GenomeNet

Database: PDB
Entry: 5MX2
LinkDB: 5MX2
Original site: 5MX2 
HEADER    OXIDOREDUCTASE                          20-JAN-17   5MX2              
TITLE     PHOTOSYSTEM II DEPLETED OF THE MN4CAO5 CLUSTER AT 2.55 A RESOLUTION   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOTOSYSTEM II PROTEIN D1 1;                               
COMPND   3 CHAIN: A, a;                                                         
COMPND   4 SYNONYM: PSII D1 PROTEIN 1,PHOTOSYSTEM II Q(B) PROTEIN 1;            
COMPND   5 EC: 1.10.3.9;                                                        
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PHOTOSYSTEM II CP47 REACTION CENTER PROTEIN;               
COMPND   8 CHAIN: B, b;                                                         
COMPND   9 SYNONYM: PSII 47 KDA PROTEIN,PROTEIN CP-47;                          
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: PHOTOSYSTEM II CP43 REACTION CENTER PROTEIN;               
COMPND  12 CHAIN: C, c;                                                         
COMPND  13 SYNONYM: PSII 43 KDA PROTEIN,PROTEIN CP-43;                          
COMPND  14 MOL_ID: 4;                                                           
COMPND  15 MOLECULE: PHOTOSYSTEM II D2 PROTEIN;                                 
COMPND  16 CHAIN: D, d;                                                         
COMPND  17 SYNONYM: PSII D2 PROTEIN,PHOTOSYSTEM II Q(A) PROTEIN;                
COMPND  18 EC: 1.10.3.9;                                                        
COMPND  19 MOL_ID: 5;                                                           
COMPND  20 MOLECULE: CYTOCHROME B559 SUBUNIT ALPHA;                             
COMPND  21 CHAIN: E, e;                                                         
COMPND  22 SYNONYM: PSII REACTION CENTER SUBUNIT V;                             
COMPND  23 MOL_ID: 6;                                                           
COMPND  24 MOLECULE: CYTOCHROME B559 SUBUNIT BETA;                              
COMPND  25 CHAIN: F, f;                                                         
COMPND  26 SYNONYM: PSII REACTION CENTER SUBUNIT VI;                            
COMPND  27 MOL_ID: 7;                                                           
COMPND  28 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN H;                  
COMPND  29 CHAIN: H, h;                                                         
COMPND  30 SYNONYM: PSII-H;                                                     
COMPND  31 MOL_ID: 8;                                                           
COMPND  32 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN I;                  
COMPND  33 CHAIN: I, i;                                                         
COMPND  34 SYNONYM: PSII-I,PSII 4.4 KDA PROTEIN;                                
COMPND  35 MOL_ID: 9;                                                           
COMPND  36 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN J;                  
COMPND  37 CHAIN: J, j;                                                         
COMPND  38 SYNONYM: PSII-J;                                                     
COMPND  39 MOL_ID: 10;                                                          
COMPND  40 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN K;                  
COMPND  41 CHAIN: K, k;                                                         
COMPND  42 SYNONYM: PSII-K;                                                     
COMPND  43 MOL_ID: 11;                                                          
COMPND  44 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN L;                  
COMPND  45 CHAIN: L, l;                                                         
COMPND  46 SYNONYM: PSII-L;                                                     
COMPND  47 MOL_ID: 12;                                                          
COMPND  48 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN M;                  
COMPND  49 CHAIN: M, m;                                                         
COMPND  50 SYNONYM: PSII-M;                                                     
COMPND  51 MOL_ID: 13;                                                          
COMPND  52 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;          
COMPND  53 CHAIN: O, o;                                                         
COMPND  54 SYNONYM: MSP;                                                        
COMPND  55 MOL_ID: 14;                                                          
COMPND  56 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN T;                  
COMPND  57 CHAIN: T, t;                                                         
COMPND  58 SYNONYM: PSII-TC;                                                    
COMPND  59 MOL_ID: 15;                                                          
COMPND  60 MOLECULE: PHOTOSYSTEM II 12 KDA EXTRINSIC PROTEIN;                   
COMPND  61 CHAIN: U, u;                                                         
COMPND  62 SYNONYM: PS II COMPLEX 12 KDA EXTRINSIC PROTEIN,PSII-U;              
COMPND  63 MOL_ID: 16;                                                          
COMPND  64 MOLECULE: CYTOCHROME C-550;                                          
COMPND  65 CHAIN: V, v;                                                         
COMPND  66 SYNONYM: CYTOCHROME C-549,CYTOCHROME C550,LOW-POTENTIAL CYTOCHROME C;
COMPND  67 MOL_ID: 17;                                                          
COMPND  68 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN YCF12;              
COMPND  69 CHAIN: Y, y;                                                         
COMPND  70 MOL_ID: 18;                                                          
COMPND  71 MOLECULE: PHOTOSYSTEM II REACTION CENTER X PROTEIN;                  
COMPND  72 CHAIN: X, x;                                                         
COMPND  73 MOL_ID: 19;                                                          
COMPND  74 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Z;                  
COMPND  75 CHAIN: Z, z;                                                         
COMPND  76 SYNONYM: PSII-Z;                                                     
COMPND  77 MOL_ID: 20;                                                          
COMPND  78 MOLECULE: PHOTOSYSTEM II PROTEIN Y;                                  
COMPND  79 CHAIN: R, r                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE   3 ORGANISM_TAXID: 197221;                                              
SOURCE   4 STRAIN: BP-1;                                                        
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE   7 ORGANISM_TAXID: 197221;                                              
SOURCE   8 STRAIN: BP-1;                                                        
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  11 ORGANISM_TAXID: 197221;                                              
SOURCE  12 STRAIN: BP-1;                                                        
SOURCE  13 MOL_ID: 4;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  15 ORGANISM_TAXID: 197221;                                              
SOURCE  16 STRAIN: BP-1;                                                        
SOURCE  17 MOL_ID: 5;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  19 ORGANISM_TAXID: 197221;                                              
SOURCE  20 STRAIN: BP-1;                                                        
SOURCE  21 MOL_ID: 6;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  23 ORGANISM_TAXID: 197221;                                              
SOURCE  24 STRAIN: BP-1;                                                        
SOURCE  25 MOL_ID: 7;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  27 ORGANISM_TAXID: 197221;                                              
SOURCE  28 STRAIN: BP-1;                                                        
SOURCE  29 MOL_ID: 8;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  31 ORGANISM_TAXID: 197221;                                              
SOURCE  32 STRAIN: BP-1;                                                        
SOURCE  33 MOL_ID: 9;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  35 ORGANISM_TAXID: 197221;                                              
SOURCE  36 STRAIN: BP-1;                                                        
SOURCE  37 MOL_ID: 10;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  39 ORGANISM_TAXID: 197221;                                              
SOURCE  40 STRAIN: BP-1;                                                        
SOURCE  41 MOL_ID: 11;                                                          
SOURCE  42 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  43 ORGANISM_TAXID: 197221;                                              
SOURCE  44 STRAIN: BP-1;                                                        
SOURCE  45 MOL_ID: 12;                                                          
SOURCE  46 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  47 ORGANISM_TAXID: 197221;                                              
SOURCE  48 STRAIN: BP-1;                                                        
SOURCE  49 MOL_ID: 13;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  51 ORGANISM_TAXID: 197221;                                              
SOURCE  52 STRAIN: BP-1;                                                        
SOURCE  53 MOL_ID: 14;                                                          
SOURCE  54 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  55 ORGANISM_TAXID: 197221;                                              
SOURCE  56 STRAIN: BP-1;                                                        
SOURCE  57 MOL_ID: 15;                                                          
SOURCE  58 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  59 ORGANISM_TAXID: 197221;                                              
SOURCE  60 STRAIN: BP-1;                                                        
SOURCE  61 MOL_ID: 16;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  63 ORGANISM_TAXID: 197221;                                              
SOURCE  64 STRAIN: BP-1;                                                        
SOURCE  65 MOL_ID: 17;                                                          
SOURCE  66 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  67 ORGANISM_TAXID: 197221;                                              
SOURCE  68 STRAIN: BP-1;                                                        
SOURCE  69 MOL_ID: 18;                                                          
SOURCE  70 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  71 ORGANISM_TAXID: 197221;                                              
SOURCE  72 STRAIN: BP-1;                                                        
SOURCE  73 MOL_ID: 19;                                                          
SOURCE  74 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  75 ORGANISM_TAXID: 197221;                                              
SOURCE  76 STRAIN: BP-1;                                                        
SOURCE  77 MOL_ID: 20;                                                          
SOURCE  78 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  79 ORGANISM_TAXID: 197221;                                              
SOURCE  80 STRAIN: BP-1                                                         
KEYWDS    PHOTOSYNTHESIS, METAL CLUSTER, EDTA, HYDROXYLAMINE, OXIDOREDUCTASE,   
KEYWDS   2 THERMOSYNECHOCOCCUS ELONGATUS                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.ZHANG,M.BOMMER,R.CHATTERJEE,R.HUSSAIN,J.KERN,J.YANO,H.DAU,H.DOBBEK, 
AUTHOR   2 A.ZOUNI                                                              
REVDAT   5   20-NOV-19 5MX2    1       LINK                                     
REVDAT   4   25-SEP-19 5MX2    1       REMARK LINK   SITE                       
REVDAT   3   28-MAR-18 5MX2    1       JRNL                                     
REVDAT   2   21-FEB-18 5MX2    1       JRNL                                     
REVDAT   1   02-AUG-17 5MX2    0                                                
JRNL        AUTH   M.ZHANG,M.BOMMER,R.CHATTERJEE,R.HUSSEIN,J.YANO,H.DAU,J.KERN, 
JRNL        AUTH 2 H.DOBBEK,A.ZOUNI                                             
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE LIGHT-DRIVEN AUTO-ASSEMBLY      
JRNL        TITL 2 PROCESS OF THE WATER-OXIDIZING MN4CAO5-CLUSTER IN            
JRNL        TITL 3 PHOTOSYSTEM II.                                              
JRNL        REF    ELIFE                         V.   6       2017              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   28718766                                                     
JRNL        DOI    10.7554/ELIFE.26933                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.65                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 364474                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 18225                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.6643 -  6.8221    1.00    13093   690  0.1599 0.1898        
REMARK   3     2  6.8221 -  5.4170    1.00    12739   670  0.1607 0.2080        
REMARK   3     3  5.4170 -  4.7329    1.00    12637   665  0.1502 0.1977        
REMARK   3     4  4.7329 -  4.3004    1.00    12570   662  0.1505 0.2016        
REMARK   3     5  4.3004 -  3.9923    1.00    12535   660  0.1583 0.2064        
REMARK   3     6  3.9923 -  3.7570    1.00    12516   658  0.1685 0.2230        
REMARK   3     7  3.7570 -  3.5689    1.00    12547   661  0.1794 0.2370        
REMARK   3     8  3.5689 -  3.4136    1.00    12448   655  0.1891 0.2648        
REMARK   3     9  3.4136 -  3.2822    1.00    12478   657  0.2001 0.2512        
REMARK   3    10  3.2822 -  3.1690    1.00    12454   655  0.2120 0.2720        
REMARK   3    11  3.1690 -  3.0699    1.00    12395   653  0.2284 0.2843        
REMARK   3    12  3.0699 -  2.9822    1.00    12470   656  0.2304 0.2835        
REMARK   3    13  2.9822 -  2.9037    1.00    12409   653  0.2309 0.2913        
REMARK   3    14  2.9037 -  2.8328    1.00    12448   655  0.2367 0.3071        
REMARK   3    15  2.8328 -  2.7684    1.00    12401   653  0.2418 0.2881        
REMARK   3    16  2.7684 -  2.7095    1.00    12389   652  0.2495 0.3053        
REMARK   3    17  2.7095 -  2.6553    1.00    12424   654  0.2587 0.3131        
REMARK   3    18  2.6553 -  2.6052    1.00    12379   651  0.2765 0.3163        
REMARK   3    19  2.6052 -  2.5587    1.00    12417   654  0.2872 0.3294        
REMARK   3    20  2.5587 -  2.5153    0.99    12169   641  0.3024 0.3242        
REMARK   3    21  2.5153 -  2.4748    0.96    11876   625  0.3152 0.3462        
REMARK   3    22  2.4748 -  2.4367    0.90    11183   589  0.3241 0.3456        
REMARK   3    23  2.4367 -  2.4009    0.87    10766   567  0.3420 0.3663        
REMARK   3    24  2.4009 -  2.3670    0.83    10233   538  0.3514 0.3857        
REMARK   3    25  2.3670 -  2.3351    0.79     9764   515  0.3664 0.3880        
REMARK   3    26  2.3351 -  2.3047    0.76     9430   496  0.3748 0.4044        
REMARK   3    27  2.3047 -  2.2759    0.73     8946   470  0.3824 0.4108        
REMARK   3    28  2.2759 -  2.2485    0.69     8598   452  0.3936 0.4361        
REMARK   3    29  2.2485 -  2.2223    0.66     8174   431  0.3979 0.4037        
REMARK   3    30  2.2223 -  2.1974    0.60     7361   387  0.4098 0.4521        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.360            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.900           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 37.11                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.05                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.013          51587                                  
REMARK   3   ANGLE     :  1.179          70715                                  
REMARK   3   CHIRALITY :  0.067           7098                                  
REMARK   3   PLANARITY :  0.007          10859                                  
REMARK   3   DIHEDRAL  : 17.133          30460                                  
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 5MX2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003131.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAY-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91841                            
REMARK 200  MONOCHROMATOR                  : SI-111 CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS VERSION OCT 15, 2015           
REMARK 200  DATA SCALING SOFTWARE          : XDS VERSION OCT 15, 2015           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 364603                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.197                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY                : 11.20                              
