS ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY          
SEQRES   8 C  461  GLU VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL          
SEQRES   9 C  461  VAL HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY          
SEQRES  10 C  461  VAL TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU          
SEQRES  11 C  461  TYR SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN          
SEQRES  12 C  461  LYS MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU          
SEQRES  13 C  461  GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE          
SEQRES  14 C  461  PHE GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY          
SEQRES  15 C  461  ASP VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG          
SEQRES  16 C  461  VAL ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY          
SEQRES  17 C  461  GLU GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL          
SEQRES  18 C  461  VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA          
SEQRES  19 C  461  GLY GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP          
SEQRES  20 C  461  ALA ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU          
SEQRES  21 C  461  SER TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE          
SEQRES  22 C  461  ALA THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO          
SEQRES  23 C  461  SER GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN          
SEQRES  24 C  461  ALA GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU          
SEQRES  25 C  461  GLY ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU          
SEQRES  26 C  461  GLY LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE          
SEQRES  27 C  461  PHE GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY          
SEQRES  28 C  461  PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP          
SEQRES  29 C  461  LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU          
SEQRES  30 C  461  ARG ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY          
SEQRES  31 C  461  SER LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN          
SEQRES  32 C  461  SER VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR          
SEQRES  33 C  461  SER HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS          
SEQRES  34 C  461  LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY          
SEQRES  35 C  461  PHE GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU          
SEQRES  36 C  461  SER MET PRO SER LEU ASP                                      
SEQRES   1 D  352  MET THR ILE ALA ILE GLY ARG ALA PRO ALA GLU ARG GLY          
SEQRES   2 D  352  TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS ARG ASP ARG          
SEQRES   3 D  352  PHE VAL PHE VAL GLY TRP SER GLY ILE LEU LEU PHE PRO          
SEQRES   4 D  352  CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU THR GLY THR          
SEQRES   5 D  352  THR PHE VAL THR SER TRP TYR THR HIS GLY LEU ALA SER          
SEQRES   6 D  352  SER TYR LEU GLU GLY CYS ASN PHE LEU THR VAL ALA VAL          
SEQRES   7 D  352  SER THR PRO ALA ASN SER MET GLY HIS SER LEU LEU LEU          
SEQRES   8 D  352  LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE THR ARG TRP          
SEQRES   9 D  352  CYS GLN LEU GLY GLY LEU TRP THR PHE ILE ALA LEU HIS          
SEQRES  10 D  352  GLY ALA PHE GLY LEU ILE GLY PHE MET LEU ARG GLN PHE          
SEQRES  11 D  352  GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO TYR ASN ALA          
SEQRES  12 D  352  ILE ALA PHE SER ALA PRO ILE ALA VAL PHE VAL SER VAL          
SEQRES  13 D  352  PHE LEU ILE TYR PRO LEU GLY GLN SER SER TRP PHE PHE          
SEQRES  14 D  352  ALA PRO SER PHE GLY VAL ALA ALA ILE PHE ARG PHE LEU          
SEQRES  15 D  352  LEU PHE PHE GLN GLY PHE HIS ASN TRP THR LEU ASN PRO          
SEQRES  16 D  352  PHE HIS MET MET GLY VAL ALA GLY VAL LEU GLY GLY ALA          
SEQRES  17 D  352  LEU LEU CYS ALA ILE HIS GLY ALA THR VAL GLU ASN THR          
SEQRES  18 D  352  LEU PHE GLN ASP GLY GLU GLY ALA SER THR PHE ARG ALA          
SEQRES  19 D  352  PHE ASN PRO THR GLN ALA GLU GLU THR TYR SER MET VAL          
SEQRES  20 D  352  THR ALA ASN ARG PHE TRP SER GLN ILE PHE GLY ILE ALA          
SEQRES  21 D  352  PHE SER ASN LYS ARG TRP LEU HIS PHE PHE MET LEU PHE          
SEQRES  22 D  352  VAL PRO VAL THR GLY LEU TRP MET SER ALA ILE GLY VAL          
SEQRES  23 D  352  VAL GLY LEU ALA LEU ASN LEU ARG SER TYR ASP PHE ILE          
SEQRES  24 D  352  SER GLN GLU ILE ARG ALA ALA GLU ASP PRO GLU PHE GLU          
SEQRES  25 D  352  THR PHE TYR THR LYS ASN LEU LEU LEU ASN GLU GLY ILE          
SEQRES  26 D  352  ARG ALA TRP MET ALA PRO GLN ASP GLN PRO HIS GLU ASN          
SEQRES  27 D  352  PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG GLY ASN ALA          
SEQRES  28 D  352  LEU                                                          
SEQRES   1 E   83  ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE ILE          
SEQRES   2 E   83  THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR ILE          
SEQRES   3 E   83  PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER THR          
SEQRES   4 E   83  GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO ASP          
SEQRES   5 E   83  SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU VAL          
SEQRES   6 E   83  THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR PHE          
SEQRES   7 E   83  LEU GLU GLN LEU LYS                                          
SEQRES   1 F   44  THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR PRO          
SEQRES   2 F   44  ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU ALA          
SEQRES   3 F   44  VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA MET          
SEQRES   4 F   44  GLN PHE ILE GLN ARG                                          
SEQRES   1 H   65  ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO LEU          
SEQRES   2 H   65  ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY THR          
SEQRES   3 H   65  THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU VAL          
SEQRES   4 H   65  PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR LEU          
SEQRES   5 H   65  ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU GLY          
SEQRES   1 I   38  MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR          
SEQRES   2 I   38  PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY          
SEQRES   3 I   38  ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU              
SEQRES   1 J   39  MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL ALA          
SEQRES   2 J   39  THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY LEU          
SEQRES   3 J   39  PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER LEU          
SEQRES   1 K   37  LYS LEU PRO GLU ALA TYR ALA ILE PHE ASP PRO LEU VAL          
SEQRES   2 K   37  ASP VAL LEU PRO VAL ILE PRO VAL LEU PHE LEU ALA LEU          
SEQRES   3 K   37  ALA PHE VAL TRP GLN ALA ALA VAL GLY PHE ARG                  
SEQRES   1 L   37  MET GLU PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN          
SEQRES   2 L   37  ARG THR SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL          
SEQRES   3 L   37  LEU ALA LEU LEU PHE SER SER TYR PHE PHE ASN                  
SEQRES   1 M   36  MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU          
SEQRES   2 M   36  PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR          
SEQRES   3 M   36  VAL GLN THR GLU SER GLN GLN LYS SER SER                      
SEQRES   1 O  246  ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY THR          
SEQRES   2 O  246  GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR ALA          
SEQRES   3 O  246  ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR ARG          
SEQRES   4 O  246  ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU VAL          
SEQRES   5 O  246  LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE          
SEQRES   6 O  246  VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER LEU          
SEQRES   7 O  246  ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP GLY          
SEQRES   8 O  246  SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN          
SEQRES   9 O  246  PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE PRO          
SEQRES  10 O  246  LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR GLN          
SEQRES  11 O  246  PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE LYS          
SEQRES  12 O  246  GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN PHE          
SEQRES  13 O  246  LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR ASP          
SEQRES  14 O  246  SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU          
SEQRES  15 O  246  ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS GLY          
SEQRES  16 O  246  GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG THR          
SEQRES  17 O  246  GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU SER          
SEQRES  18 O  246  ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL LYS          
SEQRES  19 O  246  ILE GLN GLY VAL PHE TYR ALA SER ILE GLU PRO ALA              
SEQRES   1 T   32  MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE          
SEQRES   2 T   32  ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO          
SEQRES   3 T   32  PRO ARG ILE THR LYS LYS                                      
SEQRES   1 U  104  ALA THR ALA SER THR GLU GLU GLU LEU VAL ASN VAL VAL          
SEQRES   2 U  104  ASP GLU LYS LEU GLY THR ALA TYR GLY GLU LYS ILE ASP          
SEQRES   3 U  104  LEU ASN ASN THR ASN ILE ALA ALA PHE ILE GLN TYR ARG          
SEQRES   4 U  104  GLY LEU TYR PRO THR LEU ALA LYS LEU ILE VAL LYS ASN          
SEQRES   5 U  104  ALA PRO TYR GLU SER VAL GLU ASP VAL LEU ASN ILE PRO          
SEQRES   6 U  104  GLY LEU THR GLU ARG GLN LYS GLN ILE LEU ARG GLU ASN          
SEQRES   7 U  104  LEU GLU HIS PHE THR VAL THR GLU VAL GLU THR ALA LEU          
SEQRES   8 U  104  VAL GLU GLY GLY ASP ARG TYR ASN ASN GLY LEU TYR LYS          
SEQRES   1 V  137  ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN          
SEQRES   2 V  137  SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR          
SEQRES   3 V  137  LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER          
SEQRES   4 V  137  CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU          
SEQRES   5 V  137  ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO          
SEQRES   6 V  137  ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN          
SEQRES   7 V  137  PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL          
SEQRES   8 V  137  HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET          
SEQRES   9 V  137  ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY          
SEQRES  10 V  137  HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP          
SEQRES  11 V  137  GLY GLY GLY LYS VAL TYR TYR                                  
SEQRES   1 y   46  MET GLY ILE PHE ASN GLY ILE ILE GLU PHE LEU SER ASN          
SEQRES   2 y   46  ILE ASN PHE GLU VAL ILE ALA GLN LEU THR MET ILE ALA          
SEQRES   3 y   46  MET ILE GLY ILE ALA GLY PRO MET ILE ILE PHE LEU LEU          
SEQRES   4 y   46  ALA VAL ARG ARG GLY ASN LEU                                  
SEQRES   1 X   40  THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY LEU          
SEQRES   2 X   40  LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA VAL          
SEQRES   3 X   40  LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG SER          
SEQRES   4 X   40  LEU                                                          
SEQRES   1 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                                                      
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  344  MET THR THR THR LEU GLN ARG ARG GLU SER ALA ASN LEU          
SEQRES   2 G  344  TRP GLU ARG PHE CYS ASN TRP VAL THR SER THR ASP ASN          
SEQRES   3 G  344  ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE MET ILE PRO          
SEQRES   4 G  344  THR LEU LEU ALA ALA THR ILE CYS PHE VAL ILE ALA PHE          
SEQRES   5 G  344  ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY ILE ARG GLU          
SEQRES   6 G  344  PRO VAL SER GLY SER LEU LEU TYR GLY ASN ASN ILE ILE          
SEQRES   7 G  344  THR GLY ALA VAL VAL PRO SER SER ASN ALA ILE GLY LEU          
SEQRES   8 G  344  HIS PHE TYR PRO ILE TRP GLU ALA ALA SER LEU ASP GLU          
SEQRES   9 G  344  TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU ILE ILE PHE          
SEQRES  10 G  344  HIS PHE LEU LEU GLY ALA SER CYS TYR MET GLY ARG GLN          
SEQRES  11 G  344  TRP GLU LEU SER TYR ARG LEU GLY MET ARG PRO TRP ILE          
SEQRES  12 G  344  CYS VAL ALA TYR SER ALA PRO LEU ALA SER ALA PHE ALA          
SEQRES  13 G  344  VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY SER PHE SER          
SEQRES  14 G  344  ASP GLY MET PRO LEU GLY ILE SER GLY THR PHE ASN PHE          
SEQRES  15 G  344  MET ILE VAL PHE GLN ALA GLU HIS ASN ILE LEU MET HIS          
SEQRES  16 G  344  PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL PHE GLY GLY          
SEQRES  17 G  344  ALA LEU PHE CYS ALA MET HIS GLY SER LEU VAL THR SER          
SEQRES  18 G  344  SER LEU ILE ARG GLU THR THR GLU THR GLU SER ALA ASN          
SEQRES  19 G  344  TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU THR TYR ASN          
SEQRES  20 G  344  ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG LEU ILE PHE          
SEQRES  21 G  344  GLN TYR ALA SER PHE ASN ASN SER ARG SER LEU HIS PHE          
SEQRES  22 G  344  PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL TRP PHE THR          
SEQRES  23 G  344  ALA LEU GLY ILE SER THR MET ALA PHE ASN LEU ASN GLY          
SEQRES  24 G  344  PHE ASN PHE ASN HIS SER VAL ILE ASP ALA LYS GLY ASN          
SEQRES  25 G  344  VAL ILE ASN THR TRP ALA ASP ILE ILE ASN ARG ALA ASN          
SEQRES  26 G  344  LEU GLY MET GLU VAL MET HIS GLU ARG ASN ALA HIS ASN          
SEQRES  27 G  344  PHE PRO LEU ASP LEU ALA                                      
SEQRES   1 N  510  MET GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE          
SEQRES   2 N  510  ASN ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS          
SEQRES   3 N  510  THR ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU          
SEQRES   4 N  510  TYR GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU          
SEQRES   5 N  510  ASN PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE          
SEQRES   6 N  510  MET ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP          
SEQRES   7 N  510  SER ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP          
SEQRES   8 N  510  SER PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER          
SEQRES   9 N  510  GLY LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR          
SEQRES  10 N  510  TRP ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU          
SEQRES  11 N  510  PRO ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU          
SEQRES  12 N  510  PHE LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE          
