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Database: PDB
Entry: 4RVY
LinkDB: 4RVY
Original site: 4RVY 
HEADER    OXIDOREDUCTASE                          29-NOV-14   4RVY              
TITLE     SERIAL TIME RESOLVED CRYSTALLOGRAPHY OF PHOTOSYSTEM II USING A        
TITLE    2 FEMTOSECOND X-RAY LASER. THE S STATE AFTER TWO FLASHES (S3)          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOTOSYSTEM II PROTEIN D1 1;                               
COMPND   3 CHAIN: A, a;                                                         
COMPND   4 SYNONYM: 32 KDA THYLAKOID MEMBRANE PROTEIN 1, PHOTOSYSTEM II Q(B)    
COMPND   5 PROTEIN 1;                                                           
COMPND   6 EC: 1.10.3.9;                                                        
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PHOTOSYSTEM II CP47 REACTION CENTER PROTEIN;               
COMPND   9 CHAIN: B, b;                                                         
COMPND  10 SYNONYM: PSII 47 KDA PROTEIN, PROTEIN CP-47;                         
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: PHOTOSYSTEM II CP43 REACTION CENTER PROTEIN;               
COMPND  13 CHAIN: C, c;                                                         
COMPND  14 SYNONYM: PSII 43 KDA PROTEIN, PROTEIN CP-43;                         
COMPND  15 MOL_ID: 4;                                                           
COMPND  16 MOLECULE: PHOTOSYSTEM II D2 PROTEIN;                                 
COMPND  17 CHAIN: D, d;                                                         
COMPND  18 SYNONYM: PSII D2 PROTEIN, PHOTOSYSTEM II Q(A) PROTEIN;               
COMPND  19 EC: 1.10.3.9;                                                        
COMPND  20 MOL_ID: 5;                                                           
COMPND  21 MOLECULE: CYTOCHROME B559 SUBUNIT ALPHA;                             
COMPND  22 CHAIN: E, e;                                                         
COMPND  23 SYNONYM: PSII REACTION CENTER SUBUNIT V;                             
COMPND  24 MOL_ID: 6;                                                           
COMPND  25 MOLECULE: CYTOCHROME B559 SUBUNIT BETA;                              
COMPND  26 CHAIN: F, f;                                                         
COMPND  27 SYNONYM: PSII REACTION CENTER SUBUNIT VI;                            
COMPND  28 MOL_ID: 7;                                                           
COMPND  29 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN H;                  
COMPND  30 CHAIN: H, h;                                                         
COMPND  31 SYNONYM: PSII-H;                                                     
COMPND  32 MOL_ID: 8;                                                           
COMPND  33 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN I;                  
COMPND  34 CHAIN: I, i;                                                         
COMPND  35 SYNONYM: PSII-I, PSII 4.4 KDA PROTEIN;                               
COMPND  36 MOL_ID: 9;                                                           
COMPND  37 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN J;                  
COMPND  38 CHAIN: J, j;                                                         
COMPND  39 SYNONYM: PSII-J;                                                     
COMPND  40 MOL_ID: 10;                                                          
COMPND  41 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN K;                  
COMPND  42 CHAIN: K, k;                                                         
COMPND  43 SYNONYM: PSII-K;                                                     
COMPND  44 MOL_ID: 11;                                                          
COMPND  45 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN L;                  
COMPND  46 CHAIN: L, l;                                                         
COMPND  47 SYNONYM: PSII-L, PSII 5 KDA PROTEIN;                                 
COMPND  48 MOL_ID: 12;                                                          
COMPND  49 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN M;                  
COMPND  50 CHAIN: M, m;                                                         
COMPND  51 SYNONYM: PSII-M;                                                     
COMPND  52 MOL_ID: 13;                                                          
COMPND  53 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;          
COMPND  54 CHAIN: O, o;                                                         
COMPND  55 SYNONYM: MSP;                                                        
COMPND  56 MOL_ID: 14;                                                          
COMPND  57 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN T;                  
COMPND  58 CHAIN: T, t;                                                         
COMPND  59 SYNONYM: PSII-T, PSII-TC;                                            
COMPND  60 MOL_ID: 15;                                                          
COMPND  61 MOLECULE: PHOTOSYSTEM II 12 KDA EXTRINSIC PROTEIN;                   
COMPND  62 CHAIN: U, u;                                                         
COMPND  63 SYNONYM: PS II COMPLEX 12 KDA EXTRINSIC PROTEIN, PSII-U;             
COMPND  64 MOL_ID: 16;                                                          
COMPND  65 MOLECULE: CYTOCHROME C-550;                                          
COMPND  66 CHAIN: V, v;                                                         
COMPND  67 SYNONYM: CYTOCHROME C-549, CYTOCHROME C550, LOW-POTENTIAL CYTOCHROME 
COMPND  68 C;                                                                   
COMPND  69 MOL_ID: 17;                                                          
COMPND  70 MOLECULE: PHOTOSYSTEM II REACTION CENTER X PROTEIN;                  
COMPND  71 CHAIN: X, x;                                                         
COMPND  72 MOL_ID: 18;                                                          
COMPND  73 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN YCF12;              
COMPND  74 CHAIN: Y, y;                                                         
COMPND  75 MOL_ID: 19;                                                          
COMPND  76 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Z;                  
COMPND  77 CHAIN: Z, z;                                                         
COMPND  78 SYNONYM: PSII-Z                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE   3 ORGANISM_TAXID: 197221;                                              
SOURCE   4 STRAIN: BP-1;                                                        
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE   7 ORGANISM_TAXID: 197221;                                              
SOURCE   8 STRAIN: BP-1;                                                        
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  11 ORGANISM_TAXID: 197221;                                              
SOURCE  12 STRAIN: BP-1;                                                        
SOURCE  13 MOL_ID: 4;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  15 ORGANISM_TAXID: 197221;                                              
SOURCE  16 STRAIN: BP-1;                                                        
SOURCE  17 MOL_ID: 5;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  19 ORGANISM_TAXID: 197221;                                              
SOURCE  20 STRAIN: BP-1;                                                        
SOURCE  21 MOL_ID: 6;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  23 ORGANISM_TAXID: 197221;                                              
SOURCE  24 STRAIN: BP-1;                                                        
SOURCE  25 MOL_ID: 7;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  27 ORGANISM_TAXID: 197221;                                              
SOURCE  28 STRAIN: BP-1;                                                        
SOURCE  29 MOL_ID: 8;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  31 ORGANISM_TAXID: 197221;                                              
SOURCE  32 STRAIN: BP-1;                                                        
SOURCE  33 MOL_ID: 9;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  35 ORGANISM_TAXID: 197221;                                              
SOURCE  36 STRAIN: BP-1;                                                        
SOURCE  37 MOL_ID: 10;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  39 ORGANISM_TAXID: 197221;                                              
SOURCE  40 STRAIN: BP-1;                                                        
SOURCE  41 MOL_ID: 11;                                                          
SOURCE  42 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  43 ORGANISM_TAXID: 197221;                                              
SOURCE  44 STRAIN: BP-1;                                                        
SOURCE  45 MOL_ID: 12;                                                          
SOURCE  46 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  47 ORGANISM_TAXID: 197221;                                              
SOURCE  48 STRAIN: BP-1;                                                        
SOURCE  49 MOL_ID: 13;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  51 ORGANISM_TAXID: 197221;                                              
SOURCE  52 STRAIN: BP-1;                                                        
SOURCE  53 MOL_ID: 14;                                                          
SOURCE  54 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  55 ORGANISM_TAXID: 197221;                                              
SOURCE  56 STRAIN: BP-1;                                                        
SOURCE  57 MOL_ID: 15;                                                          
SOURCE  58 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  59 ORGANISM_TAXID: 197221;                                              
SOURCE  60 STRAIN: BP-1;                                                        
SOURCE  61 MOL_ID: 16;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  63 ORGANISM_TAXID: 197221;                                              
SOURCE  64 STRAIN: BP-1;                                                        
SOURCE  65 MOL_ID: 17;                                                          
SOURCE  66 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  67 ORGANISM_TAXID: 197221;                                              
SOURCE  68 STRAIN: BP-1;                                                        
SOURCE  69 MOL_ID: 18;                                                          
SOURCE  70 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  71 ORGANISM_TAXID: 197221;                                              
SOURCE  72 STRAIN: BP-1;                                                        
SOURCE  73 MOL_ID: 19;                                                          
SOURCE  74 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  75 ORGANISM_TAXID: 197221;                                              
SOURCE  76 STRAIN: BP-1                                                         
KEYWDS    PHOTOSYSTEM II, TIME RESOLVED, FREE ELECTRON LASER, ELECTRON          
KEYWDS   2 TRANSPORT, MEMBRANE, OXIDOREDUCTASE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.KUPITZ,S.BASU,I.GROTJOHANN,R.FROMME,N.ZATSEPIN,K.N.RENDEK,M.HUNTER, 
AUTHOR   2 R.L.SHOEMAN,T.A.WHITE,D.WANG,D.JAMES,J.-H.YANG,D.E.COBB,B.REEDER,    
AUTHOR   3 R.G.SIERRA,H.LIU,A.BARTY,A.AQUILA,D.DEPONTE,R.KIRIAN,S.BARI,         
AUTHOR   4 J.J.BERGKAMP,K.BEYERLEIN,M.J.BOGAN,C.CALEMAN,T.-C.CHAO,C.E.CONRAD,   
AUTHOR   5 K.M.DAVIS,H.FLECKENSTEIN,L.GALLI,S.P.HAU-RIEGE,S.KASSEMEYER,         
AUTHOR   6 H.LAKSMONO,M.LIANG,L.LOMB,S.MARCHESINI,A.V.MARTIN,M.MESSERSCHMIDT,   
AUTHOR   7 D.MILATHIANAKI,K.NASS,A.ROS,S.ROY-CHOWDHURY,K.SCHMIDT,M.SEIBERT,     
AUTHOR   8 J.STEINBRENER,F.STELLATO,L.YAN,C.YOON,T.A.MOORE,A.L.MOORE,Y.PUSHKAR, 
AUTHOR   9 G.J.WILLIAMS,S.BOUTET,R.B.DOAK,U.WEIERSTALL,M.FRANK,H.N.CHAPMAN,     
AUTHOR  10 J.C.H.SPENCE,P.FROMME                                                
REVDAT   3   19-SEP-18 4RVY    1       REMARK                                   
REVDAT   2   14-FEB-18 4RVY    1       REMARK                                   
REVDAT   1   04-NOV-15 4RVY    0                                                
SPRSDE     04-NOV-15 4RVY      4Q54                                             
JRNL        AUTH   C.KUPITZ,S.BASU,I.GROTJOHANN,R.FROMME,N.A.ZATSEPIN,          
JRNL        AUTH 2 K.N.RENDEK,M.S.HUNTER,R.L.SHOEMAN,T.A.WHITE,D.WANG,D.JAMES,  
JRNL        AUTH 3 J.H.YANG,D.E.COBB,B.REEDER,R.G.SIERRA,H.LIU,A.BARTY,         
JRNL        AUTH 4 A.L.AQUILA,D.DEPONTE,R.A.KIRIAN,S.BARI,J.J.BERGKAMP,         
JRNL        AUTH 5 K.R.BEYERLEIN,M.J.BOGAN,C.CALEMAN,T.C.CHAO,C.E.CONRAD,       
JRNL        AUTH 6 K.M.DAVIS,H.FLECKENSTEIN,L.GALLI,S.P.HAU-RIEGE,S.KASSEMEYER, 
JRNL        AUTH 7 H.LAKSMONO,M.LIANG,L.LOMB,S.MARCHESINI,A.V.MARTIN,           
JRNL        AUTH 8 M.MESSERSCHMIDT,D.MILATHIANAKI,K.NASS,A.ROS,S.ROY-CHOWDHURY, 
JRNL        AUTH 9 K.SCHMIDT,M.SEIBERT,J.STEINBRENER,F.STELLATO,L.YAN,C.YOON,   
JRNL        AUTH10 T.A.MOORE,A.L.MOORE,Y.PUSHKAR,G.J.WILLIAMS,S.BOUTET,         
JRNL        AUTH11 R.B.DOAK,U.WEIERSTALL,M.FRANK,H.N.CHAPMAN,J.C.SPENCE,        
JRNL        AUTH12 P.FROMME                                                     
JRNL        TITL   SERIAL TIME-RESOLVED CRYSTALLOGRAPHY OF PHOTOSYSTEM II USING 
JRNL        TITL 2 A FEMTOSECOND X-RAY LASER.                                   
JRNL        REF    NATURE                        V. 513   261 2014              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   25043005                                                     
JRNL        DOI    10.1038/NATURE13453                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    5.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1336)                   
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 5.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 102.30                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 33992                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.281                           
REMARK   3   R VALUE            (WORKING SET) : 0.281                           
REMARK   3   FREE R VALUE                     : 0.291                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1626                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1102.3120 - 12.5850    0.00        0   143  0.3372 0.3628        
REMARK   3     2 12.5850 -  9.9919    0.00        0   148  0.2107 0.2107        
REMARK   3     3  9.9919 -  8.7296    0.00        0   142  0.2272 0.2297        
REMARK   3     4  8.7296 -  7.9318    0.00        0   132  0.2275 0.2607        
REMARK   3     5  7.9318 -  7.3634    0.00        0   133  0.2843 0.2813        
REMARK   3     6  7.3634 -  6.9294    0.00        0   129  0.2782 0.2787        
REMARK   3     7  6.9294 -  6.5824    0.00        0   144  0.2934 0.3198        
REMARK   3     8  6.5824 -  6.2959    0.00        0   131  0.3483 0.3664        
REMARK   3     9  6.2959 -  6.0536    0.00        0   134  0.3396 0.3627        
REMARK   3    10  6.0536 -  5.8447    0.00        0   145  0.3097 0.3277        
REMARK   3    11  5.8447 -  5.6620    0.00        0   123  0.3503 0.3543        
REMARK   3    12  5.6620 -  5.5000    0.00        0   122  0.3820 0.3477        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
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 4RVY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000087862.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JAN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 283                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 18772                              
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) : 2.05                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : CS-PAD CXI-1                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL                           
REMARK 200  DATA SCALING SOFTWARE          : CRYSTFEL                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32066                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 5.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 102.295                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
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) : 5.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 5.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3ARC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM PIPES PH 7.0, 5 MM CACL2, 10 MM   
REMARK 280  TOCOPHEROL, AND 10-17% PEG 2000 , FREE INTERFACE DIFFUSION,         
REMARK 280  TEMPERATURE 283K, TEMPERATURE 283.0K                                
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       68.30500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      154.34000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      114.04500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      154.34000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       68.30500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      114.04500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 38-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, a, B, b, C, c, D, d, E, e,         
REMARK 350                    AND CHAINS: F, f, H, h, I, i, J, j, K,            
REMARK 350                    AND CHAINS: k, L, l, M, m, O, o, T, t, U,         
REMARK 350                    AND CHAINS: u, V, v, X, x, Y, y, Z, z             
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET 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     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     MET J     1                                                      
REMARK 465     MET J     2                                                      
REMARK 465     MET j     1                                                      
REMARK 465     MET j     2                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   C20  SQD b   621     C20  SQD L   101              0.03            
REMARK 500   C33  SQD b   621     C33  SQD L   101              0.20            
REMARK 500   C26  SQD b   621     C26  SQD L   101              0.27            
REMARK 500   O9   SQD l   101     O9   SQD l   102              0.28            
REMARK 500   C33  SQD l   101     C33  SQD l   102              0.32            
REMARK 500   C28  SQD b   621     C28  SQD L   101              0.34            
REMARK 500   C37  SQD b   621     C37  SQD L   101              0.35            
REMARK 500   C26  SQD l   101     C26  SQD l   102              0.41            
REMARK 500   C20  SQD l   101     C20  SQD l   102              0.43            
REMARK 500   C35  SQD l   101     C35  SQD l   102              0.45            
REMARK 500   C44  SQD b   621     C44  SQD L   101              0.45            
REMARK 500   C25  SQD b   621     C25  SQD L   101              0.47            
REMARK 500   O9   SQD b   621     O9   SQD L   101              0.48            
REMARK 500   C36  SQD l   101     C36  SQD l   102              0.48            
REMARK 500   C29  SQD b   621     C29  SQD L   101              0.49            
REMARK 500   C28  SQD l   101     C28  SQD l   102              0.50            
REMARK 500   S    SQD b   621     S    SQD L   101              0.51            
REMARK 500   O8   SQD b   621     O8   SQD L   101              0.52            
REMARK 500   C1   SQD l   101     O6   SQD l   102              0.53            
REMARK 500   S    SQD l   101     S    SQD l   102              0.54            
REMARK 500   C29  SQD l   101     C29  SQD l   102              0.58            
REMARK 500   C15  SQD l   101     C16  SQD l   102              0.58            
REMARK 500   C21  SQD b   621     C21  SQD L   101              0.58            
REMARK 500   C31  SQD b   621     C31  SQD L   101              0.59            
REMARK 500   C19  SQD l   101     C19  SQD l   102              0.60            
REMARK 500   O8   SQD l   101     O8   SQD l   102              0.60            
REMARK 500   C10  SQD l   101     C11  SQD l   102              0.60            
REMARK 500   C37  SQD l   101     C37  SQD l   102              0.61            
REMARK 500   C6   SQD b   621     C6   SQD L   101              0.62            
REMARK 500   C25  SQD l   101     C25  SQD l   102              0.62            
REMARK 500   C11  SQD b   621     C10  SQD L   101              0.63            
REMARK 500   C35  SQD b   621     C35  SQD L   101              0.66            
REMARK 500   O7   SQD b   621     O7   SQD L   101              0.66            
REMARK 500   C30  SQD b   621     C30  SQD L   101              0.66            
REMARK 500   C16  SQD b   621     C15  SQD L   101              0.66            
REMARK 500   O5   SQD b   621     O5   SQD L   101              0.69            
REMARK 500   C6   SQD l   101     C6   SQD l   102              0.70            
REMARK 500   C31  SQD l   101     C31  SQD l   102              0.70            
REMARK 500   C36  SQD b   621     C36  SQD L   101              0.70            