REMARK 200  R MERGE                    (I) : 0.25000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.3400                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 65.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 3.27000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.440                              
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: 4PJ0                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: EQUAL VOLUMES OF BUFFER: 0.1 M TRIS      
REMARK 280  -HCL PH 7.5, 0.1 M (NH4)2SO4, 14-18 % PEG 5000 MME AND PROTEIN:     
REMARK 280  2 MM CHLOROPHYLL EQUIVALENT OF PSII IN C12E8 DETERGENT, POST        
REMARK 280  CRYSTALLISATION TREATMENT, MICROBATCH, TEMPERATURE 291K             
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       58.16300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      152.02150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      109.80850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      152.02150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       58.16300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      109.80850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: EICOSAMERIC                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, I, J, K,         
REMARK 350                    AND CHAINS: L, M, O, T, U, V, Y, X, Z, R          
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: EICOSAMERIC                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: a, b, c, d, e, f, h, i, j, k,         
REMARK 350                    AND CHAINS: l, m, o, t, u, v, x, r, y, z          
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     ARG A     7                                                      
REMARK 465     ARG A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LYS B   507                                                      
REMARK 465     GLU B   508                                                      
REMARK 465     ALA B   509                                                      
REMARK 465     VAL B   510                                                      
REMARK 465     MET C    13                                                      
REMARK 465     VAL C    14                                                      
REMARK 465     THR C    15                                                      
REMARK 465     LEU C    16                                                      
REMARK 465     SER C    17                                                      
REMARK 465     SER C    18                                                      
REMARK 465     ASN C    19                                                      
REMARK 465     SER C    20                                                      
REMARK 465     ILE C    21                                                      
REMARK 465     PHE C    22                                                      
REMARK 465     ALA C    23                                                      
REMARK 465     THR C    24                                                      
REMARK 465     ASN C    25                                                      
REMARK 465     ARG C    26                                                      
REMARK 465     MET D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     ILE D     3                                                      
REMARK 465     ALA D     4                                                      
REMARK 465     ILE D     5                                                      
REMARK 465     GLY D     6                                                      
REMARK 465     ARG D     7                                                      
REMARK 465     ALA D     8                                                      
REMARK 465     PRO D     9                                                      
REMARK 465     ALA D    10                                                      
REMARK 465     GLU D    11                                                      
REMARK 465     ARG D    12                                                      
REMARK 465     MET E     1                                                      
REMARK 465     ALA E     2                                                      
REMARK 465     LYS E    84                                                      
REMARK 465     MET F     1                                                      
REMARK 465     THR F     2                                                      
REMARK 465     SER F     3                                                      
REMARK 465     ASN F     4                                                      
REMARK 465     THR F     5                                                      
REMARK 465     PRO F     6                                                      
REMARK 465     ASN F     7                                                      
REMARK 465     GLN F     8                                                      
REMARK 465     GLU F     9                                                      
REMARK 465     PRO F    10                                                      
REMARK 465     VAL F    11                                                      
REMARK 465     SER F    12                                                      
REMARK 465     MET H     1                                                      
REMARK 465     ALA H    64                                                      
REMARK 465     LEU H    65                                                      
REMARK 465     GLY H    66                                                      
REMARK 465     ARG I    34                                                      
REMARK 465     LYS I    35                                                      
REMARK 465     ASP I    36                                                      
REMARK 465     LEU I    37                                                      
REMARK 465     GLU I    38                                                      
REMARK 465     MET J     1                                                      
REMARK 465     MET J     2                                                      
REMARK 465     SER J     3                                                      
REMARK 465     GLU J     4                                                      
REMARK 465     GLY J     5                                                      
REMARK 465     GLY J     6                                                      
REMARK 465     ARG J     7                                                      
REMARK 465     MET K     1                                                      
REMARK 465     ILE K     2                                                      
REMARK 465     ASP K     3                                                      
REMARK 465     ALA K     4                                                      
REMARK 465     LEU K     5                                                      
REMARK 465     VAL K     6                                                      
REMARK 465     LEU K     7                                                      
REMARK 465     VAL K     8                                                      
REMARK 465     ALA K     9                                                      
REMARK 465     LYS K    10                                                      
REMARK 465     ARG K    46                                                      
REMARK 465     MET L     1                                                      
REMARK 465     GLN M    33                                                      
REMARK 465     LYS M    34                                                      
REMARK 465     SER M    35                                                      
REMARK 465     SER M    36                                                      
REMARK 465     MET O   -25                                                      
REMARK 465     LYS O   -24                                                      
REMARK 465     TYR O   -23                                                      
REMARK 465     ARG O   -22                                                      
REMARK 465     ILE O   -21                                                      
REMARK 465     LEU O   -20                                                      
REMARK 465     MET O   -19                                                      
REMARK 465     ALA O   -18                                                      
REMARK 465     THR O   -17                                                      
REMARK 465     LEU O   -16                                                      
REMARK 465     LEU O   -15                                                      
REMARK 465     ALA O   -14                                                      
REMARK 465     VAL O   -13                                                      
REMARK 465     CYS O   -12                                                      
REMARK 465     LEU O   -11                                                      
REMARK 465     GLY O   -10                                                      
REMARK 465     ILE O    -9                                                      
REMARK 465     PHE O    -8                                                      
REMARK 465     SER O    -7                                                      
REMARK 465     LEU O    -6                                                      
REMARK 465     SER O    -5                                                      
REMARK 465     ALA O    -4                                                      
REMARK 465     PRO O    -3                                                      
REMARK 465     ALA O    -2                                                      
REMARK 465     PHE O    -1                                                      
REMARK 465     ALA O     0                                                      
REMARK 465     ALA O     1                                                      
REMARK 465     LYS O     2                                                      
REMARK 465     GLN O     3                                                      
REMARK 465     ALA O   246                                                      
REMARK 465     ILE T    29                                                      
REMARK 465     THR T    30                                                      
REMARK 465     LYS T    31                                                      
REMARK 465     LYS T    32                                                      
REMARK 465     MET U   -29                                                      
REMARK 465     GLN U   -28                                                      
REMARK 465     ARG U   -27                                                      
REMARK 465     LEU U   -26                                                      
REMARK 465     GLY U   -25                                                      
REMARK 465     ARG U   -24                                                      
REMARK 465     TRP U   -23                                                      
REMARK 465     LEU U   -22                                                      
REMARK 465     ALA U   -21                                                      
REMARK 465     LEU U   -20                                                      
REMARK 465     ALA U   -19                                                      
REMARK 465     TYR U   -18                                                      
REMARK 465     PHE U   -17                                                      
REMARK 465     VAL U   -16                                                      
REMARK 465     GLY U   -15                                                      
REMARK 465     VAL U   -14                                                      
REMARK 465     SER U   -13                                                      
REMARK 465     LEU U   -12                                                      
REMARK 465     LEU U   -11                                                      
REMARK 465     GLY U   -10                                                      
REMARK 465     TRP U    -9                                                      
REMARK 465     ILE U    -8                                                      
REMARK 465     ASN U    -7                                                      
REMARK 465     TRP U    -6                                                      
REMARK 465     SER U    -5                                                      
REMARK 465     ALA U    -4                                                      
REMARK 465     PRO U    -3                                                      
REMARK 465     THR U    -2                                                      
REMARK 465     LEU U    -1                                                      
REMARK 465     ALA U     0                                                      
REMARK 465     ALA U     1                                                      
REMARK 465     THR U     2                                                      
REMARK 465     ALA U     3                                                      
REMARK 465     SER U     4                                                      
REMARK 465     THR U     5                                                      
REMARK 465     GLU U     6                                                      
REMARK 465     GLU U     7                                                      
REMARK 465     GLU U     8                                                      
REMARK 465     MET V   -25                                                      
REMARK 465     LEU V   -24                                                      
REMARK 465     LYS V   -23                                                      
REMARK 465     LYS V   -22                                                      
REMARK 465     CYS V   -21                                                      
REMARK 465     VAL V   -20                                                      
REMARK 465     TRP V   -19                                                      
REMARK 465     LEU V   -18                                                      
REMARK 465     ALA V   -17                                                      
REMARK 465     VAL V   -16                                                      
REMARK 465     ALA V   -15                                                      
REMARK 465     LEU V   -14                                                      
REMARK 465     CYS V   -13                                                      
REMARK 465     LEU V   -12                                                      
REMARK 465     CYS V   -11                                                      
REMARK 465     LEU V   -10                                                      
REMARK 465     TRP V    -9                                                      
REMARK 465     GLN V    -8                                                      
REMARK 465     PHE V    -7                                                      
REMARK 465     THR V    -6                                                      
REMARK 465     MET V    -5                                                      
REMARK 465     GLY V    -4                                                      
REMARK 465     THR V    -3                                                      
REMARK 465     ALA V    -2                                                      
REMARK 465     LEU V    -1                                                      
REMARK 465     ALA V     0                                                      
REMARK 465     MET Y     1                                                      
REMARK 465     GLY Y     2                                                      
REMARK 465     ILE Y     3                                                      
REMARK 465     PHE Y     4                                                      
REMARK 465     ASN Y     5                                                      
REMARK 465     GLY Y     6                                                      
REMARK 465     ILE Y     7                                                      
REMARK 465     ILE Y     8                                                      
REMARK 465     GLU Y     9                                                      
REMARK 465     PHE Y    10                                                      
REMARK 465     LEU Y    11                                                      
REMARK 465     SER Y    12                                                      
REMARK 465     ASN Y    13                                                      
REMARK 465     ILE Y    14                                                      