SEQRES  13 N  510  HIS LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER          
SEQRES  14 N  510  ASP PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA          
SEQRES  15 N  510  PRO GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO          
SEQRES  16 N  510  GLY GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL          
SEQRES  17 N  510  GLY ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO          
SEQRES  18 N  510  PRO GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE          
SEQRES  19 N  510  GLU THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE          
SEQRES  20 N  510  ALA ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER          
SEQRES  21 N  510  ALA THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR          
SEQRES  22 N  510  GLN TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG          
SEQRES  23 N  510  ARG VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU          
SEQRES  24 N  510  GLU ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR          
SEQRES  25 N  510  ASP TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE          
SEQRES  26 N  510  ARG THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN          
SEQRES  27 N  510  ALA TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY          
SEQRES  28 N  510  GLU GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU          
SEQRES  29 N  510  SER PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL          
SEQRES  30 N  510  LYS ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR          
SEQRES  31 N  510  SER PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY          
SEQRES  32 N  510  GLY GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR          
SEQRES  33 N  510  VAL LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE          
SEQRES  34 N  510  PHE GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE          
SEQRES  35 N  510  PHE ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS          
SEQRES  36 N  510  ALA VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP          
SEQRES  37 N  510  HIS GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY          
SEQRES  38 N  510  ILE ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY          
SEQRES  39 N  510  PHE TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG LYS          
SEQRES  40 N  510  GLU ALA VAL                                                  
SEQRES   1 P  461  MET VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN          
SEQRES   2 P  461  ARG ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY          
SEQRES   3 P  461  ASN ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY          
SEQRES   4 P  461  ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA          
SEQRES   5 P  461  GLY ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO          
SEQRES   6 P  461  GLU LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO          
SEQRES   7 P  461  HIS ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY          
SEQRES   8 P  461  GLU VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL          
SEQRES   9 P  461  VAL HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY          
SEQRES  10 P  461  VAL TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU          
SEQRES  11 P  461  TYR SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN          
SEQRES  12 P  461  LYS MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU          
SEQRES  13 P  461  GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE          
SEQRES  14 P  461  PHE GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY          
SEQRES  15 P  461  ASP VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG          
SEQRES  16 P  461  VAL ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY          
SEQRES  17 P  461  GLU GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL          
SEQRES  18 P  461  VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA          
SEQRES  19 P  461  GLY GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP          
SEQRES  20 P  461  ALA ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU          
SEQRES  21 P  461  SER TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE          
SEQRES  22 P  461  ALA THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO          
SEQRES  23 P  461  SER GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN          
SEQRES  24 P  461  ALA GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU          
SEQRES  25 P  461  GLY ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU          
SEQRES  26 P  461  GLY LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE          
SEQRES  27 P  461  PHE GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY          
SEQRES  28 P  461  PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP          
SEQRES  29 P  461  LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU          
SEQRES  30 P  461  ARG ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY          
SEQRES  31 P  461  SER LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN          
SEQRES  32 P  461  SER VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR          
SEQRES  33 P  461  SER HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS          
SEQRES  34 P  461  LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY          
SEQRES  35 P  461  PHE GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU          
SEQRES  36 P  461  SER MET PRO SER LEU ASP                                      
SEQRES   1 Q  352  MET THR ILE ALA ILE GLY ARG ALA PRO ALA GLU ARG GLY          
SEQRES   2 Q  352  TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS ARG ASP ARG          
SEQRES   3 Q  352  PHE VAL PHE VAL GLY TRP SER GLY ILE LEU LEU PHE PRO          
SEQRES   4 Q  352  CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU THR GLY THR          
SEQRES   5 Q  352  THR PHE VAL THR SER TRP TYR THR HIS GLY LEU ALA SER          
SEQRES   6 Q  352  SER TYR LEU GLU GLY CYS ASN PHE LEU THR VAL ALA VAL          
SEQRES   7 Q  352  SER THR PRO ALA ASN SER MET GLY HIS SER LEU LEU LEU          
SEQRES   8 Q  352  LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE THR ARG TRP          
SEQRES   9 Q  352  CYS GLN LEU GLY GLY LEU TRP THR PHE ILE ALA LEU HIS          
SEQRES  10 Q  352  GLY ALA PHE GLY LEU ILE GLY PHE MET LEU ARG GLN PHE          
SEQRES  11 Q  352  GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO TYR ASN ALA          
SEQRES  12 Q  352  ILE ALA PHE SER ALA PRO ILE ALA VAL PHE VAL SER VAL          
SEQRES  13 Q  352  PHE LEU ILE TYR PRO LEU GLY GLN SER SER TRP PHE PHE          
SEQRES  14 Q  352  ALA PRO SER PHE GLY VAL ALA ALA ILE PHE ARG PHE LEU          
SEQRES  15 Q  352  LEU PHE PHE GLN GLY PHE HIS ASN TRP THR LEU ASN PRO          
SEQRES  16 Q  352  PHE HIS MET MET GLY VAL ALA GLY VAL LEU GLY GLY ALA          
SEQRES  17 Q  352  LEU LEU CYS ALA ILE HIS GLY ALA THR VAL GLU ASN THR          
SEQRES  18 Q  352  LEU PHE GLN ASP GLY GLU GLY ALA SER THR PHE ARG ALA          
SEQRES  19 Q  352  PHE ASN PRO THR GLN ALA GLU GLU THR TYR SER MET VAL          
SEQRES  20 Q  352  THR ALA ASN ARG PHE TRP SER GLN ILE PHE GLY ILE ALA          
SEQRES  21 Q  352  PHE SER ASN LYS ARG TRP LEU HIS PHE PHE MET LEU PHE          
SEQRES  22 Q  352  VAL PRO VAL THR GLY LEU TRP MET SER ALA ILE GLY VAL          
SEQRES  23 Q  352  VAL GLY LEU ALA LEU ASN LEU ARG SER TYR ASP PHE ILE          
SEQRES  24 Q  352  SER GLN GLU ILE ARG ALA ALA GLU ASP PRO GLU PHE GLU          
SEQRES  25 Q  352  THR PHE TYR THR LYS ASN LEU LEU LEU ASN GLU GLY ILE          
SEQRES  26 Q  352  ARG ALA TRP MET ALA PRO GLN ASP GLN PRO HIS GLU ASN          
SEQRES  27 Q  352  PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG GLY ASN ALA          
SEQRES  28 Q  352  LEU                                                          
SEQRES   1 R   83  ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE ILE          
SEQRES   2 R   83  THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR ILE          
SEQRES   3 R   83  PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER THR          
SEQRES   4 R   83  GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO ASP          
SEQRES   5 R   83  SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU VAL          
SEQRES   6 R   83  THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR PHE          
SEQRES   7 R   83  LEU GLU GLN LEU LYS                                          
SEQRES   1 S   44  THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR PRO          
SEQRES   2 S   44  ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU ALA          
SEQRES   3 S   44  VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA MET          
SEQRES   4 S   44  GLN PHE ILE GLN ARG                                          
SEQRES   1 W   65  ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO LEU          
SEQRES   2 W   65  ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY THR          
SEQRES   3 W   65  THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU VAL          
SEQRES   4 W   65  PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR LEU          
SEQRES   5 W   65  ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU GLY          
SEQRES   1 a   38  MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR          
SEQRES   2 a   38  PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY          
SEQRES   3 a   38  ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU              
SEQRES   1 b   39  MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL ALA          
SEQRES   2 b   39  THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY LEU          
SEQRES   3 b   39  PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER LEU          
SEQRES   1 c   37  LYS LEU PRO GLU ALA TYR ALA ILE PHE ASP PRO LEU VAL          
SEQRES   2 c   37  ASP VAL LEU PRO VAL ILE PRO VAL LEU PHE LEU ALA LEU          
SEQRES   3 c   37  ALA PHE VAL TRP GLN ALA ALA VAL GLY PHE ARG                  
SEQRES   1 d   37  MET GLU PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN          
SEQRES   2 d   37  ARG THR SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL          
SEQRES   3 d   37  LEU ALA LEU LEU PHE SER SER TYR PHE PHE ASN                  
SEQRES   1 e   36  MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU          
SEQRES   2 e   36  PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR          
SEQRES   3 e   36  VAL GLN THR GLU SER GLN GLN LYS SER SER                      
SEQRES   1 f  246  ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY THR          
SEQRES   2 f  246  GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR ALA          
SEQRES   3 f  246  ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR ARG          
SEQRES   4 f  246  ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU VAL          
SEQRES   5 f  246  LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE          
SEQRES   6 f  246  VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER LEU          
SEQRES   7 f  246  ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP GLY          
SEQRES   8 f  246  SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN          
SEQRES   9 f  246  PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE PRO          
SEQRES  10 f  246  LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR GLN          
SEQRES  11 f  246  PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE LYS          
SEQRES  12 f  246  GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN PHE          
SEQRES  13 f  246  LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR ASP          
SEQRES  14 f  246  SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU          
SEQRES  15 f  246  ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS GLY          
SEQRES  16 f  246  GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG THR          
SEQRES  17 f  246  GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU SER          
SEQRES  18 f  246  ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL LYS          
SEQRES  19 f  246  ILE GLN GLY VAL PHE TYR ALA SER ILE GLU PRO ALA              
SEQRES   1 g   32  MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE          
SEQRES   2 g   32  ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO          
SEQRES   3 g   32  PRO ARG ILE THR LYS LYS                                      
SEQRES   1 h  104  ALA THR ALA SER THR GLU GLU GLU LEU VAL ASN VAL VAL          
SEQRES   2 h  104  ASP GLU LYS LEU GLY THR ALA TYR GLY GLU LYS ILE ASP          
SEQRES   3 h  104  LEU ASN ASN THR ASN ILE ALA ALA PHE ILE GLN TYR ARG          
SEQRES   4 h  104  GLY LEU TYR PRO THR LEU ALA LYS LEU ILE VAL LYS ASN          
SEQRES   5 h  104  ALA PRO TYR GLU SER VAL GLU ASP VAL LEU ASN ILE PRO          
SEQRES   6 h  104  GLY LEU THR GLU ARG GLN LYS GLN ILE LEU ARG GLU ASN          
SEQRES   7 h  104  LEU GLU HIS PHE THR VAL THR GLU VAL GLU THR ALA LEU          
SEQRES   8 h  104  VAL GLU GLY GLY ASP ARG TYR ASN ASN GLY LEU TYR LYS          
SEQRES   1 i  137  ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN          
SEQRES   2 i  137  SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR          
SEQRES   3 i  137  LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER          
SEQRES   4 i  137  CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU          
SEQRES   5 i  137  ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO          
SEQRES   6 i  137  ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN          
SEQRES   7 i  137  PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL          
SEQRES   8 i  137  HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET          
SEQRES   9 i  137  ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY          
SEQRES  10 i  137  HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP          
SEQRES  11 i  137  GLY GLY GLY LYS VAL TYR TYR                                  
SEQRES   1 m   46  MET GLY ILE PHE ASN GLY ILE ILE GLU PHE LEU SER ASN          
SEQRES   2 m   46  ILE ASN PHE GLU VAL ILE ALA GLN LEU THR MET ILE ALA          
SEQRES   3 m   46  MET ILE GLY ILE ALA GLY PRO MET ILE ILE PHE LEU LEU          
SEQRES   4 m   46  ALA VAL ARG ARG GLY ASN LEU                                  
SEQRES   1 j   40  THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY LEU          
SEQRES   2 j   40  LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA VAL          
SEQRES   3 j   40  LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG SER          
SEQRES   4 j   40  LEU                                                          
SEQRES   1 k   28  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 k   28  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   3 k   28  UNK UNK                                                      
SEQRES   1 l   62  MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL          
SEQRES   2 l   62  ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA          
SEQRES   3 l   62  TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU          