REMARK 500   C7   SQD l   101     C8   SQD l   102              0.72            
REMARK 500   C1   SQD b   621     C1   SQD L   101              0.72            
REMARK 500   O7   SQD l   101     O7   SQD l   102              0.72            
REMARK 500   C38  SQD b   621     C38  SQD L   101              0.73            
REMARK 500   C13  SQD l   101     C14  SQD l   102              0.73            
REMARK 500   C14  SQD b   621     C14  SQD L   101              0.74            
REMARK 500   C18  SQD b   621     C18  SQD L   101              0.74            
REMARK 500   C5   SQD b   621     C5   SQD L   101              0.75            
REMARK 500   O5   SQD l   101     O5   SQD l   102              0.75            
REMARK 500   C23  SQD l   101     C23  SQD l   102              0.75            
REMARK 500   C34  SQD b   621     C34  SQD L   101              0.76            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     382 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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   OE1  GLN u    73     CD   GLU V    70     3544     0.80            
REMARK 500   OE1  GLN u    73     OE1  GLU V    70     3544     1.22            
REMARK 500   OE1  GLN u    73     OE2  GLU V    70     3544     1.45            
REMARK 500   CD   GLN u    73     OE1  GLU V    70     3544     1.79            
REMARK 500   CD   GLN u    73     CD   GLU V    70     3544     1.89            
REMARK 500   OE1  GLN u    73     CG   GLU V    70     3544     1.98            
REMARK 500   OD2  ASP u    60     CD   LYS V   110     3544     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    MET I   1   N     MET I   1   CA      0.739                       
REMARK 500    MET I   1   CA    MET I   1   C       0.319                       
REMARK 500    MET i   1   N     MET i   1   CA      0.739                       
REMARK 500    MET i   1   CA    MET i   1   C       0.319                       
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    MET I   1   CB  -  CA  -  C   ANGL. DEV. = -12.4 DEGREES          
REMARK 500    MET I   1   N   -  CA  -  CB  ANGL. DEV. = -32.1 DEGREES          
REMARK 500    MET I   1   N   -  CA  -  C   ANGL. DEV. = -35.1 DEGREES          
REMARK 500    MET I   1   CA  -  C   -  N   ANGL. DEV. = -13.9 DEGREES          
REMARK 500    MET i   1   CB  -  CA  -  C   ANGL. DEV. = -12.4 DEGREES          
REMARK 500    MET i   1   N   -  CA  -  CB  ANGL. DEV. = -32.2 DEGREES          
REMARK 500    MET i   1   N   -  CA  -  C   ANGL. DEV. = -35.1 DEGREES          
REMARK 500    MET i   1   CA  -  C   -  N   ANGL. DEV. = -13.9 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    VAL A  30      -82.81    -93.29                                   
REMARK 500    LEU A 159      -54.92   -124.72                                   
REMARK 500    ILE A 259      -93.43   -101.19                                   
REMARK 500    VAL a  30      -82.87    -93.26                                   
REMARK 500    LEU a 159      -55.03   -124.72                                   
REMARK 500    ILE a 259      -93.46   -101.25                                   
REMARK 500    TYR B 117       55.91    -92.34                                   
REMARK 500    ASP B 313       45.55    -93.40                                   
REMARK 500    PHE B 383      -77.80    -86.95                                   
REMARK 500    TYR b 117       55.91    -92.29                                   
REMARK 500    ASP b 313       45.49    -93.44                                   
REMARK 500    PHE b 383      -77.87    -86.85                                   
REMARK 500    ASP C 107      113.97   -160.67                                   
REMARK 500    GLU C 221      -65.01   -125.03                                   
REMARK 500    TRP C 223     -137.65     46.79                                   
REMARK 500    THR C 295      -60.15   -100.82                                   
REMARK 500    SER C 416      -45.02    173.34                                   
REMARK 500    ASP c 107      113.97   -160.64                                   
REMARK 500    GLU c 221      -64.97   -125.07                                   
REMARK 500    TRP c 223     -137.60     46.79                                   
REMARK 500    THR c 295      -60.13   -100.82                                   
REMARK 500    SER c 416      -44.99    173.30                                   
REMARK 500    ARG D  12       42.40   -156.14                                   
REMARK 500    VAL D  30      -70.41   -107.17                                   
REMARK 500    SER D  65       14.84   -148.60                                   
REMARK 500    PRO D 140       44.90    -91.55                                   
REMARK 500    ALA D 234       32.80    -77.92                                   
REMARK 500    PRO D 309        1.90    -66.07                                   
REMARK 500    ALA D 351      -52.33     71.50                                   
REMARK 500    ARG d  12       42.38   -156.07                                   
REMARK 500    VAL d  30      -70.44   -107.14                                   
REMARK 500    SER d  65       14.90   -148.61                                   
REMARK 500    PRO d 140       44.94    -91.67                                   
REMARK 500    ALA d 234       32.72    -77.96                                   
REMARK 500    PRO d 309        1.81    -66.06                                   
REMARK 500    ALA d 351      -52.29     71.44                                   
REMARK 500    LYS H  63       31.89    -82.88                                   
REMARK 500    LEU H  65      -88.03   -150.54                                   
REMARK 500    LYS h  63       31.91    -82.95                                   
REMARK 500    LEU h  65      -87.96   -150.56                                   
REMARK 500    LYS I  33     -119.80   -110.32                                   
REMARK 500    LYS i  33     -119.80   -110.30                                   
REMARK 500    SER J  39       -4.10     73.47                                   
REMARK 500    SER j  39       -4.15     73.53                                   
REMARK 500    ASN O  58       -3.66    149.36                                   
REMARK 500    ARG O  73     -163.39     70.21                                   
REMARK 500    THR O 138        8.10    -69.28                                   
REMARK 500    ASN o  58       -3.64    149.35                                   
REMARK 500    ARG o  73     -163.41     70.17                                   
REMARK 500    THR o 138        8.13    -69.34                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      62 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    MET I   1         17.53                                           
REMARK 500    MET i   1         17.49                                           
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     LMG A  614                                                       
REMARK 610     LMG a  614                                                       
REMARK 610     LMG B  620                                                       
REMARK 610     LMG b  619                                                       
REMARK 610     DGD C  516                                                       
REMARK 610     DGD C  517                                                       
REMARK 610     DGD C  518                                                       
REMARK 610     LMG C  519                                                       
REMARK 610     LMG C  520                                                       
REMARK 610     DGD c  516                                                       
REMARK 610     DGD c  517                                                       
REMARK 610     DGD c  518                                                       
REMARK 610     LMG c  519                                                       
REMARK 610     LMG c  520                                                       
REMARK 610     LMG D  406                                                       
REMARK 610     DGD D  410                                                       
REMARK 610     SQD D  411                                                       
REMARK 610     LMG d  406                                                       
REMARK 610     DGD d  410                                                       
REMARK 610     SQD d  411                                                       
REMARK 610     LHG E  101                                                       
REMARK 610     LHG e  101                                                       
REMARK 610     DGD H  102                                                       
REMARK 610     DGD h  102                                                       
REMARK 610     LMG Z  101                                                       
REMARK 610     LMG z  101                                                       
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                             OEX A 601  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 189   OE2                                                    
REMARK 620 2 OEX A 601   O1   93.3                                              
REMARK 620 3 OEX A 601   O5   96.4  82.4                                        
REMARK 620 4 OEX A 601   O3  174.1  92.0  81.7                                  
REMARK 620 5 HIS A 332   NE2  86.4 178.3  99.3  88.4                            
REMARK 620 6 ASP A 342   OD2  94.2  91.9 168.2  88.2  86.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 189   OE2                                                    
REMARK 620 2 OEX a 601   O1   93.3                                              
REMARK 620 3 OEX a 601   O5   96.4  82.4                                        
REMARK 620 4 OEX a 601   O3  174.1  92.0  81.7                                  
REMARK 620 5 HIS a 332   NE2  86.4 178.3  99.3  88.4                            
REMARK 620 6 ASP a 342   OD2  94.2  91.9 168.2  88.2  86.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA a 344   OXT                                                    
REMARK 620 2 OEX a 601   O1   94.4                                              
REMARK 620 3 OEX a 601   O2   89.7  89.0                                        
REMARK 620 4 OEX a 601   O3  172.5  78.9  86.8                                  
REMARK 620 5 GLU c 354   OE1  94.2 171.2  88.9  92.4                            
REMARK 620 6 ASP a 342   OD1  90.1  90.2 179.2  93.3  91.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A 344   OXT                                                    
REMARK 620 2 OEX A 601   O1   94.4                                              
REMARK 620 3 OEX A 601   O2   89.7  89.0                                        
REMARK 620 4 OEX A 601   O3  172.5  78.9  86.8                                  
REMARK 620 5 GLU C 354   OE1  94.1 171.2  88.8  92.4                            
REMARK 620 6 ASP A 342   OD1  90.1  90.2 179.2  93.3  92.0                      
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  41   NE2                                                    
REMARK 620 2 HEM v 201   NA   88.7                                              
REMARK 620 3 HEM v 201   NB   87.3  91.3                                        
REMARK 620 4 HEM v 201   NC   91.8 179.4  88.4                                  
REMARK 620 5 HEM v 201   ND   91.3  88.5 178.5  91.8                            
REMARK 620 6 HIS v  92   NE2 177.7  93.2  91.5  86.2  90.0                      
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  41   NE2                                                    
REMARK 620 2 HEM V 201   NA   88.7                                              
REMARK 620 3 HEM V 201   NB   87.3  91.3                                        
REMARK 620 4 HEM V 201   NC   91.8 179.4  88.4                                  
REMARK 620 5 HEM V 201   ND   91.2  88.5 178.5  91.8                            
REMARK 620 6 HIS V  92   NE2 177.7  93.2  91.5  86.3  90.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM f 101  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS e  23   NE2                                                    
REMARK 620 2 HEM f 101   NA   97.1                                              
REMARK 620 3 HEM f 101   NB   94.6  88.7                                        
REMARK 620 4 HEM f 101   NC   88.2 174.6  90.6                                  
REMARK 620 5 HEM f 101   ND   85.2  93.0 178.3  87.7                            
REMARK 620 6 HIS f  24   NE2 179.4  83.4  85.8  91.3  94.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM F 101  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  23   NE2                                                    
REMARK 620 2 HEM F 101   NA   97.2                                              
REMARK 620 3 HEM F 101   NB   94.5  88.7                                        
REMARK 620 4 HEM F 101   NC   88.2 174.6  90.6                                  
REMARK 620 5 HEM F 101   ND   85.2  93.0 178.3  87.7                            
REMARK 620 6 HIS F  24   NE2 179.4  83.4  85.8  91.3  94.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 333   OE1                                                    
REMARK 620 2 OEX a 601   O2  176.2                                              
REMARK 620 3 OEX a 601   O3   88.7  93.2                                        
REMARK 620 4 OEX a 601   O4   95.0  83.2 175.9                                  
REMARK 620 5 OEX a 601   O5   91.1  92.4  81.5  96.6                            
REMARK 620 6 GLU c 354   OE2  88.9  88.0  86.4  95.4 167.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 333   OE1                                                    
REMARK 620 2 OEX A 601   O2  176.2                                              
REMARK 620 3 OEX A 601   O3   88.7  93.2                                        
REMARK 620 4 OEX A 601   O4   95.0  83.2 175.9                                  
REMARK 620 5 OEX A 601   O5   91.1  92.4  81.5  96.6                            
REMARK 620 6 GLU C 354   OE2  88.9  88.0  86.4  95.4 167.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 170   OD2                                                    
REMARK 620 2 OEX a 601   O5   99.8                                              
REMARK 620 3 OEX a 601   O4   90.3  92.5                                        
REMARK 620 4 GLU a 333   OE2 171.6  84.4  96.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 170   OD2                                                    
REMARK 620 2 OEX A 601   O5   99.8                                              
REMARK 620 3 OEX A 601   O4   90.3  92.5                                        
REMARK 620 4 GLU A 333   OE2 171.6  84.3  96.8                                  
REMARK 620 N                    1     2     3                                   
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  100.0                                              
REMARK 620 3 CLA c 511   NB  102.4  87.7                                        
REMARK 620 4 CLA c 511   NC   97.9 160.9  95.1                                  
REMARK 620 5 CLA c 511   ND   98.8  90.4 158.7  80.1                            
REMARK 620 N                    1     2     3     4                             
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  100.0                                              
REMARK 620 3 CLA C 511   NB  102.4  87.7                                        
REMARK 620 4 CLA C 511   NC   97.9 160.9  95.1                                  
REMARK 620 5 CLA C 511   ND   98.8  90.4 158.7  80.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 A 602  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 214   NE2                                                    
REMARK 620 2 HIS A 215   NE2 110.4                                              
REMARK 620 3 HIS A 272   NE2  92.3  93.0                                        
REMARK 620 4 BCT A 612   O2   92.8 155.9  92.3                                  
REMARK 620 5 BCT A 612   O1  150.1  99.4  84.4  57.8                            
REMARK 620 6 HIS D 268   NE2  92.2  87.4 175.1  85.4  90.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 a 602  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS d 214   NE2                                                    
REMARK 620 2 HIS a 215   NE2 110.4                                              
REMARK 620 3 HIS a 272   NE2  92.2  93.0                                        
REMARK 620 4 BCT a 612   O1   92.8 155.9  92.3                                  
REMARK 620 5 BCT a 612   O2  150.1  99.4  84.4  57.8                            
REMARK 620 6 HIS d 268   NE2  92.2  87.3 175.1  85.5  90.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG j 101  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY j  31   O                                                      
REMARK 620 2 ALA j  34   O    80.0                                              
REMARK 620 3 LEU j  36   O   106.4 105.6                                        
REMARK 620 4 LMG d 406   O4   78.5 157.0  88.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG J 101  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY J  31   O                                                      
REMARK 620 2 ALA J  34   O    80.0                                              
REMARK 620 3 LEU J  36   O   106.3 105.6                                        
REMARK 620 4 LMG D 406   O4   78.5 157.0  88.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA O 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL O 201   O                                                      
REMARK 620 2 ASN O 200   OD1  81.2                                              
REMARK 620 3 THR O 138   O    81.5 152.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA o 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL o 201   O                                                      
REMARK 620 2 ASN o 200   OD1  81.2                                              
REMARK 620 3 THR o 138   O    81.5 152.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 170   OD1                                                    
REMARK 620 2 OEX a 601   O1  155.9                                              
REMARK 620 3 OEX a 601   O2   84.6  75.2                                        
REMARK 620 4 OEX a 601   O5  111.5  76.8  76.6                                  
REMARK 620 5 ALA a 344   O    84.3  78.3  76.2 146.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 170   OD1                                                    
REMARK 620 2 OEX A 601   O1  156.0                                              
REMARK 620 3 OEX A 601   O2   84.6  75.2                                        
REMARK 620 4 OEX A 601   O5  111.5  76.8  76.6                                  
REMARK 620 5 ALA A 344   O    84.3  78.3  76.2 146.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA f 102  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG f  45   OXT                                                    
REMARK 620 2 ARG f  45   O    43.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F 102  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG F  45   OXT                                                    