REMARK 465     ASN Y    15                                                      
REMARK 465     PHE Y    16                                                      
REMARK 465     GLU Y    17                                                      
REMARK 465     VAL Y    18                                                      
REMARK 465     ILE Y    19                                                      
REMARK 465     ALA Y    20                                                      
REMARK 465     GLN Y    21                                                      
REMARK 465     LEU Y    22                                                      
REMARK 465     THR Y    23                                                      
REMARK 465     MET Y    24                                                      
REMARK 465     ILE Y    25                                                      
REMARK 465     MET X     1                                                      
REMARK 465     ARG X    39                                                      
REMARK 465     SER X    40                                                      
REMARK 465     LEU X    41                                                      
REMARK 465     VAL Z    62                                                      
REMARK 465     MET a     1                                                      
REMARK 465     THR a     2                                                      
REMARK 465     THR a     3                                                      
REMARK 465     THR a     4                                                      
REMARK 465     LEU a     5                                                      
REMARK 465     GLN a     6                                                      
REMARK 465     ARG a     7                                                      
REMARK 465     ARG a     8                                                      
REMARK 465     GLU a     9                                                      
REMARK 465     SER a    10                                                      
REMARK 465     ALA a    11                                                      
REMARK 465     MET b     1                                                      
REMARK 465     ARG b   505                                                      
REMARK 465     ARG b   506                                                      
REMARK 465     LYS b   507                                                      
REMARK 465     GLU b   508                                                      
REMARK 465     ALA b   509                                                      
REMARK 465     VAL b   510                                                      
REMARK 465     MET c    13                                                      
REMARK 465     VAL c    14                                                      
REMARK 465     THR c    15                                                      
REMARK 465     LEU c    16                                                      
REMARK 465     SER c    17                                                      
REMARK 465     SER c    18                                                      
REMARK 465     ASN c    19                                                      
REMARK 465     SER c    20                                                      
REMARK 465     ILE c    21                                                      
REMARK 465     PHE c    22                                                      
REMARK 465     ALA c    23                                                      
REMARK 465     THR c    24                                                      
REMARK 465     ASN c    25                                                      
REMARK 465     MET d     1                                                      
REMARK 465     THR d     2                                                      
REMARK 465     ILE d     3                                                      
REMARK 465     ALA d     4                                                      
REMARK 465     ILE d     5                                                      
REMARK 465     GLY d     6                                                      
REMARK 465     ARG d     7                                                      
REMARK 465     ALA d     8                                                      
REMARK 465     PRO d     9                                                      
REMARK 465     ALA d    10                                                      
REMARK 465     GLU d    11                                                      
REMARK 465     ARG d    12                                                      
REMARK 465     MET e     1                                                      
REMARK 465     ALA e     2                                                      
REMARK 465     GLY e     3                                                      
REMARK 465     THR e     4                                                      
REMARK 465     LYS e    84                                                      
REMARK 465     MET f     1                                                      
REMARK 465     THR f     2                                                      
REMARK 465     SER f     3                                                      
REMARK 465     ASN f     4                                                      
REMARK 465     THR f     5                                                      
REMARK 465     PRO f     6                                                      
REMARK 465     ASN f     7                                                      
REMARK 465     GLN f     8                                                      
REMARK 465     GLU f     9                                                      
REMARK 465     PRO f    10                                                      
REMARK 465     VAL f    11                                                      
REMARK 465     SER f    12                                                      
REMARK 465     MET h     1                                                      
REMARK 465     LEU h    65                                                      
REMARK 465     GLY h    66                                                      
REMARK 465     ARG i    34                                                      
REMARK 465     LYS i    35                                                      
REMARK 465     ASP i    36                                                      
REMARK 465     LEU i    37                                                      
REMARK 465     GLU i    38                                                      
REMARK 465     MET j     1                                                      
REMARK 465     MET j     2                                                      
REMARK 465     SER j     3                                                      
REMARK 465     GLU j     4                                                      
REMARK 465     GLY j     5                                                      
REMARK 465     GLY j     6                                                      
REMARK 465     ARG j     7                                                      
REMARK 465     MET k     1                                                      
REMARK 465     ILE k     2                                                      
REMARK 465     ASP k     3                                                      
REMARK 465     ALA k     4                                                      
REMARK 465     LEU k     5                                                      
REMARK 465     VAL k     6                                                      
REMARK 465     LEU k     7                                                      
REMARK 465     VAL k     8                                                      
REMARK 465     ALA k     9                                                      
REMARK 465     LYS k    10                                                      
REMARK 465     MET l     1                                                      
REMARK 465     GLN m    33                                                      
REMARK 465     LYS m    34                                                      
REMARK 465     SER m    35                                                      
REMARK 465     SER m    36                                                      
REMARK 465     MET o   -25                                                      
REMARK 465     LYS o   -24                                                      
REMARK 465     TYR o   -23                                                      
REMARK 465     ARG o   -22                                                      
REMARK 465     ILE o   -21                                                      
REMARK 465     LEU o   -20                                                      
REMARK 465     MET o   -19                                                      
REMARK 465     ALA o   -18                                                      
REMARK 465     THR o   -17                                                      
REMARK 465     LEU o   -16                                                      
REMARK 465     LEU o   -15                                                      
REMARK 465     ALA o   -14                                                      
REMARK 465     VAL o   -13                                                      
REMARK 465     CYS o   -12                                                      
REMARK 465     LEU o   -11                                                      
REMARK 465     GLY o   -10                                                      
REMARK 465     ILE o    -9                                                      
REMARK 465     PHE o    -8                                                      
REMARK 465     SER o    -7                                                      
REMARK 465     LEU o    -6                                                      
REMARK 465     SER o    -5                                                      
REMARK 465     ALA o    -4                                                      
REMARK 465     PRO o    -3                                                      
REMARK 465     ALA o    -2                                                      
REMARK 465     PHE o    -1                                                      
REMARK 465     ALA o     0                                                      
REMARK 465     ALA o     1                                                      
REMARK 465     LYS o     2                                                      
REMARK 465     GLN o     3                                                      
REMARK 465     THR o     4                                                      
REMARK 465     ALA o   246                                                      
REMARK 465     THR t    30                                                      
REMARK 465     LYS t    31                                                      
REMARK 465     LYS t    32                                                      
REMARK 465     MET u   -29                                                      
REMARK 465     GLN u   -28                                                      
REMARK 465     ARG u   -27                                                      
REMARK 465     LEU u   -26                                                      
REMARK 465     GLY u   -25                                                      
REMARK 465     ARG u   -24                                                      
REMARK 465     TRP u   -23                                                      
REMARK 465     LEU u   -22                                                      
REMARK 465     ALA u   -21                                                      
REMARK 465     LEU u   -20                                                      
REMARK 465     ALA u   -19                                                      
REMARK 465     TYR u   -18                                                      
REMARK 465     PHE u   -17                                                      
REMARK 465     VAL u   -16                                                      
REMARK 465     GLY u   -15                                                      
REMARK 465     VAL u   -14                                                      
REMARK 465     SER u   -13                                                      
REMARK 465     LEU u   -12                                                      
REMARK 465     LEU u   -11                                                      
REMARK 465     GLY u   -10                                                      
REMARK 465     TRP u    -9                                                      
REMARK 465     ILE u    -8                                                      
REMARK 465     ASN u    -7                                                      
REMARK 465     TRP u    -6                                                      
REMARK 465     SER u    -5                                                      
REMARK 465     ALA u    -4                                                      
REMARK 465     PRO u    -3                                                      
REMARK 465     THR u    -2                                                      
REMARK 465     LEU u    -1                                                      
REMARK 465     ALA u     0                                                      
REMARK 465     ALA u     1                                                      
REMARK 465     THR u     2                                                      
REMARK 465     ALA u     3                                                      
REMARK 465     SER u     4                                                      
REMARK 465     THR u     5                                                      
REMARK 465     GLU u     6                                                      
REMARK 465     GLU u     7                                                      
REMARK 465     GLU u     8                                                      
REMARK 465     MET v   -25                                                      
REMARK 465     LEU v   -24                                                      
REMARK 465     LYS v   -23                                                      
REMARK 465     LYS v   -22                                                      
REMARK 465     CYS v   -21                                                      
REMARK 465     VAL v   -20                                                      
REMARK 465     TRP v   -19                                                      
REMARK 465     LEU v   -18                                                      
REMARK 465     ALA v   -17                                                      
REMARK 465     VAL v   -16                                                      
REMARK 465     ALA v   -15                                                      
REMARK 465     LEU v   -14                                                      
REMARK 465     CYS v   -13                                                      
REMARK 465     LEU v   -12                                                      
REMARK 465     CYS v   -11                                                      
REMARK 465     LEU v   -10                                                      
REMARK 465     TRP v    -9                                                      
REMARK 465     GLN v    -8                                                      
REMARK 465     PHE v    -7                                                      
REMARK 465     THR v    -6                                                      
REMARK 465     MET v    -5                                                      
REMARK 465     GLY v    -4                                                      
REMARK 465     THR v    -3                                                      
REMARK 465     ALA v    -2                                                      
REMARK 465     LEU v    -1                                                      
REMARK 465     ALA v     0                                                      
REMARK 465     MET x     1                                                      
REMARK 465     SER x    40                                                      
REMARK 465     LEU x    41                                                      
REMARK 465     MET R     1                                                      
REMARK 465     LYS R    37                                                      
REMARK 465     ALA R    38                                                      
REMARK 465     LYS R    39                                                      