SEQRES   4 l   62  ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU          
SEQRES   5 l   62  VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL                      
HET    CLA  A 401      65                                                       
HET    CLA  A 402      65                                                       
HET    CLA  A 403      65                                                       
HET    PHO  A 404      64                                                       
HET    CLA  A 405      65                                                       
HET    PL9  A 406      45                                                       
HET    DGD  A 407      56                                                       
HET    LHG  A 408      39                                                       
HET    SQD  A 409      51                                                       
HET    LMG  A 410      51                                                       
HET    LHG  A 411      37                                                       
HET    OEC  A 412       5                                                       
HET    FE2  A 413       1                                                       
HET    SQD  A 414      54                                                       
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    SQD  B 624      43                                                       
HET    LMT  B 625      35                                                       
HET    LMT  B 626      35                                                       
HET    SQD  B 627      47                                                       
HET    DGD  B 628      52                                                       
HET    LMT  B 629      35                                                       
HET    LMT  B 630      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    BCR  C 514      40                                                       
HET    CLA  C 510      65                                                       
HET    BCR  C 515      40                                                       
HET    CLA  C 511      65                                                       
HET    DGD  C 516      53                                                       
HET    CLA  C 512      65                                                       
HET    DGD  C 517      62                                                       
HET    CLA  C 513      65                                                       
HET    DGD  C 518      66                                                       
HET    LMG  C 519      48                                                       
HET    LMG  C 520      45                                                       
HET    PHO  D 402      64                                                       
HET    PL9  D 404      55                                                       
HET    CLA  D 401      65                                                       
HET    LMG  D 406      46                                                       
HET    LMG  D 407      48                                                       
HET    CLA  D 403      65                                                       
HET    BCR  D 405      40                                                       
HET    BCT  D 410       4                                                       
HET     CL  D 411       1                                                       
HET    DGD  D 408      63                                                       
HET    LMT  D 409      31                                                       
HET    LMG  D 412      42                                                       
HET    HEM  E 101      43                                                       
HET    LMG  E 102      44                                                       
HET    SQD  F 101      45                                                       
HET    BCR  H 101      40                                                       
HET    BCR  I 101      40                                                       
HET    LMG  I 102      43                                                       
HET    LMT  I 103      35                                                       
HET    PL9  J 101      35                                                       
HET    BCR  J 102      40                                                       
HET    BCR  K 101      40                                                       
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    BCR  T 103      40                                                       
HET    HEM  V 201      43                                                       
HET    BCR  Z 101      40                                                       
HET    SQD  G 401      54                                                       
HET    CLA  G 402      65                                                       
HET    CLA  G 403      65                                                       
HET    PHO  G 405      64                                                       
HET    CLA  G 404      65                                                       
HET    PL9  G 407      45                                                       
HET    CLA  G 406      65                                                       
HET    DGD  G 408      56                                                       
HET    SQD  G 410      51                                                       
HET    LHG  G 409      39                                                       
HET    LMG  G 411      51                                                       
HET    LHG  G 412      37                                                       
HET    OEC  G 413       5                                                       
HET    FE2  G 414       1                                                       
HET     CL  G 415       1                                                       
HET    SQD  N 601      47                                                       
HET    DGD  N 602      52                                                       
HET    LMT  N 603      35                                                       
HET    LMT  N 604      35                                                       
HET    CLA  N 605      65                                                       
HET    CLA  N 606      65                                                       
HET    CLA  N 607      65                                                       
HET    CLA  N 608      65                                                       
HET    CLA  N 609      65                                                       
HET    CLA  N 610      65                                                       
HET    CLA  N 611      65                                                       
HET    CLA  N 612      65                                                       
HET    CLA  N 613      65                                                       
HET    CLA  N 614      65                                                       
HET    CLA  N 615      65                                                       
HET    CLA  N 616      65                                                       
HET    CLA  N 617      65                                                       
HET    BCR  N 621      40                                                       
HET    CLA  N 618      65                                                       
HET    CLA  N 619      65                                                       
HET    LMG  N 623      49                                                       
HET    CLA  N 620      65                                                       
HET    LMT  N 625      35                                                       
HET    LMG  N 622      49                                                       
HET    LMT  N 624      35                                                       
HET    CLA  P 501      65                                                       
HET    CLA  P 502      65                                                       
HET    CLA  P 503      65                                                       
HET    CLA  P 504      65                                                       
HET    CLA  P 505      65                                                       
HET    CLA  P 506      65                                                       
HET    CLA  P 507      65                                                       
HET    CLA  P 508      65                                                       
HET    CLA  P 509      65                                                       
HET    CLA  P 510      65                                                       
HET    CLA  P 511      65                                                       
HET    BCR  P 514      40                                                       
HET    CLA  P 512      65                                                       
HET    BCR  P 515      40                                                       
HET    CLA  P 513      65                                                       
HET    DGD  P 517      53                                                       
HET    DGD  P 518      62                                                       
HET    BCR  P 516      40                                                       
HET    LMG  P 520      48                                                       
HET    DGD  P 519      66                                                       
HET    LMG  P 521      45                                                       
HET    PHO  Q 403      64                                                       
HET    LMG  Q 401      42                                                       
HET    PL9  Q 405      55                                                       
HET    CLA  Q 402      65                                                       
HET    LMG  Q 407      48                                                       
HET    CLA  Q 404      65                                                       
HET    SQD  Q 408      43                                                       
HET    DGD  Q 409      63                                                       
HET    LMG  Q 406      46                                                       
HET    LMT  Q 410      31                                                       
HET    BCT  Q 411       4                                                       
HET    HEM  R 101      43                                                       
HET    LMG  R 102      44                                                       
HET    BCR  S 101      40                                                       
HET    SQD  S 102      45                                                       
HET    BCR  W 101      40                                                       
HET    DGD  W 102      58                                                       
HET    BCR  a 101      40                                                       
HET    LMG  a 102      43                                                       
HET    LMT  a 103      35                                                       
HET    PL9  b 101      35                                                       
HET    BCR  b 102      40                                                       
HET    BCR  c 101      40                                                       
HET    LMT  e 101      35                                                       
HET    LMG  e 102      42                                                       
HET     CA  f 301       1                                                       
HET    HEM  i 201      43                                                       
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     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     OEC OXYGEN EVOLVING SYSTEM                                           
HETNAM     FE2 FE (II) ION                                                      
HETNAM     BCR BETA-CAROTENE                                                    
HETNAM     LMT DODECYL-BETA-D-MALTOSIDE                                         
HETNAM     BCT BICARBONATE ION                                                  
HETNAM      CL CHLORIDE ION                                                     
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM      CA CALCIUM ION                                                      
HETSYN     PL9 PLASTOQUINONE 9                                                  
HETSYN     SQD SULFOQUINOVOSYLDIACYLGLYCEROL                                    
HETSYN     HEM HEME                                                             
FORMUL  41  CLA    70(C55 H72 MG N4 O5 2+)                                      
FORMUL  44  PHO    4(C55 H74 N4 O5)                                             
FORMUL  46  PL9    6(C53 H80 O2)                                                
FORMUL  47  DGD    14(C51 H96 O15)                                              
FORMUL  48  LHG    4(C38 H75 O10 P)                                             
FORMUL  49  SQD    10(C41 H78 O12 S)                                            
FORMUL  50  LMG    22(C45 H86 O10)                                              
FORMUL  52  OEC    2(CA MN4 O4)                                                 
FORMUL  53  FE2    2(FE 2+)                                                     
FORMUL  71  BCR    24(C40 H56)                                                  
FORMUL  79  LMT    14(C24 H46 O11)                                              
FORMUL  12  BCT    2(C H O3 1-)                                                 
FORMUL  13   CL    2(CL 1-)                                                     
FORMUL  17  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL  29   CA    2(CA 2+)                                                     
HELIX    1   1 ASN A   12  THR A   22  1                                  11    
HELIX    2   2 PHE A   33  ALA A   55  1                                  23    
HELIX    3   3 SER A   70  GLY A   74  5                                   5    
HELIX    4   4 PRO A   95  ALA A   99  5                                   5    
HELIX    5   5 SER A  101  ASN A  108  1                                   8    
HELIX    6   6 GLY A  109  LEU A  137  1                                  29    
HELIX    7   7 TRP A  142  TYR A  147  1                                   6    
HELIX    8   8 TYR A  147  LEU A  159  1                                  13    
HELIX    9   9 LEU A  159  GLY A  166  1                                   8    
HELIX   10  10 SER A  167  GLY A  171  5                                   5    
HELIX   11  11 ILE A  176  ASN A  191  1                                  16    
HELIX   12  12 ILE A  192  MET A  194  5                                   3    
HELIX   13  13 HIS A  195  SER A  222  1                                  28    
HELIX   14  14 ASN A  247  ILE A  259  1                                  13    
HELIX   15  15 PHE A  260  SER A  264  5                                   5    