REMARK 620 2 ARG F  45   O    43.9                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OEX A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 610                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 611                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT A 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 A 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG A 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OEX a 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 a 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO a 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO a 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR a 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD a 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL a 610                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL a 611                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT a 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 a 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG a 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG B 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 621                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD b 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR b 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG b 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA b 620                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD b 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR b 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR C 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR C 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD C 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG C 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG C 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR c 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR c 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD c 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD c 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD c 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG c 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG c 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR D 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG D 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG D 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG D 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 D 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG D 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD D 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD D 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA d 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA d 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA d 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR d 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG d 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG d 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG d 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 d 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG d 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD d 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD d 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG E 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG e 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM F 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM f 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA f 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR H 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD H 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR h 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DGD h 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG J 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG j 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR K 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR K 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR k 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR k 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD L 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG L 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD l 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SQD l 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG l 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA O 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA o 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR T 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR T 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR t 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM V 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM v 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG Z 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG z 101                 
DBREF  4RVY A   11   344  UNP    P0A444   PSBA1_THEEB     11    344             
DBREF  4RVY a   11   344  UNP    P0A444   PSBA1_THEEB     11    344             
DBREF  4RVY B    2   505  UNP    Q8DIQ1   PSBB_THEEB       2    505             
DBREF  4RVY b    2   505  UNP    Q8DIQ1   PSBB_THEEB       2    505             
DBREF  4RVY C   13   473  UNP    Q8DIF8   PSBC_THEEB       1    461             
DBREF  4RVY c   13   473  UNP    Q8DIF8   PSBC_THEEB       1    461             
DBREF  4RVY D   11   352  UNP    Q8CM25   PSBD_THEEB      11    352             
DBREF  4RVY d   11   352  UNP    Q8CM25   PSBD_THEEB      11    352             
DBREF  4RVY E    4    84  UNP    Q8DIP0   PSBE_THEEB       4     84             
DBREF  4RVY e    4    84  UNP    Q8DIP0   PSBE_THEEB       4     84             
DBREF  4RVY F   12    45  UNP    Q8DIN9   PSBF_THEEB      12     45             
DBREF  4RVY f   12    45  UNP    Q8DIN9   PSBF_THEEB      12     45             
DBREF  4RVY H    2    66  UNP    Q8DJ43   PSBH_THEEB       2     66             
DBREF  4RVY h    2    66  UNP    Q8DJ43   PSBH_THEEB       2     66             
DBREF  4RVY I    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  4RVY i    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  4RVY J    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  4RVY j    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  4RVY K   10    46  UNP    Q9F1K9   PSBK_THEEB      10     46             
DBREF  4RVY k   10    46  UNP    Q9F1K9   PSBK_THEEB      10     46             
DBREF  4RVY L    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  4RVY l    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  4RVY M    1    34  UNP    Q8DHA7   PSBM_THEEB       1     34             
DBREF  4RVY m    1    34  UNP    Q8DHA7   PSBM_THEEB       1     34             
DBREF  4RVY O    4   246  UNP    P0A431   PSBO_THEEB      30    272             
DBREF  4RVY o    4   246  UNP    P0A431   PSBO_THEEB      30    272             
DBREF  4RVY T    1    30  UNP    Q8DIQ0   PSBT_THEEB       1     30             
DBREF  4RVY t    1    30  UNP    Q8DIQ0   PSBT_THEEB       1     30             
DBREF  4RVY U    8   104  UNP    Q9F1L5   PSBU_THEEB      38    134             
DBREF  4RVY u    8   104  UNP    Q9F1L5   PSBU_THEEB      38    134             
DBREF  4RVY V    1   137  UNP    P0A386   CY550_THEEB     27    163             
DBREF  4RVY v    1   137  UNP    P0A386   CY550_THEEB     27    163             
DBREF  4RVY X    2    40  UNP    Q9F1R6   PSBX_THEEB       2     40             
DBREF  4RVY x    2    40  UNP    Q9F1R6   PSBX_THEEB       2     40             
DBREF  4RVY Y   18    46  UNP    Q8DJI1   YCF12_THEEB     18     46             
DBREF  4RVY y   18    46  UNP    Q8DJI1   YCF12_THEEB     18     46             
DBREF  4RVY Z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
DBREF  4RVY z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
SEQADV 4RVY ALA A  286  UNP  P0A444    THR   286 CONFLICT                       
SEQADV 4RVY ALA a  286  UNP  P0A444    THR   286 CONFLICT                       
SEQRES   1 A  334  ALA ASN LEU TRP GLU ARG PHE CYS ASN TRP VAL THR SER          
SEQRES   2 A  334  THR ASP ASN ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE          
SEQRES   3 A  334  MET ILE PRO THR LEU LEU ALA ALA THR ILE CYS PHE VAL          
SEQRES   4 A  334  ILE ALA PHE ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY          
SEQRES   5 A  334  ILE ARG GLU PRO VAL SER GLY SER LEU LEU TYR GLY ASN          
SEQRES   6 A  334  ASN ILE ILE THR GLY ALA VAL VAL PRO SER SER ASN ALA          
SEQRES   7 A  334  ILE GLY LEU HIS PHE TYR PRO ILE TRP GLU ALA ALA SER          
SEQRES   8 A  334  LEU ASP GLU TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU          
SEQRES   9 A  334  ILE ILE PHE HIS PHE LEU LEU GLY ALA SER CYS TYR MET          
SEQRES  10 A  334  GLY ARG GLN TRP GLU LEU SER TYR ARG LEU GLY MET ARG          
SEQRES  11 A  334  PRO TRP ILE CYS VAL ALA TYR SER ALA PRO LEU ALA SER          
SEQRES  12 A  334  ALA PHE ALA VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY          
SEQRES  13 A  334  SER PHE SER ASP GLY MET PRO LEU GLY ILE SER GLY THR          
SEQRES  14 A  334  PHE ASN PHE MET ILE VAL PHE GLN ALA GLU HIS ASN ILE          
SEQRES  15 A  334  LEU MET HIS PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL          
SEQRES  16 A  334  PHE GLY GLY ALA LEU PHE CYS ALA MET HIS GLY SER LEU          
SEQRES  17 A  334  VAL THR SER SER LEU ILE ARG GLU THR THR GLU THR GLU          
SEQRES  18 A  334  SER ALA ASN TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU          
SEQRES  19 A  334  THR TYR ASN ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG          
SEQRES  20 A  334  LEU ILE PHE GLN TYR ALA SER PHE ASN ASN SER ARG SER          
SEQRES  21 A  334  LEU HIS PHE PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL          
SEQRES  22 A  334  TRP PHE ALA ALA LEU GLY ILE SER THR MET ALA PHE ASN          
SEQRES  23 A  334  LEU ASN GLY PHE ASN PHE ASN HIS SER VAL ILE ASP ALA          
SEQRES  24 A  334  LYS GLY ASN VAL ILE ASN THR TRP ALA ASP ILE ILE ASN          
SEQRES  25 A  334  ARG ALA ASN LEU GLY MET GLU VAL MET HIS GLU ARG ASN          
SEQRES  26 A  334  ALA HIS ASN PHE PRO LEU ASP LEU ALA                          
SEQRES   1 a  334  ALA ASN LEU TRP GLU ARG PHE CYS ASN TRP VAL THR SER          
SEQRES   2 a  334  THR ASP ASN ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE          
SEQRES   3 a  334  MET ILE PRO THR LEU LEU ALA ALA THR ILE CYS PHE VAL          
SEQRES   4 a  334  ILE ALA PHE ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY          
SEQRES   5 a  334  ILE ARG GLU PRO VAL SER GLY SER LEU LEU TYR GLY ASN          
SEQRES   6 a  334  ASN ILE ILE THR GLY ALA VAL VAL PRO SER SER ASN ALA          
SEQRES   7 a  334  ILE GLY LEU HIS PHE TYR PRO ILE TRP GLU ALA ALA SER          
SEQRES   8 a  334  LEU ASP GLU TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU          
SEQRES   9 a  334  ILE ILE PHE HIS PHE LEU LEU GLY ALA SER CYS TYR MET          
SEQRES  10 a  334  GLY ARG GLN TRP GLU LEU SER TYR ARG LEU GLY MET ARG          
SEQRES  11 a  334  PRO TRP ILE CYS VAL ALA TYR SER ALA PRO LEU ALA SER          
SEQRES  12 a  334  ALA PHE ALA VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY          
SEQRES  13 a  334  SER PHE SER ASP GLY MET PRO LEU GLY ILE SER GLY THR          
SEQRES  14 a  334  PHE ASN PHE MET ILE VAL PHE GLN ALA GLU HIS ASN ILE          
SEQRES  15 a  334  LEU MET HIS PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL          
SEQRES  16 a  334  PHE GLY GLY ALA LEU PHE CYS ALA MET HIS GLY SER LEU          
SEQRES  17 a  334  VAL THR SER SER LEU ILE ARG GLU THR THR GLU THR GLU          
SEQRES  18 a  334  SER ALA ASN TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU          
SEQRES  19 a  334  THR TYR ASN ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG          
SEQRES  20 a  334  LEU ILE PHE GLN TYR ALA SER PHE ASN ASN SER ARG SER          
SEQRES  21 a  334  LEU HIS PHE PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL          
SEQRES  22 a  334  TRP PHE ALA ALA LEU GLY ILE SER THR MET ALA PHE ASN          
SEQRES  23 a  334  LEU ASN GLY PHE ASN PHE ASN HIS SER VAL ILE ASP ALA          
SEQRES  24 a  334  LYS GLY ASN VAL ILE ASN THR TRP ALA ASP ILE ILE ASN          
SEQRES  25 a  334  ARG ALA ASN LEU GLY MET GLU VAL MET HIS GLU ARG ASN          
SEQRES  26 a  334  ALA HIS ASN PHE PRO LEU ASP LEU ALA                          
SEQRES   1 B  504  GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE ASN          
SEQRES   2 B  504  ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS THR          
SEQRES   3 B  504  ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU TYR          
SEQRES   4 B  504  GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU ASN          
SEQRES   5 B  504  PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE MET          
SEQRES   6 B  504  ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP SER          
SEQRES   7 B  504  ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP SER          
SEQRES   8 B  504  PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER GLY          
SEQRES   9 B  504  LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR TRP          
SEQRES  10 B  504  ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU PRO          
SEQRES  11 B  504  ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU PHE          
SEQRES  12 B  504  LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE HIS          
SEQRES  13 B  504  LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER ASP          
SEQRES  14 B  504  PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA PRO          
SEQRES  15 B  504  GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO GLY          
SEQRES  16 B  504  GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL GLY          
SEQRES  17 B  504  ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO PRO          
SEQRES  18 B  504  GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE GLU          
SEQRES  19 B  504  THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE ALA          
SEQRES  20 B  504  ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER ALA          
SEQRES  21 B  504  THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR GLN          
SEQRES  22 B  504  TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG ARG          
SEQRES  23 B  504  VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU GLU          
SEQRES  24 B  504  ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR ASP          
SEQRES  25 B  504  TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE ARG          
SEQRES  26 B  504  THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN ALA          
SEQRES  27 B  504  TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY GLU          
SEQRES  28 B  504  GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU SER          
SEQRES  29 B  504  PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL LYS          
SEQRES  30 B  504  ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR SER          
SEQRES  31 B  504  PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY GLY          
SEQRES  32 B  504  GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR VAL          
SEQRES  33 B  504  LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE PHE          
SEQRES  34 B  504  GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE PHE          
SEQRES  35 B  504  ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS ALA          
SEQRES  36 B  504  VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP HIS          
SEQRES  37 B  504  GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY ILE          
SEQRES  38 B  504  ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY PHE          
SEQRES  39 B  504  TYR GLN LYS VAL GLY ASP VAL THR THR ARG                      
SEQRES   1 b  504  GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE ASN          
SEQRES   2 b  504  ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS THR          
SEQRES   3 b  504  ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU TYR          
SEQRES   4 b  504  GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU ASN          
SEQRES   5 b  504  PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE MET          
SEQRES   6 b  504  ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP SER          
SEQRES   7 b  504  ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP SER          
SEQRES   8 b  504  PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER GLY          
SEQRES   9 b  504  LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR TRP          
SEQRES  10 b  504  ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU PRO          
SEQRES  11 b  504  ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU PHE          
SEQRES  12 b  504  LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE HIS          
SEQRES  13 b  504  LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER ASP          
SEQRES  14 b  504  PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA PRO          
SEQRES  15 b  504  GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO GLY          
SEQRES  16 b  504  GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL GLY          
SEQRES  17 b  504  ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO PRO          
SEQRES  18 b  504  GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE GLU          
SEQRES  19 b  504  THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE ALA          
SEQRES  20 b  504  ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER ALA          
SEQRES  21 b  504  THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR GLN          
SEQRES  22 b  504  TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG ARG          
SEQRES  23 b  504  VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU GLU          
SEQRES  24 b  504  ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR ASP          
SEQRES  25 b  504  TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE ARG          
SEQRES  26 b  504  THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN ALA          
SEQRES  27 b  504  TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY GLU          
SEQRES  28 b  504  GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU SER          
SEQRES  29 b  504  PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL LYS          
SEQRES  30 b  504  ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR SER          
SEQRES  31 b  504  PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY GLY          
SEQRES  32 b  504  GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR VAL          
SEQRES  33 b  504  LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE PHE          
SEQRES  34 b  504  GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE PHE          
SEQRES  35 b  504  ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS ALA          
SEQRES  36 b  504  VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP HIS          
SEQRES  37 b  504  GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY ILE          
SEQRES  38 b  504  ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY PHE          
SEQRES  39 b  504  TYR GLN LYS VAL GLY ASP VAL THR THR ARG                      
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 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  342  GLU ARG GLY TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS          
SEQRES   2 D  342  ARG ASP ARG PHE VAL PHE VAL GLY TRP SER GLY ILE LEU          
SEQRES   3 D  342  LEU PHE PRO CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU          
SEQRES   4 D  342  THR GLY THR THR PHE VAL THR SER TRP TYR THR HIS GLY          
SEQRES   5 D  342  LEU ALA SER SER TYR LEU GLU GLY CYS ASN PHE LEU THR          
SEQRES   6 D  342  VAL ALA VAL SER THR PRO ALA ASN SER MET GLY HIS SER          
SEQRES   7 D  342  LEU LEU LEU LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE          
SEQRES   8 D  342  THR ARG TRP CYS GLN LEU GLY GLY LEU TRP THR PHE ILE          
SEQRES   9 D  342  ALA LEU HIS GLY ALA PHE GLY LEU ILE GLY PHE MET LEU          
SEQRES  10 D  342  ARG GLN PHE GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO          
SEQRES  11 D  342  TYR ASN ALA ILE ALA PHE SER ALA PRO ILE ALA VAL PHE          
SEQRES  12 D  342  VAL SER VAL PHE LEU ILE TYR PRO LEU GLY GLN SER SER          
SEQRES  13 D  342  TRP PHE PHE ALA PRO SER PHE GLY VAL ALA ALA ILE PHE          
SEQRES  14 D  342  ARG PHE LEU LEU PHE PHE GLN GLY PHE HIS ASN TRP THR          
SEQRES  15 D  342  LEU ASN PRO PHE HIS MET MET GLY VAL ALA GLY VAL LEU          
SEQRES  16 D  342  GLY GLY ALA LEU LEU CYS ALA ILE HIS GLY ALA THR VAL          
SEQRES  17 D  342  GLU ASN THR LEU PHE GLN ASP GLY GLU GLY ALA SER THR          
SEQRES  18 D  342  PHE ARG ALA PHE ASN PRO THR GLN ALA GLU GLU THR TYR          
SEQRES  19 D  342  SER MET VAL THR ALA ASN ARG PHE TRP SER GLN ILE PHE          
SEQRES  20 D  342  GLY ILE ALA PHE SER ASN LYS ARG TRP LEU HIS PHE PHE          
SEQRES  21 D  342  MET LEU PHE VAL PRO VAL THR GLY LEU TRP MET SER ALA          
SEQRES  22 D  342  ILE GLY VAL VAL GLY LEU ALA LEU ASN LEU ARG SER TYR          
SEQRES  23 D  342  ASP PHE ILE SER GLN GLU ILE ARG ALA ALA GLU ASP PRO          
SEQRES  24 D  342  GLU PHE GLU THR PHE TYR THR LYS ASN LEU LEU LEU ASN          
SEQRES  25 D  342  GLU GLY ILE ARG ALA TRP MET ALA PRO GLN ASP GLN PRO          
SEQRES  26 D  342  HIS GLU ASN PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG          
SEQRES  27 D  342  GLY ASN ALA LEU                                              
SEQRES   1 d  342  GLU ARG GLY TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS          
SEQRES   2 d  342  ARG ASP ARG PHE VAL PHE VAL GLY TRP SER GLY ILE LEU          
SEQRES   3 d  342  LEU PHE PRO CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU          
SEQRES   4 d  342  THR GLY THR THR PHE VAL THR SER TRP TYR THR HIS GLY          
SEQRES   5 d  342  LEU ALA SER SER TYR LEU GLU GLY CYS ASN PHE LEU THR          
SEQRES   6 d  342  VAL ALA VAL SER THR PRO ALA ASN SER MET GLY HIS SER          
SEQRES   7 d  342  LEU LEU LEU LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE          
SEQRES   8 d  342  THR ARG TRP CYS GLN LEU GLY GLY LEU TRP THR PHE ILE          
SEQRES   9 d  342  ALA LEU HIS GLY ALA PHE GLY LEU ILE GLY PHE MET LEU          
SEQRES  10 d  342  ARG GLN PHE GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO          
SEQRES  11 d  342  TYR ASN ALA ILE ALA PHE SER ALA PRO ILE ALA VAL PHE          
SEQRES  12 d  342  VAL SER VAL PHE LEU ILE TYR PRO LEU GLY GLN SER SER          
SEQRES  13 d  342  TRP PHE PHE ALA PRO SER PHE GLY VAL ALA ALA ILE PHE          
SEQRES  14 d  342  ARG PHE LEU LEU PHE PHE GLN GLY PHE HIS ASN TRP THR          
SEQRES  15 d  342  LEU ASN PRO PHE HIS MET MET GLY VAL ALA GLY VAL LEU          
SEQRES  16 d  342  GLY GLY ALA LEU LEU CYS ALA ILE HIS GLY ALA THR VAL          
SEQRES  17 d  342  GLU ASN THR LEU PHE GLN ASP GLY GLU GLY ALA SER THR          
SEQRES  18 d  342  PHE ARG ALA PHE ASN PRO THR GLN ALA GLU GLU THR TYR          
SEQRES  19 d  342  SER MET VAL THR ALA ASN ARG PHE TRP SER GLN ILE PHE          
SEQRES  20 d  342  GLY ILE ALA PHE SER ASN LYS ARG TRP LEU HIS PHE PHE          