REMARK 465     ALA R    40                                                      
REMARK 465     ALA R    41                                                      
REMARK 465     MET r     1                                                      
REMARK 465     ASP r     2                                                      
REMARK 465     LEU r    35                                                      
REMARK 465     GLN r    36                                                      
REMARK 465     LYS r    37                                                      
REMARK 465     ALA r    38                                                      
REMARK 465     LYS r    39                                                      
REMARK 465     ALA r    40                                                      
REMARK 465     ALA r    41                                                      
REMARK 465     MET y     1                                                      
REMARK 465     GLY y     2                                                      
REMARK 465     ILE y     3                                                      
REMARK 465     PHE y     4                                                      
REMARK 465     ASN y     5                                                      
REMARK 465     GLY y     6                                                      
REMARK 465     ILE y     7                                                      
REMARK 465     ILE y     8                                                      
REMARK 465     GLU y     9                                                      
REMARK 465     PHE y    10                                                      
REMARK 465     LEU y    11                                                      
REMARK 465     SER y    12                                                      
REMARK 465     ASN y    13                                                      
REMARK 465     ILE y    14                                                      
REMARK 465     ASN y    15                                                      
REMARK 465     PHE y    16                                                      
REMARK 465     GLU y    17                                                      
REMARK 465     VAL y    18                                                      
REMARK 465     ILE y    19                                                      
REMARK 465     ALA y    20                                                      
REMARK 465     GLN y    21                                                      
REMARK 465     LEU y    22                                                      
REMARK 465     THR y    23                                                      
REMARK 465     VAL z    62                                                      
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   OH   TYR d   141     O4   LHG b   628              1.99            
REMARK 500   O    HOH c   657     O    HOH c   665              2.01            
REMARK 500   O    ALA b   155     OG1  THR b   159              2.03            
REMARK 500   O    ILE D   144     OG   SER D   147              2.03            
REMARK 500   O    ALA B   155     OG1  THR B   159              2.04            
REMARK 500   OG1  THR a   286     O1D  CLA a   404              2.06            
REMARK 500   NH2  ARG b   357     O    GLU d   337              2.07            
REMARK 500   O    ALA c   411     O    HOH c   601              2.07            
REMARK 500   OD1  ASP B   119     O    HOH B   701              2.08            
REMARK 500   OG1  THR O    75     O    HOH O   301              2.08            
REMARK 500   NH2  ARG L     7     O8   SQD L   101              2.09            
REMARK 500   O    ASP Z    32     OG   SER Z    36              2.10            
REMARK 500   NH2  ARG U    39     O    ALA V    60              2.10            
REMARK 500   OE1  GLU D   302     OH   TYR D   315              2.11            
REMARK 500   OH   TYR D   296     O    HOH D   501              2.11            
REMARK 500   O    ALA o   111     O    HOH o   301              2.11            
REMARK 500   OG1  THR v    56     O    HOH v   301              2.11            
REMARK 500   O    GLY a   299     O    HOH a   501              2.12            
REMARK 500   OD2  ASP v    83     O    HOH v   302              2.12            
REMARK 500   OG   SER a   232     O5   LHG l   101              2.13            
REMARK 500   OD2  ASP U    26     OG1  THR U    85              2.13            
REMARK 500   O    GLU L     2     O    HOH L   201              2.13            
REMARK 500   O    ASN o   155     O    HOH o   302              2.14            
REMARK 500   O    TRP c   359     O    HOH c   602              2.14            
REMARK 500   OG   SER a    86     O    HOH a   502              2.14            
REMARK 500   OE1  GLU D   344     O    HOH D   502              2.14            
REMARK 500   O5E  DGD c   517     O3   LMG c   519              2.14            
REMARK 500   O    GLU a   231     O    HOH a   503              2.14            
REMARK 500   OG   SER B    74     OE2  GLU B    94              2.16            
REMARK 500   O    HOH A   558     O    HOH C   651              2.16            
REMARK 500   OD1  ASP B   276     O    HOH B   702              2.16            
REMARK 500   OG1  THR D   316     O    HOH D   503              2.16            
REMARK 500   O    GLN Z    31     N    TRP Z    33              2.16            
REMARK 500   OE1  GLN f    41     O4   LMG f   101              2.16            
REMARK 500   O    ASP c    27     OG   SER c    31              2.16            
REMARK 500   OD2  ASP B   433     OG1  THR B   436              2.17            
REMARK 500   OG   SER a   101     O    HOH a   504              2.17            
REMARK 500   NH2  ARG o   189     O    HOH o   303              2.17            
REMARK 500   O    ASP c   360     O2E  DGD c   516              2.17            
REMARK 500   OH   TYR D   141     O4   LHG D   406              2.17            
REMARK 500   O    ARG b   124     NH2  ARG h    12              2.17            
REMARK 500   O    GLY o    28     O    HOH o   304              2.18            
REMARK 500   O    TYR c    82     O    HOH c   603              2.18            
REMARK 500   O    HOH b   756     O    HOH b   767              2.18            
REMARK 500   OD2  ASP C   473     O    HOH C   601              2.18            
REMARK 500   OE2  GLU c   300     O    HOH c   604              2.19            
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    ALA c 399   C     PRO c 400   N      -0.145                       
REMARK 500    ILE e  63   C     PRO e  64   N      -0.206                       
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    ARG B 476   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG D 233   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG c 135   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG r   4   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    LEU z  39   CA  -  CB  -  CG  ANGL. DEV. =  21.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A  30      -79.54    -91.80                                   
REMARK 500    SER A 167      132.28   -175.14                                   
REMARK 500    TYR A 235        2.07    -68.99                                   
REMARK 500    PHE A 239      106.71    -51.79                                   
REMARK 500    ILE A 259      -95.75   -108.67                                   
REMARK 500    TYR B 117       53.96   -112.65                                   
REMARK 500    PHE B 162       72.69   -163.82                                   
REMARK 500    THR B 175       51.83   -142.70                                   
REMARK 500    ASP B 188        6.41    -65.09                                   
REMARK 500    ASP B 313       47.42    -93.26                                   
REMARK 500    ALA B 320       44.72   -100.61                                   
REMARK 500    LYS B 321       21.27   -148.02                                   
REMARK 500    ARG B 326       91.80    -68.25                                   
REMARK 500    ASP C 205      108.78    -46.50                                   
REMARK 500    GLU C 221      -87.12   -113.25                                   
REMARK 500    TRP C 223     -143.42     49.27                                   
REMARK 500    THR C 295      -66.30   -102.55                                   
REMARK 500    PRO C 400       73.36    -67.94                                   
REMARK 500    SER C 416      -50.99    167.88                                   
REMARK 500    ARG D  26     -166.41   -119.79                                   
REMARK 500    VAL D  30      -73.43   -105.40                                   
REMARK 500    SER D  57       22.36   -146.98                                   
REMARK 500    SER D  65        7.86   -161.47                                   
REMARK 500    LEU D 158      -62.10   -109.98                                   
REMARK 500    ALA D 234       31.98    -83.50                                   
REMARK 500    ALA D 351      -61.82     72.37                                   
REMARK 500    PRO E  52      -17.97    -49.78                                   
REMARK 500    ASN H  15       64.27   -116.41                                   
REMARK 500    SER I  25       44.67    -79.17                                   
REMARK 500    SER J  39      -12.82     75.64                                   
REMARK 500    ARG O  42      118.07   -167.38                                   
REMARK 500    LYS O  57      -93.79    -57.19                                   
REMARK 500    ASN O  58       34.83   -144.69                                   
REMARK 500    ARG O  60       18.53     57.33                                   
REMARK 500    GLU O  62      100.12    -37.38                                   
REMARK 500    ARG O  73     -159.44     60.86                                   
REMARK 500    GLU O  98      -61.61   -124.17                                   
REMARK 500    ILE O 101       77.12    -67.22                                   
REMARK 500    ASN O 132       77.10     54.52                                   
REMARK 500    LEU O 164      -68.46   -104.90                                   
REMARK 500    LEU O 192       97.70   -160.88                                   
REMARK 500    THR O 193     -169.22   -101.58                                   
REMARK 500    SER O 221     -157.89    -87.13                                   
REMARK 500    LEU U  27        2.51    -66.87                                   
REMARK 500    ASN U  99       89.80   -167.41                                   
REMARK 500    TYR U 103      -89.18   -108.99                                   
REMARK 500    LEU V  12      -67.37    -91.67                                   
REMARK 500    ASN V  13     -161.38   -110.54                                   
REMARK 500    ASN V  49       80.69   -170.61                                   
REMARK 500    ASN V  78       77.08   -157.82                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     122 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA a   81     VAL a   82                  149.42                    
REMARK 500 ARG z   35     SER z   36                 -145.75                    
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     LFA A  410                                                       
REMARK 610     LFA A  413                                                       
REMARK 610     LMG B  619                                                       
REMARK 610     LFA B  620                                                       
REMARK 610     LMG B  621                                                       
REMARK 610     LFA B  622                                                       
REMARK 610     LFA B  623                                                       
REMARK 610     LFA B  624                                                       
REMARK 610     LFA B  625                                                       
REMARK 610     LFA B  626                                                       
REMARK 610     LFA B  627                                                       
REMARK 610     LFA B  628                                                       
REMARK 610     LMG C  501                                                       
REMARK 610     DGD C  517                                                       
REMARK 610     DGD C  518                                                       
REMARK 610     DGD C  519                                                       
REMARK 610     LMG C  520                                                       
REMARK 610     LFA C  521                                                       
REMARK 610     LMG C  522                                                       
REMARK 610     LMG D  409                                                       
REMARK 610     LFA D  410                                                       
REMARK 610     SQD D  411                                                       
REMARK 610     LFA D  412                                                       
REMARK 610     LFA D  413                                                       
REMARK 610     LHG E  101                                                       
REMARK 610     DGD H  103                                                       
REMARK 610     LFA I  101                                                       
REMARK 610     LFA J  101                                                       
REMARK 610     SQD L  101                                                       
REMARK 610     LFA M  101                                                       
REMARK 610     LFA M  102                                                       
REMARK 610     LFA T  102                                                       
REMARK 610     LFA a  411                                                       
REMARK 610     SQD a  412                                                       
REMARK 610     LFA b  602                                                       
REMARK 610     LFA b  622                                                       
REMARK 610     LFA b  623                                                       
REMARK 610     LMG b  624                                                       
REMARK 610     LFA b  625                                                       
REMARK 610     LFA b  626                                                       
REMARK 610     LFA b  627                                                       
REMARK 610     LFA b  629                                                       
REMARK 610     LFA b  630                                                       
REMARK 610     LMG c  501                                                       
REMARK 610     DGD c  516                                                       
REMARK 610     DGD c  517                                                       
REMARK 610     DGD c  518                                                       
REMARK 610     LMG c  519                                                       
REMARK 610     LFA c  520                                                       
REMARK 610     LFA c  521                                                       
REMARK 610     LMG c  522                                                       
REMARK 610     LFA d  408                                                       
REMARK 610     LFA d  409                                                       
REMARK 610     LFA d  410                                                       
REMARK 610     LHG e  101                                                       
REMARK 610     LMG f  101                                                       
REMARK 610     SQD f  102                                                       
REMARK 610     DGD h  102                                                       
REMARK 610     LFA i  101                                                       
REMARK 610     LFA i  102                                                       
REMARK 610     LFA j  101                                                       
REMARK 610     LFA m  101                                                       
REMARK 610     LFA m  102                                                       
REMARK 610     LMG m  103                                                       
REMARK 610     LFA t  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                              FE A 414  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 215   NE2                                                    
REMARK 620 2 HIS A 272   NE2  95.8                                              
REMARK 620 3 HIS D 214   NE2 104.5  91.1                                        