HELIX   16  16 ASN A  267  MET A  293  1                                  27    
HELIX   17  17 THR A  316  HIS A  332  1                                  17    
HELIX   18  18 GLU A  333  HIS A  337  5                                   5    
HELIX   19  19 PRO B    4  ILE B   13  5                                  10    
HELIX   20  20 ASP B   15  ALA B   43  1                                  29    
HELIX   21  21 PRO B   54  GLN B   58  5                                   5    
HELIX   22  22 VAL B   62  ARG B   68  1                                   7    
HELIX   23  23 SER B   92  TYR B  117  1                                  26    
HELIX   24  24 LEU B  120  ARG B  124  5                                   5    
HELIX   25  25 ASP B  134  HIS B  157  1                                  24    
HELIX   26  26 GLY B  186  ASN B  191  5                                   6    
HELIX   27  27 ASN B  194  VAL B  219  1                                  26    
HELIX   28  28 PRO B  222  LEU B  229  1                                   8    
HELIX   29  29 ASN B  233  GLU B  235  5                                   3    
HELIX   30  30 THR B  236  GLY B  259  1                                  24    
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 ARG B  384  SER B  388  5                                   5    
HELIX   39  39 SER B  391  GLY B  396  1                                   6    
HELIX   40  40 ASP B  413  ILE B  425  1                                  13    
HELIX   41  41 SER B  446  PHE B  475  1                                  30    
HELIX   42  42 ALA C   34  ILE C   43  5                                  10    
HELIX   43  43 GLY C   47  PHE C   75  1                                  29    
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  ARG C  370  5                                   5    
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  ALA C  453  1                                  33    
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 ASP D  100  LEU D  107  1                                   8    
HELIX   67  67 GLY D  108  GLY D  137  1                                  30    
HELIX   68  68 PRO D  140  PHE D  146  1                                   7    
HELIX   69  69 PHE D  146  LEU D  158  1                                  13    
HELIX   70  70 LEU D  158  GLN D  164  1                                   7    
HELIX   71  71 SER D  166  ALA D  170  5                                   5    
HELIX   72  72 VAL D  175  ASN D  190  1                                  16    
HELIX   73  73 TRP D  191  LEU D  193  5                                   3    
HELIX   74  74 ASN D  194  ASN D  220  1                                  27    
HELIX   75  75 SER D  245  PHE D  257  1                                  13    
HELIX   76  76 ASN D  263  LEU D  291  1                                  29    
HELIX   77  77 PHE D  298  ASP D  308  1                                  11    
HELIX   78  78 THR D  313  GLN D  334  1                                  22    
HELIX   79  79 PRO D  335  ASN D  338  5                                   4    
HELIX   80  80 PRO E    9  SER E   16  1                                   8    
HELIX   81  81 SER E   16  THR E   40  1                                  25    
HELIX   82  82 GLY E   41  PHE E   47  1                                   7    
HELIX   83  83 GLU E   71  GLN E   82  1                                  12    
HELIX   84  84 THR F   17  GLN F   41  1                                  25    
HELIX   85  85 THR H    5  ARG H   12  1                                   8    
HELIX   86  86 THR H   27  ASN H   50  1                                  24    
HELIX   87  87 GLU I    2  SER I   25  1                                  24    
HELIX   88  88 PRO J    9  ALA J   32  1                                  24    
HELIX   89  89 PRO K   12  ILE K   17  5                                   6    
HELIX   90  90 PHE K   18  ASP K   23  1                                   6    
HELIX   91  91 VAL K   24  PRO K   26  5                                   3    
HELIX   92  92 VAL K   27  VAL K   43  1                                  17    
HELIX   93  93 ASN L   13  ASN L   37  1                                  25    
HELIX   94  94 LEU M    6  SER M   31  1                                  26    
HELIX   95  95 THR O   32  ILE O   36  5                                   5    
HELIX   96  96 GLY O   40  LYS O   44  5                                   5    
HELIX   97  97 LEU O  208  VAL O  213  1                                   6    
HELIX   98  98 GLU T    2  PHE T   23  1                                  22    
HELIX   99  99 ASN U   41  LEU U   47  1                                   7    
HELIX  100 100 ASN U   61  TYR U   68  5                                   8    
HELIX  101 101 TYR U   72  ASN U   82  1                                  11    
HELIX  102 102 SER U   87  ILE U   94  5                                   8    
HELIX  103 103 THR U   98  LEU U  109  1                                  12    
HELIX  104 104 GLU U  118  GLU U  123  1                                   6    
HELIX  105 105 GLY U  124  ASP U  126  5                                   3    
HELIX  106 106 THR V   48  CYS V   63  1                                  16    
HELIX  107 107 CYS V   63  VAL V   68  1                                   6    
HELIX  108 108 GLY V   69  ILE V   71  5                                   3    
HELIX  109 109 ARG V   81  LEU V   87  1                                   7    
HELIX  110 110 ASN V   94  MET V  102  1                                   9    
HELIX  111 111 SER V  120  ALA V  124  5                                   5    
HELIX  112 112 PRO V  128  LEU V  133  1                                   6    
HELIX  113 113 THR V  134  GLY V  153  1                                  20    
HELIX  114 114 GLY V  153  GLY V  158  1                                   6    
HELIX  115 115 GLN y   21  ARG y   42  1                                  22    
HELIX  116 116 THR X   13  GLN X   42  1                                  30    
HELIX  117 117 UNK Y    2  UNK Y   13  1                                  12    
HELIX  118 118 UNK Y   14  UNK Y   25  1                                  12    
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 ASN G   12  THR G   22  1                                  11    
HELIX  122 122 PHE G   33  ALA G   55  1                                  23    
HELIX  123 123 SER G   70  GLY G   74  5                                   5    
HELIX  124 124 PRO G   95  ALA G   99  5                                   5    
HELIX  125 125 SER G  101  ASN G  108  1                                   8    
HELIX  126 126 GLY G  109  LEU G  137  1                                  29    
HELIX  127 127 TRP G  142  TYR G  147  1                                   6    
HELIX  128 128 TYR G  147  LEU G  159  1                                  13    
HELIX  129 129 LEU G  159  GLY G  166  1                                   8    
HELIX  130 130 SER G  167  GLY G  171  5                                   5    
HELIX  131 131 ILE G  176  ASN G  191  1                                  16    
HELIX  132 132 ILE G  192  MET G  194  5                                   3    
HELIX  133 133 HIS G  195  SER G  222  1                                  28    
HELIX  134 134 ASN G  247  ILE G  259  1                                  13    
HELIX  135 135 PHE G  260  SER G  264  5                                   5    
HELIX  136 136 ASN G  267  MET G  293  1                                  27    
HELIX  137 137 THR G  316  HIS G  332  1                                  17    
HELIX  138 138 GLU G  333  HIS G  337  5                                   5    
HELIX  139 139 PRO N    4  ILE N   13  5                                  10    
HELIX  140 140 ASP N   15  ALA N   43  1                                  29    
HELIX  141 141 PRO N   54  GLN N   58  5                                   5    
HELIX  142 142 VAL N   62  ARG N   68  1                                   7    
HELIX  143 143 SER N   92  TYR N  117  1                                  26    
HELIX  144 144 LEU N  120  ARG N  124  5                                   5    
HELIX  145 145 ASP N  134  HIS N  157  1                                  24    
HELIX  146 146 GLY N  186  ASN N  191  5                                   6    
HELIX  147 147 ASN N  194  VAL N  219  1                                  26    
HELIX  148 148 PRO N  222  LEU N  229  1                                   8    
HELIX  149 149 ASN N  233  GLU N  235  5                                   3    
HELIX  150 150 THR N  236  GLY N  259  1                                  24    
HELIX  151 151 PRO N  264  GLY N  269  1                                   6    
HELIX  152 152 THR N  271  SER N  277  1                                   7    
HELIX  153 153 SER N  278  SER N  294  1                                  17    
HELIX  154 154 THR N  297  ILE N  305  1                                   9    
HELIX  155 155 PRO N  306  TYR N  312  1                                   7    
HELIX  156 156 ASP N  313  ASN N  318  5                                   6    
HELIX  157 157 PRO N  329  GLY N  333  5                                   5    
HELIX  158 158 ARG N  384  SER N  388  5                                   5    
HELIX  159 159 SER N  391  GLY N  396  1                                   6    
HELIX  160 160 ASP N  413  ILE N  425  1                                  13    
HELIX  161 161 SER N  446  PHE N  475  1                                  30    
HELIX  162 162 ALA P   34  ILE P   43  5                                  10    
HELIX  163 163 GLY P   47  PHE P   75  1                                  29    
HELIX  164 164 LEU P   88  LEU P   95  1                                   8    
HELIX  165 165 GLY P  100  GLU P  104  5                                   5    
HELIX  166 166 THR P  108  ARG P  135  1                                  28    
HELIX  167 167 ASP P  153  PHE P  181  1                                  29    
HELIX  168 168 ASP P  205  PHE P  210  1                                   6    
HELIX  169 169 GLY P  211  LYS P  215  5                                   5    
HELIX  170 170 GLY P  222  VAL P  227  5                                   6    
HELIX  171 171 ASN P  229  LEU P  253  1                                  25    
HELIX  172 172 GLY P  258  PHE P  264  1                                   7    
HELIX  173 173 SER P  267  ASN P  293  1                                  27    
HELIX  174 174 THR P  305  LEU P  324  1                                  20    
HELIX  175 175 ASN P  327  ALA P  331  5                                   5    
HELIX  176 176 GLY P  353  TRP P  359  5                                   7    
HELIX  177 177 LEU P  366  ARG P  370  5                                   5    
HELIX  178 178 ASP P  376  ASP P  383  1                                   8    
HELIX  179 179 GLN P  385  THR P  397  1                                  13    
HELIX  180 180 SER P  421  GLY P  454  1                                  34    
HELIX  181 181 GLU P  464  MET P  469  5                                   6    
HELIX  182 182 TRP Q   14  LYS Q   23  1                                  10    
HELIX  183 183 VAL Q   30  PHE Q   54  1                                  25    
HELIX  184 184 SER Q   57  GLY Q   62  1                                   6    
HELIX  185 185 SER Q   66  GLY Q   70  5                                   5    
HELIX  186 186 ASP Q  100  LEU Q  107  1                                   8    
HELIX  187 187 GLY Q  108  GLY Q  137  1                                  30    
HELIX  188 188 PRO Q  140  PHE Q  146  1                                   7    
HELIX  189 189 PHE Q  146  LEU Q  158  1                                  13    
HELIX  190 190 LEU Q  158  GLN Q  164  1                                   7    
HELIX  191 191 SER Q  166  ALA Q  170  5                                   5    
HELIX  192 192 VAL Q  175  ASN Q  190  1                                  16    
HELIX  193 193 TRP Q  191  LEU Q  193  5                                   3    
HELIX  194 194 ASN Q  194  ASN Q  220  1                                  27    
HELIX  195 195 SER Q  245  PHE Q  257  1                                  13    
HELIX  196 196 ASN Q  263  LEU Q  291  1                                  29    
HELIX  197 197 PHE Q  298  ASP Q  308  1                                  11    
HELIX  198 198 THR Q  313  GLN Q  334  1                                  22    
HELIX  199 199 PRO Q  335  ASN Q  338  5                                   4    
HELIX  200 200 PRO Q  342  LEU Q  346  5                                   5    
HELIX  201 201 PRO R    9  SER R   16  1                                   8    
HELIX  202 202 SER R   16  THR R   40  1                                  25    
HELIX  203 203 GLY R   41  PHE R   47  1                                   7    
HELIX  204 204 GLU R   71  GLN R   82  1                                  12    
HELIX  205 205 THR S   17  GLN S   41  1                                  25    
HELIX  206 206 THR W    5  ARG W   12  1                                   8    
HELIX  207 207 THR W   27  ASN W   50  1                                  24    
HELIX  208 208 GLU a    2  SER a   25  1                                  24    
HELIX  209 209 PRO b    9  ALA b   32  1                                  24    
HELIX  210 210 PRO c   12  ILE c   17  5                                   6    
HELIX  211 211 PHE c   18  ASP c   23  1                                   6    
HELIX  212 212 VAL c   24  PRO c   26  5                                   3    
HELIX  213 213 VAL c   27  VAL c   43  1                                  17    
HELIX  214 214 ASN d   13  ASN d   37  1                                  25    
HELIX  215 215 LEU e    6  SER e   31  1                                  26    
HELIX  216 216 THR f   32  ILE f   36  5                                   5    
HELIX  217 217 GLY f   40  LYS f   44  5                                   5    
HELIX  218 218 LEU f  208  VAL f  213  1                                   6    
HELIX  219 219 GLU g    2  PHE g   23  1                                  22    
HELIX  220 220 ASN h   41  LEU h   47  1                                   7    
HELIX  221 221 ASN h   61  TYR h   68  5                                   8    
HELIX  222 222 TYR h   72  ASN h   82  1                                  11    
HELIX  223 223 SER h   87  ILE h   94  5                                   8    
HELIX  224 224 THR h   98  LEU h  109  1                                  12    
HELIX  225 225 GLU h  118  GLU h  123  1                                   6    
HELIX  226 226 GLY h  124  ASP h  126  5                                   3    
HELIX  227 227 THR i   48  CYS i   63  1                                  16    
HELIX  228 228 CYS i   63  VAL i   68  1                                   6    
HELIX  229 229 GLY i   69  ILE i   71  5                                   3    
HELIX  230 230 ARG i   81  LEU i   87  1                                   7    
HELIX  231 231 ASN i   94  MET i  102  1                                   9    