SEQRES  21 d  342  MET LEU PHE VAL PRO VAL THR GLY LEU TRP MET SER ALA          
SEQRES  22 d  342  ILE GLY VAL VAL GLY LEU ALA LEU ASN LEU ARG SER TYR          
SEQRES  23 d  342  ASP PHE ILE SER GLN GLU ILE ARG ALA ALA GLU ASP PRO          
SEQRES  24 d  342  GLU PHE GLU THR PHE TYR THR LYS ASN LEU LEU LEU ASN          
SEQRES  25 d  342  GLU GLY ILE ARG ALA TRP MET ALA PRO GLN ASP GLN PRO          
SEQRES  26 d  342  HIS GLU ASN PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG          
SEQRES  27 d  342  GLY ASN ALA LEU                                              
SEQRES   1 E   81  THR THR GLY GLU ARG PRO PHE SER ASP ILE ILE THR SER          
SEQRES   2 E   81  VAL ARG TYR TRP VAL ILE HIS SER ILE THR ILE PRO ALA          
SEQRES   3 E   81  LEU PHE ILE ALA GLY TRP LEU PHE VAL SER THR GLY LEU          
SEQRES   4 E   81  ALA TYR ASP VAL PHE GLY THR PRO ARG PRO ASP SER TYR          
SEQRES   5 E   81  TYR ALA GLN GLU GLN ARG SER ILE PRO LEU VAL THR ASP          
SEQRES   6 E   81  ARG PHE GLU ALA LYS GLN GLN VAL GLU THR PHE LEU GLU          
SEQRES   7 E   81  GLN LEU LYS                                                  
SEQRES   1 e   81  THR THR GLY GLU ARG PRO PHE SER ASP ILE ILE THR SER          
SEQRES   2 e   81  VAL ARG TYR TRP VAL ILE HIS SER ILE THR ILE PRO ALA          
SEQRES   3 e   81  LEU PHE ILE ALA GLY TRP LEU PHE VAL SER THR GLY LEU          
SEQRES   4 e   81  ALA TYR ASP VAL PHE GLY THR PRO ARG PRO ASP SER TYR          
SEQRES   5 e   81  TYR ALA GLN GLU GLN ARG SER ILE PRO LEU VAL THR ASP          
SEQRES   6 e   81  ARG PHE GLU ALA LYS GLN GLN VAL GLU THR PHE LEU GLU          
SEQRES   7 e   81  GLN LEU LYS                                                  
SEQRES   1 F   34  SER TYR PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS          
SEQRES   2 F   34  THR LEU ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE          
SEQRES   3 F   34  ALA ALA MET GLN PHE ILE GLN ARG                              
SEQRES   1 f   34  SER TYR PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS          
SEQRES   2 f   34  THR LEU ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE          
SEQRES   3 f   34  ALA ALA MET 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 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 i   38  MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR          
SEQRES   2 i   38  PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY          
SEQRES   3 i   38  ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU              
SEQRES   1 J   40  MET MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL          
SEQRES   2 J   40  ALA THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY          
SEQRES   3 J   40  LEU PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER          
SEQRES   4 J   40  LEU                                                          
SEQRES   1 j   40  MET MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL          
SEQRES   2 j   40  ALA THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY          
SEQRES   3 j   40  LEU PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER          
SEQRES   4 j   40  LEU                                                          
SEQRES   1 K   37  LYS LEU PRO GLU ALA TYR ALA ILE PHE ASP PRO LEU VAL          
SEQRES   2 K   37  ASP VAL LEU PRO VAL ILE PRO VAL LEU PHE LEU ALA LEU          
SEQRES   3 K   37  ALA PHE VAL TRP GLN ALA ALA VAL GLY PHE ARG                  
SEQRES   1 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 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   34  MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU          
SEQRES   2 M   34  PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR          
SEQRES   3 M   34  VAL GLN THR GLU SER GLN GLN LYS                              
SEQRES   1 m   34  MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU          
SEQRES   2 m   34  PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR          
SEQRES   3 m   34  VAL GLN THR GLU SER GLN GLN LYS                              
SEQRES   1 O  243  THR LEU THR TYR ASP ASP ILE VAL GLY THR GLY LEU ALA          
SEQRES   2 O  243  ASN LYS CYS PRO THR LEU ASP ASP THR ALA ARG GLY ALA          
SEQRES   3 O  243  TYR PRO ILE ASP SER SER GLN THR TYR ARG ILE ALA ARG          
SEQRES   4 O  243  LEU CYS LEU GLN PRO THR THR PHE LEU VAL LYS GLU GLU          
SEQRES   5 O  243  PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE VAL PRO THR          
SEQRES   6 O  243  LYS LEU VAL THR ARG GLU THR THR SER LEU ASP GLN ILE          
SEQRES   7 O  243  GLN GLY GLU LEU LYS VAL ASN SER ASP GLY SER LEU THR          
SEQRES   8 O  243  PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN PRO VAL THR          
SEQRES   9 O  243  VAL GLN MET ALA GLY GLY GLU ARG ILE PRO LEU LEU PHE          
SEQRES  10 O  243  THR VAL LYS ASN LEU VAL ALA SER THR GLN PRO ASN VAL          
SEQRES  11 O  243  THR SER ILE THR THR SER THR ASP PHE LYS GLY GLU PHE          
SEQRES  12 O  243  ASN VAL PRO SER TYR ARG THR ALA ASN PHE LEU ASP PRO          
SEQRES  13 O  243  LYS GLY ARG GLY LEU ALA SER GLY TYR ASP SER ALA ILE          
SEQRES  14 O  243  ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU ALA ARG ALA          
SEQRES  15 O  243  ASN VAL LYS ARG PHE SER LEU THR LYS GLY GLN ILE SER          
SEQRES  16 O  243  LEU ASN VAL ALA LYS VAL ASP GLY ARG THR GLY GLU ILE          
SEQRES  17 O  243  ALA GLY THR PHE GLU SER GLU GLN LEU SER ASP ASP ASP          
SEQRES  18 O  243  MET GLY ALA HIS GLU PRO HIS GLU VAL LYS ILE GLN GLY          
SEQRES  19 O  243  VAL PHE TYR ALA SER ILE GLU PRO ALA                          
SEQRES   1 o  243  THR LEU THR TYR ASP ASP ILE VAL GLY THR GLY LEU ALA          
SEQRES   2 o  243  ASN LYS CYS PRO THR LEU ASP ASP THR ALA ARG GLY ALA          
SEQRES   3 o  243  TYR PRO ILE ASP SER SER GLN THR TYR ARG ILE ALA ARG          
SEQRES   4 o  243  LEU CYS LEU GLN PRO THR THR PHE LEU VAL LYS GLU GLU          
SEQRES   5 o  243  PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE VAL PRO THR          
SEQRES   6 o  243  LYS LEU VAL THR ARG GLU THR THR SER LEU ASP GLN ILE          
SEQRES   7 o  243  GLN GLY GLU LEU LYS VAL ASN SER ASP GLY SER LEU THR          
SEQRES   8 o  243  PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN PRO VAL THR          
SEQRES   9 o  243  VAL GLN MET ALA GLY GLY GLU ARG ILE PRO LEU LEU PHE          
SEQRES  10 o  243  THR VAL LYS ASN LEU VAL ALA SER THR GLN PRO ASN VAL          
SEQRES  11 o  243  THR SER ILE THR THR SER THR ASP PHE LYS GLY GLU PHE          
SEQRES  12 o  243  ASN VAL PRO SER TYR ARG THR ALA ASN PHE LEU ASP PRO          
SEQRES  13 o  243  LYS GLY ARG GLY LEU ALA SER GLY TYR ASP SER ALA ILE          
SEQRES  14 o  243  ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU ALA ARG ALA          
SEQRES  15 o  243  ASN VAL LYS ARG PHE SER LEU THR LYS GLY GLN ILE SER          
SEQRES  16 o  243  LEU ASN VAL ALA LYS VAL ASP GLY ARG THR GLY GLU ILE          
SEQRES  17 o  243  ALA GLY THR PHE GLU SER GLU GLN LEU SER ASP ASP ASP          
SEQRES  18 o  243  MET GLY ALA HIS GLU PRO HIS GLU VAL LYS ILE GLN GLY          
SEQRES  19 o  243  VAL PHE TYR ALA SER ILE GLU PRO ALA                          
SEQRES   1 T   30  MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE          
SEQRES   2 T   30  ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO          
SEQRES   3 T   30  PRO ARG ILE THR                                              
SEQRES   1 t   30  MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE          
SEQRES   2 t   30  ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO          
SEQRES   3 t   30  PRO ARG ILE THR                                              
SEQRES   1 U   97  GLU LEU VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA          
SEQRES   2 U   97  TYR GLY GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA          
SEQRES   3 U   97  ALA PHE ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA          
SEQRES   4 U   97  LYS LEU ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU          
SEQRES   5 U   97  ASP VAL LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS          
SEQRES   6 U   97  GLN ILE LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR          
SEQRES   7 U   97  GLU VAL GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR          
SEQRES   8 U   97  ASN ASN GLY LEU TYR LYS                                      
SEQRES   1 u   97  GLU LEU VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA          
SEQRES   2 u   97  TYR GLY GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA          
SEQRES   3 u   97  ALA PHE ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA          
SEQRES   4 u   97  LYS LEU ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU          
SEQRES   5 u   97  ASP VAL LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS          
SEQRES   6 u   97  GLN ILE LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR          
SEQRES   7 u   97  GLU VAL GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR          
SEQRES   8 u   97  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 v  137  ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN          
SEQRES   2 v  137  SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR          
SEQRES   3 v  137  LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER          
SEQRES   4 v  137  CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU          
SEQRES   5 v  137  ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO          
SEQRES   6 v  137  ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN          
SEQRES   7 v  137  PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL          
SEQRES   8 v  137  HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET          
SEQRES   9 v  137  ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY          
SEQRES  10 v  137  HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP          
SEQRES  11 v  137  GLY GLY GLY LYS VAL TYR TYR                                  
SEQRES   1 X   39  THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY LEU          
SEQRES   2 X   39  LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA VAL          
SEQRES   3 X   39  LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG SER          
SEQRES   1 x   39  THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY LEU          
SEQRES   2 x   39  LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA VAL          
SEQRES   3 x   39  LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG SER          
SEQRES   1 Y   29  VAL ILE ALA GLN LEU THR MET ILE ALA MET ILE GLY ILE          
SEQRES   2 Y   29  ALA GLY PRO MET ILE ILE PHE LEU LEU ALA VAL ARG ARG          
SEQRES   3 Y   29  GLY ASN LEU                                                  
SEQRES   1 y   29  VAL ILE ALA GLN LEU THR MET ILE ALA MET ILE GLY ILE          
SEQRES   2 y   29  ALA GLY PRO MET ILE ILE PHE LEU LEU ALA VAL ARG ARG          
SEQRES   3 y   29  GLY ASN LEU                                                  
SEQRES   1 Z   62  MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL          
SEQRES   2 Z   62  ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA          
SEQRES   3 Z   62  TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU          
SEQRES   4 Z   62  ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU          
SEQRES   5 Z   62  VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL                      
SEQRES   1 z   62  MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL          
SEQRES   2 z   62  ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA          
SEQRES   3 z   62  TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU          
SEQRES   4 z   62  ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU          
SEQRES   5 z   62  VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL                      
HET    OEX  A 601      10                                                       
HET    FE2  A 602       1                                                       
HET    CLA  A 603      65                                                       
HET    CLA  A 604      65                                                       
HET    PHO  A 605      64                                                       
HET    PHO  A 606      64                                                       
HET    CLA  A 607      65                                                       
HET    BCR  A 608      40                                                       
HET    SQD  A 609      54                                                       
HET     CL  A 610       1                                                       
HET     CL  A 611       1                                                       
HET    BCT  A 612       4                                                       
HET    PL9  A 613      55                                                       
HET    LMG  A 614      51                                                       
HET    OEX  a 601      10                                                       
HET    FE2  a 602       1                                                       
HET    CLA  a 603      65                                                       
HET    CLA  a 604      65                                                       
HET    PHO  a 605      64                                                       
HET    PHO  a 606      64                                                       
HET    CLA  a 607      65                                                       
HET    BCR  a 608      40                                                       
HET    SQD  a 609      54                                                       
HET     CL  a 610       1                                                       
HET     CL  a 611       1                                                       
HET    BCT  a 612       4                                                       
HET    PL9  a 613      55                                                       
HET    LMG  a 614      51                                                       
HET    SQD  B 601      54                                                       
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    CLA  B 617      65                                                       
HET    BCR  B 618      40                                                       
HET    BCR  B 619      40                                                       
HET    LMG  B 620      51                                                       
HET     CA  B 621       1                                                       
HET    BCR  B 622      40                                                       
HET    SQD  b 601      54                                                       
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    CLA  b 617      65                                                       
HET    BCR  b 618      40                                                       
HET    LMG  b 619      51                                                       
HET     CA  b 620       1                                                       
HET    SQD  b 621      54                                                       
HET    BCR  b 622      40                                                       
HET    CLA  C 501      65                                                       
HET    CLA  C 502      65                                                       
HET    CLA  C 503      65                                                       
HET    CLA  C 504      65                                                       
HET    CLA  C 505      65                                                       
HET    CLA  C 506      65                                                       
HET    CLA  C 507      65                                                       
HET    CLA  C 508      65                                                       
HET    CLA  C 509      65                                                       
HET    CLA  C 510      65                                                       
HET    CLA  C 511      65                                                       
HET    CLA  C 512      65                                                       
HET    CLA  C 513      65                                                       
HET    BCR  C 514      40                                                       
HET    BCR  C 515      40                                                       
HET    DGD  C 516      62                                                       
HET    DGD  C 517      62                                                       
HET    DGD  C 518      62                                                       
HET    LMG  C 519      51                                                       
HET    LMG  C 520      51                                                       
HET    CLA  c 501      65                                                       
HET    CLA  c 502      65                                                       
HET    CLA  c 503      65                                                       
HET    CLA  c 504      65                                                       
HET    CLA  c 505      65                                                       
HET    CLA  c 506      65                                                       
HET    CLA  c 507      65                                                       
HET    CLA  c 508      65                                                       
HET    CLA  c 509      65                                                       
HET    CLA  c 510      65                                                       
HET    CLA  c 511      65                                                       
HET    CLA  c 512      65                                                       
HET    CLA  c 513      65                                                       
HET    BCR  c 514      40                                                       
HET    BCR  c 515      40                                                       
HET    DGD  c 516      62                                                       
HET    DGD  c 517      62                                                       
HET    DGD  c 518      62                                                       
HET    LMG  c 519      51                                                       
HET    LMG  c 520      51                                                       
HET    CLA  D 401      65                                                       
HET    CLA  D 402      65                                                       
HET    CLA  D 403      65                                                       
HET    BCR  D 404      40                                                       
HET    LHG  D 405      49                                                       
HET    LMG  D 406      51                                                       
HET    LHG  D 407      49                                                       
HET    PL9  D 408      55                                                       
HET    LHG  D 409      49                                                       
HET    DGD  D 410      62                                                       
HET    SQD  D 411      43                                                       
HET    CLA  d 401      65                                                       
HET    CLA  d 402      65                                                       
HET    CLA  d 403      65                                                       
HET    BCR  d 404      40                                                       
HET    LHG  d 405      49                                                       
HET    LMG  d 406      51                                                       
HET    LHG  d 407      49                                                       
HET    PL9  d 408      55                                                       
HET    LHG  d 409      49                                                       
HET    DGD  d 410      62                                                       
HET    SQD  d 411      43                                                       
HET    LHG  E 101      42                                                       
HET    LHG  e 101      42                                                       
HET    HEM  F 101      43                                                       
HET     CA  F 102       1                                                       
HET    HEM  f 101      43                                                       
HET     CA  f 102       1                                                       
HET    BCR  H 101      40                                                       
HET    DGD  H 102      62                                                       
HET    BCR  h 101      40                                                       
HET    DGD  h 102      62                                                       
HET     MG  J 101       1                                                       
HET     MG  j 101       1                                                       