REMARK 620 4 HIS D 268   NE2  86.6 170.4  97.4                                  
REMARK 620 5 BCT A 415   O1  102.2  75.7 151.2  94.7                            
REMARK 620 6 BCT A 415   O2  158.1  94.2  94.8  80.5  61.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 512  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C  39   OD1                                                    
REMARK 620 2 CLA C 512   NA  104.9                                              
REMARK 620 3 CLA C 512   NB   99.2  89.6                                        
REMARK 620 4 CLA C 512   NC   89.8 165.0  90.8                                  
REMARK 620 5 CLA C 512   ND   94.7  92.7 164.8  83.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM E 102  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  23   NE2                                                    
REMARK 620 2 HEM E 102   NA   88.2                                              
REMARK 620 3 HEM E 102   NB   91.3  90.2                                        
REMARK 620 4 HEM E 102   NC   86.6 174.7  90.8                                  
REMARK 620 5 HEM E 102   ND   83.9  88.9 175.1  89.6                            
REMARK 620 6 HIS F  24   NE2 175.1  87.3  90.6  97.9  94.1                      
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   99.3                                              
REMARK 620 3 HEM V 201   NB   91.8  91.0                                        
REMARK 620 4 HEM V 201   NC   85.7 174.1  91.9                                  
REMARK 620 5 HEM V 201   ND   93.1  88.3 175.1  88.4                            
REMARK 620 6 HIS V  92   NE2 174.0  84.2  93.1  90.6  82.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE a 401  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS a 215   NE2                                                    
REMARK 620 2 HIS a 272   NE2  93.0                                              
REMARK 620 3 HIS d 214   NE2 104.5  92.3                                        
REMARK 620 4 HIS d 268   NE2  85.7 167.2 100.3                                  
REMARK 620 5 BCT a 413   O1  156.0  95.2  97.7  81.3                            
REMARK 620 6 BCT a 413   O2   98.9  73.1 153.0  94.5  62.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c 512  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN c  39   OD1                                                    
REMARK 620 2 CLA c 512   NA  108.4                                              
REMARK 620 3 CLA c 512   NB  100.6  89.6                                        
REMARK 620 4 CLA c 512   NC   87.1 164.2  90.9                                  
REMARK 620 5 CLA c 512   ND   94.0  92.6 163.8  82.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM e 102  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS e  23   NE2                                                    
REMARK 620 2 HEM e 102   NA   94.4                                              
REMARK 620 3 HEM e 102   NB  100.8  90.5                                        
REMARK 620 4 HEM e 102   NC   89.5 173.9  93.3                                  
REMARK 620 5 HEM e 102   ND   83.6  87.1 175.1  88.8                            
REMARK 620 6 HIS f  24   NE2 170.4  82.8  88.4  92.6  87.1                      
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  105.9                                              
REMARK 620 3 HEM v 201   NB   90.6  90.2                                        
REMARK 620 4 HEM v 201   NC   78.6 174.4  93.1                                  
REMARK 620 5 HEM v 201   ND   94.4  86.8 174.7  89.6                            
REMARK 620 6 HIS v  92   NE2 170.9  81.7  94.5  93.5  80.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A 404  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 531   O                                                      
REMARK 620 2 CLA A 404   NA   97.5                                              
REMARK 620 3 CLA A 404   NB  108.9  88.8                                        
REMARK 620 4 CLA A 404   NC   92.3 169.4  91.9                                  
REMARK 620 5 CLA A 404   ND   82.3  94.0 168.0  83.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A 412  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 540   O                                                      
REMARK 620 2 CLA A 412   NA   99.1                                              
REMARK 620 3 CLA A 412   NB   96.0  89.5                                        
REMARK 620 4 CLA A 412   NC   91.4 169.2  92.1                                  
REMARK 620 5 CLA A 412   ND   95.7  93.5 167.3  82.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 606  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 762   O                                                      
REMARK 620 2 CLA B 606   NA   97.6                                              
REMARK 620 3 CLA B 606   NB  104.5  88.7                                        
REMARK 620 4 CLA B 606   NC   96.7 165.2  91.5                                  
REMARK 620 5 CLA B 606   ND   92.9  93.2 162.1  82.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 609  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 748   O                                                      
REMARK 620 2 CLA B 609   NA   92.5                                              
REMARK 620 3 CLA B 609   NB  100.9  89.6                                        
REMARK 620 4 CLA B 609   NC   96.1 170.8  92.0                                  
REMARK 620 5 CLA B 609   ND   89.5  93.7 169.1  83.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 505  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 649   O                                                      
REMARK 620 2 CLA C 505   NA   90.7                                              
REMARK 620 3 CLA C 505   NB   96.3  88.5                                        
REMARK 620 4 CLA C 505   NC  103.8 165.3  92.2                                  
REMARK 620 5 CLA C 505   ND   95.3  94.5 168.0  81.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 508  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 604   O                                                      
REMARK 620 2 CLA C 508   NA   80.7                                              
REMARK 620 3 CLA C 508   NB  104.1  89.4                                        
REMARK 620 4 CLA C 508   NC  110.4 168.1  92.1                                  
REMARK 620 5 CLA C 508   ND   91.8  93.3 164.1  82.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA H 101  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 755   O                                                      
REMARK 620 2 CLA H 101   NA   94.1                                              
REMARK 620 3 CLA H 101   NB   98.1  89.8                                        
REMARK 620 4 CLA H 101   NC   97.1 168.3  91.9                                  
REMARK 620 5 CLA H 101   ND   95.0  93.2 166.4  82.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA a 405  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH a 544   O                                                      
REMARK 620 2 CLA a 405   NA   86.1                                              
REMARK 620 3 CLA a 405   NB   98.6  88.6                                        
REMARK 620 4 CLA a 405   NC  106.8 166.9  91.5                                  
REMARK 620 5 CLA a 405   ND   93.9  93.7 167.4  83.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b 603  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH b 734   O                                                      
REMARK 620 2 CLA b 603   NA   95.8                                              
REMARK 620 3 CLA b 603   NB  107.7  89.2                                        
REMARK 620 4 CLA b 603   NC   94.2 169.0  92.1                                  
REMARK 620 5 CLA b 603   ND   86.2  93.8 165.3  82.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b 609  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH b 756   O                                                      
REMARK 620 2 CLA b 609   NA   90.8                                              
REMARK 620 3 CLA b 609   NB  100.5  87.9                                        
REMARK 620 4 CLA b 609   NC  103.1 165.8  92.5                                  
REMARK 620 5 CLA b 609   ND   93.7  93.8 165.7  82.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b 612  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH b 723   O                                                      
REMARK 620 2 CLA b 612   NA   97.2                                              
REMARK 620 3 CLA b 612   NB   97.0  89.2                                        
REMARK 620 4 CLA b 612   NC   95.9 166.6  91.9                                  
REMARK 620 5 CLA b 612   ND   99.5  92.2 163.1  83.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c 505  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH c 655   O                                                      
REMARK 620 2 CLA c 505   NA   98.8                                              
REMARK 620 3 CLA c 505   NB  101.8  88.6                                        
REMARK 620 4 CLA c 505   NC   96.2 164.6  91.5                                  
REMARK 620 5 CLA c 505   ND   92.1  93.5 165.4  82.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c 508  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH c 637   O                                                      
REMARK 620 2 CLA c 508   NA   92.7                                              
REMARK 620 3 CLA c 508   NB  109.3  89.9                                        
REMARK 620 4 CLA c 508   NC   98.0 168.2  91.3                                  
REMARK 620 5 CLA c 508   ND   84.9  92.8 165.4  83.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA d 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH d 542   O                                                      
REMARK 620 2 CLA d 401   NA   95.0                                              
REMARK 620 3 CLA d 401   NB   97.9  89.4                                        
REMARK 620 4 CLA d 401   NC   95.6 169.0  92.1                                  
REMARK 620 5 CLA d 401   ND   93.0  94.2 168.2  82.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA A 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA A 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE A 414                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT A 415                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA B 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA B 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA B 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA B 624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA B 625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA B 626                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA B 627                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA B 628                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA C 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 522                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR D 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 D 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG D 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA D 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD D 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA D 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA D 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG E 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM E 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA H 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR H 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD H 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA I 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA J 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR K 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR K 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD L 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG L 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA M 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA M 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR T 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA T 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM V 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE a 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO a 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR a 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 a 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA a 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT a 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO a 414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD b 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA b 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA b 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA b 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA b 625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA b 626                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA b 627                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG b 628                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA b 629                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA b 630                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA c 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA c 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 522                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 523                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 524                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR d 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 d 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA d 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA d 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG e 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM e 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG f 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD f 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR h 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD h 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA i 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA j 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AV9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR k 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AW1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG l 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AW2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA m 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AW3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA m 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AW4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG m 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AW5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LFA t 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AW6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR t 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AW7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HEM v 201 and CYS v    
REMARK 800  40                                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AW8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HEM v 201 and CYS v    
REMARK 800  37                                                                  
DBREF  5MX2 A    1   344  UNP    P0A444   PSBA1_THEEB      1    344             
DBREF  5MX2 B    1   510  UNP    Q8DIQ1   PSBB_THEEB       1    510             
DBREF  5MX2 C   13   473  UNP    Q8DIF8   PSBC_THEEB       1    461             
DBREF  5MX2 D    1   352  UNP    Q8CM25   PSBD_THEEB       1    352             
DBREF  5MX2 E    1    84  UNP    Q8DIP0   PSBE_THEEB       1     84             
DBREF  5MX2 F    1    45  UNP    Q8DIN9   PSBF_THEEB       1     45             
DBREF  5MX2 H    1    66  UNP    Q8DJ43   PSBH_THEEB       1     66             
DBREF  5MX2 I    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  5MX2 J    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  5MX2 K    1    46  UNP    Q9F1K9   PSBK_THEEB       1     46             
DBREF  5MX2 L    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  5MX2 M    1    36  UNP    Q8DHA7   PSBM_THEEB       1     36             
DBREF  5MX2 O  -25   246  UNP    P0A431   PSBO_THEEB       1    272             
DBREF  5MX2 T    1    32  UNP    Q8DIQ0   PSBT_THEEB       1     32             
DBREF  5MX2 U  -29   104  UNP    Q9F1L5   PSBU_THEEB       1    134             
DBREF  5MX2 V  -25   137  UNP    P0A386   CY550_THEEB      1    163             
DBREF  5MX2 Y    1    46  UNP    Q8DJI1   YCF12_THEEB      1     46             