HELIX  232 232 SER i  120  ALA i  124  5                                   5    
HELIX  233 233 PHE i  127  ARG i  131  5                                   5    
HELIX  234 234 THR i  134  GLY i  153  1                                  20    
HELIX  235 235 GLY i  153  GLY i  158  1                                   6    
HELIX  236 236 GLN m   21  ARG m   42  1                                  22    
HELIX  237 237 THR j   13  GLN j   42  1                                  30    
HELIX  238 238 UNK k    2  UNK k   13  1                                  12    
HELIX  239 239 UNK k   14  UNK k   25  1                                  12    
HELIX  240 240 THR l    2  SER l   29  1                                  28    
HELIX  241 241 ARG l   35  VAL l   62  1                                  28    
SHEET    1   A 2 ALA A  81  VAL A  82  0                                        
SHEET    2   A 2 LEU A 174  GLY A 175 -1  O  LEU A 174   N  VAL A  82           
SHEET    1   B 2 LEU A 297  ASN A 298  0                                        
SHEET    2   B 2 GLY C 402  SER C 403  1  O  GLY C 402   N  ASN A 298           
SHEET    1   C 2 MET B 166  VAL B 168  0                                        
SHEET    2   C 2 SER B 177  GLN B 179 -1  O  SER B 177   N  VAL B 168           
SHEET    1   D 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 ALA D  77  VAL D  78  0                                        
SHEET    2   H 2 PHE D 173  GLY D 174 -1  O  PHE D 173   N  VAL D  78           
SHEET    1   I 2 TYR O  56  PRO O  57  0                                        
SHEET    2   I 2 SER O 161  ILE O 162 -1  O  ILE O 162   N  TYR O  56           
SHEET    1   J10 PHE O  91  PRO O  93  0                                        
SHEET    2   J10 ARG O  65  LYS O  79 -1  N  VAL O  78   O  VAL O  92           
SHEET    3   J10 GLU O 258  GLU O 270 -1  O  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  LYS O 229   O  ALA O 238           
SHEET    6   J10 PHE O 168  PRO O 175 -1  N  VAL O 174   O  THR O 219           
SHEET    7   J10 LYS O 149  SER O 154 -1  N  LYS O 149   O  ASN O 173           
SHEET    8   J10 LEU O 119  ILE O 127 -1  N  PHE O 121   O  ALA O 153           
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 G  81  VAL G  82  0                                        
SHEET    2   N 2 LEU G 174  GLY G 175 -1  O  LEU G 174   N  VAL G  82           
SHEET    1   O 2 LEU G 297  ASN G 298  0                                        
SHEET    2   O 2 GLY P 402  SER P 403  1  O  GLY P 402   N  ASN G 298           
SHEET    1   P 2 MET N 166  VAL N 168  0                                        
SHEET    2   P 2 SER N 177  GLN N 179 -1  O  SER N 177   N  VAL N 168           
SHEET    1   Q 6 VAL N 377  ASP N 380  0                                        
SHEET    2   Q 6 ILE N 369  THR N 371 -1  N  LEU N 370   O  ALA N 379           
SHEET    3   Q 6 GLU N 353  VAL N 356 -1  N  PHE N 355   O  THR N 371           
SHEET    4   Q 6 ILE N 336  ARG N 347 -1  N  PHE N 346   O  LEU N 354           
SHEET    5   Q 6 THR N 398  TYR N 402 -1  O  SER N 400   N  VAL N 345           
SHEET    6   Q 6 THR N 410  PHE N 411 -1  O  PHE N 411   N  VAL N 399           
SHEET    1   R 5 VAL N 377  ASP N 380  0                                        
SHEET    2   R 5 ILE N 369  THR N 371 -1  N  LEU N 370   O  ALA N 379           
SHEET    3   R 5 GLU N 353  VAL N 356 -1  N  PHE N 355   O  THR N 371           
SHEET    4   R 5 ILE N 336  ARG N 347 -1  N  PHE N 346   O  LEU N 354           
SHEET    5   R 5 ILE N 429  ASP N 433 -1  O  GLU N 431   N  GLN N 338           
SHEET    1   S 2 LEU P 185  ASP P 187  0                                        
SHEET    2   S 2 ASP P 195  ARG P 197 -1  O  ARG P 197   N  LEU P 185           
SHEET    1   T 2 LEU P 341  ARG P 343  0                                        
SHEET    2   T 2 ILE P 349  PHE P 351 -1  O  ILE P 350   N  MET P 342           
SHEET    1   U 2 ALA Q  77  VAL Q  78  0                                        
SHEET    2   U 2 PHE Q 173  GLY Q 174 -1  O  PHE Q 173   N  VAL Q  78           
SHEET    1   V 2 TYR f  56  PRO f  57  0                                        
SHEET    2   V 2 SER f 161  ILE f 162 -1  O  ILE f 162   N  TYR f  56           
SHEET    1   W10 PHE f  91  PRO f  93  0                                        
SHEET    2   W10 ARG f  65  LYS f  79 -1  N  VAL f  78   O  VAL f  92           
SHEET    3   W10 GLU f 258  GLU f 270 -1  O  VAL f 264   N  GLN f  72           
SHEET    4   W10 GLU f 236  LEU f 246 -1  N  SER f 243   O  ILE f 261           
SHEET    5   W10 LEU f 218  LYS f 229 -1  N  LYS f 229   O  ALA f 238           
SHEET    6   W10 PHE f 168  PRO f 175 -1  N  VAL f 174   O  THR f 219           
SHEET    7   W10 LYS f 149  SER f 154 -1  N  LYS f 149   O  ASN f 173           
SHEET    8   W10 LEU f 119  ILE f 127 -1  N  PHE f 121   O  ALA f 153           
SHEET    9   W10 LEU f 104  VAL f 113 -1  N  GLN f 108   O  GLU f 124           
SHEET   10   W10 ARG f  65  LYS f  79 -1  N  LEU f  71   O  LEU f 104           
SHEET    1   X 3 LYS f  95  LEU f  96  0                                        
SHEET    2   X 3 PHE f 129  GLN f 135 -1  O  GLN f 135   N  LYS f  95           
SHEET    3   X 3 ARG f 141  THR f 147 -1  O  ILE f 142   N  VAL f 134           
SHEET    1   Y 2 ILE h  55  ASP h  56  0                                        
SHEET    2   Y 2 PHE h 112  THR h 113  1  O  THR h 113   N  ILE h  55           
SHEET    1   Z 2 THR i  35  PRO i  37  0                                        
SHEET    2   Z 2 THR i  44  THR i  46 -1  O  ILE i  45   N  VAL i  36           
SSBOND   1 CYS O   45    CYS O   70                          1555   1555  2.03  
SSBOND   2 CYS f   45    CYS f   70                          1555   1555  2.03  
LINK         NE2 HIS A 215                FE   FE2 A 413     1555   1555  2.43  
LINK         NE2 HIS Q 214                FE   FE2 G 414     1555   1555  2.43  
LINK         NE2 HIS G 215                FE   FE2 G 414     1555   1555  2.44  
LINK         NE2 HIS R  23                FE   HEM R 101     1555   1555  2.46  
LINK         NE2 HIS E  23                FE   HEM E 101     1555   1555  2.46  
LINK         NE2 HIS V  67                FE   HEM V 201     1555   1555  2.46  
LINK         NE2 HIS D 214                FE   FE2 A 413     1555   1555  2.46  
LINK         OD1 ASP A 342                MN2  OEC A 412     1555   1555  2.48  
LINK         NE2 HIS i 118                FE   HEM i 201     1555   1555  2.48  
LINK         NE2 HIS V 118                FE   HEM V 201     1555   1555  2.49  
LINK         NE2 HIS A 272                FE   FE2 A 413     1555   1555  2.50  
LINK         NE2 HIS i  67                FE   HEM i 201     1555   1555  2.50  
LINK         NE2 HIS G 272                FE   FE2 G 414     1555   1555  2.51  
LINK        FE   FE2 G 414                 O3  BCT Q 411     1555   1555  2.52  
LINK         NE2 HIS S  24                FE   HEM R 101     1555   1555  2.53  
LINK         NE2 HIS F  24                FE   HEM E 101     1555   1555  2.54  
LINK        FE   FE2 A 413                 O3  BCT D 410     1555   1555  2.54  
LINK         OXT ALA A 344                MN2  OEC A 412     1555   1555  2.55  
LINK         OE2 GLU C 354                MN3  OEC A 412     1555   1555  2.56  
LINK        FE   FE2 A 413                 O2  BCT D 410     1555   1555  2.56  
LINK        FE   FE2 G 414                 O2  BCT Q 411     1555   1555  2.57  
LINK         OE1 GLU G 333                MN3  OEC G 413     1555   1555  2.58  
LINK         OXT ALA G 344                MN2  OEC G 413     1555   1555  2.59  
LINK         OE1 GLU A 333                MN3  OEC A 412     1555   1555  2.60  
LINK         NE2 HIS Q 268                FE   FE2 G 414     1555   1555  2.62  
LINK         NE2 HIS D 268                FE   FE2 A 413     1555   1555  2.62  
LINK         OE2 GLU A 333                MN4  OEC A 412     1555   1555  2.63  
LINK         NE2 HIS A 332                MN1  OEC A 412     1555   1555  2.64  
LINK         OD1 ASP G 342                MN2  OEC G 413     1555   1555  2.64  
LINK         OD2 ASP A 170                MN4  OEC A 412     1555   1555  2.67  
LINK         OE2 GLU G 333                MN4  OEC G 413     1555   1555  2.69  
LINK         OD2 ASP G 170                MN4  OEC G 413     1555   1555  2.73  
LINK         NE2 HIS G 332                MN1  OEC G 413     1555   1555  2.77  
LINK         OD2 ASP A 342                MN2  OEC A 412     1555   1555  2.78  
LINK         OD1 ASN C  39                MG   CLA C 511     1555   1555  2.86  
LINK         OD1 ASN P  39                MG   CLA P 511     1555   1555  2.87  
LINK         OE1 GLU G 189                CA1  OEC G 413     1555   1555  2.91  
LINK         OE1 GLU A 189                CA1  OEC A 412     1555   1555  2.94  
LINK         OD1 ASP G 170                CA1  OEC G 413     1555   1555  3.01  
LINK         OD1 ASP A 170                CA1  OEC A 412     1555   1555  3.06  
LINK         OD2 ASP A 170                CA1  OEC A 412     1555   1555  3.13  
LINK         OD2 ASP G 170                CA1  OEC G 413     1555   1555  3.14  
LINK         OE1 GLU f 140                CA    CA f 301     1555   1555  3.17  
CISPEP   1 THR V   89    PRO V   90          0        -0.66                     
CISPEP   2 THR i   89    PRO i   90          0        -0.52                     
SITE     1 AC1 21 PHE A 119  TYR A 147  PRO A 150  SER A 153                    
SITE     2 AC1 21 VAL A 157  MET A 183  PHE A 186  GLN A 187                    
SITE     3 AC1 21 LEU A 193  HIS A 198  GLY A 201  VAL A 205                    
SITE     4 AC1 21 THR A 286  ILE A 290  CLA A 402  CLA A 403                    
SITE     5 AC1 21 PHO A 404  LEU D 182  LEU D 205  CLA D 401                    
SITE     6 AC1 21 PHE T  17                                                     
SITE     1 AC2 15 THR A  45  VAL A 157  PHE A 158  MET A 172                    
SITE     2 AC2 15 ILE A 176  THR A 179  PHE A 180  MET A 183                    
SITE     3 AC2 15 CLA A 401  PHO A 404  MET D 198  VAL D 201                    
SITE     4 AC2 15 GLY D 206  CLA D 401  PL9 D 404                               
SITE     1 AC3 15 GLN A 199  VAL A 202  ALA A 203  LEU A 210                    
SITE     2 AC3 15 TRP A 278  CLA A 401  DGD C 518  PHE D 157                    
SITE     3 AC3 15 VAL D 175  ILE D 178  PHE D 179  PHE D 181                    
SITE     4 AC3 15 LEU D 182  CLA D 401  PHO D 402                               
SITE     1 AC4 18 LEU A  41  ALA A  44  THR A  45  TYR A 126                    
SITE     2 AC4 18 GLN A 130  ALA A 146  TYR A 147  LEU A 174                    
SITE     3 AC4 18 VAL A 283  CLA A 401  CLA A 402  SQD A 414                    
SITE     4 AC4 18 LEU D 205  ALA D 208  LEU D 209  ILE D 213                    
SITE     5 AC4 18 TRP D 253  PHE D 257                                          
SITE     1 AC5 16 ILE A  36  PRO A  39  THR A  40  PHE A  93                    
SITE     2 AC5 16 PRO A  95  ILE A  96  TRP A  97  LEU A 114                    
SITE     3 AC5 16 HIS A 118  LEU A 121  DGD A 407  SQD A 414                    
SITE     4 AC5 16 TYR I   9  VAL I  12  BCR I 101  LMG I 102                    
SITE     1 AC6 16 PHE A 211  HIS A 215  LEU A 218  HIS A 252                    
SITE     2 AC6 16 PHE A 255  SER A 264  PHE A 265  LEU A 271                    
SITE     3 AC6 16 PHE A 274  PHE D  38  ALA D  41  TYR D  42                    
SITE     4 AC6 16 LEU D  45  ALA F  22  THR F  25  PL9 J 101                    
SITE     1 AC7 14 PHE A  93  PRO A  95  TRP A  97  GLU A  98                    
SITE     2 AC7 14 CLA A 405  LEU C 214  LYS C 215  SER C 216                    
SITE     3 AC7 14 PRO C 217  TRP C 223  PHE C 284  LYS I   5                    
SITE     4 AC7 14 TYR I   9  GLY O  38                                          
SITE     1 AC8 15 ARG A 140  TRP A 142  VAL A 145  PHE A 273                    
SITE     2 AC8 15 SQD A 409  TRP C  36  TRP C 443  ARG C 447                    
SITE     3 AC8 15 CLA C 504  CLA C 508  ASN D 220  ALA D 229                    
SITE     4 AC8 15 SER D 230  THR D 231  PHE D 232                               
SITE     1 AC9 14 ASN A 267  SER A 270  PHE A 273  PHE A 274                    
SITE     2 AC9 14 LHG A 408  LHG A 411  TRP C  36  CLA C 508                    
SITE     3 AC9 14 DGD C 517  DGD C 518  PHE D 232  ARG D 233                    
SITE     4 AC9 14 PL9 J 101  PHE K  37                                          
SITE     1 BC1 17 SER A 232  ASN A 234  TRP B   5  TYR B   6                    
SITE     2 BC1 17 CLA B 611  LMG B 622  TRP D 266  PHE D 273                    
SITE     3 BC1 17 GLU L  11  LEU L  12  ASN L  13  SER L  16                    
SITE     4 BC1 17 LEU L  19  GLY L  20  LEU L  22  ILE L  24                    
SITE     5 BC1 17 VAL L  26                                                     
SITE     1 BC2  8 TYR A 262  ASN A 266  SQD A 409  TRP C  35                    
SITE     2 BC2  8 DGD C 517  LMG E 102  BCR J 102  PHE K  45                    
SITE     1 BC3  8 ASP A 170  GLU A 189  HIS A 332  GLU A 333                    
SITE     2 BC3  8 HIS A 337  ASP A 342  ALA A 344  GLU C 354                    
SITE     1 BC4  5 HIS A 215  HIS A 272  HIS D 214  HIS D 268                    
SITE     2 BC4  5 BCT D 410                                                     
SITE     1 BC5 17 TRP A  20  ASN A  26  ARG A  27  LEU A  28                    
SITE     2 BC5 17 VAL A  30  ILE A  38  LEU A  41  LEU A  42                    
SITE     3 BC5 17 THR A  45  PHO A 404  CLA A 405  BCR I 101                    
SITE     4 BC5 17 TRP N 113  TYR N 117  CLA N 610  CLA N 620                    
SITE     5 BC5 17 BCR T 103                                                     
SITE     1 BC6  9 TRP B 185  PRO B 187  PHE B 190  ILE B 207                    
SITE     2 BC6  9 VAL B 208  CLA B 602  PHE H  41  ILE H  44                    
SITE     3 BC6  9 BCR H 101                                                     
SITE     1 BC7 18 GLU B 184  GLY B 189  GLY B 197  ALA B 200                    
SITE     2 BC7 18 HIS B 201  ALA B 204  ALA B 205  VAL B 208                    
SITE     3 BC7 18 PHE B 246  PHE B 247  CLA B 601  CLA B 603                    
SITE     4 BC7 18 DGD B 621  VAL D 154  PHE H  38  PHE H  41                    
SITE     5 BC7 18 ILE H  45  TYR H  49                                          
SITE     1 BC8 19 ARG B  68  LEU B  69  ALA B 146  LEU B 149                    
SITE     2 BC8 19 CYS B 150  PHE B 153  VAL B 198  HIS B 201                    
SITE     3 BC8 19 HIS B 202  PHE B 247  VAL B 252  THR B 262                    
SITE     4 BC8 19 CLA B 602  CLA B 604  CLA B 605  CLA B 606                    
SITE     5 BC8 19 CLA B 609  PHE H  38  LEU H  42                               
SITE     1 BC9 18 TRP B  33  PHE B  61  PHE B  65  ARG B  68                    
SITE     2 BC9 18 VAL B 245  ALA B 248  ALA B 249  VAL B 252                    
SITE     3 BC9 18 PHE B 451  HIS B 455  PHE B 458  PHE B 462                    
SITE     4 BC9 18 CLA B 603  CLA B 605  CLA B 607  CLA B 612                    
SITE     5 BC9 18 CLA B 613  CLA B 615                                          