HET    BCR  K 101      40                                                       
HET    BCR  K 102      40                                                       
HET    BCR  k 101      40                                                       
HET    BCR  k 102      40                                                       
HET    SQD  L 101      54                                                       
HET    LHG  L 102      49                                                       
HET    SQD  l 101      54                                                       
HET    SQD  l 102      54                                                       
HET    LHG  l 103      49                                                       
HET     CA  O 301       1                                                       
HET     CA  o 301       1                                                       
HET    BCR  T 101      40                                                       
HET    BCR  T 102      40                                                       
HET    BCR  t 101      40                                                       
HET     CL  U 201       1                                                       
HET     CL  u 201       1                                                       
HET    HEM  V 201      43                                                       
HET    HEM  v 201      43                                                       
HET    LMG  Z 101      37                                                       
HET    LMG  z 101      37                                                       
HETNAM     OEX CA-MN4-O5 CLUSTER                                                
HETNAM     FE2 FE (II) ION                                                      
HETNAM     CLA CHLOROPHYLL A                                                    
HETNAM     PHO PHEOPHYTIN A                                                     
HETNAM     BCR BETA-CAROTENE                                                    
HETNAM     SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-                      
HETNAM   2 SQD  GLUCOPYRANOSYL]-SN-GLYCEROL                                     
HETNAM      CL CHLORIDE ION                                                     
HETNAM     BCT BICARBONATE ION                                                  
HETNAM     PL9 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,           
HETNAM   2 PL9  6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-               
HETNAM   3 PL9  CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-          
HETNAM   4 PL9  BENZOQUINONE                                                    
HETNAM     LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE                        
HETNAM      CA CALCIUM ION                                                      
HETNAM     DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)                              
HETNAM     LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE                           
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     SQD SULFOQUINOVOSYLDIACYLGLYCEROL                                    
HETSYN     PL9 PLASTOQUINONE 9                                                  
HETSYN     HEM HEME                                                             
FORMUL  39  OEX    2(CA MN4 O5)                                                 
FORMUL  40  FE2    2(FE 2+)                                                     
FORMUL  41  CLA    70(C55 H72 MG N4 O5 2+)                                      
FORMUL  43  PHO    4(C55 H74 N4 O5)                                             
FORMUL  46  BCR    22(C40 H56)                                                  
FORMUL  47  SQD    10(C41 H78 O12 S)                                            
FORMUL  48   CL    6(CL 1-)                                                     
FORMUL  50  BCT    2(C H O3 1-)                                                 
FORMUL  51  PL9    4(C53 H80 O2)                                                
FORMUL  52  LMG    12(C45 H86 O10)                                              
FORMUL  87   CA    6(CA 2+)                                                     
FORMUL  26  DGD    10(C51 H96 O15)                                              
FORMUL  55  LHG    10(C38 H75 O10 P)                                            
FORMUL  75  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL  83   MG    2(MG 2+)                                                     
HELIX    1   1 ASN A   12  THR A   22  1                                  11    
HELIX    2   2 VAL A   30  ALA A   55  1                                  26    
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  LEU A  159  1                                  18    
HELIX    8   8 LEU A  159  GLY A  166  1                                   8    
HELIX    9   9 SER A  167  GLY A  171  5                                   5    
HELIX   10  10 ILE A  176  ASN A  191  1                                  16    
HELIX   11  11 ILE A  192  MET A  194  5                                   3    
HELIX   12  12 HIS A  195  SER A  222  1                                  28    
HELIX   13  13 SER A  232  TYR A  237  5                                   6    
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  ALA A  294  1                                  28    
HELIX   17  17 THR A  316  HIS A  332  1                                  17    
HELIX   18  18 ASN a   12  THR a   22  1                                  11    
HELIX   19  19 VAL a   30  ALA a   55  1                                  26    
HELIX   20  20 SER a   70  GLY a   74  5                                   5    
HELIX   21  21 PRO a   95  ALA a   99  5                                   5    
HELIX   22  22 SER a  101  ASN a  108  1                                   8    
HELIX   23  23 GLY a  109  LEU a  137  1                                  29    
HELIX   24  24 TRP a  142  LEU a  159  1                                  18    
HELIX   25  25 LEU a  159  GLY a  166  1                                   8    
HELIX   26  26 SER a  167  GLY a  171  5                                   5    
HELIX   27  27 ILE a  176  ASN a  191  1                                  16    
HELIX   28  28 ILE a  192  MET a  194  5                                   3    
HELIX   29  29 HIS a  195  SER a  222  1                                  28    
HELIX   30  30 SER a  232  TYR a  237  5                                   6    
HELIX   31  31 ASN a  247  ILE a  259  1                                  13    
HELIX   32  32 PHE a  260  SER a  264  5                                   5    
HELIX   33  33 ASN a  267  ALA a  294  1                                  28    
HELIX   34  34 THR a  316  HIS a  332  1                                  17    
HELIX   35  35 PRO B    4  ILE B   13  5                                  10    
HELIX   36  36 ASP B   15  PHE B   45  1                                  31    
HELIX   37  37 PRO B   54  GLN B   58  5                                   5    
HELIX   38  38 VAL B   62  LEU B   69  1                                   8    
HELIX   39  39 SER B   92  TYR B  117  1                                  26    
HELIX   40  40 LEU B  120  ARG B  124  5                                   5    
HELIX   41  41 ASP B  134  PHE B  156  1                                  23    
HELIX   42  42 GLY B  186  ASN B  191  5                                   6    
HELIX   43  43 ASN B  194  VAL B  219  1                                  26    
HELIX   44  44 PRO B  222  LEU B  229  1                                   8    
HELIX   45  45 ASN B  233  GLY B  259  1                                  27    
HELIX   46  46 PRO B  264  GLY B  269  1                                   6    
HELIX   47  47 THR B  271  SER B  277  1                                   7    
HELIX   48  48 SER B  278  SER B  294  1                                  17    
HELIX   49  49 THR B  297  ALA B  304  1                                   8    
HELIX   50  50 PRO B  306  ASP B  313  1                                   8    
HELIX   51  51 TYR B  314  GLY B  322  5                                   9    
HELIX   52  52 PRO B  329  GLY B  333  5                                   5    
HELIX   53  53 SER B  391  GLY B  396  1                                   6    
HELIX   54  54 ASP B  413  ILE B  425  1                                  13    
HELIX   55  55 SER B  446  PHE B  475  1                                  30    
HELIX   56  56 ARG B  476  PHE B  479  5                                   4    
HELIX   57  57 SER B  487  VAL B  491  5                                   5    
HELIX   58  58 ASP B  501  ARG B  505  5                                   5    
HELIX   59  59 PRO b    4  ILE b   13  5                                  10    
HELIX   60  60 ASP b   15  PHE b   45  1                                  31    
HELIX   61  61 PRO b   54  GLN b   58  5                                   5    
HELIX   62  62 VAL b   62  LEU b   69  1                                   8    
HELIX   63  63 SER b   92  TYR b  117  1                                  26    
HELIX   64  64 LEU b  120  ARG b  124  5                                   5    
HELIX   65  65 ASP b  134  PHE b  156  1                                  23    
HELIX   66  66 GLY b  186  ASN b  191  5                                   6    
HELIX   67  67 ASN b  194  VAL b  219  1                                  26    
HELIX   68  68 PRO b  222  LEU b  229  1                                   8    
HELIX   69  69 ASN b  233  GLY b  259  1                                  27    
HELIX   70  70 PRO b  264  GLY b  269  1                                   6    
HELIX   71  71 THR b  271  SER b  277  1                                   7    
HELIX   72  72 SER b  278  SER b  294  1                                  17    
HELIX   73  73 THR b  297  ALA b  304  1                                   8    
HELIX   74  74 PRO b  306  ASP b  313  1                                   8    
HELIX   75  75 TYR b  314  GLY b  322  5                                   9    
HELIX   76  76 PRO b  329  GLY b  333  5                                   5    
HELIX   77  77 SER b  391  GLY b  396  1                                   6    
HELIX   78  78 ASP b  413  ILE b  425  1                                  13    
HELIX   79  79 SER b  446  PHE b  475  1                                  30    
HELIX   80  80 ARG b  476  PHE b  479  5                                   4    
HELIX   81  81 SER b  487  VAL b  491  5                                   5    
HELIX   82  82 ASP b  501  ARG b  505  5                                   5    
HELIX   83  83 ASP C   27  GLY C   32  1                                   6    
HELIX   84  84 ALA C   34  ILE C   43  5                                  10    
HELIX   85  85 LEU C   45  PHE C   75  1                                  31    
HELIX   86  86 PRO C   80  GLN C   84  5                                   5    
HELIX   87  87 ILE C   87  LEU C   95  1                                   9    
HELIX   88  88 GLY C  100  GLU C  104  5                                   5    
HELIX   89  89 THR C  108  ARG C  135  1                                  28    
HELIX   90  90 ASP C  153  PHE C  182  1                                  30    
HELIX   91  91 ASP C  205  LEU C  214  1                                  10    
HELIX   92  92 GLY C  222  VAL C  227  5                                   6    
HELIX   93  93 ASN C  229  THR C  254  1                                  26    
HELIX   94  94 PHE C  257  PHE C  264  1                                   8    
HELIX   95  95 SER C  267  ASN C  293  1                                  27    
HELIX   96  96 PRO C  298  GLY C  303  1                                   6    
HELIX   97  97 THR C  305  LEU C  324  1                                  20    
HELIX   98  98 GLY C  353  TRP C  359  5                                   7    
HELIX   99  99 LEU C  366  PRO C  368  5                                   3    
HELIX  100 100 ASP C  376  ASP C  383  1                                   8    
HELIX  101 101 GLN C  385  THR C  397  1                                  13    
HELIX  102 102 SER C  421  GLY C  454  1                                  34    
HELIX  103 103 GLU C  464  MET C  469  5                                   6    
HELIX  104 104 ASP c   27  GLY c   32  1                                   6    
HELIX  105 105 ALA c   34  ILE c   43  5                                  10    
HELIX  106 106 LEU c   45  PHE c   75  1                                  31    
HELIX  107 107 PRO c   80  GLN c   84  5                                   5    
HELIX  108 108 ILE c   87  LEU c   95  1                                   9    
HELIX  109 109 GLY c  100  GLU c  104  5                                   5    
HELIX  110 110 THR c  108  ARG c  135  1                                  28    
HELIX  111 111 ASP c  153  PHE c  182  1                                  30    
HELIX  112 112 ASP c  205  LEU c  214  1                                  10    
HELIX  113 113 GLY c  222  VAL c  227  5                                   6    
HELIX  114 114 ASN c  229  THR c  254  1                                  26    
HELIX  115 115 PHE c  257  PHE c  264  1                                   8    
HELIX  116 116 SER c  267  ASN c  293  1                                  27    
HELIX  117 117 PRO c  298  GLY c  303  1                                   6    
HELIX  118 118 THR c  305  LEU c  324  1                                  20    
HELIX  119 119 GLY c  353  TRP c  359  5                                   7    
HELIX  120 120 LEU c  366  PRO c  368  5                                   3    
HELIX  121 121 ASP c  376  ASP c  383  1                                   8    
HELIX  122 122 GLN c  385  THR c  397  1                                  13    
HELIX  123 123 SER c  421  GLY c  454  1                                  34    
HELIX  124 124 GLU c  464  MET c  469  5                                   6    
HELIX  125 125 GLY D   13  LYS D   23  1                                  11    
HELIX  126 126 VAL D   30  VAL D   55  1                                  26    
HELIX  127 127 SER D   66  GLY D   70  5                                   5    
HELIX  128 128 ALA D   82  GLY D   86  5                                   5    
HELIX  129 129 ASP D  100  LEU D  107  1                                   8    
HELIX  130 130 GLY D  108  GLY D  137  1                                  30    
HELIX  131 131 PRO D  140  LEU D  158  1                                  19    
HELIX  132 132 LEU D  158  GLN D  164  1                                   7    
HELIX  133 133 SER D  166  ALA D  170  5                                   5    
HELIX  134 134 VAL D  175  ASN D  190  1                                  16    
HELIX  135 135 TRP D  191  LEU D  193  5                                   3    
HELIX  136 136 ASN D  194  ASN D  220  1                                  27    
HELIX  137 137 THR D  231  PHE D  235  5                                   5    
HELIX  138 138 SER D  245  PHE D  257  1                                  13    
HELIX  139 139 ASN D  263  ALA D  290  1                                  28    
HELIX  140 140 PHE D  298  ASP D  308  1                                  11    
HELIX  141 141 THR D  313  GLN D  334  1                                  22    
HELIX  142 142 PRO D  335  ASN D  338  5                                   4    
HELIX  143 143 PRO D  342  LEU D  346  5                                   5    
HELIX  144 144 GLY d   13  LYS d   23  1                                  11    
HELIX  145 145 VAL d   30  VAL d   55  1                                  26    
HELIX  146 146 SER d   66  GLY d   70  5                                   5    
HELIX  147 147 ALA d   82  GLY d   86  5                                   5    
HELIX  148 148 ASP d  100  LEU d  107  1                                   8    
HELIX  149 149 GLY d  108  GLY d  137  1                                  30    
HELIX  150 150 PRO d  140  LEU d  158  1                                  19    
HELIX  151 151 LEU d  158  GLN d  164  1                                   7    
HELIX  152 152 SER d  166  ALA d  170  5                                   5    
HELIX  153 153 VAL d  175  ASN d  190  1                                  16    
HELIX  154 154 TRP d  191  LEU d  193  5                                   3    
HELIX  155 155 ASN d  194  ASN d  220  1                                  27    
HELIX  156 156 THR d  231  PHE d  235  5                                   5    
HELIX  157 157 SER d  245  PHE d  257  1                                  13    
HELIX  158 158 ASN d  263  ALA d  290  1                                  28    
HELIX  159 159 PHE d  298  ASP d  308  1                                  11    
HELIX  160 160 THR d  313  GLN d  334  1                                  22    
HELIX  161 161 PRO d  335  ASN d  338  5                                   4    
HELIX  162 162 PRO d  342  LEU d  346  5                                   5    
HELIX  163 163 PRO E    9  ILE E   14  1                                   6    
HELIX  164 164 SER E   16  THR E   40  1                                  25    
HELIX  165 165 GLY E   41  GLY E   48  1                                   8    
HELIX  166 166 GLU E   71  GLN E   82  1                                  12    
HELIX  167 167 PRO e    9  ILE e   14  1                                   6    
HELIX  168 168 SER e   16  THR e   40  1                                  25    
HELIX  169 169 GLY e   41  GLY e   48  1                                   8    
HELIX  170 170 GLU e   71  GLN e   82  1                                  12    
HELIX  171 171 THR F   17  GLN F   41  1                                  25    
HELIX  172 172 THR f   17  GLN f   41  1                                  25    
HELIX  173 173 THR H    5  ARG H   12  1                                   8    
HELIX  174 174 PRO H   13  SER H   16  5                                   4    
HELIX  175 175 THR H   27  ASN H   50  1                                  24    
HELIX  176 176 THR h    5  ARG h   12  1                                   8    
HELIX  177 177 PRO h   13  SER h   16  5                                   4    
HELIX  178 178 THR h   27  ASN h   50  1                                  24    
HELIX  179 179 GLU I    2  SER I   25  1                                  24    
HELIX  180 180 GLY I   26  ARG I   30  5                                   5    
HELIX  181 181 GLU i    2  SER i   25  1                                  24    
HELIX  182 182 GLY i   26  ARG i   30  5                                   5    
HELIX  183 183 PRO J    9  TYR J   33  1                                  25    
HELIX  184 184 PRO j    9  TYR j   33  1                                  25    
HELIX  185 185 PRO K   12  ILE K   17  5                                   6    
HELIX  186 186 PHE K   18  LEU K   25  1                                   8    
HELIX  187 187 VAL K   27  VAL K   43  1                                  17    
HELIX  188 188 PRO k   12  ILE k   17  5                                   6    
HELIX  189 189 PHE k   18  LEU k   25  1                                   8    
HELIX  190 190 VAL k   27  VAL k   43  1                                  17    
HELIX  191 191 ASN L   13  ASN L   37  1                                  25    
HELIX  192 192 ASN l   13  ASN l   37  1                                  25    
HELIX  193 193 LEU M    6  SER M   31  1                                  26    
HELIX  194 194 LEU m    6  SER m   31  1                                  26    
HELIX  195 195 THR O    6  VAL O   11  1                                   6    
HELIX  196 196 GLY O   14  LYS O   18  5                                   5    
HELIX  197 197 GLU O  179  GLU O  181  5                                   3    
HELIX  198 198 LEU O  182  VAL O  187  1                                   6    
HELIX  199 199 THR o    6  VAL o   11  1                                   6    
HELIX  200 200 GLY o   14  LYS o   18  5                                   5    
HELIX  201 201 GLU o  179  GLU o  181  5                                   3    
HELIX  202 202 LEU o  182  VAL o  187  1                                   6    
HELIX  203 203 GLU T    2  PHE T   23  1                                  22    
HELIX  204 204 GLU t    2  PHE t   23  1                                  22    
HELIX  205 205 ASN U   11  LEU U   17  1                                   7    
HELIX  206 206 GLY U   18  GLU U   23  5                                   6    
HELIX  207 207 ASN U   31  TYR U   38  5                                   8    
HELIX  208 208 PRO U   43  ALA U   53  1                                  11    
HELIX  209 209 SER U   57  ILE U   64  5                                   8    
HELIX  210 210 THR U   68  ASN U   78  1                                  11    
HELIX  211 211 GLU U   88  GLU U   93  1                                   6    
HELIX  212 212 GLY U   94  ASP U   96  5                                   3    
HELIX  213 213 ASN u   11  LEU u   17  1                                   7    
HELIX  214 214 GLY u   18  GLU u   23  5                                   6    
HELIX  215 215 ASN u   31  TYR u   38  5                                   8    