DBREF  5MX2 X    1    41  UNP    Q9F1R6   PSBX_THEEB       1     41             
DBREF  5MX2 Z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
DBREF  5MX2 a    1   344  UNP    P0A444   PSBA1_THEEB      1    344             
DBREF  5MX2 b    1   510  UNP    Q8DIQ1   PSBB_THEEB       1    510             
DBREF  5MX2 c   13   473  UNP    Q8DIF8   PSBC_THEEB       1    461             
DBREF  5MX2 d    1   352  UNP    Q8CM25   PSBD_THEEB       1    352             
DBREF  5MX2 e    1    84  UNP    Q8DIP0   PSBE_THEEB       1     84             
DBREF  5MX2 f    1    45  UNP    Q8DIN9   PSBF_THEEB       1     45             
DBREF  5MX2 h    1    66  UNP    Q8DJ43   PSBH_THEEB       1     66             
DBREF  5MX2 i    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  5MX2 j    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  5MX2 k    1    46  UNP    Q9F1K9   PSBK_THEEB       1     46             
DBREF  5MX2 l    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  5MX2 m    1    36  UNP    Q8DHA7   PSBM_THEEB       1     36             
DBREF  5MX2 o  -25   246  UNP    P0A431   PSBO_THEEB       1    272             
DBREF  5MX2 t    1    32  UNP    Q8DIQ0   PSBT_THEEB       1     32             
DBREF  5MX2 u  -29   104  UNP    Q9F1L5   PSBU_THEEB       1    134             
DBREF  5MX2 v  -25   137  UNP    P0A386   CY550_THEEB      1    163             
DBREF  5MX2 x    1    41  UNP    Q9F1R6   PSBX_THEEB       1     41             
DBREF  5MX2 R    1    41  UNP    Q8DKM3   PSBY_THEEB       1     41             
DBREF  5MX2 r    1    41  UNP    Q8DKM3   PSBY_THEEB       1     41             
DBREF  5MX2 y    1    46  UNP    Q8DJI1   YCF12_THEEB      1     46             
DBREF  5MX2 z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
SEQRES   1 A  344  MET THR THR THR LEU GLN ARG ARG GLU SER ALA ASN LEU          
SEQRES   2 A  344  TRP GLU ARG PHE CYS ASN TRP VAL THR SER THR ASP ASN          
SEQRES   3 A  344  ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE MET ILE PRO          
SEQRES   4 A  344  THR LEU LEU ALA ALA THR ILE CYS PHE VAL ILE ALA PHE          
SEQRES   5 A  344  ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY ILE ARG GLU          
SEQRES   6 A  344  PRO VAL SER GLY SER LEU LEU TYR GLY ASN ASN ILE ILE          
SEQRES   7 A  344  THR GLY ALA VAL VAL PRO SER SER ASN ALA ILE GLY LEU          
SEQRES   8 A  344  HIS PHE TYR PRO ILE TRP GLU ALA ALA SER LEU ASP GLU          
SEQRES   9 A  344  TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU ILE ILE PHE          
SEQRES  10 A  344  HIS PHE LEU LEU GLY ALA SER CYS TYR MET GLY ARG GLN          
SEQRES  11 A  344  TRP GLU LEU SER TYR ARG LEU GLY MET ARG PRO TRP ILE          
SEQRES  12 A  344  CYS VAL ALA TYR SER ALA PRO LEU ALA SER ALA PHE ALA          
SEQRES  13 A  344  VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY SER PHE SER          
SEQRES  14 A  344  ASP GLY MET PRO LEU GLY ILE SER GLY THR PHE ASN PHE          
SEQRES  15 A  344  MET ILE VAL PHE GLN ALA GLU HIS ASN ILE LEU MET HIS          
SEQRES  16 A  344  PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL PHE GLY GLY          
SEQRES  17 A  344  ALA LEU PHE CYS ALA MET HIS GLY SER LEU VAL THR SER          
SEQRES  18 A  344  SER LEU ILE ARG GLU THR THR GLU THR GLU SER ALA ASN          
SEQRES  19 A  344  TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU THR TYR ASN          
SEQRES  20 A  344  ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG LEU ILE PHE          
SEQRES  21 A  344  GLN TYR ALA SER PHE ASN ASN SER ARG SER LEU HIS PHE          
SEQRES  22 A  344  PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL TRP PHE THR          
SEQRES  23 A  344  ALA LEU GLY ILE SER THR MET ALA PHE ASN LEU ASN GLY          
SEQRES  24 A  344  PHE ASN PHE ASN HIS SER VAL ILE ASP ALA LYS GLY ASN          
SEQRES  25 A  344  VAL ILE ASN THR TRP ALA ASP ILE ILE ASN ARG ALA ASN          
SEQRES  26 A  344  LEU GLY MET GLU VAL MET HIS GLU ARG ASN ALA HIS ASN          
SEQRES  27 A  344  PHE PRO LEU ASP LEU ALA                                      
SEQRES   1 B  510  MET GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE          
SEQRES   2 B  510  ASN ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS          
SEQRES   3 B  510  THR ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU          
SEQRES   4 B  510  TYR GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU          
SEQRES   5 B  510  ASN PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE          
SEQRES   6 B  510  MET ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP          
SEQRES   7 B  510  SER ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP          
SEQRES   8 B  510  SER PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER          
SEQRES   9 B  510  GLY LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR          
SEQRES  10 B  510  TRP ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU          
SEQRES  11 B  510  PRO ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU          
SEQRES  12 B  510  PHE LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE          
SEQRES  13 B  510  HIS LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER          
SEQRES  14 B  510  ASP PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA          
SEQRES  15 B  510  PRO GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO          
SEQRES  16 B  510  GLY GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL          
SEQRES  17 B  510  GLY ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO          
SEQRES  18 B  510  PRO GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE          
SEQRES  19 B  510  GLU THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE          
SEQRES  20 B  510  ALA ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER          
SEQRES  21 B  510  ALA THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR          
SEQRES  22 B  510  GLN TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG          
SEQRES  23 B  510  ARG VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU          
SEQRES  24 B  510  GLU ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR          
SEQRES  25 B  510  ASP TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE          
SEQRES  26 B  510  ARG THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN          
SEQRES  27 B  510  ALA TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY          
SEQRES  28 B  510  GLU GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU          
SEQRES  29 B  510  SER PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL          
SEQRES  30 B  510  LYS ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR          
SEQRES  31 B  510  SER PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY          
SEQRES  32 B  510  GLY GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR          
SEQRES  33 B  510  VAL LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE          
SEQRES  34 B  510  PHE GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE          
SEQRES  35 B  510  PHE ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS          
SEQRES  36 B  510  ALA VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP          
SEQRES  37 B  510  HIS GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY          
SEQRES  38 B  510  ILE ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY          
SEQRES  39 B  510  PHE TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG LYS          
SEQRES  40 B  510  GLU ALA VAL                                                  
SEQRES   1 C  461  MET VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN          
SEQRES   2 C  461  ARG ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY          
SEQRES   3 C  461  ASN ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY          
SEQRES   4 C  461  ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA          
SEQRES   5 C  461  GLY ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO          
SEQRES   6 C  461  GLU LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO          
SEQRES   7 C  461  HIS ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY          
SEQRES   8 C  461  GLU VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL          
SEQRES   9 C  461  VAL HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY          
SEQRES  10 C  461  VAL TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU          
SEQRES  11 C  461  TYR SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN          
SEQRES  12 C  461  LYS MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU          
SEQRES  13 C  461  GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE          
SEQRES  14 C  461  PHE GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY          
SEQRES  15 C  461  ASP VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG          
SEQRES  16 C  461  VAL ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY          
SEQRES  17 C  461  GLU GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL          
SEQRES  18 C  461  VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA          
SEQRES  19 C  461  GLY GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP          
SEQRES  20 C  461  ALA ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU          
SEQRES  21 C  461  SER TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE          
SEQRES  22 C  461  ALA THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO          
SEQRES  23 C  461  SER GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN          
SEQRES  24 C  461  ALA GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU          
SEQRES  25 C  461  GLY ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU          
SEQRES  26 C  461  GLY LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE          
SEQRES  27 C  461  PHE GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY          
SEQRES  28 C  461  PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP          
SEQRES  29 C  461  LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU          
SEQRES  30 C  461  ARG ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY          
SEQRES  31 C  461  SER LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN          
SEQRES  32 C  461  SER VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR          
SEQRES  33 C  461  SER HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS          
SEQRES  34 C  461  LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY          
SEQRES  35 C  461  PHE GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU          
SEQRES  36 C  461  SER MET PRO SER LEU ASP                                      
SEQRES   1 D  352  MET THR ILE ALA ILE GLY ARG ALA PRO ALA GLU ARG GLY          
SEQRES   2 D  352  TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS ARG ASP ARG          
SEQRES   3 D  352  PHE VAL PHE VAL GLY TRP SER GLY ILE LEU LEU PHE PRO          
SEQRES   4 D  352  CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU THR GLY THR          
SEQRES   5 D  352  THR PHE VAL THR SER TRP TYR THR HIS GLY LEU ALA SER          
SEQRES   6 D  352  SER TYR LEU GLU GLY CYS ASN PHE LEU THR VAL ALA VAL          
SEQRES   7 D  352  SER THR PRO ALA ASN SER MET GLY HIS SER LEU LEU LEU          
SEQRES   8 D  352  LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE THR ARG TRP          
SEQRES   9 D  352  CYS GLN LEU GLY GLY LEU TRP THR PHE ILE ALA LEU HIS          
SEQRES  10 D  352  GLY ALA PHE GLY LEU ILE GLY PHE MET LEU ARG GLN PHE          
SEQRES  11 D  352  GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO TYR ASN ALA          
SEQRES  12 D  352  ILE ALA PHE SER ALA PRO ILE ALA VAL PHE VAL SER VAL          
SEQRES  13 D  352  PHE LEU ILE TYR PRO LEU GLY GLN SER SER TRP PHE PHE          
SEQRES  14 D  352  ALA PRO SER PHE GLY VAL ALA ALA ILE PHE ARG PHE LEU          
SEQRES  15 D  352  LEU PHE PHE GLN GLY PHE HIS ASN TRP THR LEU ASN PRO          
SEQRES  16 D  352  PHE HIS MET MET GLY VAL ALA GLY VAL LEU GLY GLY ALA          
SEQRES  17 D  352  LEU LEU CYS ALA ILE HIS GLY ALA THR VAL GLU ASN THR          
SEQRES  18 D  352  LEU PHE GLN ASP GLY GLU GLY ALA SER THR PHE ARG ALA          
SEQRES  19 D  352  PHE ASN PRO THR GLN ALA GLU GLU THR TYR SER MET VAL          
SEQRES  20 D  352  THR ALA ASN ARG PHE TRP SER GLN ILE PHE GLY ILE ALA          
SEQRES  21 D  352  PHE SER ASN LYS ARG TRP LEU HIS PHE PHE MET LEU PHE          
SEQRES  22 D  352  VAL PRO VAL THR GLY LEU TRP MET SER ALA ILE GLY VAL          
SEQRES  23 D  352  VAL GLY LEU ALA LEU ASN LEU ARG SER TYR ASP PHE ILE          
SEQRES  24 D  352  SER GLN GLU ILE ARG ALA ALA GLU ASP PRO GLU PHE GLU          
SEQRES  25 D  352  THR PHE TYR THR LYS ASN LEU LEU LEU ASN GLU GLY ILE          
SEQRES  26 D  352  ARG ALA TRP MET ALA PRO GLN ASP GLN PRO HIS GLU ASN          
SEQRES  27 D  352  PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG GLY ASN ALA          
SEQRES  28 D  352  LEU                                                          
SEQRES   1 E   84  MET ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE          
SEQRES   2 E   84  ILE THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR          
SEQRES   3 E   84  ILE PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER          
SEQRES   4 E   84  THR GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO          
SEQRES   5 E   84  ASP SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU          
SEQRES   6 E   84  VAL THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR          
SEQRES   7 E   84  PHE LEU GLU GLN LEU LYS                                      
SEQRES   1 F   45  MET THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR          
SEQRES   2 F   45  PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU          
SEQRES   3 F   45  ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA          
SEQRES   4 F   45  MET GLN PHE ILE GLN ARG                                      
SEQRES   1 H   66  MET ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO          
SEQRES   2 H   66  LEU ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY          
SEQRES   3 H   66  THR THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU          
SEQRES   4 H   66  VAL PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR          
SEQRES   5 H   66  LEU ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU          
SEQRES   6 H   66  GLY                                                          
SEQRES   1 I   38  MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR          
SEQRES   2 I   38  PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY          
SEQRES   3 I   38  ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU              
SEQRES   1 J   40  MET MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL          
SEQRES   2 J   40  ALA THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY          
SEQRES   3 J   40  LEU PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER          
SEQRES   4 J   40  LEU                                                          
SEQRES   1 K   46  MET ILE ASP ALA LEU VAL LEU VAL ALA LYS LEU PRO GLU          
SEQRES   2 K   46  ALA TYR ALA ILE PHE ASP PRO LEU VAL ASP VAL LEU PRO          
SEQRES   3 K   46  VAL ILE PRO VAL LEU PHE LEU ALA LEU ALA PHE VAL TRP          
SEQRES   4 K   46  GLN ALA ALA VAL GLY PHE ARG                                  
SEQRES   1 L   37  MET GLU PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN          
SEQRES   2 L   37  ARG THR SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL          
SEQRES   3 L   37  LEU ALA LEU LEU PHE SER SER TYR PHE PHE ASN                  
SEQRES   1 M   36  MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU          
SEQRES   2 M   36  PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR          
SEQRES   3 M   36  VAL GLN THR GLU SER GLN GLN LYS SER SER                      
SEQRES   1 O  272  MET LYS TYR ARG ILE LEU MET ALA THR LEU LEU ALA VAL          
SEQRES   2 O  272  CYS LEU GLY ILE PHE SER LEU SER ALA PRO ALA PHE ALA          
SEQRES   3 O  272  ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY THR          
SEQRES   4 O  272  GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR ALA          
SEQRES   5 O  272  ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR ARG          
SEQRES   6 O  272  ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU VAL          
SEQRES   7 O  272  LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE          
SEQRES   8 O  272  VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER LEU          
SEQRES   9 O  272  ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP GLY          
SEQRES  10 O  272  SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN          
SEQRES  11 O  272  PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE PRO          