SITE     1 CC1 20 THR B  27  VAL B  30  ALA B  31  TRP B  33                    
SITE     2 CC1 20 ALA B  34  VAL B  62  PHE B  65  MET B  66                    
SITE     3 CC1 20 ARG B  68  LEU B  69  HIS B 100  LEU B 103                    
SITE     4 CC1 20 GLY B 147  ALA B 205  CLA B 603  CLA B 604                    
SITE     5 CC1 20 CLA B 606  CLA B 610  CLA B 612  CLA B 615                    
SITE     1 CC2 17 LEU B  69  TRP B  91  ALA B  99  LEU B 103                    
SITE     2 CC2 17 LEU B 106  GLY B 152  PHE B 153  PHE B 156                    
SITE     3 CC2 17 HIS B 157  PHE B 162  PRO B 164  CLA B 603                    
SITE     4 CC2 17 CLA B 605  CLA B 616  BCR B 620  LMT B 625                    
SITE     5 CC2 17 SQD G 401                                                     
SITE     1 CC3 18 TRP B  33  MET B  37  TYR B  40  GLN B  58                    
SITE     2 CC3 18 GLY B  59  PHE B  61  GLY B 328  PRO B 329                    
SITE     3 CC3 18 TRP B 450  ALA B 454  CLA B 604  BCR B 617                    
SITE     4 CC3 18 BCR B 618  BCR B 619  LMG B 623  MET D 281                    
SITE     5 CC3 18 LEU L  27  PHE M  14                                          
SITE     1 CC4 17 THR B 236  SER B 239  ALA B 243  PHE B 246                    
SITE     2 CC4 17 PHE B 463  HIS B 466  LEU B 474  CLA B 609                    
SITE     3 CC4 17 CLA B 610  SQD B 624  PHE D 120  ILE D 123                    
SITE     4 CC4 17 MET D 126  LEU D 127  PHE D 130  CLA D 403                    
SITE     5 CC4 17 LEU H  43                                                     
SITE     1 CC5 17 PHE B 139  LEU B 143  VAL B 208  ALA B 212                    
SITE     2 CC5 17 PHE B 215  HIS B 216  PRO B 221  PRO B 222                    
SITE     3 CC5 17 LEU B 229  CLA B 603  CLA B 608  CLA B 610                    
SITE     4 CC5 17 THR H  27  MET H  31  PHE H  34  LEU H  46                    
SITE     5 CC5 17 BCR H 101                                                     
SITE     1 CC6 12 HIS B  23  PHE B 139  HIS B 142  LEU B 143                    
SITE     2 CC6 12 VAL B 237  SER B 240  CLA B 605  CLA B 608                    
SITE     3 CC6 12 CLA B 609  CLA B 612  CLA B 615  BCR H 101                    
SITE     1 CC7 18 LMG A 410  TRP B   5  TYR B   6  ARG B   7                    
SITE     2 CC7 18 VAL B   8  HIS B   9  LEU B 238  ILE B 242                    
SITE     3 CC7 18 PHE B 462  PHE B 464  GLY B 465  TRP B 468                    
SITE     4 CC7 18 HIS B 469  ARG B 472  CLA B 612  CLA B 613                    
SITE     5 CC7 18 CLA B 614  LMG B 622                                          
SITE     1 CC8 19 HIS B   9  LEU B  12  LEU B  19  ALA B  22                    
SITE     2 CC8 19 HIS B  23  HIS B  26  THR B  27  ILE B 234                    
SITE     3 CC8 19 VAL B 237  LEU B 238  SER B 241  VAL B 245                    
SITE     4 CC8 19 CLA B 604  CLA B 605  CLA B 610  CLA B 611                    
SITE     5 CC8 19 CLA B 613  CLA B 614  CLA B 615                               
SITE     1 CC9  8 HIS B   9  HIS B  26  VAL B  30  PHE B 462                    
SITE     2 CC9  8 CLA B 604  CLA B 611  CLA B 612  CLA B 614                    
SITE     1 DC1 11 VAL B   8  HIS B   9  TRP B 115  CLA B 611                    
SITE     2 DC1 11 CLA B 612  CLA B 613  BCR B 617  SQD B 627                    
SITE     3 DC1 11 VAL L  10  LMG e 102  PHE g   8                               
SITE     1 DC2 12 HIS B  23  MET B 138  ILE B 141  HIS B 142                    
SITE     2 DC2 12 LEU B 145  CLA B 604  CLA B 605  CLA B 610                    
SITE     3 DC2 12 CLA B 612  CLA B 616  LEU H  14  ASN H  15                    
SITE     1 DC3 10 ILE B  20  LEU B  24  TRP B 113  HIS B 114                    
SITE     2 DC3 10 LEU B 120  CLA B 606  CLA B 615  BCR B 620                    
SITE     3 DC3 10 SQD G 401  THR H   5                                          
SITE     1 DC4 15 ALA B  21  MET B  25  LEU B  29  TRP B 115                    
SITE     2 DC4 15 CLA B 607  CLA B 614  BCR B 618  BCR B 619                    
SITE     3 DC4 15 LMG B 623  SQD B 627  ILE M   9  ALA M  10                    
SITE     4 DC4 15 LEU M  13  LMT M 102  PHE g  19                               
SITE     1 DC5 14 TRP B  33  SER B  36  MET B  37  TYR B  40                    
SITE     2 DC5 14 CLA B 607  BCR B 617  BCR B 619  LMT B 629                    
SITE     3 DC5 14 LMG Q 407  ILE g   4  PHE g   8  ALA g  11                    
SITE     4 DC5 14 PHE g  17  PHE g  22                                          
SITE     1 DC6  9 LEU B  29  GLY B  32  TRP B  33  ILE B 101                    
SITE     2 DC6  9 GLY B 105  CLA B 607  BCR B 617  BCR B 618                    
SITE     3 DC6  9 DGD B 628                                                     
SITE     1 DC7  9 LEU B 109  CYS B 112  TRP B 113  TYR B 117                    
SITE     2 DC7  9 CLA B 606  CLA B 616  LMT B 625  SQD G 401                    
SITE     3 DC7  9 PHE g  22                                                     
SITE     1 DC8 14 TYR B 193  PHE B 250  TYR B 258  TYR B 273                    
SITE     2 DC8 14 SER B 277  PHE B 463  CLA B 602  HIS D  87                    
SITE     3 DC8 14 SER D 165  TYR H  49  ASN H  50  VAL H  60                    
SITE     4 DC8 14 SER H  61  TRP H  62                                          
SITE     1 DC9  9 LMG A 410  TRP B   5  TYR B   6  ARG B   7                    
SITE     2 DC9  9 PHE B 464  TRP B 468  CLA B 611  TYR D 141                    
SITE     3 DC9  9 PHE D 269                                                     
SITE     1 EC1 11 THR B 327  GLY B 328  PRO B 329  LYS B 332                    
SITE     2 EC1 11 PHE B 453  CLA B 607  BCR B 617  ILE D 284                    
SITE     3 EC1 11 PHE L  35  LEU M   6  LMT M 102                               
SITE     1 EC2 10 LYS B 227  ALA B 228  ARG B 230  LEU B 474                    
SITE     2 EC2 10 CLA B 608  LMT B 626  LYS D  23  TRP D  32                    
SITE     3 EC2 10 ARG D 134  LEU D 135                                          
SITE     1 EC3  5 TRP B  91  PHE B 162  CLA B 606  BCR B 620                    
SITE     2 EC3  5 DGD B 628                                                     
SITE     1 EC4  8 ARG B 224  LEU B 225  LYS B 227  SQD B 624                    
SITE     2 EC4  8 ASP D  16  ASP D  19  ALA H  32  MET H  35                    
SITE     1 EC5 13 ARG B  18  LEU B  29  SER B 104  TRP B 115                    
SITE     2 EC5 13 CLA B 614  BCR B 617  ASN L   4  ARG d  14                    
SITE     3 EC5 13 TYR d  18  TYR e  26  LMG e 102  PHE g  19                    
SITE     4 EC5 13 PHE g  23                                                     
SITE     1 EC6 10 TRP B  75  ASP B  87  GLY B  89  PHE B  90                    
SITE     2 EC6 10 TRP B  91  VAL B 102  BCR B 619  LMT B 625                    
SITE     3 EC6 10 LMT B 630  LMG a 102                                          
SITE     1 EC7  6 SER B  36  ALA B  43  THR B  44  BCR B 618                    
SITE     2 EC7  6 LEU G  72  VAL g   7                                          
SITE     1 EC8  7 GLY B  85  ASP B  87  DGD B 628  ALA G 100                    
SITE     2 EC8  7 BCR a 101  LMG a 102  LYS f  95                               
SITE     1 EC9 16 LEU C  95  LEU C 168  GLY C 171  ALA C 172                    
SITE     2 EC9 16 ILE C 224  VAL C 233  HIS C 237  ILE C 240                    
SITE     3 EC9 16 ALA C 278  MET C 282  VAL C 296  TYR C 297                    
SITE     4 EC9 16 CLA C 502  CLA C 503  CLA C 507  BCR C 515                    
SITE     1 FC1 16 TRP C  63  HIS C  91  TRP C  97  LEU C 174                    
SITE     2 FC1 16 LYS C 178  PHE C 182  LEU C 279  MET C 282                    
SITE     3 FC1 16 ALA C 286  TYR C 297  HIS C 430  LEU C 433                    
SITE     4 FC1 16 PHE C 437  CLA C 501  CLA C 503  CLA C 510                    
SITE     1 FC2 15 ILE C  60  VAL C  61  ALA C  64  THR C  68                    
SITE     2 FC2 15 LEU C  88  HIS C  91  VAL C 114  HIS C 118                    
SITE     3 FC2 15 MET C 282  CLA C 501  CLA C 502  CLA C 509                    
SITE     4 FC2 15 CLA C 510  CLA C 512  LMG C 520                               
SITE     1 FC3 17 PHE A 285  LHG A 408  TRP C  63  MET C  67                    
SITE     2 FC3 17 PHE C  70  GLN C  84  GLY C  85  ILE C  87                    
SITE     3 FC3 17 LEU C 404  TRP C 425  SER C 429  CLA C 508                    
SITE     4 FC3 17 CLA C 510  DGD C 517  DGD C 518  LMG C 519                    
SITE     5 FC3 17 PRO K  26                                                     
SITE     1 FC4 15 PHE A  33  MET A 127  TRP A 131  ILE C 265                    
SITE     2 FC4 15 TYR C 274  GLY C 277  ALA C 278  LEU C 438                    
SITE     3 FC4 15 HIS C 441  LEU C 442  ALA C 445  ARG C 449                    
SITE     4 FC4 15 CLA C 507  BCR C 515  PHE I  23                               
SITE     1 FC5 15 LEU C 161  LEU C 165  LEU C 213  ILE C 243                    
SITE     2 FC5 15 GLY C 247  TRP C 250  HIS C 251  THR C 255                    
SITE     3 FC5 15 PRO C 256  PHE C 257  TRP C 259  ALA C 260                    
SITE     4 FC5 15 PHE C 264  CLA C 507  BCR C 515                               
SITE     1 FC6 14 MET C 157  LEU C 161  HIS C 164  ILE C 240                    
SITE     2 FC6 14 PHE C 264  TRP C 266  TYR C 271  TYR C 274                    
SITE     3 FC6 14 SER C 275  CLA C 501  CLA C 505  CLA C 506                    
SITE     4 FC6 14 CLA C 509  BCR C 515                                          
SITE     1 FC7 18 LHG A 408  SQD A 409  TRP C  36  ALA C  37                    
SITE     2 FC7 18 ASN C  39  ALA C  40  GLU C 269  LEU C 276                    
SITE     3 FC7 18 PHE C 436  PHE C 437  GLY C 440  TRP C 443                    
SITE     4 FC7 18 HIS C 444  ARG C 447  CLA C 504  CLA C 509                    
SITE     5 FC7 18 CLA C 510  VAL K  30                                          
SITE     1 FC8 20 ASN C  39  LEU C  42  ILE C  43  LEU C  49                    
SITE     2 FC8 20 ALA C  52  HIS C  53  HIS C  56  TYR C 149                    
SITE     3 FC8 20 TRP C 151  GLY C 268  TYR C 271  LEU C 272                    
SITE     4 FC8 20 SER C 275  LEU C 279  CLA C 503  CLA C 507                    
SITE     5 FC8 20 CLA C 508  CLA C 510  CLA C 511  CLA C 512                    
SITE     1 FC9 13 ASN C  39  HIS C  56  LEU C  59  PHE C 436                    
SITE     2 FC9 13 PHE C 437  CLA C 502  CLA C 503  CLA C 504                    
SITE     3 FC9 13 CLA C 508  CLA C 509  PRO K  29  VAL K  30                    
SITE     4 FC9 13 LEU K  33                                                     
SITE     1 GC1 21 GLN C  28  TRP C  35  GLY C  38  ASN C  39                    
SITE     2 GC1 21 ARG C  41  LEU C  42  LYS C  48  ALA C  52                    
SITE     3 GC1 21 PHE C 127  ILE C 134  CLA C 509  BCR C 514                    
SITE     4 GC1 21 PHE K  32  LEU K  33  TRP K  39  GLN K  40                    
SITE     5 GC1 21 MET Z  19  VAL Z  20  PRO Z  24  ILE y  35                    
SITE     6 GC1 21 LEU y  46                                                     
SITE     1 GC2 14 LEU C  50  HIS C  53  ALA C  57  PHE C 147                    
SITE     2 GC2 14 PHE C 163  HIS C 164  VAL C 167  ILE C 170                    
SITE     3 GC2 14 GLY C 171  LEU C 174  CLA C 503  CLA C 509                    
SITE     4 GC2 14 CLA C 513  BCR Z 101                                          
SITE     1 GC3  9 VAL C  54  GLY C 128  TYR C 131  HIS C 132                    
SITE     2 GC3  9 PRO C 137  LEU C 140  PHE C 147  CLA C 512                    
SITE     3 GC3  9 BCR Z 101                                                     
SITE     1 GC4 14 ALA C  55  LEU C  59  VAL C 116  LEU C 119                    
SITE     2 GC4 14 ILE C 120  SER C 122  ALA C 123  CLA C 511                    
SITE     3 GC4 14 PHE K  18  PHE K  32  BCR K 101  LEU Z   9                    
SITE     4 GC4 14 VAL Z  13  BCR Z 101                                          
SITE     1 GC5 15 ILE C 209  PHE C 210  TYR C 212  LEU C 213                    
SITE     2 GC5 15 VAL C 227  ASP C 232  VAL C 233  ILE C 240                    
SITE     3 GC5 15 PHE C 264  CLA C 501  CLA C 505  CLA C 506                    
SITE     4 GC5 15 CLA C 507  VAL I  20  LEU I  24                               
SITE     1 GC6 14 PHE A 155  ILE A 163  PRO C 217  PHE C 218                    
SITE     2 GC6 14 GLY C 219  GLY C 220  GLY C 222  VAL C 225                    
SITE     3 GC6 14 CYS C 288  PHE C 292  ASN C 294  PRO C 307                    
SITE     4 GC6 14 PHE C 361  ARG C 362                                          
SITE     1 GC7 20 PHE A 197  THR A 292  SQD A 409  LHG A 411                    
SITE     2 GC7 20 TYR C  82  GLU C  83  GLN C  84  GLY C  85                    
SITE     3 GC7 20 LEU C 404  SER C 406  ASN C 418  VAL C 420                    
SITE     4 GC7 20 TRP C 425  THR C 428  SER C 429  CLA C 504                    
SITE     5 GC7 20 DGD C 518  LMG C 519  TYR J  33  BCR J 102                    
SITE     1 GC8 23 LEU A 200  TRP A 278  PHE A 300  ASN A 301                    
SITE     2 GC8 23 PHE A 302  SER A 305  CLA A 403  SQD A 409                    
SITE     3 GC8 23 ASN C 405  ASN C 415  SER C 416  ASN C 418                    
SITE     4 GC8 23 CLA C 504  DGD C 517  LMG D 406  PHE J  29                    
SITE     5 GC8 23 ALA J  32  TYR J  33  GLY J  37  SER J  38                    
SITE     6 GC8 23 SER J  39  BCR J 102  GLN V  60                               
SITE     1 GC9  7 HIS C  74  CLA C 504  DGD C 517  ASP K  23                    
SITE     2 GC9  7 VAL K  27  VAL K  30  ILE y  25                               
SITE     1 HC1  7 ASP C 107  PHE C 109  VAL C 114  VAL C 117                    
SITE     2 HC1  7 HIS C 118  CLA C 503  PHE Z  59                               
SITE     1 HC2 22 PHE A 206  CLA A 401  CLA A 402  CLA A 403                    
SITE     2 HC2 22 TRP D  48  LEU D 122  PRO D 149  VAL D 152                    
SITE     3 HC2 22 VAL D 156  LEU D 182  PHE D 185  GLN D 186                    
SITE     4 HC2 22 TRP D 191  THR D 192  HIS D 197  GLY D 200                    
SITE     5 HC2 22 VAL D 201  VAL D 204  LEU D 279  SER D 282                    
SITE     6 HC2 22 ALA D 283  PHO D 402                                          
SITE     1 HC3 20 PHE A 206  ALA A 209  LEU A 210  MET A 214                    
SITE     2 HC3 20 CLA A 403  ALA D  41  TRP D  48  ILE D 114                    
SITE     3 HC3 20 GLY D 118  LEU D 122  PHE D 125  ASN D 142                    
SITE     4 HC3 20 ALA D 145  PHE D 146  ALA D 148  PRO D 149                    
SITE     5 HC3 20 PHE D 153  PRO D 275  LEU D 279  CLA D 401                    
SITE     1 HC4 15 CLA B 608  PRO D  39  LEU D  43  LEU D  89                    
SITE     2 HC4 15 LEU D  90  LEU D  91  LEU D  92  TRP D  93                    
SITE     3 HC4 15 THR D 112  PHE D 113  HIS D 117  LMT D 409                    
SITE     4 HC4 15 GLY X  22  LEU X  23  GLY X  26                               
SITE     1 HC5 19 PHE A  52  ILE A  53  CLA A 402  MET D 199                    