HELIX  216 216 PRO u   43  ALA u   53  1                                  11    
HELIX  217 217 SER u   57  ILE u   64  5                                   8    
HELIX  218 218 THR u   68  ASN u   78  1                                  11    
HELIX  219 219 GLU u   88  GLU u   93  1                                   6    
HELIX  220 220 GLY u   94  ASP u   96  5                                   3    
HELIX  221 221 THR V   22  CYS V   37  1                                  16    
HELIX  222 222 CYS V   37  VAL V   42  1                                   6    
HELIX  223 223 GLY V   43  ILE V   45  5                                   3    
HELIX  224 224 ARG V   55  ALA V   62  1                                   8    
HELIX  225 225 ASN V   68  ASN V   78  1                                  11    
HELIX  226 226 PHE V  101  ARG V  105  5                                   5    
HELIX  227 227 THR V  108  GLY V  127  1                                  20    
HELIX  228 228 ASP V  128  TRP V  130  5                                   3    
HELIX  229 229 GLY V  133  TYR V  137  5                                   5    
HELIX  230 230 THR v   22  CYS v   37  1                                  16    
HELIX  231 231 CYS v   37  VAL v   42  1                                   6    
HELIX  232 232 GLY v   43  ILE v   45  5                                   3    
HELIX  233 233 ARG v   55  ALA v   62  1                                   8    
HELIX  234 234 ASN v   68  ASN v   78  1                                  11    
HELIX  235 235 PHE v  101  ARG v  105  5                                   5    
HELIX  236 236 THR v  108  GLY v  127  1                                  20    
HELIX  237 237 ASP v  128  TRP v  130  5                                   3    
HELIX  238 238 GLY v  133  TYR v  137  5                                   5    
HELIX  239 239 THR X    4  ASP X   35  1                                  32    
HELIX  240 240 THR x    4  ASP x   35  1                                  32    
HELIX  241 241 ILE Y   19  ARG Y   42  1                                  24    
HELIX  242 242 ILE y   19  ARG y   42  1                                  24    
HELIX  243 243 THR Z    2  SER Z   29  1                                  28    
HELIX  244 244 ASP Z   32  ASN Z   58  1                                  27    
HELIX  245 245 PHE Z   59  VAL Z   61  5                                   3    
HELIX  246 246 THR z    2  SER z   29  1                                  28    
HELIX  247 247 ASP z   32  ASN z   58  1                                  27    
HELIX  248 248 PHE z   59  VAL z   61  5                                   3    
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 ALA a  81  VAL a  82  0                                        
SHEET    2   C 2 LEU a 174  GLY a 175 -1  O  LEU a 174   N  VAL a  82           
SHEET    1   D 2 LEU a 297  ASN a 298  0                                        
SHEET    2   D 2 GLY c 402  SER c 403  1  O  GLY c 402   N  ASN a 298           
SHEET    1   E 2 MET B 166  VAL B 168  0                                        
SHEET    2   E 2 SER B 177  GLN B 179 -1  O  GLN B 179   N  MET B 166           
SHEET    1   F 6 VAL B 377  ASP B 380  0                                        
SHEET    2   F 6 ILE B 369  THR B 371 -1  N  LEU B 370   O  ALA B 379           
SHEET    3   F 6 GLU B 353  VAL B 356 -1  N  PHE B 355   O  THR B 371           
SHEET    4   F 6 ILE B 336  ARG B 347 -1  N  PHE B 346   O  LEU B 354           
SHEET    5   F 6 THR B 398  TYR B 402 -1  O  TYR B 402   N  HIS B 343           
SHEET    6   F 6 THR B 410  PHE B 411 -1  O  PHE B 411   N  VAL B 399           
SHEET    1   G 5 VAL B 377  ASP B 380  0                                        
SHEET    2   G 5 ILE B 369  THR B 371 -1  N  LEU B 370   O  ALA B 379           
SHEET    3   G 5 GLU B 353  VAL B 356 -1  N  PHE B 355   O  THR B 371           
SHEET    4   G 5 ILE B 336  ARG B 347 -1  N  PHE B 346   O  LEU B 354           
SHEET    5   G 5 ILE B 429  ASP B 433 -1  O  GLU B 431   N  GLN B 338           
SHEET    1   H 2 MET b 166  VAL b 168  0                                        
SHEET    2   H 2 SER b 177  GLN b 179 -1  O  GLN b 179   N  MET b 166           
SHEET    1   I 6 VAL b 377  ASP b 380  0                                        
SHEET    2   I 6 ILE b 369  THR b 371 -1  N  LEU b 370   O  ALA b 379           
SHEET    3   I 6 GLU b 353  VAL b 356 -1  N  PHE b 355   O  THR b 371           
SHEET    4   I 6 ILE b 336  ARG b 347 -1  N  PHE b 346   O  LEU b 354           
SHEET    5   I 6 THR b 398  TYR b 402 -1  O  TYR b 402   N  HIS b 343           
SHEET    6   I 6 THR b 410  PHE b 411 -1  O  PHE b 411   N  VAL b 399           
SHEET    1   J 5 VAL b 377  ASP b 380  0                                        
SHEET    2   J 5 ILE b 369  THR b 371 -1  N  LEU b 370   O  ALA b 379           
SHEET    3   J 5 GLU b 353  VAL b 356 -1  N  PHE b 355   O  THR b 371           
SHEET    4   J 5 ILE b 336  ARG b 347 -1  N  PHE b 346   O  LEU b 354           
SHEET    5   J 5 ILE b 429  ASP b 433 -1  O  GLU b 431   N  GLN b 338           
SHEET    1   K 2 LEU C 185  ASP C 187  0                                        
SHEET    2   K 2 ASP C 195  ARG C 197 -1  O  ASP C 195   N  ASP C 187           
SHEET    1   L 2 LEU C 341  ARG C 343  0                                        
SHEET    2   L 2 ILE C 349  PHE C 351 -1  O  ILE C 350   N  MET C 342           
SHEET    1   M 2 ARG C 370  GLY C 371  0                                        
SHEET    2   M 2 GLY C 374  LEU C 375 -1  O  GLY C 374   N  GLY C 371           
SHEET    1   N 2 LEU c 185  ASP c 187  0                                        
SHEET    2   N 2 ASP c 195  ARG c 197 -1  O  ASP c 195   N  ASP c 187           
SHEET    1   O 2 LEU c 341  ARG c 343  0                                        
SHEET    2   O 2 ILE c 349  PHE c 351 -1  O  ILE c 350   N  MET c 342           
SHEET    1   P 2 ARG c 370  GLY c 371  0                                        
SHEET    2   P 2 GLY c 374  LEU c 375 -1  O  GLY c 374   N  GLY c 371           
SHEET    1   Q 2 ALA D  77  VAL D  78  0                                        
SHEET    2   Q 2 PHE D 173  GLY D 174 -1  O  PHE D 173   N  VAL D  78           
SHEET    1   R 2 ALA d  77  VAL d  78  0                                        
SHEET    2   R 2 PHE d 173  GLY d 174 -1  O  PHE d 173   N  VAL d  78           
SHEET    1   S 2 TYR O  30  PRO O  31  0                                        
SHEET    2   S 2 SER O 135  ILE O 136 -1  O  ILE O 136   N  TYR O  30           
SHEET    1   T10 PHE O  65  PRO O  67  0                                        
SHEET    2   T10 TYR O  38  LYS O  53 -1  N  VAL O  52   O  VAL O  66           
SHEET    3   T10 GLU O 232  PRO O 245 -1  O  GLN O 236   N  THR O  48           
SHEET    4   T10 GLU O 210  LEU O 220 -1  N  ILE O 211   O  ALA O 241           
SHEET    5   T10 LEU O 192  ASP O 205 -1  N  ASN O 200   O  THR O 214           
SHEET    6   T10 ASP O 141  PRO O 149 -1  N  PHE O 142   O  LEU O 199           
SHEET    7   T10 VAL O 126  SER O 128 -1  N  SER O 128   O  LYS O 143           
SHEET    8   T10 LEU O  93  ILE O 101 -1  N  PHE O  95   O  ALA O 127           
SHEET    9   T10 LEU O  78  VAL O  87 -1  N  LYS O  86   O  THR O  94           
SHEET   10   T10 TYR O  38  LYS O  53 -1  N  LEU O  45   O  LEU O  78           
SHEET    1   U 3 LYS O  69  LEU O  70  0                                        
SHEET    2   U 3 PHE O 103  GLN O 109 -1  O  GLN O 109   N  LYS O  69           
SHEET    3   U 3 ARG O 115  THR O 121 -1  O  ILE O 116   N  VAL O 108           
SHEET    1   V 2 TYR o  30  PRO o  31  0                                        
SHEET    2   V 2 SER o 135  ILE o 136 -1  O  ILE o 136   N  TYR o  30           
SHEET    1   W10 PHE o  65  PRO o  67  0                                        
SHEET    2   W10 TYR o  38  LYS o  53 -1  N  VAL o  52   O  VAL o  66           
SHEET    3   W10 GLU o 232  PRO o 245 -1  O  GLN o 236   N  THR o  48           
SHEET    4   W10 GLU o 210  LEU o 220 -1  N  ILE o 211   O  ALA o 241           
SHEET    5   W10 LEU o 192  ASP o 205 -1  N  ASN o 200   O  THR o 214           
SHEET    6   W10 ASP o 141  PRO o 149 -1  N  PHE o 142   O  LEU o 199           
SHEET    7   W10 VAL o 126  SER o 128 -1  N  SER o 128   O  LYS o 143           
SHEET    8   W10 LEU o  93  ILE o 101 -1  N  PHE o  95   O  ALA o 127           
SHEET    9   W10 LEU o  78  VAL o  87 -1  N  LYS o  86   O  THR o  94           
SHEET   10   W10 TYR o  38  LYS o  53 -1  N  LEU o  45   O  LEU o  78           
SHEET    1   X 3 LYS o  69  LEU o  70  0                                        
SHEET    2   X 3 PHE o 103  GLN o 109 -1  O  GLN o 109   N  LYS o  69           
SHEET    3   X 3 ARG o 115  THR o 121 -1  O  ILE o 116   N  VAL o 108           
SHEET    1   Y 2 ILE U  25  ASP U  26  0                                        
SHEET    2   Y 2 PHE U  82  THR U  83  1  O  THR U  83   N  ILE U  25           
SHEET    1   Z 2 ILE u  25  ASP u  26  0                                        
SHEET    2   Z 2 PHE u  82  THR u  83  1  O  THR u  83   N  ILE u  25           
SHEET    1  AA 2 THR V   9  PRO V  11  0                                        
SHEET    2  AA 2 THR V  18  THR V  20 -1  O  ILE V  19   N  VAL V  10           
SHEET    1  AB 2 THR v   9  PRO v  11  0                                        
SHEET    2  AB 2 THR v  18  THR v  20 -1  O  ILE v  19   N  VAL v  10           
SSBOND   1 CYS O   19    CYS O   44                          1555   1555  2.05  
SSBOND   2 CYS o   19    CYS o   44                          1555   1555  2.05  
LINK         OE2 GLU A 189                MN1  OEX A 601     1555   1555  1.90  
LINK         OE2 GLU a 189                MN1  OEX a 601     1555   1555  1.90  
LINK         OXT ALA a 344                MN2  OEX a 601     1555   1555  1.99  
LINK         OXT ALA A 344                MN2  OEX A 601     1555   1555  1.99  
LINK         NE2 HIS v  41                FE   HEM v 201     1555   1555  2.05  
LINK         NE2 HIS V  41                FE   HEM V 201     1555   1555  2.05  
LINK         NE2 HIS e  23                FE   HEM f 101     1555   1555  2.06  
LINK         NE2 HIS E  23                FE   HEM F 101     1555   1555  2.06  
LINK         OE1 GLU a 333                MN3  OEX a 601     1555   1555  2.07  
LINK         OE1 GLU A 333                MN3  OEX A 601     1555   1555  2.07  
LINK         OE1 GLU c 354                MN2  OEX a 601     1555   1555  2.08  
LINK         OE1 GLU C 354                MN2  OEX A 601     1555   1555  2.08  
LINK         OD2 ASP a 170                MN4  OEX a 601     1555   1555  2.08  
LINK         OD2 ASP A 170                MN4  OEX A 601     1555   1555  2.08  
LINK         NE2 HIS f  24                FE   HEM f 101     1555   1555  2.10  
LINK         NE2 HIS F  24                FE   HEM F 101     1555   1555  2.10  
LINK         OD1 ASN c  39                MG   CLA c 511     1555   1555  2.11  
LINK         OD1 ASN C  39                MG   CLA C 511     1555   1555  2.11  
LINK         NE2 HIS D 214                FE   FE2 A 602     1555   1555  2.11  
LINK         NE2 HIS d 214                FE   FE2 a 602     1555   1555  2.11  
LINK         NE2 HIS V  92                FE   HEM V 201     1555   1555  2.13  
LINK         NE2 HIS v  92                FE   HEM v 201     1555   1555  2.13  
LINK         NE2 HIS A 332                MN1  OEX A 601     1555   1555  2.14  
LINK         NE2 HIS a 332                MN1  OEX a 601     1555   1555  2.14  
LINK         OD1 ASP A 342                MN2  OEX A 601     1555   1555  2.15  
LINK         OD1 ASP a 342                MN2  OEX a 601     1555   1555  2.15  
LINK         NE2 HIS A 215                FE   FE2 A 602     1555   1555  2.16  
LINK         NE2 HIS a 215                FE   FE2 a 602     1555   1555  2.16  
LINK         OE2 GLU a 333                MN4  OEX a 601     1555   1555  2.17  
LINK         OE2 GLU A 333                MN4  OEX A 601     1555   1555  2.17  
LINK         O   GLY j  31                MG    MG j 101     1555   1555  2.20  
LINK         O   GLY J  31                MG    MG J 101     1555   1555  2.20  
LINK         OE2 GLU C 354                MN3  OEX A 601     1555   1555  2.23  
LINK         OE2 GLU c 354                MN3  OEX a 601     1555   1555  2.23  
LINK         NE2 HIS A 272                FE   FE2 A 602     1555   1555  2.25  
LINK         NE2 HIS a 272                FE   FE2 a 602     1555   1555  2.25  
LINK        FE   FE2 a 602                 O1  BCT a 612     1555   1555  2.26  
LINK         O   ALA J  34                MG    MG J 101     1555   1555  2.26  
LINK        FE   FE2 A 602                 O2  BCT A 612     1555   1555  2.26  
LINK         OD2 ASP a 342                MN1  OEX a 601     1555   1555  2.26  
LINK         O   ALA j  34                MG    MG j 101     1555   1555  2.26  
LINK         OD2 ASP A 342                MN1  OEX A 601     1555   1555  2.26  
LINK        FE   FE2 a 602                 O2  BCT a 612     1555   1555  2.29  
LINK        FE   FE2 A 602                 O1  BCT A 612     1555   1555  2.29  
LINK         O   VAL O 201                CA    CA O 301     1555   1555  2.29  
LINK         O   VAL o 201                CA    CA o 301     1555   1555  2.29  
LINK         NE2 HIS D 268                FE   FE2 A 602     1555   1555  2.33  
LINK         NE2 HIS d 268                FE   FE2 a 602     1555   1555  2.34  
LINK         O   LEU j  36                MG    MG j 101     1555   1555  2.38  
LINK         O   LEU J  36                MG    MG J 101     1555   1555  2.38  
LINK         O4  LMG D 406                MG    MG J 101     1555   1555  2.39  
LINK         O4  LMG d 406                MG    MG j 101     1555   1555  2.39  
LINK         OD1 ASN o 200                CA    CA o 301     1555   1555  2.42  
LINK         OD1 ASN O 200                CA    CA O 301     1555   1555  2.42  
LINK         OD1 ASP a 170                CA1  OEX a 601     1555   1555  2.44  
LINK         OD1 ASP A 170                CA1  OEX A 601     1555   1555  2.44  
LINK         O   ALA A 344                CA1  OEX A 601     1555   1555  2.54  
LINK         O   ALA a 344                CA1  OEX a 601     1555   1555  2.54  
LINK         O   THR o 138                CA    CA o 301     1555   1555  2.55  
LINK         O   THR O 138                CA    CA O 301     1555   1555  2.55  
LINK         OXT ARG f  45                CA    CA f 102     1555   1555  2.58  
LINK         OXT ARG F  45                CA    CA F 102     1555   1555  2.58  
LINK         OD1 ASN b 438                CA    CA b 620     1555   1555  2.65  
LINK         OD1 ASN B 438                CA    CA B 621     1555   1555  2.65  
LINK         O   ARG F  45                CA    CA F 102     1555   1555  2.97  
LINK         O   ARG f  45                CA    CA f 102     1555   1555  2.97  
CISPEP   1 TYR U   42    PRO U   43          0         3.68                     
CISPEP   2 ALA U   53    PRO U   54          0         2.00                     
CISPEP   3 TYR u   42    PRO u   43          0         3.81                     
CISPEP   4 ALA u   53    PRO u   54          0         1.89                     
CISPEP   5 THR V   63    PRO V   64          0       -10.49                     
CISPEP   6 THR v   63    PRO v   64          0       -10.62                     
SITE     1 AC1 10 ASP A 170  VAL A 185  GLU A 189  HIS A 332                    
SITE     2 AC1 10 GLU A 333  HIS A 337  ASP A 342  ALA A 344                    
SITE     3 AC1 10 GLU C 354  ARG C 357                                          
SITE     1 AC2  5 HIS A 215  HIS A 272  BCT A 612  HIS D 214                    
SITE     2 AC2  5 HIS D 268                                                     
SITE     1 AC3 18 TYR A 147  PRO A 150  SER A 153  VAL A 157                    
SITE     2 AC3 18 MET A 183  PHE A 186  GLN A 187  ILE A 192                    
SITE     3 AC3 18 HIS A 198  GLY A 201  PHE A 206  ALA A 286                    
SITE     4 AC3 18 ALA A 287  ILE A 290  PHO A 605  CLA D 401                    
SITE     5 AC3 18 CLA D 402  PHE T  17                                          
SITE     1 AC4 15 GLN A 199  VAL A 202  ALA A 203  PHE A 206                    
SITE     2 AC4 15 GLY A 207  LEU A 210  TRP A 278  PHO A 606                    
SITE     3 AC4 15 DGD C 518  VAL D 175  ILE D 178  PHE D 179                    
SITE     4 AC4 15 LEU D 182  CLA D 401  LMG D 406                               
SITE     1 AC5 19 LEU A  41  ALA A  44  THR A  45  PHE A  48                    
SITE     2 AC5 19 TYR A 126  GLN A 130  ALA A 146  TYR A 147                    
SITE     3 AC5 19 PRO A 150  GLY A 175  PRO A 279  CLA A 603                    
SITE     4 AC5 19 LEU D 205  ALA D 208  LEU D 209  ILE D 213                    
SITE     5 AC5 19 TRP D 253  PHE D 257  CLA D 402                               
SITE     1 AC6 22 PHE A 206  ALA A 209  LEU A 210  MET A 214                    
SITE     2 AC6 22 LEU A 258  CLA A 604  PL9 A 613  ALA D  41                    
SITE     3 AC6 22 TRP D  48  ILE D 114  GLY D 121  LEU D 122                    
SITE     4 AC6 22 PHE D 125  GLN D 129  ASN D 142  PHE D 146                    
SITE     5 AC6 22 PRO D 149  PHE D 153  GLY D 174  PRO D 275                    
SITE     6 AC6 22 LEU D 279  CLA D 401                                          
SITE     1 AC7 12 ILE A  36  THR A  40  PHE A  93  PRO A  95                    
SITE     2 AC7 12 ILE A  96  TRP A  97  LEU A 114  HIS A 118                    
SITE     3 AC7 12 VAL I   8  TYR I   9  VAL I  12  PHE I  15                    
SITE     1 AC8  2 ALA A  43  ILE A  96                                          
SITE     1 AC9 15 LEU A 200  GLY A 204  ASN A 267  SER A 270                    
SITE     2 AC9 15 PHE A 273  PHE A 274  TRP A 278  GLN C  28                    
SITE     3 AC9 15 ALA C  34  TRP C  36  CLA C 508  PHE D 232                    
SITE     4 AC9 15 ARG D 233  LHG D 409  PHE K  37                               
SITE     1 BC1  4 ASN A 181  HIS A 332  GLU A 333  LYS D 317                    
SITE     1 BC2  3 ASN A 338  PHE A 339  GLU C 354                               
SITE     1 BC3  8 HIS A 215  GLU A 244  TYR A 246  HIS A 272                    
SITE     2 BC3  8 FE2 A 602  HIS D 214  TYR D 244  HIS D 268                    
SITE     1 BC4 15 PHE A 211  MET A 214  HIS A 215  LEU A 218                    
SITE     2 BC4 15 HIS A 252  PHE A 255  SER A 264  PHE A 265                    
SITE     3 BC4 15 LEU A 271  PHE A 274  PHO A 606  PRO D  39                    
SITE     4 BC4 15 THR F  25  LEU F  26  THR X  24                               
SITE     1 BC5 15 PHE A  93  TRP A  97  GLU A  98  LEU A 121                    
SITE     2 BC5 15 SER A 124  PHE A 155  LEU C 214  LYS C 215                    
SITE     3 BC5 15 SER C 216  PHE C 218  GLU C 221  TRP C 223                    
SITE     4 BC5 15 CLA C 505  LYS I   5  TYR I   9                               
SITE     1 BC6 10 ASP a 170  VAL a 185  GLU a 189  HIS a 332                    
SITE     2 BC6 10 GLU a 333  HIS a 337  ASP a 342  ALA a 344                    
SITE     3 BC6 10 GLU c 354  ARG c 357                                          
SITE     1 BC7  5 HIS a 215  HIS a 272  BCT a 612  HIS d 214                    
SITE     2 BC7  5 HIS d 268                                                     
SITE     1 BC8 18 TYR a 147  PRO a 150  SER a 153  VAL a 157                    
SITE     2 BC8 18 MET a 183  PHE a 186  GLN a 187  ILE a 192                    
SITE     3 BC8 18 HIS a 198  GLY a 201  PHE a 206  ALA a 286                    
SITE     4 BC8 18 ALA a 287  ILE a 290  PHO a 605  CLA d 401                    
SITE     5 BC8 18 CLA d 402  PHE t  17                                          
SITE     1 BC9 15 GLN a 199  VAL a 202  ALA a 203  PHE a 206                    
SITE     2 BC9 15 GLY a 207  LEU a 210  TRP a 278  PHO a 606                    
SITE     3 BC9 15 DGD c 518  VAL d 175  ILE d 178  PHE d 179                    
SITE     4 BC9 15 LEU d 182  CLA d 401  LMG d 406                               
SITE     1 CC1 19 LEU a  41  ALA a  44  THR a  45  PHE a  48                    
SITE     2 CC1 19 TYR a 126  GLN a 130  ALA a 146  TYR a 147                    
SITE     3 CC1 19 PRO a 150  GLY a 175  PRO a 279  CLA a 603                    
SITE     4 CC1 19 LEU d 205  ALA d 208  LEU d 209  ILE d 213                    
SITE     5 CC1 19 TRP d 253  PHE d 257  CLA d 402                               
SITE     1 CC2 22 PHE a 206  ALA a 209  LEU a 210  MET a 214                    
SITE     2 CC2 22 LEU a 258  CLA a 604  PL9 a 613  ALA d  41                    
SITE     3 CC2 22 TRP d  48  ILE d 114  GLY d 121  LEU d 122                    
SITE     4 CC2 22 PHE d 125  GLN d 129  ASN d 142  PHE d 146                    
SITE     5 CC2 22 PRO d 149  PHE d 153  GLY d 174  PRO d 275                    
SITE     6 CC2 22 LEU d 279  CLA d 401                                          
SITE     1 CC3 12 ILE a  36  THR a  40  PHE a  93  PRO a  95                    
SITE     2 CC3 12 ILE a  96  TRP a  97  LEU a 114  HIS a 118                    
SITE     3 CC3 12 VAL i   8  TYR i   9  VAL i  12  PHE i  15                    
SITE     1 CC4  2 ALA a  43  ILE a  96                                          
SITE     1 CC5 15 LEU a 200  GLY a 204  ASN a 267  SER a 270                    