SEQRES  12 O  272  LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR GLN          
SEQRES  13 O  272  PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE LYS          
SEQRES  14 O  272  GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN PHE          
SEQRES  15 O  272  LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR ASP          
SEQRES  16 O  272  SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU          
SEQRES  17 O  272  ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS GLY          
SEQRES  18 O  272  GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG THR          
SEQRES  19 O  272  GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU SER          
SEQRES  20 O  272  ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL LYS          
SEQRES  21 O  272  ILE GLN GLY VAL PHE TYR ALA SER ILE GLU PRO ALA              
SEQRES   1 T   32  MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE          
SEQRES   2 T   32  ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO          
SEQRES   3 T   32  PRO ARG ILE THR LYS LYS                                      
SEQRES   1 U  134  MET GLN ARG LEU GLY ARG TRP LEU ALA LEU ALA TYR PHE          
SEQRES   2 U  134  VAL GLY VAL SER LEU LEU GLY TRP ILE ASN TRP SER ALA          
SEQRES   3 U  134  PRO THR LEU ALA ALA THR ALA SER THR GLU GLU GLU LEU          
SEQRES   4 U  134  VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA TYR GLY          
SEQRES   5 U  134  GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA ALA PHE          
SEQRES   6 U  134  ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA LYS LEU          
SEQRES   7 U  134  ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU ASP VAL          
SEQRES   8 U  134  LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS GLN ILE          
SEQRES   9 U  134  LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR GLU VAL          
SEQRES  10 U  134  GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR ASN ASN          
SEQRES  11 U  134  GLY LEU TYR LYS                                              
SEQRES   1 V  163  MET LEU LYS LYS CYS VAL TRP LEU ALA VAL ALA LEU CYS          
SEQRES   2 V  163  LEU CYS LEU TRP GLN PHE THR MET GLY THR ALA LEU ALA          
SEQRES   3 V  163  ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN          
SEQRES   4 V  163  SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR          
SEQRES   5 V  163  LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER          
SEQRES   6 V  163  CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU          
SEQRES   7 V  163  ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO          
SEQRES   8 V  163  ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN          
SEQRES   9 V  163  PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL          
SEQRES  10 V  163  HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET          
SEQRES  11 V  163  ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY          
SEQRES  12 V  163  HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP          
SEQRES  13 V  163  GLY GLY GLY LYS VAL TYR TYR                                  
SEQRES   1 Y   46  MET GLY ILE PHE ASN GLY ILE ILE GLU PHE LEU SER ASN          
SEQRES   2 Y   46  ILE ASN PHE GLU VAL ILE ALA GLN LEU THR MET ILE ALA          
SEQRES   3 Y   46  MET ILE GLY ILE ALA GLY PRO MET ILE ILE PHE LEU LEU          
SEQRES   4 Y   46  ALA VAL ARG ARG GLY ASN LEU                                  
SEQRES   1 X   41  MET THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY          
SEQRES   2 X   41  LEU LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA          
SEQRES   3 X   41  VAL LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG          
SEQRES   4 X   41  SER LEU                                                      
SEQRES   1 Z   62  MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL          
SEQRES   2 Z   62  ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA          
SEQRES   3 Z   62  TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU          
SEQRES   4 Z   62  ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU          
SEQRES   5 Z   62  VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL                      
SEQRES   1 a  344  MET THR THR THR LEU GLN ARG ARG GLU SER ALA ASN LEU          
SEQRES   2 a  344  TRP GLU ARG PHE CYS ASN TRP VAL THR SER THR ASP ASN          
SEQRES   3 a  344  ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE MET ILE PRO          
SEQRES   4 a  344  THR LEU LEU ALA ALA THR ILE CYS PHE VAL ILE ALA PHE          
SEQRES   5 a  344  ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY ILE ARG GLU          
SEQRES   6 a  344  PRO VAL SER GLY SER LEU LEU TYR GLY ASN ASN ILE ILE          
SEQRES   7 a  344  THR GLY ALA VAL VAL PRO SER SER ASN ALA ILE GLY LEU          
SEQRES   8 a  344  HIS PHE TYR PRO ILE TRP GLU ALA ALA SER LEU ASP GLU          
SEQRES   9 a  344  TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU ILE ILE PHE          
SEQRES  10 a  344  HIS PHE LEU LEU GLY ALA SER CYS TYR MET GLY ARG GLN          
SEQRES  11 a  344  TRP GLU LEU SER TYR ARG LEU GLY MET ARG PRO TRP ILE          
SEQRES  12 a  344  CYS VAL ALA TYR SER ALA PRO LEU ALA SER ALA PHE ALA          
SEQRES  13 a  344  VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY SER PHE SER          
SEQRES  14 a  344  ASP GLY MET PRO LEU GLY ILE SER GLY THR PHE ASN PHE          
SEQRES  15 a  344  MET ILE VAL PHE GLN ALA GLU HIS ASN ILE LEU MET HIS          
SEQRES  16 a  344  PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL PHE GLY GLY          
SEQRES  17 a  344  ALA LEU PHE CYS ALA MET HIS GLY SER LEU VAL THR SER          
SEQRES  18 a  344  SER LEU ILE ARG GLU THR THR GLU THR GLU SER ALA ASN          
SEQRES  19 a  344  TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU THR TYR ASN          
SEQRES  20 a  344  ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG LEU ILE PHE          
SEQRES  21 a  344  GLN TYR ALA SER PHE ASN ASN SER ARG SER LEU HIS PHE          
SEQRES  22 a  344  PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL TRP PHE THR          
SEQRES  23 a  344  ALA LEU GLY ILE SER THR MET ALA PHE ASN LEU ASN GLY          
SEQRES  24 a  344  PHE ASN PHE ASN HIS SER VAL ILE ASP ALA LYS GLY ASN          
SEQRES  25 a  344  VAL ILE ASN THR TRP ALA ASP ILE ILE ASN ARG ALA ASN          
SEQRES  26 a  344  LEU GLY MET GLU VAL MET HIS GLU ARG ASN ALA HIS ASN          
SEQRES  27 a  344  PHE PRO LEU ASP LEU ALA                                      
SEQRES   1 b  510  MET GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE          
SEQRES   2 b  510  ASN ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS          
SEQRES   3 b  510  THR ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU          
SEQRES   4 b  510  TYR GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU          
SEQRES   5 b  510  ASN PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE          
SEQRES   6 b  510  MET ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP          
SEQRES   7 b  510  SER ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP          
SEQRES   8 b  510  SER PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER          
SEQRES   9 b  510  GLY LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR          
SEQRES  10 b  510  TRP ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU          
SEQRES  11 b  510  PRO ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU          
SEQRES  12 b  510  PHE LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE          
SEQRES  13 b  510  HIS LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER          
SEQRES  14 b  510  ASP PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA          
SEQRES  15 b  510  PRO GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO          
SEQRES  16 b  510  GLY GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL          
SEQRES  17 b  510  GLY ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO          
SEQRES  18 b  510  PRO GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE          
SEQRES  19 b  510  GLU THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE          
SEQRES  20 b  510  ALA ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER          
SEQRES  21 b  510  ALA THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR          
SEQRES  22 b  510  GLN TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG          
SEQRES  23 b  510  ARG VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU          
SEQRES  24 b  510  GLU ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR          
SEQRES  25 b  510  ASP TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE          
SEQRES  26 b  510  ARG THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN          
SEQRES  27 b  510  ALA TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY          
SEQRES  28 b  510  GLU GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU          
SEQRES  29 b  510  SER PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL          
SEQRES  30 b  510  LYS ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR          
SEQRES  31 b  510  SER PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY          
SEQRES  32 b  510  GLY GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR          
SEQRES  33 b  510  VAL LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE          
SEQRES  34 b  510  PHE GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE          
SEQRES  35 b  510  PHE ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS          
SEQRES  36 b  510  ALA VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP          
SEQRES  37 b  510  HIS GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY          
SEQRES  38 b  510  ILE ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY          
SEQRES  39 b  510  PHE TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG LYS          
SEQRES  40 b  510  GLU ALA VAL                                                  
SEQRES   1 c  461  MET VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN          
SEQRES   2 c  461  ARG ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY          
SEQRES   3 c  461  ASN ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY          
SEQRES   4 c  461  ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA          
SEQRES   5 c  461  GLY ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO          
SEQRES   6 c  461  GLU LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO          
SEQRES   7 c  461  HIS ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY          
SEQRES   8 c  461  GLU VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL          
SEQRES   9 c  461  VAL HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY          
SEQRES  10 c  461  VAL TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU          
SEQRES  11 c  461  TYR SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN          
SEQRES  12 c  461  LYS MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU          
SEQRES  13 c  461  GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE          
SEQRES  14 c  461  PHE GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY          
SEQRES  15 c  461  ASP VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG          
SEQRES  16 c  461  VAL ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY          
SEQRES  17 c  461  GLU GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL          
SEQRES  18 c  461  VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA          
SEQRES  19 c  461  GLY GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP          
SEQRES  20 c  461  ALA ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU          
SEQRES  21 c  461  SER TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE          
SEQRES  22 c  461  ALA THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO          
SEQRES  23 c  461  SER GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN          
SEQRES  24 c  461  ALA GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU          
SEQRES  25 c  461  GLY ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU          
SEQRES  26 c  461  GLY LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE          
SEQRES  27 c  461  PHE GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY          
SEQRES  28 c  461  PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP          
SEQRES  29 c  461  LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU          
SEQRES  30 c  461  ARG ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY          
SEQRES  31 c  461  SER LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN          
SEQRES  32 c  461  SER VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR          
SEQRES  33 c  461  SER HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS          
SEQRES  34 c  461  LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY          
SEQRES  35 c  461  PHE GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU          
SEQRES  36 c  461  SER MET PRO SER LEU ASP                                      
SEQRES   1 d  352  MET THR ILE ALA ILE GLY ARG ALA PRO ALA GLU ARG GLY          
SEQRES   2 d  352  TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS ARG ASP ARG          
SEQRES   3 d  352  PHE VAL PHE VAL GLY TRP SER GLY ILE LEU LEU PHE PRO          
SEQRES   4 d  352  CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU THR GLY THR          
SEQRES   5 d  352  THR PHE VAL THR SER TRP TYR THR HIS GLY LEU ALA SER          
SEQRES   6 d  352  SER TYR LEU GLU GLY CYS ASN PHE LEU THR VAL ALA VAL          
SEQRES   7 d  352  SER THR PRO ALA ASN SER MET GLY HIS SER LEU LEU LEU          
SEQRES   8 d  352  LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE THR ARG TRP          
SEQRES   9 d  352  CYS GLN LEU GLY GLY LEU TRP THR PHE ILE ALA LEU HIS          
SEQRES  10 d  352  GLY ALA PHE GLY LEU ILE GLY PHE MET LEU ARG GLN PHE          
SEQRES  11 d  352  GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO TYR ASN ALA          
SEQRES  12 d  352  ILE ALA PHE SER ALA PRO ILE ALA VAL PHE VAL SER VAL          
SEQRES  13 d  352  PHE LEU ILE TYR PRO LEU GLY GLN SER SER TRP PHE PHE          
SEQRES  14 d  352  ALA PRO SER PHE GLY VAL ALA ALA ILE PHE ARG PHE LEU          
SEQRES  15 d  352  LEU PHE PHE GLN GLY PHE HIS ASN TRP THR LEU ASN PRO          
SEQRES  16 d  352  PHE HIS MET MET GLY VAL ALA GLY VAL LEU GLY GLY ALA          
SEQRES  17 d  352  LEU LEU CYS ALA ILE HIS GLY ALA THR VAL GLU ASN THR          
SEQRES  18 d  352  LEU PHE GLN ASP GLY GLU GLY ALA SER THR PHE ARG ALA          
SEQRES  19 d  352  PHE ASN PRO THR GLN ALA GLU GLU THR TYR SER MET VAL          
SEQRES  20 d  352  THR ALA ASN ARG PHE TRP SER GLN ILE PHE GLY ILE ALA          
SEQRES  21 d  352  PHE SER ASN LYS ARG TRP LEU HIS PHE PHE MET LEU PHE          
SEQRES  22 d  352  VAL PRO VAL THR GLY LEU TRP MET SER ALA ILE GLY VAL          
SEQRES  23 d  352  VAL GLY LEU ALA LEU ASN LEU ARG SER TYR ASP PHE ILE          
SEQRES  24 d  352  SER GLN GLU ILE ARG ALA ALA GLU ASP PRO GLU PHE GLU          
SEQRES  25 d  352  THR PHE TYR THR LYS ASN LEU LEU LEU ASN GLU GLY ILE          
SEQRES  26 d  352  ARG ALA TRP MET ALA PRO GLN ASP GLN PRO HIS GLU ASN          
SEQRES  27 d  352  PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG GLY ASN ALA          
SEQRES  28 d  352  LEU                                                          
SEQRES   1 e   84  MET ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE          
SEQRES   2 e   84  ILE THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR          
SEQRES   3 e   84  ILE PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER          
SEQRES   4 e   84  THR GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO          
SEQRES   5 e   84  ASP SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU          
SEQRES   6 e   84  VAL THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR          
SEQRES   7 e   84  PHE LEU GLU GLN LEU LYS                                      
SEQRES   1 f   45  MET THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR          
SEQRES   2 f   45  PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU          
SEQRES   3 f   45  ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA          
SEQRES   4 f   45  MET GLN PHE ILE GLN ARG                                      
SEQRES   1 h   66  MET ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO          
SEQRES   2 h   66  LEU ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY          
SEQRES   3 h   66  THR THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU          
SEQRES   4 h   66  VAL PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR          
SEQRES   5 h   66  LEU ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU          
SEQRES   6 h   66  GLY                                                          