SITE     2 HC5 19 ILE D 213  HIS D 214  THR D 217  TRP D 253                    
SITE     3 HC5 19 ALA D 260  PHE D 261  LEU D 267  PHE D 273                    
SITE     4 HC5 19 VAL D 274  THR D 277  LMG D 407  LEU L  23                    
SITE     5 HC5 19 VAL L  26  LEU L  29  PHE T  10                               
SITE     1 HC6 11 TYR D  42  GLY D  46  GLY D  47  LEU D  49                    
SITE     2 HC6 11 THR D  50  PHE D 101  LMG D 406  PRO F  29                    
SITE     3 HC6 11 PHE F  33  VAL J  21  VAL J  25                               
SITE     1 HC7 12 DGD C 518  TYR D  67  GLY D  70  CYS D  71                    
SITE     2 HC7 12 PHE D  73  BCR D 405  ILE F  37  GLN F  41                    
SITE     3 HC7 12 PHE J  28  GLY J  31  ALA J  32  GLY J  37                    
SITE     1 HC8 12 PHE D 257  ALA D 260  PHE D 261  SER D 262                    
SITE     2 HC8 12 ASN D 263  TRP D 266  PL9 D 404  THR L  15                    
SITE     3 HC8 12 TYR L  18  LEU L  19  ALA T  20  BCR T 102                    
SITE     1 HC9  6 ASP D 100  PHE D 101  LMT D 409  LEU E  42                    
SITE     2 HC9  6 ASP E  45  VAL E  46                                          
SITE     1 IC1  8 LEU D  92  TRP D  93  GLY D  99  CLA D 403                    
SITE     2 IC1  8 DGD D 408  ILE X  21  SER X  25  GLY X  26                    
SITE     1 IC2  9 HIS A 215  GLU A 244  TYR A 246  HIS A 272                    
SITE     2 IC2  9 FE2 A 413  HIS D 214  TYR D 244  LYS D 264                    
SITE     3 IC2  9 HIS D 268                                                     
SITE     1 IC3  2 GLU A 333  LYS D 317                                          
SITE     1 IC4  9 LEU A  72  LEU A 102  ASP A 103  ARG D 304                    
SITE     2 IC4  9 ALA N  43  TRP N  75  SER N  76  LEU N  98                    
SITE     3 IC4  9 GLY O 138                                                     
SITE     1 IC5 14 ARG E   8  PHE E  10  ILE E  13  ARG E  18                    
SITE     2 IC5 14 TYR E  19  HIS E  23  THR E  26  LEU E  30                    
SITE     3 IC5 14 ILE F  15  ARG F  19  TRP F  20  HIS F  24                    
SITE     4 IC5 14 ALA F  27  ILE F  31                                          
SITE     1 IC6  7 TYR A 262  LHG A 411  PHE D  27  PRO E   9                    
SITE     2 IC6  7 PHE E  10  SER E  11  PL9 J 101                               
SITE     1 IC7  7 TRP D  21  ARG D  26  GLU E   7  PHE F  16                    
SITE     2 IC7  7 THR F  17  VAL F  18  THR X  33                               
SITE     1 IC8  9 CLA B 601  CLA B 609  CLA B 610  MET H  35                    
SITE     2 IC8  9 LEU H  37  PHE H  38  PHE H  41  THR X  11                    
SITE     3 IC8  9 LEU X  16                                                     
SITE     1 IC9  9 VAL A  35  ILE A  38  LEU A  42  ALA A  43                    
SITE     2 IC9  9 TRP A 105  CLA A 405  SQD A 414  PHE I  15                    
SITE     3 IC9  9 LMT N 604                                                     
SITE     1 JC1  7 CLA A 405  MET I   1  THR I   3  LEU I   4                    
SITE     2 JC1  7 LMT I 103  DGD N 602  LMT N 604                               
SITE     1 JC2  6 THR I   3  ILE I   6  ILE I  10  VAL I  11                    
SITE     2 JC2  6 PHE I  14  LMG I 102                                          
SITE     1 JC3  4 PL9 A 406  SQD A 409  LMG E 102  VAL J  16                    
SITE     1 JC4  5 LHG A 411  DGD C 517  DGD C 518  PHE J  29                    
SITE     2 JC4  5 TYR J  33                                                     
SITE     1 JC5 15 BCR C 514  ALA J  14  THR J  15  GLY J  18                    
SITE     2 JC5 15 MET J  19  LEU K  21  LEU K  31  PHE K  37                    
SITE     3 JC5 15 VAL K  38  ALA K  41  SER Z  16  PHE Z  17                    
SITE     4 JC5 15 ILE y  28  GLY y  29  GLY y  32                               
SITE     1 JC6  7 GLU M  30  SER M  31  CLA N 618  PRO d   9                    
SITE     2 JC6  7 VAL d  10  LEU e  25  GLN e  32                               
SITE     1 JC7  6 TYR B  40  BCR B 617  LMG B 623  GLN M   5                    
SITE     2 JC7  6 MET e   1  MET g   1                                          
SITE     1 JC8  3 GLU O  81  GLU O 140  HIS O 257                               
SITE     1 JC9 14 ALA N  21  MET N  25  LEU N  29  TRP N 115                    
SITE     2 JC9 14 SQD N 601  CLA N 618  BCR N 621  LMG N 623                    
SITE     3 JC9 14 PHE T  19  BCR T 102  ILE e   9  ALA e  10                    
SITE     4 JC9 14 LEU e  13  LMT e 101                                          
SITE     1 KC1 15 LMG D 407  TRP N  33  SER N  36  MET N  37                    
SITE     2 KC1 15 LMT N 603  CLA N 611  BCR N 621  ILE T   4                    
SITE     3 KC1 15 PHE T   8  ALA T  11  PHE T  17  PHE T  18                    
SITE     4 KC1 15 ILE T  21  PHE T  22  BCR T 101                               
SITE     1 KC2  8 SQD A 414  LEU N 106  LEU N 109  CYS N 112                    
SITE     2 KC2  8 TYR N 117  CLA N 610  CLA N 620  PHE T  22                    
SITE     1 KC3 14 ALA V  62  CYS V  63  HIS V  67  THR V  74                    
SITE     2 KC3 14 LEU V  78  ASP V  79  THR V  84  LEU V  85                    
SITE     3 KC3 14 LEU V  98  TYR V 101  MET V 102  TYR V 108                    
SITE     4 KC3 14 HIS V 118  PRO V 119                                          
SITE     1 KC4 11 PHE C 112  VAL C 116  SER C 121  VAL C 124                    
SITE     2 KC4 11 CLA C 512  CLA C 513  BCR C 514  TYR K  15                    
SITE     3 KC4 11 VAL Z  54  GLY Z  55  ASN Z  58                               
SITE     1 KC5 17 TRP B 113  TYR B 117  CLA B 606  CLA B 616                    
SITE     2 KC5 17 BCR B 620  TRP G  20  ASN G  26  ARG G  27                    
SITE     3 KC5 17 LEU G  28  VAL G  30  ILE G  38  LEU G  41                    
SITE     4 KC5 17 LEU G  42  THR G  45  PHO G 405  CLA G 406                    
SITE     5 KC5 17 BCR a 101                                                     
SITE     1 KC6 20 PHE G 119  TYR G 147  PRO G 150  SER G 153                    
SITE     2 KC6 20 VAL G 157  MET G 183  PHE G 186  GLN G 187                    
SITE     3 KC6 20 LEU G 193  HIS G 198  VAL G 205  THR G 286                    
SITE     4 KC6 20 ILE G 290  CLA G 403  CLA G 404  PHO G 405                    
SITE     5 KC6 20 LEU Q 182  LEU Q 205  CLA Q 402  PHE g  17                    
SITE     1 KC7 14 THR G  45  VAL G 157  PHE G 158  MET G 172                    
SITE     2 KC7 14 ILE G 176  THR G 179  MET G 183  CLA G 402                    
SITE     3 KC7 14 PHO G 405  MET Q 198  VAL Q 201  GLY Q 206                    
SITE     4 KC7 14 CLA Q 402  PL9 Q 405                                          
SITE     1 KC8 16 GLN G 199  VAL G 202  ALA G 203  LEU G 210                    
SITE     2 KC8 16 TRP G 278  CLA G 402  DGD P 519  PHE Q 157                    
SITE     3 KC8 16 VAL Q 175  ILE Q 178  PHE Q 179  PHE Q 181                    
SITE     4 KC8 16 LEU Q 182  CLA Q 402  PHO Q 403  PL9 b 101                    
SITE     1 KC9 19 ALA G  44  THR G  45  ILE G 115  TYR G 126                    
SITE     2 KC9 19 GLN G 130  ALA G 146  TYR G 147  PRO G 150                    
SITE     3 KC9 19 LEU G 174  VAL G 283  SQD G 401  CLA G 402                    
SITE     4 KC9 19 CLA G 403  LEU Q 205  ALA Q 208  LEU Q 209                    
SITE     5 KC9 19 ILE Q 213  TRP Q 253  PHE Q 257                               
SITE     1 LC1 15 ILE G  36  PRO G  39  THR G  40  PHE G  93                    
SITE     2 LC1 15 PRO G  95  ILE G  96  TRP G  97  LEU G 114                    
SITE     3 LC1 15 HIS G 118  LEU G 121  SQD G 401  DGD G 408                    
SITE     4 LC1 15 TYR a   9  VAL a  12  LMG a 102                               
SITE     1 LC2 16 PHE G 211  HIS G 215  LEU G 218  HIS G 252                    
SITE     2 LC2 16 PHE G 255  SER G 264  PHE G 265  LEU G 271                    
SITE     3 LC2 16 PHE G 274  PHE Q  38  ALA Q  41  TYR Q  42                    
SITE     4 LC2 16 LEU Q  45  ALA S  22  THR S  25  PL9 b 101                    
SITE     1 LC3 14 PHE G  93  PRO G  95  TRP G  97  GLU G  98                    
SITE     2 LC3 14 CLA G 406  LEU P 214  LYS P 215  SER P 216                    
SITE     3 LC3 14 PRO P 217  TRP P 223  PHE P 284  LYS a   5                    
SITE     4 LC3 14 TYR a   9  GLY f  38                                          
SITE     1 LC4 14 ARG G 140  TRP G 142  PHE G 273  SQD G 410                    
SITE     2 LC4 14 TRP P  36  ARG P 447  CLA P 504  CLA P 508                    
SITE     3 LC4 14 CLA P 510  ASN Q 220  ALA Q 229  SER Q 230                    
SITE     4 LC4 14 THR Q 231  PHE Q 232                                          
SITE     1 LC5 13 ASN G 267  SER G 270  PHE G 273  PHE G 274                    
SITE     2 LC5 13 LHG G 409  LHG G 412  TRP P  36  CLA P 508                    
SITE     3 LC5 13 DGD P 518  DGD P 519  ARG Q 233  PL9 b 101                    
SITE     4 LC5 13 PHE c  37                                                     
SITE     1 LC6 17 SER G 232  ASN G 234  TRP N   5  TYR N   6                    
SITE     2 LC6 17 CLA N 615  LMG N 622  TRP Q 266  PHE Q 270                    
SITE     3 LC6 17 PHE Q 273  PL9 Q 405  GLU d  11  LEU d  12                    
SITE     4 LC6 17 ASN d  13  SER d  16  GLY d  20  ILE d  24                    
SITE     5 LC6 17 VAL d  26                                                     
SITE     1 LC7  8 TYR G 262  ASN G 266  SQD G 410  TRP P  35                    
SITE     2 LC7  8 DGD P 518  LMG R 102  BCR b 102  PHE c  45                    
SITE     1 LC8  7 ASP G 170  GLU G 189  HIS G 332  GLU G 333                    
SITE     2 LC8  7 ASP G 342  ALA G 344  GLU P 354                               
SITE     1 LC9  5 HIS G 215  HIS G 272  HIS Q 214  HIS Q 268                    
SITE     2 LC9  5 BCT Q 411                                                     
SITE     1 MC1  2 GLU G 333  LYS Q 317                                          
SITE     1 MC2 12 ARG L  14  TYR L  18  TYR M  26  ARG N  18                    
SITE     2 MC2 12 LEU N  29  SER N 104  TRP N 115  CLA N 618                    
SITE     3 MC2 12 PHE T  19  PHE T  23  BCR T 101  ASN d   4                    
SITE     1 MC3 10 LMG I 102  TRP N  75  ASP N  87  GLY N  89                    
SITE     2 MC3 10 PHE N  90  TRP N  91  LEU N  98  VAL N 102                    
SITE     3 MC3 10 LMT N 604  LMT N 624                                          
SITE     1 MC4  7 LEU A  72  SER N  36  ALA N  43  LEU N 437                    
SITE     2 MC4  7 ILE T   4  VAL T   7  BCR T 102                               
SITE     1 MC5  7 ALA A 100  BCR I 101  LMG I 102  GLY N  85                    
SITE     2 MC5  7 ASP N  87  DGD N 602  LYS O  95                               
SITE     1 MC6  8 TRP N 185  PHE N 190  ILE N 207  VAL N 208                    
SITE     2 MC6  8 CLA N 606  PHE W  41  ILE W  44  BCR W 101                    
SITE     1 MC7 18 GLU N 184  GLY N 189  GLY N 197  ALA N 200                    
SITE     2 MC7 18 HIS N 201  ALA N 204  ALA N 205  VAL N 208                    
SITE     3 MC7 18 PHE N 246  PHE N 247  CLA N 605  CLA N 607                    
SITE     4 MC7 18 VAL Q 154  PHE W  38  PHE W  41  ILE W  45                    
SITE     5 MC7 18 TYR W  49  DGD W 102                                          
SITE     1 MC8 20 ARG N  68  LEU N  69  ALA N 146  LEU N 149                    
SITE     2 MC8 20 CYS N 150  PHE N 153  VAL N 198  HIS N 201                    
SITE     3 MC8 20 HIS N 202  PHE N 247  ALA N 248  VAL N 252                    
SITE     4 MC8 20 THR N 262  CLA N 606  CLA N 608  CLA N 609                    
SITE     5 MC8 20 CLA N 610  CLA N 613  PHE W  38  LEU W  42                    
SITE     1 MC9 19 TRP N  33  PHE N  61  PHE N  65  ARG N  68                    
SITE     2 MC9 19 VAL N 245  ALA N 248  ALA N 249  VAL N 252                    
SITE     3 MC9 19 PHE N 451  HIS N 455  PHE N 458  PHE N 462                    
SITE     4 MC9 19 CLA N 607  CLA N 609  CLA N 611  CLA N 615                    
SITE     5 MC9 19 CLA N 616  CLA N 617  CLA N 619                               
SITE     1 NC1 20 THR N  27  VAL N  30  ALA N  31  TRP N  33                    
SITE     2 NC1 20 ALA N  34  VAL N  62  PHE N  65  MET N  66                    
SITE     3 NC1 20 ARG N  68  LEU N  69  HIS N 100  LEU N 103                    
SITE     4 NC1 20 GLY N 147  ALA N 205  CLA N 607  CLA N 608                    
SITE     5 NC1 20 CLA N 610  CLA N 614  CLA N 616  CLA N 619                    
SITE     1 NC2 17 SQD A 414  LEU N  69  TRP N  91  ALA N  99                    
SITE     2 NC2 17 LEU N 103  LEU N 106  GLY N 152  PHE N 153                    
SITE     3 NC2 17 PHE N 156  HIS N 157  PHE N 162  PRO N 164                    
SITE     4 NC2 17 CLA N 607  CLA N 609  CLA N 620  LMT N 624                    
SITE     5 NC2 17 BCR T 103                                                     
SITE     1 NC3 16 TRP N  33  MET N  37  TYR N  40  GLN N  58                    
SITE     2 NC3 16 GLY N  59  PHE N  61  GLY N 328  PRO N 329                    
SITE     3 NC3 16 TRP N 450  ALA N 454  CLA N 608  BCR N 621                    
SITE     4 NC3 16 LMG N 623  MET Q 281  BCR T 102  PHE e  14                    
SITE     1 NC4 15 THR N 236  SER N 239  SER N 240  ALA N 243                    
SITE     2 NC4 15 PHE N 246  PHE N 463  HIS N 466  LEU N 474                    
SITE     3 NC4 15 CLA N 613  CLA N 614  PHE Q 120  ILE Q 123                    
SITE     4 NC4 15 MET Q 126  LEU Q 127  PHE Q 130                               
SITE     1 NC5 16 PHE N 139  LEU N 143  ALA N 212  PHE N 215                    
SITE     2 NC5 16 HIS N 216  ARG N 220  PRO N 221  PRO N 222                    
SITE     3 NC5 16 LEU N 229  CLA N 607  CLA N 612  CLA N 614                    
SITE     4 NC5 16 THR W  27  MET W  31  PHE W  34  BCR W 101                    
SITE     1 NC6 11 PHE N 139  HIS N 142  LEU N 143  THR N 236                    
SITE     2 NC6 11 VAL N 237  SER N 240  CLA N 609  CLA N 612                    
SITE     3 NC6 11 CLA N 613  CLA N 616  CLA N 619                               
SITE     1 NC7 20 LMG G 411  TRP N   5  TYR N   6  ARG N   7                    
SITE     2 NC7 20 VAL N   8  HIS N   9  LEU N 238  ILE N 242                    
SITE     3 NC7 20 LEU N 461  PHE N 462  PHE N 464  GLY N 465                    
SITE     4 NC7 20 TRP N 468  HIS N 469  ARG N 472  CLA N 608                    
SITE     5 NC7 20 CLA N 616  CLA N 617  CLA N 618  LMG N 622                    
SITE     1 NC8 19 HIS N   9  LEU N  12  LEU N  19  ALA N  22                    
SITE     2 NC8 19 HIS N  23  HIS N  26  THR N  27  ILE N 234                    
SITE     3 NC8 19 VAL N 237  LEU N 238  SER N 241  VAL N 245                    
SITE     4 NC8 19 CLA N 608  CLA N 609  CLA N 614  CLA N 615                    
SITE     5 NC8 19 CLA N 617  CLA N 618  CLA N 619                               
SITE     1 NC9  9 HIS N   9  HIS N  26  VAL N  30  LEU N 461                    
SITE     2 NC9  9 PHE N 462  CLA N 608  CLA N 615  CLA N 616                    