SITE     2 CC5 15 PHE a 273  PHE a 274  TRP a 278  GLN c  28                    
SITE     3 CC5 15 ALA c  34  TRP c  36  CLA c 508  PHE d 232                    
SITE     4 CC5 15 ARG d 233  LHG d 409  PHE k  37                               
SITE     1 CC6  4 ASN a 181  HIS a 332  GLU a 333  LYS d 317                    
SITE     1 CC7  3 ASN a 338  PHE a 339  GLU c 354                               
SITE     1 CC8  8 HIS a 215  GLU a 244  TYR a 246  HIS a 272                    
SITE     2 CC8  8 FE2 a 602  HIS d 214  TYR d 244  HIS d 268                    
SITE     1 CC9 15 PHE a 211  MET a 214  HIS a 215  LEU a 218                    
SITE     2 CC9 15 HIS a 252  PHE a 255  SER a 264  PHE a 265                    
SITE     3 CC9 15 LEU a 271  PHE a 274  PHO a 606  PRO d  39                    
SITE     4 CC9 15 THR f  25  LEU f  26  THR x  24                               
SITE     1 DC1 15 PHE a  93  TRP a  97  GLU a  98  LEU a 121                    
SITE     2 DC1 15 SER a 124  PHE a 155  LEU c 214  LYS c 215                    
SITE     3 DC1 15 SER c 216  PHE c 218  GLU c 221  TRP c 223                    
SITE     4 DC1 15 CLA c 505  LYS i   5  TYR i   9                               
SITE     1 DC2 14 VAL B 102  TRP B 113  TYR B 117  CLA B 607                    
SITE     2 DC2 14 BCR B 622  TRP a  20  ASN a  26  ARG a  27                    
SITE     3 DC2 14 LEU a  28  ILE a  38  THR a  45  CLA d 402                    
SITE     4 DC2 14 PHE t  22  BCR t 101                                          
SITE     1 DC3  6 TRP B 185  GLY B 186  PHE B 190  CLA B 603                    
SITE     2 DC3  6 PHE H  41  BCR H 101                                          
SITE     1 DC4 15 GLY B 189  PHE B 190  GLY B 197  ALA B 200                    
SITE     2 DC4 15 HIS B 201  ALA B 204  VAL B 208  PHE B 250                    
SITE     3 DC4 15 CLA B 602  CLA B 604  CLA B 606  PHE H  38                    
SITE     4 DC4 15 PHE H  41  LEU H  46  TYR H  49                               
SITE     1 DC5 16 ARG B  68  LEU B  69  ALA B 146  LEU B 149                    
SITE     2 DC5 16 PHE B 153  HIS B 201  HIS B 202  PHE B 247                    
SITE     3 DC5 16 ALA B 248  VAL B 252  THR B 262  CLA B 603                    
SITE     4 DC5 16 CLA B 605  CLA B 606  CLA B 607  CLA B 611                    
SITE     1 DC6 18 TRP B  33  PHE B  61  PHE B  65  ARG B  68                    
SITE     2 DC6 18 LEU B 149  VAL B 245  ALA B 248  ALA B 249                    
SITE     3 DC6 18 VAL B 252  PHE B 451  HIS B 455  PHE B 458                    
SITE     4 DC6 18 PHE B 462  CLA B 604  CLA B 606  CLA B 608                    
SITE     5 DC6 18 CLA B 613  CLA B 614                                          
SITE     1 DC7 22 THR B  27  VAL B  30  TRP B  33  ALA B  34                    
SITE     2 DC7 22 VAL B  62  PHE B  65  MET B  66  ARG B  68                    
SITE     3 DC7 22 LEU B  69  VAL B  96  HIS B 100  LEU B 103                    
SITE     4 DC7 22 ALA B 205  CLA B 603  CLA B 604  CLA B 605                    
SITE     5 DC7 22 CLA B 607  CLA B 610  CLA B 611  CLA B 613                    
SITE     6 DC7 22 CLA B 616  BCR t 101                                          
SITE     1 DC8 15 LEU B  69  GLY B  70  TRP B  91  HIS B 100                    
SITE     2 DC8 15 VAL B 102  GLY B 152  PHE B 153  HIS B 157                    
SITE     3 DC8 15 PHE B 162  GLY B 163  PRO B 164  SQD B 601                    
SITE     4 DC8 15 CLA B 604  CLA B 606  BCR t 101                               
SITE     1 DC9 17 TRP B  33  TYR B  40  GLN B  58  GLY B  59                    
SITE     2 DC9 17 PHE B  61  LEU B 324  PHE B 325  THR B 327                    
SITE     3 DC9 17 GLY B 328  PRO B 329  TRP B 450  ALA B 454                    
SITE     4 DC9 17 CLA B 605  CLA B 614  BCR B 619  LMG B 620                    
SITE     5 DC9 17 PHE M  14                                                     
SITE     1 EC1 15 LEU B 229  THR B 236  SER B 239  SER B 240                    
SITE     2 EC1 15 ALA B 243  PHE B 463  HIS B 466  ILE B 467                    
SITE     3 EC1 15 THR B 473  CLA B 611  PHE D 120  ILE D 123                    
SITE     4 EC1 15 MET D 126  LEU D 127  ILE D 150                               
SITE     1 EC2 15 PHE B 139  VAL B 208  ALA B 212  PHE B 215                    
SITE     2 EC2 15 HIS B 216  VAL B 219  PRO B 221  PRO B 222                    
SITE     3 EC2 15 LEU B 229  CLA B 606  CLA B 611  THR H  27                    
SITE     4 EC2 15 MET H  31  PHE H  34  BCR H 101                               
SITE     1 EC3 15 LEU B 135  PHE B 139  HIS B 142  LEU B 143                    
SITE     2 EC3 15 ALA B 146  MET B 231  VAL B 237  SER B 240                    
SITE     3 EC3 15 SER B 241  CLA B 604  CLA B 606  CLA B 609                    
SITE     4 EC3 15 CLA B 610  CLA B 613  CLA B 616                               
SITE     1 EC4 17 TRP B   5  TYR B   6  ARG B   7  VAL B   8                    
SITE     2 EC4 17 HIS B   9  THR B  10  ILE B 242  LEU B 461                    
SITE     3 EC4 17 PHE B 462  GLY B 465  TRP B 468  HIS B 469                    
SITE     4 EC4 17 ARG B 472  CLA B 613  CLA B 614  CLA B 615                    
SITE     5 EC4 17 LHG D 405                                                     
SITE     1 EC5 16 HIS B   9  LEU B  19  HIS B  23  HIS B  26                    
SITE     2 EC5 16 THR B  27  ILE B 234  VAL B 237  LEU B 238                    
SITE     3 EC5 16 SER B 241  CLA B 605  CLA B 606  CLA B 611                    
SITE     4 EC5 16 CLA B 612  CLA B 614  CLA B 615  CLA B 616                    
SITE     1 EC6 13 HIS B   9  HIS B  26  VAL B  30  TRP B  33                    
SITE     2 EC6 13 PHE B 462  CLA B 605  CLA B 608  CLA B 612                    
SITE     3 EC6 13 CLA B 613  CLA B 615  BCR B 618  BCR B 619                    
SITE     4 EC6 13 LMG B 620                                                     
SITE     1 EC7 18 VAL B   8  HIS B   9  VAL B  11  ALA B  22                    
SITE     2 EC7 18 MET B  25  LEU B  29  TRP B 115  CLA B 612                    
SITE     3 EC7 18 CLA B 613  CLA B 614  BCR B 618  LMG B 620                    
SITE     4 EC7 18 VAL L  10  PHE M  21  LEU M  25  SQD l 101                    
SITE     5 EC7 18 SQD l 102  PHE t   8                                          
SITE     1 EC8 12 ILE B  20  HIS B  23  LEU B  24  MET B 138                    
SITE     2 EC8 12 HIS B 142  LEU B 145  CLA B 606  CLA B 611                    
SITE     3 EC8 12 CLA B 613  CLA B 617  LEU H  14  ASN H  15                    
SITE     1 EC9  8 LEU B  24  TRP B 113  HIS B 114  CLA B 616                    
SITE     2 EC9  8 THR H   5  LEU H   7  GLY H   8  BCR t 101                    
SITE     1 FC1  9 MET B  25  LEU B  29  CLA B 614  CLA B 615                    
SITE     2 FC1  9 BCR B 619  LMG B 620  BCR B 622  SQD l 102                    
SITE     3 FC1  9 PHE t  19                                                     
SITE     1 FC2 10 LEU B  29  GLY B  32  TRP B  33  SER B  36                    
SITE     2 FC2 10 VAL B 102  GLY B 105  CLA B 608  CLA B 614                    
SITE     3 FC2 10 BCR B 618  BCR B 622                                          
SITE     1 FC3 13 TYR B  40  THR B 327  GLY B 328  PRO B 329                    
SITE     2 FC3 13 LYS B 332  CLA B 608  CLA B 614  CLA B 615                    
SITE     3 FC3 13 BCR B 618  ILE D 284  PHE L  35  ASN M   4                    
SITE     4 FC3 13 ALA M  10                                                     
SITE     1 FC4  1 ASN B 438                                                     
SITE     1 FC5  9 TRP B  33  MET B  37  LEU B 109  SQD B 601                    
SITE     2 FC5  9 BCR B 618  BCR B 619  LEU a  28  SQD l 101                    
SITE     3 FC5  9 PHE t  18                                                     
SITE     1 FC6 14 TRP A  20  ASN A  26  ARG A  27  LEU A  28                    
SITE     2 FC6 14 ILE A  38  THR A  45  CLA D 402  PHE T  22                    
SITE     3 FC6 14 BCR T 102  VAL b 102  TRP b 113  TYR b 117                    
SITE     4 FC6 14 CLA b 607  BCR b 622                                          
SITE     1 FC7  6 TRP b 185  GLY b 186  PHE b 190  CLA b 603                    
SITE     2 FC7  6 PHE h  41  BCR h 101                                          
SITE     1 FC8 15 GLY b 189  PHE b 190  GLY b 197  ALA b 200                    
SITE     2 FC8 15 HIS b 201  ALA b 204  VAL b 208  PHE b 250                    
SITE     3 FC8 15 CLA b 602  CLA b 604  CLA b 606  PHE h  38                    
SITE     4 FC8 15 PHE h  41  LEU h  46  TYR h  49                               
SITE     1 FC9 16 ARG b  68  LEU b  69  ALA b 146  LEU b 149                    
SITE     2 FC9 16 PHE b 153  HIS b 201  HIS b 202  PHE b 247                    
SITE     3 FC9 16 ALA b 248  VAL b 252  THR b 262  CLA b 603                    
SITE     4 FC9 16 CLA b 605  CLA b 606  CLA b 607  CLA b 611                    
SITE     1 GC1 18 TRP b  33  PHE b  61  PHE b  65  ARG b  68                    
SITE     2 GC1 18 LEU b 149  VAL b 245  ALA b 248  ALA b 249                    
SITE     3 GC1 18 VAL b 252  PHE b 451  HIS b 455  PHE b 458                    
SITE     4 GC1 18 PHE b 462  CLA b 604  CLA b 606  CLA b 608                    
SITE     5 GC1 18 CLA b 613  CLA b 614                                          
SITE     1 GC2 22 BCR T 102  THR b  27  VAL b  30  TRP b  33                    
SITE     2 GC2 22 ALA b  34  VAL b  62  PHE b  65  MET b  66                    
SITE     3 GC2 22 ARG b  68  LEU b  69  VAL b  96  HIS b 100                    
SITE     4 GC2 22 LEU b 103  ALA b 205  CLA b 603  CLA b 604                    
SITE     5 GC2 22 CLA b 605  CLA b 607  CLA b 610  CLA b 611                    
SITE     6 GC2 22 CLA b 613  CLA b 616                                          
SITE     1 GC3 15 BCR T 102  LEU b  69  GLY b  70  TRP b  91                    
SITE     2 GC3 15 HIS b 100  VAL b 102  GLY b 152  PHE b 153                    
SITE     3 GC3 15 HIS b 157  PHE b 162  GLY b 163  PRO b 164                    
SITE     4 GC3 15 SQD b 601  CLA b 604  CLA b 606                               
SITE     1 GC4 18 TRP b  33  TYR b  40  GLN b  58  GLY b  59                    
SITE     2 GC4 18 PHE b  61  LEU b 324  PHE b 325  THR b 327                    
SITE     3 GC4 18 GLY b 328  PRO b 329  TRP b 450  ALA b 454                    
SITE     4 GC4 18 CLA b 605  CLA b 614  BCR b 618  LMG b 619                    
SITE     5 GC4 18 BCR b 622  PHE m  14                                          
SITE     1 GC5 15 LEU b 229  THR b 236  SER b 239  SER b 240                    
SITE     2 GC5 15 ALA b 243  PHE b 463  HIS b 466  ILE b 467                    
SITE     3 GC5 15 THR b 473  CLA b 611  PHE d 120  ILE d 123                    
SITE     4 GC5 15 MET d 126  LEU d 127  ILE d 150                               
SITE     1 GC6 15 PHE b 139  VAL b 208  ALA b 212  PHE b 215                    
SITE     2 GC6 15 HIS b 216  VAL b 219  PRO b 221  PRO b 222                    
SITE     3 GC6 15 LEU b 229  CLA b 606  CLA b 611  THR h  27                    
SITE     4 GC6 15 MET h  31  PHE h  34  BCR h 101                               
SITE     1 GC7 15 LEU b 135  PHE b 139  HIS b 142  LEU b 143                    
SITE     2 GC7 15 ALA b 146  MET b 231  VAL b 237  SER b 240                    
SITE     3 GC7 15 SER b 241  CLA b 604  CLA b 606  CLA b 609                    
SITE     4 GC7 15 CLA b 610  CLA b 613  CLA b 616                               
SITE     1 GC8 17 TRP b   5  TYR b   6  ARG b   7  VAL b   8                    
SITE     2 GC8 17 HIS b   9  THR b  10  ILE b 242  LEU b 461                    
SITE     3 GC8 17 PHE b 462  GLY b 465  TRP b 468  HIS b 469                    
SITE     4 GC8 17 ARG b 472  CLA b 613  CLA b 614  CLA b 615                    
SITE     5 GC8 17 LHG d 405                                                     
SITE     1 GC9 16 HIS b   9  LEU b  19  HIS b  23  HIS b  26                    
SITE     2 GC9 16 THR b  27  ILE b 234  VAL b 237  LEU b 238                    
SITE     3 GC9 16 SER b 241  CLA b 605  CLA b 606  CLA b 611                    
SITE     4 GC9 16 CLA b 612  CLA b 614  CLA b 615  CLA b 616                    
SITE     1 HC1 13 BCR T 101  HIS b   9  HIS b  26  VAL b  30                    
SITE     2 HC1 13 TRP b  33  PHE b 462  CLA b 605  CLA b 608                    
SITE     3 HC1 13 CLA b 612  CLA b 613  CLA b 615  BCR b 618                    
SITE     4 HC1 13 LMG b 619                                                     
SITE     1 HC2 18 SQD L 101  PHE T   8  BCR T 101  VAL b   8                    
SITE     2 HC2 18 HIS b   9  VAL b  11  ALA b  22  MET b  25                    
SITE     3 HC2 18 LEU b  29  TRP b 115  CLA b 612  CLA b 613                    
SITE     4 HC2 18 CLA b 614  LMG b 619  SQD b 621  VAL l  10                    
SITE     5 HC2 18 PHE m  21  LEU m  25                                          
SITE     1 HC3 12 ILE b  20  HIS b  23  LEU b  24  MET b 138                    
SITE     2 HC3 12 HIS b 142  LEU b 145  CLA b 606  CLA b 611                    
SITE     3 HC3 12 CLA b 613  CLA b 617  LEU h  14  ASN h  15                    
SITE     1 HC4  8 BCR T 102  LEU b  24  TRP b 113  HIS b 114                    
SITE     2 HC4  8 CLA b 616  THR h   5  LEU h   7  GLY h   8                    
SITE     1 HC5 10 BCR T 101  LEU b  29  GLY b  32  TRP b  33                    
SITE     2 HC5 10 SER b  36  VAL b 102  GLY b 105  CLA b 608                    
SITE     3 HC5 10 CLA b 614  BCR b 622                                          
SITE     1 HC6 13 BCR T 101  TYR b  40  THR b 327  GLY b 328                    
SITE     2 HC6 13 PRO b 329  LYS b 332  CLA b 608  CLA b 614                    
SITE     3 HC6 13 CLA b 615  ILE d 284  PHE l  35  ASN m   4                    
SITE     4 HC6 13 ALA m  10                                                     
SITE     1 HC7  1 ASN b 438                                                     
SITE     1 HC8 13 ARG L  14  TYR L  18  SQD L 101  CYS T  12                    
SITE     2 HC8 13 PHE T  19  PHE T  23  BCR T 101  ARG b  18                    
SITE     3 HC8 13 LEU b  29  SER b 104  TRP b 115  CLA b 615                    
SITE     4 HC8 13 ARG l   7                                                     
SITE     1 HC9 10 LEU A  28  SQD L 101  PHE T  18  TRP b  33                    
SITE     2 HC9 10 MET b  37  TYR b  40  LEU b 109  SQD b 601                    
SITE     3 HC9 10 CLA b 608  BCR b 618                                          
SITE     1 IC1 18 LEU C  95  LEU C 168  GLY C 171  ALA C 172                    
SITE     2 IC1 18 LEU C 175  ILE C 224  VAL C 233  HIS C 237                    
SITE     3 IC1 18 ILE C 240  ALA C 278  MET C 282  PHE C 289                    
SITE     4 IC1 18 TYR C 297  CLA C 502  CLA C 503  CLA C 506                    
SITE     5 IC1 18 CLA C 507  BCR C 515                                          
SITE     1 IC2 14 TRP C  63  HIS C  91  LEU C 279  MET C 282                    
SITE     2 IC2 14 ALA C 286  VAL C 290  TYR C 297  HIS C 430                    
SITE     3 IC2 14 LEU C 433  PHE C 437  CLA C 501  CLA C 503                    
SITE     4 IC2 14 CLA C 504  CLA C 510                                          
SITE     1 IC3 13 ILE C  60  VAL C  61  ALA C  64  THR C  68                    
SITE     2 IC3 13 LEU C  88  HIS C  91  VAL C 114  HIS C 118                    
SITE     3 IC3 13 CLA C 501  CLA C 502  CLA C 509  CLA C 512                    
SITE     4 IC3 13 LMG C 520                                                     
SITE     1 IC4 18 TRP C  63  MET C  67  PHE C  70  GLN C  84                    
SITE     2 IC4 18 GLY C  85  ILE C  87  TRP C 425  SER C 429                    
SITE     3 IC4 18 PHE C 436  CLA C 502  CLA C 508  CLA C 510                    
SITE     4 IC4 18 DGD C 517  DGD C 518  LMG C 519  LHG D 409                    
SITE     5 IC4 18 PRO K  26  VAL K  30                                          
SITE     1 IC5 16 PHE A  33  MET A 127  GLY A 128  TRP A 131                    
SITE     2 IC5 16 LMG A 614  PHE C 264  SER C 273  TYR C 274                    
SITE     3 IC5 16 GLY C 277  ALA C 278  HIS C 441  LEU C 442                    
SITE     4 IC5 16 ALA C 445  ARG C 449  CLA C 507  BCR C 515                    
SITE     1 IC6 16 LEU C 161  LEU C 165  LEU C 213  ILE C 243                    
SITE     2 IC6 16 GLY C 247  TRP C 250  HIS C 251  THR C 254                    
SITE     3 IC6 16 THR C 255  PRO C 256  PHE C 257  TRP C 259                    
SITE     4 IC6 16 PHE C 264  CLA C 501  CLA C 507  BCR C 515                    
SITE     1 IC7 17 MET C 157  THR C 158  LEU C 161  HIS C 164                    
SITE     2 IC7 17 LEU C 168  TRP C 259  PHE C 264  TRP C 266                    
SITE     3 IC7 17 TYR C 271  TYR C 274  SER C 275  MET C 282                    
SITE     4 IC7 17 CLA C 501  CLA C 505  CLA C 506  CLA C 509                    
SITE     5 IC7 17 BCR C 515                                                     
SITE     1 IC8 20 SQD A 609  TRP C  36  ALA C  37  GLY C  38                    
SITE     2 IC8 20 ASN C  39  ALA C  40  GLU C 269  LEU C 272                    
SITE     3 IC8 20 LEU C 276  PHE C 436  PHE C 437  GLY C 440                    
SITE     4 IC8 20 TRP C 443  HIS C 444  ARG C 447  CLA C 504                    
SITE     5 IC8 20 CLA C 509  CLA C 510  CLA C 511  LHG D 409                    
SITE     1 IC9 16 ASN C  39  LEU C  49  ALA C  52  HIS C  53                    
SITE     2 IC9 16 HIS C  56  TYR C 149  GLY C 268  GLU C 269                    
SITE     3 IC9 16 TYR C 271  LEU C 272  SER C 275  CLA C 503                    
SITE     4 IC9 16 CLA C 507  CLA C 508  CLA C 510  CLA C 511                    
SITE     1 JC1 15 ASN C  39  HIS C  56  LEU C  59  TRP C  63                    
SITE     2 JC1 15 LEU C 279  PHE C 436  PHE C 437  CLA C 502                    
SITE     3 JC1 15 CLA C 504  CLA C 508  CLA C 509  CLA C 511                    
SITE     4 JC1 15 LHG D 409  PRO K  29  LEU K  33                               
SITE     1 JC2 27 THR C  24  ARG C  26  TRP C  35  GLY C  38                    
SITE     2 JC2 27 ASN C  39  ARG C  41  LEU C  42  LEU C  45                    
SITE     3 JC2 27 LYS C  48  ALA C  52  PHE C 127  ILE C 134                    
SITE     4 JC2 27 CLA C 508  CLA C 509  CLA C 510  PHE K  32                    
SITE     5 JC2 27 LEU K  33  ALA K  36  TRP K  39  GLN K  40                    
SITE     6 JC2 27 BCR K 102  ILE Y  36  ASN Y  45  LEU Y  46                    
SITE     7 JC2 27 VAL Z  20  VAL Z  23  ALA Z  28                               
SITE     1 JC3 12 HIS C  53  ALA C  57  LEU C 125  PHE C 146                    
SITE     2 JC3 12 PHE C 147  PHE C 163  HIS C 164  VAL C 167                    
SITE     3 JC3 12 GLY C 171  CLA C 503  CLA C 513  BCR C 514                    
SITE     1 JC4 11 LEU C  50  VAL C 124  GLY C 128  TYR C 131                    
SITE     2 JC4 11 HIS C 132  PRO C 137  TYR C 143  PHE C 147                    
SITE     3 JC4 11 CLA C 512  BCR C 514  LMG Z 101                               
SITE     1 JC5 11 PHE C 112  VAL C 116  SER C 121  VAL C 124                    
SITE     2 JC5 11 PHE C 147  CLA C 512  CLA C 513  LMG C 520                    
SITE     3 JC5 11 TYR K  15  VAL Z  51  GLY Z  55                               
SITE     1 JC6 10 ILE C 209  ILE C 224  GLY C 236  HIS C 237                    
SITE     2 JC6 10 PHE C 264  CLA C 501  CLA C 505  CLA C 506                    
SITE     3 JC6 10 CLA C 507  PHE I  23                                          
SITE     1 JC7 18 LEU A  91  ILE A 163  PRO C 217  GLY C 219                    
SITE     2 JC7 18 GLY C 220  GLU C 221  GLY C 222  TRP C 223                    
SITE     3 JC7 18 VAL C 227  PHE C 284  CYS C 288  PHE C 292                    
SITE     4 JC7 18 ASN C 293  ASN C 294  THR C 295  ASP C 360                    
SITE     5 JC7 18 PHE C 361  ARG C 362                                          
SITE     1 JC8 17 HIS A 195  PHE A 197  LEU A 297  GLU C  83                    
SITE     2 JC8 17 GLN C  84  GLY C  85  LEU C 404  SER C 406                    
SITE     3 JC8 17 ASN C 418  PHE C 419  VAL C 420  TRP C 425                    
SITE     4 JC8 17 CLA C 504  DGD C 518  LMG C 519  PHE J  29                    
SITE     5 JC8 17 TYR J  33                                                     
SITE     1 JC9 19 GLN A 199  PHE A 300  ASN A 301  PHE A 302                    
SITE     2 JC9 19 SER A 305  CLA A 604  ASN C 405  VAL C 407                    
SITE     3 JC9 19 ASN C 415  SER C 416  ASN C 418  CLA C 504                    
SITE     4 JC9 19 DGD C 517  PHE J  29  ALA J  32  TYR J  33                    
SITE     5 JC9 19 GLY J  37  SER J  38  SER J  39                               
SITE     1 KC1  4 HIS C  74  CLA C 504  DGD C 517  ASP K  23                    
SITE     1 KC2  9 TRP C  97  ASP C 107  PHE C 109  HIS C 118                    
SITE     2 KC2  9 SER C 121  CLA C 503  BCR C 514  PHE Z  59                    
SITE     3 KC2  9 VAL Z  62                                                     
SITE     1 KC3 18 LEU c  95  LEU c 168  GLY c 171  ALA c 172                    
SITE     2 KC3 18 LEU c 175  ILE c 224  VAL c 233  HIS c 237                    
SITE     3 KC3 18 ILE c 240  ALA c 278  MET c 282  PHE c 289                    
SITE     4 KC3 18 TYR c 297  CLA c 502  CLA c 503  CLA c 506                    
SITE     5 KC3 18 CLA c 507  BCR c 515                                          
SITE     1 KC4 14 TRP c  63  HIS c  91  LEU c 279  MET c 282                    
SITE     2 KC4 14 ALA c 286  VAL c 290  TYR c 297  HIS c 430                    
SITE     3 KC4 14 LEU c 433  PHE c 437  CLA c 501  CLA c 503                    
SITE     4 KC4 14 CLA c 504  CLA c 510                                          
SITE     1 KC5 13 ILE c  60  VAL c  61  ALA c  64  THR c  68                    
SITE     2 KC5 13 LEU c  88  HIS c  91  VAL c 114  HIS c 118                    
SITE     3 KC5 13 CLA c 501  CLA c 502  CLA c 509  CLA c 512                    
SITE     4 KC5 13 LMG c 520                                                     
SITE     1 KC6 18 TRP c  63  MET c  67  PHE c  70  GLN c  84                    
SITE     2 KC6 18 GLY c  85  ILE c  87  TRP c 425  SER c 429                    
SITE     3 KC6 18 PHE c 436  CLA c 502  CLA c 508  CLA c 510                    
SITE     4 KC6 18 DGD c 517  DGD c 518  LMG c 519  LHG d 409                    
SITE     5 KC6 18 PRO k  26  VAL k  30                                          
SITE     1 KC7 16 PHE a  33  MET a 127  GLY a 128  TRP a 131                    
SITE     2 KC7 16 LMG a 614  PHE c 264  SER c 273  TYR c 274                    
SITE     3 KC7 16 GLY c 277  ALA c 278  HIS c 441  LEU c 442                    
SITE     4 KC7 16 ALA c 445  ARG c 449  CLA c 507  BCR c 515                    
SITE     1 KC8 16 LEU c 161  LEU c 165  LEU c 213  ILE c 243                    
SITE     2 KC8 16 GLY c 247  TRP c 250  HIS c 251  THR c 254                    
SITE     3 KC8 16 THR c 255  PRO c 256  PHE c 257  TRP c 259                    
SITE     4 KC8 16 PHE c 264  CLA c 501  CLA c 507  BCR c 515                    
SITE     1 KC9 17 MET c 157  THR c 158  LEU c 161  HIS c 164                    
SITE     2 KC9 17 LEU c 168  TRP c 259  PHE c 264  TRP c 266                    
SITE     3 KC9 17 TYR c 271  TYR c 274  SER c 275  MET c 282                    
SITE     4 KC9 17 CLA c 501  CLA c 505  CLA c 506  CLA c 509                    
SITE     5 KC9 17 BCR c 515                                                     
SITE     1 LC1 20 SQD a 609  TRP c  36  ALA c  37  GLY c  38                    
SITE     2 LC1 20 ASN c  39  ALA c  40  GLU c 269  LEU c 272                    
SITE     3 LC1 20 LEU c 276  PHE c 436  PHE c 437  GLY c 440                    
SITE     4 LC1 20 TRP c 443  HIS c 444  ARG c 447  CLA c 504                    
SITE     5 LC1 20 CLA c 509  CLA c 510  CLA c 511  LHG d 409                    
SITE     1 LC2 16 ASN c  39  LEU c  49  ALA c  52  HIS c  53                    
SITE     2 LC2 16 HIS c  56  TYR c 149  GLY c 268  GLU c 269                    
SITE     3 LC2 16 TYR c 271  LEU c 272  SER c 275  CLA c 503                    
SITE     4 LC2 16 CLA c 507  CLA c 508  CLA c 510  CLA c 511                    
SITE     1 LC3 15 ASN c  39  HIS c  56  LEU c  59  TRP c  63                    
SITE     2 LC3 15 LEU c 279  PHE c 436  PHE c 437  CLA c 502                    
SITE     3 LC3 15 CLA c 504  CLA c 508  CLA c 509  CLA c 511                    
SITE     4 LC3 15 LHG d 409  PRO k  29  LEU k  33                               
SITE     1 LC4 27 THR c  24  ARG c  26  TRP c  35  GLY c  38                    
SITE     2 LC4 27 ASN c  39  ARG c  41  LEU c  42  LEU c  45                    
SITE     3 LC4 27 LYS c  48  ALA c  52  PHE c 127  ILE c 134                    
SITE     4 LC4 27 CLA c 508  CLA c 509  CLA c 510  PHE k  32                    
SITE     5 LC4 27 LEU k  33  ALA k  36  TRP k  39  GLN k  40                    
SITE     6 LC4 27 BCR k 102  ILE y  36  ASN y  45  LEU y  46                    
SITE     7 LC4 27 VAL z  20  VAL z  23  ALA z  28                               
SITE     1 LC5 12 HIS c  53  ALA c  57  LEU c 125  PHE c 146                    
SITE     2 LC5 12 PHE c 147  PHE c 163  HIS c 164  VAL c 167                    
SITE     3 LC5 12 GLY c 171  CLA c 503  CLA c 513  BCR c 514                    
SITE     1 LC6 11 LEU c  50  VAL c 124  GLY c 128  TYR c 131                    
SITE     2 LC6 11 HIS c 132  PRO c 137  TYR c 143  PHE c 147                    
SITE     3 LC6 11 CLA c 512  BCR c 514  LMG z 101                               
SITE     1 LC7 11 PHE c 112  VAL c 116  SER c 121  VAL c 124                    
SITE     2 LC7 11 PHE c 147  CLA c 512  CLA c 513  LMG c 520                    
SITE     3 LC7 11 TYR k  15  VAL z  51  GLY z  55                               
SITE     1 LC8 10 ILE c 209  ILE c 224  GLY c 236  HIS c 237                    
SITE     2 LC8 10 PHE c 264  CLA c 501  CLA c 505  CLA c 506                    
SITE     3 LC8 10 CLA c 507  PHE i  23                                          
SITE     1 LC9 18 LEU a  91  ILE a 163  PRO c 217  GLY c 219                    
SITE     2 LC9 18 GLY c 220  GLU c 221  GLY c 222  TRP c 223                    
SITE     3 LC9 18 VAL c 227  PHE c 284  CYS c 288  PHE c 292                    
SITE     4 LC9 18 ASN c 293  ASN c 294  THR c 295  ASP c 360                    
SITE     5 LC9 18 PHE c 361  ARG c 362                                          
SITE     1 MC1 17 HIS a 195  PHE a 197  LEU a 297  GLU c  83                    
SITE     2 MC1 17 GLN c  84  GLY c  85  LEU c 404  SER c 406                    
SITE     3 MC1 17 ASN c 418  PHE c 419  VAL c 420  TRP c 425                    
SITE     4 MC1 17 CLA c 504  DGD c 518  LMG c 519  PHE j  29                    
SITE     5 MC1 17 TYR j  33                                                     
SITE     1 MC2 19 GLN a 199  PHE a 300  ASN a 301  PHE a 302                    
SITE     2 MC2 19 SER a 305  CLA a 604  ASN c 405  VAL c 407                    
SITE     3 MC2 19 ASN c 415  SER c 416  ASN c 418  CLA c 504                    
SITE     4 MC2 19 DGD c 517  PHE j  29  ALA j  32  TYR j  33                    
SITE     5 MC2 19 GLY j  37  SER j  38  SER j  39                               
SITE     1 MC3  4 HIS c  74  CLA c 504  DGD c 517  ASP k  23                    
SITE     1 MC4  9 TRP c  97  ASP c 107  PHE c 109  HIS c 118                    
SITE     2 MC4  9 SER c 121  CLA c 503  BCR c 514  PHE z  59                    
SITE     3 MC4  9 VAL z  62                                                     
SITE     1 MC5 22 MET A 183  CLA A 603  CLA A 604  PHO A 606                    
SITE     2 MC5 22 PRO D 149  VAL D 152  SER D 155  VAL D 156                    
SITE     3 MC5 22 PHE D 181  LEU D 182  PHE D 185  GLN D 186                    
SITE     4 MC5 22 TRP D 191  THR D 192  HIS D 197  GLY D 200                    
SITE     5 MC5 22 VAL D 204  LEU D 205  SER D 282  ALA D 283                    
SITE     6 MC5 22 VAL D 286  CLA D 402                                          
SITE     1 MC6 17 VAL A 157  MET A 172  ILE A 176  THR A 179                    
SITE     2 MC6 17 PHE A 180  MET A 183  CLA A 603  PHO A 605                    
SITE     3 MC6 17 MET D 198  VAL D 201  ALA D 202  LEU D 205                    
SITE     4 MC6 17 GLY D 206  CLA D 401  PL9 D 408  LHG L 102                    
SITE     5 MC6 17 SQD b 601                                                     
SITE     1 MC7 17 ILE D  35  LEU D  36  PRO D  39  CYS D  40                    
SITE     2 MC7 17 LEU D  43  LEU D  89  LEU D  90  LEU D  91                    
SITE     3 MC7 17 LEU D  92  TRP D  93  TRP D 104  THR D 112                    
SITE     4 MC7 17 PHE D 113  LEU D 116  HIS D 117  GLY X  13                    
SITE     5 MC7 17 LEU X  15                                                     
SITE     1 MC8 10 TYR D  42  LEU D  43  GLY D  46  GLY D  47                    
SITE     2 MC8 10 LEU D  49  THR D  50  LMG D 406  PRO F  29                    
SITE     3 MC8 10 THR F  30  VAL J  21                                          
SITE     1 MC9 15 SER A 232  ASN A 234  TRP B   5  TYR B   6                    
SITE     2 MC9 15 ARG B   7  PHE B 464  TRP B 468  CLA B 612                    
SITE     3 MC9 15 TYR D 141  ILE D 144  TRP D 266  PHE D 269                    
SITE     4 MC9 15 THR D 277  LEU L  23  LHG L 102                               
SITE     1 NC1 16 CLA A 604  TYR D  67  GLY D  70  CYS D  71                    
SITE     2 NC1 16 ASN D  72  PHE D  73  BCR D 404  THR F  30                    
SITE     3 NC1 16 ILE F  37  MET F  40  GLN F  41  PHE J  28                    
SITE     4 NC1 16 GLY J  31  ALA J  32  LEU J  36   MG J 101                    
SITE     1 NC2 18 MET A  37  ILE D 256  PHE D 257  ALA D 260                    
SITE     2 NC2 18 PHE D 261  SER D 262  ASN D 263  TRP D 266                    
SITE     3 NC2 18 PHE D 270  PL9 D 408  ASN L  13  THR L  15                    
SITE     4 NC2 18 SER L  16  TYR L  18  LEU L  19  LHG L 102                    
SITE     5 NC2 18 PHE T  17  ALA T  20                                          
SITE     1 NC3 18 ILE A  77  MET D 198  MET D 199  ALA D 202                    
SITE     2 NC3 18 HIS D 214  THR D 217  TRP D 253  ALA D 260                    
SITE     3 NC3 18 PHE D 261  LEU D 267  PHE D 270  PHE D 273                    
SITE     4 NC3 18 VAL D 274  CLA D 402  LHG D 407  LEU L  23                    
SITE     5 NC3 18 VAL L  26  PHE T  10                                          
SITE     1 NC4 16 ARG A 140  TRP A 142  PHE A 273  SQD A 609                    
SITE     2 NC4 16 TRP C  36  TRP C 443  ARG C 447  CLA C 504                    
SITE     3 NC4 16 CLA C 508  CLA C 510  GLU D 219  ASN D 220                    
SITE     4 NC4 16 ALA D 229  SER D 230  THR D 231  PHE D 232                    
SITE     1 NC5  6 GLY D  99  ASP D 100  PHE D 101  THR D 102                    
SITE     2 NC5  6 ASP E  45  ARG E  51                                          
SITE     1 NC6  7 ARG D  24  ARG D  26  PHE F  16  THR F  17                    
SITE     2 NC6  7 VAL F  18  ILE X  31  ASP X  35                               
SITE     1 NC7 22 MET a 183  CLA a 603  CLA a 604  PHO a 606                    
SITE     2 NC7 22 PRO d 149  VAL d 152  SER d 155  VAL d 156                    
SITE     3 NC7 22 PHE d 181  LEU d 182  PHE d 185  GLN d 186                    
SITE     4 NC7 22 TRP d 191  THR d 192  HIS d 197  GLY d 200                    
SITE     5 NC7 22 VAL d 204  LEU d 205  SER d 282  ALA d 283                    
SITE     6 NC7 22 VAL d 286  CLA d 402                                          
SITE     1 NC8 17 SQD B 601  VAL a 157  MET a 172  ILE a 176                    
SITE     2 NC8 17 THR a 179  PHE a 180  MET a 183  CLA a 603                    
SITE     3 NC8 17 PHO a 605  MET d 198  VAL d 201  ALA d 202                    
SITE     4 NC8 17 LEU d 205  GLY d 206  CLA d 401  PL9 d 408                    
SITE     5 NC8 17 LHG l 103                                                     
SITE     1 NC9 17 ILE d  35  LEU d  36  PRO d  39  CYS d  40                    
SITE     2 NC9 17 LEU d  43  LEU d  89  LEU d  90  LEU d  91                    
SITE     3 NC9 17 LEU d  92  TRP d  93  TRP d 104  THR d 112                    
SITE     4 NC9 17 PHE d 113  LEU d 116  HIS d 117  GLY x  13                    
SITE     5 NC9 17 LEU x  15                                                     
SITE     1 OC1 10 TYR d  42  LEU d  43  GLY d  46  GLY d  47                    
SITE     2 OC1 10 LEU d  49  THR d  50  LMG d 406  PRO f  29                    
SITE     3 OC1 10 THR f  30  VAL j  21                                          
SITE     1 OC2 15 SER a 232  ASN a 234  TRP b   5  TYR b   6                    
SITE     2 OC2 15 ARG b   7  PHE b 464  TRP b 468  CLA b 612                    
SITE     3 OC2 15 TYR d 141  ILE d 144  TRP d 266  PHE d 269                    
SITE     4 OC2 15 THR d 277  LEU l  23  LHG l 103                               
SITE     1 OC3 16 CLA a 604  TYR d  67  GLY d  70  CYS d  71                    
SITE     2 OC3 16 ASN d  72  PHE d  73  BCR d 404  THR f  30                    
SITE     3 OC3 16 ILE f  37  MET f  40  GLN f  41  PHE j  28                    
SITE     4 OC3 16 GLY j  31  ALA j  32  LEU j  36   MG j 101                    
SITE     1 OC4 18 MET a  37  ILE d 256  PHE d 257  ALA d 260                    
SITE     2 OC4 18 PHE d 261  SER d 262  ASN d 263  TRP d 266                    
SITE     3 OC4 18 PHE d 270  PL9 d 408  ASN l  13  THR l  15                    
SITE     4 OC4 18 SER l  16  TYR l  18  LEU l  19  LHG l 103                    
SITE     5 OC4 18 PHE t  17  ALA t  20                                          
SITE     1 OC5 18 ILE a  77  MET d 198  MET d 199  ALA d 202                    
SITE     2 OC5 18 HIS d 214  THR d 217  TRP d 253  ALA d 260                    
SITE     3 OC5 18 PHE d 261  LEU d 267  PHE d 270  PHE d 273                    
SITE     4 OC5 18 VAL d 274  CLA d 402  LHG d 407  LEU l  23                    
SITE     5 OC5 18 VAL l  26  PHE t  10                                          
SITE     1 OC6 16 ARG a 140  TRP a 142  PHE a 273  SQD a 609                    
SITE     2 OC6 16 TRP c  36  TRP c 443  ARG c 447  CLA c 504                    
SITE     3 OC6 16 CLA c 508  CLA c 510  GLU d 219  ASN d 220                    
SITE     4 OC6 16 ALA d 229  SER d 230  THR d 231  PHE d 232                    
SITE     1 OC7  6 GLY d  99  ASP d 100  PHE d 101  THR d 102                    
SITE     2 OC7  6 ASP e  45  ARG e  51                                          
SITE     1 OC8  7 ARG d  24  ARG d  26  PHE f  16  THR f  17                    
SITE     2 OC8  7 VAL f  18  ILE x  31  ASP x  35                               
SITE     1 OC9 10 LEU A 258  PHE A 260  TYR A 262  PHE D  27                    
SITE     2 OC9 10 THR E   4  THR E   5  GLU E   7  PRO E   9                    
SITE     3 OC9 10 PHE E  10  SER E  11                                          
SITE     1 PC1 10 LEU a 258  PHE a 260  TYR a 262  PHE d  27                    
SITE     2 PC1 10 THR e   4  THR e   5  GLU e   7  PRO e   9                    
SITE     3 PC1 10 PHE e  10  SER e  11                                          
SITE     1 PC2 14 ARG E   8  PHE E  10  ILE E  13  ARG E  18                    
SITE     2 PC2 14 TYR E  19  HIS E  23  THR E  26  ILE E  27                    
SITE     3 PC2 14 ARG F  19  TRP F  20  VAL F  23  HIS F  24                    
SITE     4 PC2 14 ALA F  27  ILE F  31                                          
SITE     1 PC3  1 ARG F  45                                                     
SITE     1 PC4 14 ARG e   8  PHE e  10  ILE e  13  ARG e  18                    
SITE     2 PC4 14 TYR e  19  HIS e  23  THR e  26  ILE e  27                    
SITE     3 PC4 14 ARG f  19  TRP f  20  VAL f  23  HIS f  24                    
SITE     4 PC4 14 ALA f  27  ILE f  31                                          
SITE     1 PC5  1 ARG f  45                                                     
SITE     1 PC6  5 CLA B 602  CLA B 610  PHE H  34  MET H  35                    
SITE     2 PC6  5 PHE H  38                                                     
SITE     1 PC7 17 TYR B 193  PHE B 250  TYR B 258  TYR B 273                    
SITE     2 PC7 17 GLN B 274  SER B 277  HIS D  87  ILE D 123                    
SITE     3 PC7 17 ILE D 159  LEU D 162  LEU D 291  LEU H  46                    
SITE     4 PC7 17 TYR H  49  ASN H  50  VAL H  60  SER H  61                    
SITE     5 PC7 17 TRP H  62                                                     
SITE     1 PC8  5 CLA b 602  CLA b 610  PHE h  34  MET h  35                    
SITE     2 PC8  5 PHE h  38                                                     
SITE     1 PC9 17 TYR b 193  PHE b 250  TYR b 258  TYR b 273                    
SITE     2 PC9 17 GLN b 274  SER b 277  HIS d  87  ILE d 123                    
SITE     3 PC9 17 ILE d 159  LEU d 162  LEU d 291  LEU h  46                    
SITE     4 PC9 17 TYR h  49  ASN h  50  VAL h  60  SER h  61                    
SITE     5 PC9 17 TRP h  62                                                     
SITE     1 QC1  5 LMG D 406  GLY J  31  ALA J  34  GLY J  35                    
SITE     2 QC1  5 LEU J  36                                                     
SITE     1 QC2  5 LMG d 406  GLY j  31  ALA j  34  GLY j  35                    
SITE     2 QC2  5 LEU j  36                                                     
SITE     1 QC3 13 PHE C  62  THR J  15  MET J  19  LEU K  31                    
SITE     2 QC3 13 ALA K  34  PHE K  37  VAL K  38  BCR K 102                    
SITE     3 QC3 13 ILE Y  28  GLY Y  29  GLY Y  32  PRO Y  33                    
SITE     4 QC3 13 PHE Z  17                                                     
SITE     1 QC4 11 ALA C  55  GLY C  58  LEU C  59  SER C 122                    
SITE     2 QC4 11 ALA C 123  GLY C 126  CLA C 511  TYR K  15                    
SITE     3 QC4 11 PHE K  32  BCR K 101  SER Z  16                               
SITE     1 QC5 13 PHE c  62  THR j  15  MET j  19  LEU k  31                    
SITE     2 QC5 13 ALA k  34  PHE k  37  VAL k  38  BCR k 102                    
SITE     3 QC5 13 ILE y  28  GLY y  29  GLY y  32  PRO y  33                    
SITE     4 QC5 13 PHE z  17                                                     
SITE     1 QC6 11 ALA c  55  GLY c  58  LEU c  59  SER c 122                    
SITE     2 QC6 11 ALA c 123  GLY c 126  CLA c 511  TYR k  15                    
SITE     3 QC6 11 PHE k  32  BCR k 101  SER z  16                               
SITE     1 QC7 15 ARG L  14  TYR L  18  LEU L  21  VAL M  15                    
SITE     2 QC7 15 TYR M  26  LEU T  16  PHE T  19  PHE T  23                    
SITE     3 QC7 15 ARG b  18  SER b 104  TRP b 115  CLA b 615                    
SITE     4 QC7 15 SQD b 621  BCR b 622  ARG l   7                               
SITE     1 QC8 16 SER A 232  ASN A 234  PRO B   4  TRP B   5                    
SITE     2 QC8 16 TYR B   6  TRP D 266  PHE D 273  CLA D 402                    
SITE     3 QC8 16 LHG D 405  LHG D 407  GLU L  11  LEU L  12                    
SITE     4 QC8 16 ASN L  13  SER L  16  GLY L  20  PHE M  21                    
SITE     1 QC9 15 ARG B  18  SER B 104  TRP B 115  CLA B 615                    
SITE     2 QC9 15 BCR B 622  ARG L   7  ARG l  14  TYR l  18                    
SITE     3 QC9 15 SQD l 102  VAL m  15  TYR m  26  CYS t  12                    
SITE     4 QC9 15 LEU t  16  PHE t  19  PHE t  23                               
SITE     1 RC1 14 ARG B  18  LEU B  29  SER B 104  PHE B 108                    
SITE     2 RC1 14 TRP B 115  CLA B 615  BCR B 618  ARG L   7                    
SITE     3 RC1 14 ARG l  14  TYR l  18  SQD l 101  CYS t  12                    
SITE     4 RC1 14 PHE t  19  PHE t  23                                          
SITE     1 RC2 16 SER a 232  ASN a 234  PRO b   4  TRP b   5                    
SITE     2 RC2 16 TYR b   6  TRP d 266  PHE d 273  CLA d 402                    
SITE     3 RC2 16 LHG d 405  LHG d 407  GLU l  11  LEU l  12                    
SITE     4 RC2 16 ASN l  13  SER l  16  GLY l  20  PHE m  21                    
SITE     1 RC3  3 THR O 138  ASN O 200  VAL O 201                               
SITE     1 RC4  3 THR o 138  ASN o 200  VAL o 201                               
SITE     1 RC5  8 PHE T  19  MET b  25  LEU b  29  CLA b 614                    
SITE     2 RC5  8 CLA b 615  BCR b 618  LMG b 619  SQD b 621                    
SITE     1 RC6  5 PHE T  22  SQD b 601  CLA b 606  CLA b 607                    
SITE     2 RC6  5 CLA b 617                                                     
SITE     1 RC7  6 SQD B 601  CLA B 606  CLA B 607  CLA B 617                    
SITE     2 RC7  6 PHE t  18  PHE t  22                                          
SITE     1 RC8 20 ALA V  36  CYS V  37  CYS V  40  HIS V  41                    
SITE     2 RC8 20 THR V  46  THR V  48  LEU V  52  ASP V  53                    
SITE     3 RC8 20 LEU V  54  THR V  58  LEU V  59  ALA V  62                    
SITE     4 RC8 20 LEU V  72  TYR V  75  MET V  76  TYR V  82                    
SITE     5 RC8 20 ILE V  88  HIS V  92  PRO V  93  ILE V 115                    
SITE     1 RC9 20 ALA v  36  CYS v  37  CYS v  40  HIS v  41                    
SITE     2 RC9 20 THR v  46  THR v  48  LEU v  52  ASP v  53                    
SITE     3 RC9 20 LEU v  54  THR v  58  LEU v  59  ALA v  62                    
SITE     4 RC9 20 LEU v  72  TYR v  75  MET v  76  TYR v  82                    
SITE     5 RC9 20 ILE v  88  HIS v  92  PRO v  93  ILE v 115                    
SITE     1 SC1  9 PHE C 127  TYR C 131  ARG C 135  CLA C 513                    
SITE     2 SC1  9 TYR Z  27  TRP Z  33  LYS Z  37  PHE Z  41                    
SITE     3 SC1  9 TRP Z  47                                                     
SITE     1 SC2  9 PHE c 127  TYR c 131  ARG c 135  CLA c 513                    
SITE     2 SC2  9 TYR z  27  TRP z  33  LYS z  37  PHE z  41                    
SITE     3 SC2  9 TRP z  47                                                     
CRYST1  136.610  228.090  308.680  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      0.007320  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004384  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003240        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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