SITE     3 NC9  9 CLA N 618                                                     
SITE     1 OC1 12 LMG M 101  VAL N   8  HIS N   9  ALA N  22                    
SITE     2 OC1 12 TRP N 115  SQD N 601  CLA N 615  CLA N 616                    
SITE     3 OC1 12 CLA N 617  PHE T   8  BCR T 101  VAL d  10                    
SITE     1 OC2 10 MET N 138  ILE N 141  HIS N 142  LEU N 145                    
SITE     2 OC2 10 CLA N 608  CLA N 609  CLA N 614  CLA N 616                    
SITE     3 OC2 10 CLA N 620  LEU W  14                                          
SITE     1 OC3 11 SQD A 414  ILE N  20  LEU N  24  ALA N 110                    
SITE     2 OC3 11 TRP N 113  HIS N 114  LEU N 120  CLA N 610                    
SITE     3 OC3 11 CLA N 619  BCR T 103  THR W   5                               
SITE     1 OC4  8 LEU N  29  GLY N  32  TRP N  33  SER N  36                    
SITE     2 OC4  8 ILE N 101  CLA N 611  BCR T 101  BCR T 102                    
SITE     1 OC5  9 LMG G 411  TRP N   5  TYR N   6  ARG N   7                    
SITE     2 OC5  9 PHE N 464  TRP N 468  CLA N 615  TYR Q 141                    
SITE     3 OC5  9 PHE Q 269                                                     
SITE     1 OC6 11 THR N 327  GLY N 328  PRO N 329  LYS N 332                    
SITE     2 OC6 11 PHE N 453  CLA N 611  ILE Q 284  BCR T 101                    
SITE     3 OC6 11 PHE d  35  LEU e   6  LMT e 101                               
SITE     1 OC7  4 TRP N  91  PHE N 162  DGD N 602  CLA N 610                    
SITE     1 OC8  8 ARG N 224  LEU N 225  LYS N 227  ASP Q  16                    
SITE     2 OC8  8 ASP Q  19  SQD Q 408  ALA W  32  MET W  35                    
SITE     1 OC9 15 LEU P  95  LEU P 168  GLY P 171  ALA P 172                    
SITE     2 OC9 15 ILE P 224  VAL P 233  HIS P 237  ILE P 240                    
SITE     3 OC9 15 MET P 282  VAL P 296  TYR P 297  CLA P 502                    
SITE     4 OC9 15 CLA P 503  CLA P 507  BCR P 516                               
SITE     1 PC1 14 TRP P  63  HIS P  91  TRP P  97  LEU P 174                    
SITE     2 PC1 14 LYS P 178  LEU P 279  MET P 282  ALA P 286                    
SITE     3 PC1 14 TYR P 297  HIS P 430  LEU P 433  PHE P 437                    
SITE     4 PC1 14 CLA P 501  CLA P 503                                          
SITE     1 PC2 13 ILE P  60  VAL P  61  ALA P  64  THR P  68                    
SITE     2 PC2 13 LEU P  88  HIS P  91  VAL P 114  HIS P 118                    
SITE     3 PC2 13 CLA P 501  CLA P 502  CLA P 510  CLA P 512                    
SITE     4 PC2 13 LMG P 521                                                     
SITE     1 PC3 18 PHE G 285  LHG G 409  TRP P  63  MET P  67                    
SITE     2 PC3 18 PHE P  70  GLN P  84  GLY P  85  ILE P  87                    
SITE     3 PC3 18 LEU P 404  TRP P 425  SER P 429  CLA P 508                    
SITE     4 PC3 18 CLA P 510  DGD P 518  DGD P 519  LMG P 520                    
SITE     5 PC3 18 PRO c  26  VAL c  30                                          
SITE     1 PC4 16 PHE G  33  MET G 127  TRP G 131  PHE P 264                    
SITE     2 PC4 16 ILE P 265  TYR P 274  GLY P 277  ALA P 278                    
SITE     3 PC4 16 MET P 281  HIS P 441  LEU P 442  ALA P 445                    
SITE     4 PC4 16 ARG P 449  CLA P 507  BCR P 516  PHE a  23                    
SITE     1 PC5 14 LEU P 161  LEU P 165  LEU P 213  ILE P 243                    
SITE     2 PC5 14 GLY P 247  TRP P 250  HIS P 251  THR P 255                    
SITE     3 PC5 14 PRO P 256  PHE P 257  TRP P 259  ALA P 260                    
SITE     4 PC5 14 PHE P 264  CLA P 507                                          
SITE     1 PC6 13 MET P 157  LEU P 161  HIS P 164  PHE P 264                    
SITE     2 PC6 13 TRP P 266  TYR P 271  TYR P 274  SER P 275                    
SITE     3 PC6 13 CLA P 501  CLA P 505  CLA P 506  CLA P 509                    
SITE     4 PC6 13 BCR P 516                                                     
SITE     1 PC7 19 LHG G 409  SQD G 410  TRP P  36  ALA P  37                    
SITE     2 PC7 19 ASN P  39  ALA P  40  GLU P 269  LEU P 272                    
SITE     3 PC7 19 LEU P 276  PHE P 436  PHE P 437  GLY P 440                    
SITE     4 PC7 19 TRP P 443  HIS P 444  ARG P 447  CLA P 504                    
SITE     5 PC7 19 CLA P 509  CLA P 510  VAL c  30                               
SITE     1 PC8 19 ASN P  39  LEU P  42  ILE P  43  LEU P  49                    
SITE     2 PC8 19 ALA P  52  HIS P  53  HIS P  56  TYR P 149                    
SITE     3 PC8 19 TRP P 151  GLY P 268  TYR P 271  LEU P 272                    
SITE     4 PC8 19 SER P 275  LEU P 279  CLA P 507  CLA P 508                    
SITE     5 PC8 19 CLA P 510  CLA P 511  CLA P 512                               
SITE     1 PC9 14 LHG G 409  ASN P  39  HIS P  56  LEU P  59                    
SITE     2 PC9 14 LEU P 279  PHE P 436  PHE P 437  CLA P 503                    
SITE     3 PC9 14 CLA P 504  CLA P 508  CLA P 509  CLA P 511                    
SITE     4 PC9 14 PRO c  29  LEU c  33                                          
SITE     1 QC1 23 GLN P  28  TRP P  35  GLY P  38  ASN P  39                    
SITE     2 QC1 23 ARG P  41  LEU P  42  LYS P  48  ALA P  52                    
SITE     3 QC1 23 PHE P 127  ILE P 134  CLA P 509  CLA P 510                    
SITE     4 QC1 23 BCR P 514  PHE c  32  LEU c  33  TRP c  39                    
SITE     5 QC1 23 GLN c  40  MET l  19  VAL l  20  PRO l  24                    
SITE     6 QC1 23 ILE m  35  ASN m  45  LEU m  46                               
SITE     1 QC2 14 LEU P  50  HIS P  53  ALA P  57  PHE P 147                    
SITE     2 QC2 14 PHE P 163  HIS P 164  VAL P 167  ILE P 170                    
SITE     3 QC2 14 LEU P 174  CLA P 503  CLA P 509  CLA P 513                    
SITE     4 QC2 14 BCR P 515  LMG P 521                                          
SITE     1 QC3 12 LEU P  50  VAL P  54  GLY P 128  TYR P 131                    
SITE     2 QC3 12 HIS P 132  PRO P 137  LEU P 140  TYR P 143                    
SITE     3 QC3 12 PHE P 147  ILE P 170  CLA P 512  BCR P 515                    
SITE     1 QC4 13 ALA P  55  LEU P  59  VAL P 116  LEU P 119                    
SITE     2 QC4 13 ILE P 120  SER P 122  ALA P 123  CLA P 511                    
SITE     3 QC4 13 BCR P 515  PHE c  32  BCR c 101  LEU l   9                    
SITE     4 QC4 13 VAL l  13                                                     
SITE     1 QC5 10 VAL P 116  SER P 121  VAL P 124  CLA P 512                    
SITE     2 QC5 10 CLA P 513  BCR P 514  TYR c  15  VAL l  54                    
SITE     3 QC5 10 GLY l  55  ASN l  58                                          
SITE     1 QC6 12 ILE P 209  TYR P 212  LEU P 213  VAL P 227                    
SITE     2 QC6 12 ASP P 232  VAL P 233  ILE P 240  PHE P 264                    
SITE     3 QC6 12 CLA P 501  CLA P 505  CLA P 507  VAL a  20                    
SITE     1 QC7 16 LEU G 151  PHE G 155  ILE G 163  PRO P 217                    
SITE     2 QC7 16 PHE P 218  GLY P 219  GLY P 220  GLY P 222                    
SITE     3 QC7 16 VAL P 225  PHE P 284  CYS P 288  PHE P 292                    
SITE     4 QC7 16 ASN P 294  PRO P 307  PHE P 361  ARG P 362                    
SITE     1 QC8 20 PHE G 197  THR G 292  SQD G 410  LHG G 412                    
SITE     2 QC8 20 TYR P  82  GLU P  83  GLN P  84  GLY P  85                    
SITE     3 QC8 20 LEU P 404  SER P 406  ASN P 418  VAL P 420                    
SITE     4 QC8 20 TRP P 425  THR P 428  SER P 429  CLA P 504                    
SITE     5 QC8 20 DGD P 519  LMG P 520  TYR b  33  BCR b 102                    
SITE     1 QC9 23 LEU G 200  TRP G 278  PHE G 300  ASN G 301                    
SITE     2 QC9 23 PHE G 302  SER G 305  CLA G 404  SQD G 410                    
SITE     3 QC9 23 ASN P 405  ASN P 415  SER P 416  ASN P 418                    
SITE     4 QC9 23 CLA P 504  DGD P 518  LMG Q 406  PHE b  29                    
SITE     5 QC9 23 ALA b  32  TYR b  33  GLY b  37  SER b  38                    
SITE     6 QC9 23 SER b  39  BCR b 102  GLN i  60                               
SITE     1 RC1  8 HIS P  74  CLA P 504  DGD P 518  BCR b 102                    
SITE     2 RC1  8 ASP c  23  VAL c  27  VAL c  30  ILE m  25                    
SITE     1 RC2  8 ASP P 107  PHE P 109  VAL P 114  VAL P 117                    
SITE     2 RC2  8 HIS P 118  CLA P 503  CLA P 512  PHE l  59                    
SITE     1 RC3  9 ALA B  43  TRP B  75  SER B  76  TRP B  78                    
SITE     2 RC3  9 LEU B  98  LEU G 102  ASP G 103  ARG Q 304                    
SITE     3 RC3  9 GLY f 138                                                     
SITE     1 RC4 22 PHE G 206  CLA G 402  CLA G 403  CLA G 404                    
SITE     2 RC4 22 TRP Q  48  PRO Q 149  VAL Q 152  PHE Q 153                    
SITE     3 RC4 22 VAL Q 156  LEU Q 182  PHE Q 185  GLN Q 186                    
SITE     4 RC4 22 TRP Q 191  THR Q 192  HIS Q 197  GLY Q 200                    
SITE     5 RC4 22 VAL Q 201  VAL Q 204  LEU Q 279  SER Q 282                    
SITE     6 RC4 22 ALA Q 283  PHO Q 403                                          
SITE     1 RC5 18 PHE G 206  ALA G 209  LEU G 210  MET G 214                    
SITE     2 RC5 18 CLA G 404  ALA Q  41  TRP Q  48  GLY Q 118                    
SITE     3 RC5 18 LEU Q 122  PHE Q 125  ASN Q 142  ALA Q 145                    
SITE     4 RC5 18 PHE Q 146  ALA Q 148  PHE Q 153  PRO Q 275                    
SITE     5 RC5 18 LEU Q 279  CLA Q 402                                          
SITE     1 RC6 14 LEU Q  43  LEU Q  89  LEU Q  90  LEU Q  91                    
SITE     2 RC6 14 LEU Q  92  TRP Q  93  TRP Q 104  THR Q 112                    
SITE     3 RC6 14 PHE Q 113  HIS Q 117  LMT Q 410  GLY j  22                    
SITE     4 RC6 14 LEU j  23  GLY j  26                                          
SITE     1 RC7 20 ILE G  53  ILE G  77  CLA G 403  LMG G 411                    
SITE     2 RC7 20 MET Q 199  HIS Q 214  THR Q 217  TRP Q 253                    
SITE     3 RC7 20 ALA Q 260  PHE Q 261  LEU Q 267  PHE Q 273                    
SITE     4 RC7 20 VAL Q 274  THR Q 277  LMG Q 407  LEU d  23                    
SITE     5 RC7 20 VAL d  26  LEU d  27  LEU d  29  PHE g  10                    
SITE     1 RC8 11 DGD P 519  TYR Q  67  GLY Q  70  PHE Q  73                    
SITE     2 RC8 11 ILE S  37  GLN S  41  BCR S 101  PHE b  28                    
SITE     3 RC8 11 GLY b  31  ALA b  32  GLY b  37                               
SITE     1 RC9 14 BCR B 618  PHE Q 257  ALA Q 260  PHE Q 261                    
SITE     2 RC9 14 SER Q 262  ASN Q 263  TRP Q 266  PL9 Q 405                    
SITE     3 RC9 14 THR d  15  TYR d  18  LEU d  19  PHE g  10                    
SITE     4 RC9 14 PHE g  17  ALA g  20                                          
SITE     1 SC1  8 ALA N 228  ARG N 230  LEU N 474  LMT N 625                    
SITE     2 SC1  8 LYS Q  23  TRP Q  32  ARG Q 134  LEU Q 135                    
SITE     1 SC2  6 ASP Q 100  PHE Q 101  LMT Q 410  LEU R  42                    
SITE     2 SC2  6 ASP R  45  VAL R  46                                          
SITE     1 SC3  8 LEU Q  92  TRP Q  93  GLY Q  99  CLA Q 404                    
SITE     2 SC3  8 DGD Q 409  ILE j  21  SER j  25  GLY j  26                    
SITE     1 SC4  9 HIS G 215  GLU G 244  TYR G 246  HIS G 272                    
SITE     2 SC4  9 FE2 G 414  HIS Q 214  TYR Q 244  LYS Q 264                    
SITE     3 SC4  9 HIS Q 268                                                     
SITE     1 SC5 14 ARG R   8  PHE R  10  ILE R  13  ARG R  18                    
SITE     2 SC5 14 TYR R  19  HIS R  23  THR R  26  LEU R  30                    
SITE     3 SC5 14 ILE S  15  ARG S  19  TRP S  20  HIS S  24                    
SITE     4 SC5 14 ALA S  27  ILE S  31                                          
SITE     1 SC6  7 TYR G 262  LHG G 412  PHE Q  27  PRO R   9                    
SITE     2 SC6  7 PHE R  10  SER R  11  PL9 b 101                               
SITE     1 SC7 11 TYR Q  42  GLY Q  46  GLY Q  47  LEU Q  49                    
SITE     2 SC7 11 THR Q  50  PHE Q 101  LMG Q 406  PRO S  29                    
SITE     3 SC7 11 PHE S  33  VAL b  21  VAL b  25                               
SITE     1 SC8  8 ARG Q  24  ARG Q  26  GLU R   7  PHE S  16                    
SITE     2 SC8  8 THR S  17  VAL S  18  LEU j  32  THR j  33                    
SITE     1 SC9  9 CLA N 605  CLA N 613  MET W  35  LEU W  37                    
SITE     2 SC9  9 PHE W  38  PHE W  41  THR j  11  ILE j  12                    
SITE     3 SC9  9 LEU j  16                                                     
SITE     1 TC1 14 TYR N 193  PHE N 250  TYR N 258  TYR N 273                    
SITE     2 TC1 14 SER N 277  PHE N 463  CLA N 606  HIS Q  87                    
SITE     3 TC1 14 SER Q 165  TYR W  49  ASN W  50  VAL W  60                    
SITE     4 TC1 14 SER W  61  TRP W  62                                          
SITE     1 TC2  7 LMT B 630  ILE G  38  LEU G  42  ALA G  43                    
SITE     2 TC2  7 TRP G 105  SQD G 401  PHE a  15                               
SITE     1 TC3  7 DGD B 628  LMT B 630  CLA G 406  MET a   1                    
SITE     2 TC3  7 THR a   3  LEU a   4  LMT a 103                               
SITE     1 TC4  4 THR a   3  ILE a   6  ILE a  10  LMG a 102                    
SITE     1 TC5  6 CLA G 404  PL9 G 407  SQD G 410  LMG R 102                    
SITE     2 TC5  6 VAL b  16  GLY b  20                                          
SITE     1 TC6  6 LHG G 412  DGD P 518  DGD P 519  LMG P 520                    
SITE     2 TC6  6 PHE b  29  TYR b  33                                          
SITE     1 TC7 16 BCR P 514  ALA b  14  THR b  15  GLY b  18                    
SITE     2 TC7 16 MET b  19  LEU c  21  LEU c  31  PHE c  32                    
SITE     3 TC7 16 PHE c  37  VAL c  38  ALA c  41  SER l  16                    
SITE     4 TC7 16 PHE l  17  ILE m  28  GLY m  29  GLY m  32                    
SITE     1 TC8  5 MET M   1  TYR N  40  LMG N 623  BCR T 101                    
SITE     2 TC8  5 GLN e   5                                                     
SITE     1 TC9  7 CLA B 614  SQD B 627  PRO L   9  VAL L  10                    
SITE     2 TC9  7 GLN M  32  GLU e  30  SER e  31                               
SITE     1 UC1  3 GLU f  81  GLU f 140  HIS f 257                               
SITE     1 UC2 13 ALA i  62  CYS i  63  HIS i  67  THR i  74                    
SITE     2 UC2 13 LEU i  78  ASP i  79  THR i  84  LEU i  85                    
SITE     3 UC2 13 TYR i 101  MET i 102  TYR i 108  HIS i 118                    
SITE     4 UC2 13 PRO i 119                                                     
CRYST1  130.783  227.764  308.630  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      0.007646  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004391  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003240        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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