SEQRES   1 i   38  MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR          
SEQRES   2 i   38  PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY          
SEQRES   3 i   38  ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU              
SEQRES   1 j   40  MET MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL          
SEQRES   2 j   40  ALA THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY          
SEQRES   3 j   40  LEU PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER          
SEQRES   4 j   40  LEU                                                          
SEQRES   1 k   46  MET ILE ASP ALA LEU VAL LEU VAL ALA LYS LEU PRO GLU          
SEQRES   2 k   46  ALA TYR ALA ILE PHE ASP PRO LEU VAL ASP VAL LEU PRO          
SEQRES   3 k   46  VAL ILE PRO VAL LEU PHE LEU ALA LEU ALA PHE VAL TRP          
SEQRES   4 k   46  GLN ALA ALA VAL GLY PHE ARG                                  
SEQRES   1 l   37  MET GLU PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN          
SEQRES   2 l   37  ARG THR SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL          
SEQRES   3 l   37  LEU ALA LEU LEU PHE SER SER TYR PHE PHE ASN                  
SEQRES   1 m   36  MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU          
SEQRES   2 m   36  PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR          
SEQRES   3 m   36  VAL GLN THR GLU SER GLN GLN LYS SER SER                      
SEQRES   1 o  272  MET LYS TYR ARG ILE LEU MET ALA THR LEU LEU ALA VAL          
SEQRES   2 o  272  CYS LEU GLY ILE PHE SER LEU SER ALA PRO ALA PHE ALA          
SEQRES   3 o  272  ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY THR          
SEQRES   4 o  272  GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR ALA          
SEQRES   5 o  272  ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR ARG          
SEQRES   6 o  272  ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU VAL          
SEQRES   7 o  272  LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE          
SEQRES   8 o  272  VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER LEU          
SEQRES   9 o  272  ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP GLY          
SEQRES  10 o  272  SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN          
SEQRES  11 o  272  PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE PRO          
SEQRES  12 o  272  LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR GLN          
SEQRES  13 o  272  PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE LYS          
SEQRES  14 o  272  GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN PHE          
SEQRES  15 o  272  LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR ASP          
SEQRES  16 o  272  SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU          
SEQRES  17 o  272  ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS GLY          
SEQRES  18 o  272  GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG THR          
SEQRES  19 o  272  GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU SER          
SEQRES  20 o  272  ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL LYS          
SEQRES  21 o  272  ILE GLN GLY VAL PHE TYR ALA SER ILE GLU PRO ALA              
SEQRES   1 t   32  MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE          
SEQRES   2 t   32  ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO          
SEQRES   3 t   32  PRO ARG ILE THR LYS LYS                                      
SEQRES   1 u  134  MET GLN ARG LEU GLY ARG TRP LEU ALA LEU ALA TYR PHE          
SEQRES   2 u  134  VAL GLY VAL SER LEU LEU GLY TRP ILE ASN TRP SER ALA          
SEQRES   3 u  134  PRO THR LEU ALA ALA THR ALA SER THR GLU GLU GLU LEU          
SEQRES   4 u  134  VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA TYR GLY          
SEQRES   5 u  134  GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA ALA PHE          
SEQRES   6 u  134  ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA LYS LEU          
SEQRES   7 u  134  ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU ASP VAL          
SEQRES   8 u  134  LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS GLN ILE          
SEQRES   9 u  134  LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR GLU VAL          
SEQRES  10 u  134  GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR ASN ASN          
SEQRES  11 u  134  GLY LEU TYR LYS                                              
SEQRES   1 v  163  MET LEU LYS LYS CYS VAL TRP LEU ALA VAL ALA LEU CYS          
SEQRES   2 v  163  LEU CYS LEU TRP GLN PHE THR MET GLY THR ALA LEU ALA          
SEQRES   3 v  163  ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN          
SEQRES   4 v  163  SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR          
SEQRES   5 v  163  LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER          
SEQRES   6 v  163  CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU          
SEQRES   7 v  163  ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO          
SEQRES   8 v  163  ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN          
SEQRES   9 v  163  PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL          
SEQRES  10 v  163  HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET          
SEQRES  11 v  163  ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY          
SEQRES  12 v  163  HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP          
SEQRES  13 v  163  GLY GLY GLY LYS VAL TYR TYR                                  
SEQRES   1 x   41  MET THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY          
SEQRES   2 x   41  LEU LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA          
SEQRES   3 x   41  VAL LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG          
SEQRES   4 x   41  SER LEU                                                      
SEQRES   1 R   41  MET ASP TRP ARG VAL LEU VAL VAL LEU LEU PRO VAL LEU          
SEQRES   2 R   41  LEU ALA ALA GLY TRP ALA VAL ARG ASN ILE LEU PRO TYR          
SEQRES   3 R   41  ALA VAL LYS GLN VAL GLN LYS LEU LEU GLN LYS ALA LYS          
SEQRES   4 R   41  ALA ALA                                                      
SEQRES   1 r   41  MET ASP TRP ARG VAL LEU VAL VAL LEU LEU PRO VAL LEU          
SEQRES   2 r   41  LEU ALA ALA GLY TRP ALA VAL ARG ASN ILE LEU PRO TYR          
SEQRES   3 r   41  ALA VAL LYS GLN VAL GLN LYS LEU LEU GLN LYS ALA LYS          
SEQRES   4 r   41  ALA ALA                                                      
SEQRES   1 y   46  MET GLY ILE PHE ASN GLY ILE ILE GLU PHE LEU SER ASN          
SEQRES   2 y   46  ILE ASN PHE GLU VAL ILE ALA GLN LEU THR MET ILE ALA          
SEQRES   3 y   46  MET ILE GLY ILE ALA GLY PRO MET ILE ILE PHE LEU LEU          
SEQRES   4 y   46  ALA VAL ARG ARG GLY ASN LEU                                  
SEQRES   1 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     CL  A 401       1                                                       
HET     CL  A 402       1                                                       
HET    CLA  A 403      65                                                       
HET    CLA  A 404      65                                                       
HET    PHO  A 405      64                                                       
HET    CLA  A 406      65                                                       
HET    BCR  A 407      40                                                       
HET    PL9  A 408      55                                                       
HET    SQD  A 409      54                                                       
HET    LFA  A 410      14                                                       
HET    SQD  A 411      54                                                       
HET    CLA  A 412      65                                                       
HET    LFA  A 413      11                                                       
HET     FE  A 414       1                                                       
HET    BCT  A 415       4                                                       
HET    CLA  B 601      65                                                       
HET    CLA  B 602      65                                                       
HET    CLA  B 603      65                                                       
HET    CLA  B 604      65                                                       
HET    CLA  B 605      65                                                       
HET    CLA  B 606      65                                                       
HET    CLA  B 607      65                                                       
HET    CLA  B 608      65                                                       
HET    CLA  B 609      65                                                       
HET    CLA  B 610      65                                                       
HET    CLA  B 611      65                                                       
HET    CLA  B 612      65                                                       
HET    CLA  B 613      65                                                       
HET    CLA  B 614      65                                                       
HET    CLA  B 615      65                                                       
HET    BCR  B 616      40                                                       
HET    BCR  B 617      40                                                       
HET    BCR  B 618      40                                                       
HET    LMG  B 619      51                                                       
HET    LFA  B 620      10                                                       
HET    LMG  B 621      36                                                       
HET    LFA  B 622      16                                                       
HET    LFA  B 623      13                                                       
HET    LFA  B 624      15                                                       
HET    LFA  B 625       9                                                       
HET    LFA  B 626      10                                                       
HET    LFA  B 627      14                                                       
HET    LFA  B 628      12                                                       
HET    LMG  C 501      51                                                       
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    CLA  C 514      65                                                       
HET    BCR  C 515      40                                                       
HET    BCR  C 516      40                                                       
HET    DGD  C 517      62                                                       
HET    DGD  C 518      56                                                       
HET    DGD  C 519      62                                                       
HET    LMG  C 520      48                                                       
HET    LFA  C 521      15                                                       
HET    LMG  C 522      44                                                       
HET    PHO  D 401      64                                                       
HET    CLA  D 402      65                                                       
HET    CLA  D 403      65                                                       
HET    BCR  D 404      40                                                       
HET    PL9  D 405      55                                                       
HET    LHG  D 406      49                                                       
HET    LHG  D 407      49                                                       
HET    LHG  D 408      49                                                       
HET    LMG  D 409      51                                                       
HET    LFA  D 410      15                                                       
HET    SQD  D 411      43                                                       
HET    LFA  D 412       8                                                       
HET    LFA  D 413      10                                                       
HET    LHG  E 101      42                                                       
HET    HEM  E 102      43                                                       
HET    CLA  H 101      65                                                       
HET    BCR  H 102      40                                                       
HET    DGD  H 103      60                                                       
HET    LFA  I 101      14                                                       
HET    LFA  J 101      11                                                       
HET    BCR  K 101      40                                                       
HET    BCR  K 102      40                                                       
HET    SQD  L 101      48                                                       
HET    LHG  L 102      49                                                       
HET    LFA  M 101      10                                                       
HET    LFA  M 102      16                                                       
HET    BCR  T 101      40                                                       
HET    LFA  T 102      12                                                       
HET    HEM  V 201      43                                                       
HET     FE  a 401       1                                                       
HET     CL  a 402       1                                                       
HET     CL  a 403       1                                                       
HET    CLA  a 404      65                                                       
HET    CLA  a 405      65                                                       
HET    PHO  a 406      64                                                       
HET    CLA  a 407      65                                                       
HET    BCR  a 408      40                                                       
HET    PL9  a 409      55                                                       
HET    SQD  a 410      54                                                       
HET    LFA  a 411       7                                                       
HET    SQD  a 412      50                                                       
HET    BCT  a 413       4                                                       
HET    PHO  a 414      64                                                       
HET    SQD  b 601      54                                                       
HET    LFA  b 602      15                                                       
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    CLA  b 618      65                                                       
HET    BCR  b 619      40                                                       
HET    BCR  b 620      40                                                       
HET    BCR  b 621      40                                                       
HET    LFA  b 622      10                                                       
HET    LFA  b 623      12                                                       
HET    LMG  b 624      39                                                       
HET    LFA  b 625      16                                                       
HET    LFA  b 626      12                                                       
HET    LFA  b 627      11                                                       
HET    LHG  b 628      49                                                       
HET    LFA  b 629       9                                                       
HET    LFA  b 630      15                                                       
HET    LMG  c 501      51                                                       
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    CLA  c 514      65                                                       
HET    BCR  c 515      40                                                       
HET    DGD  c 516      62                                                       
HET    DGD  c 517      55                                                       
HET    DGD  c 518      62                                                       
HET    LMG  c 519      51                                                       
HET    LFA  c 520       9                                                       
HET    LFA  c 521      15                                                       
HET    LMG  c 522      41                                                       
HET    BCR  c 523      40                                                       
HET    BCR  c 524      40                                                       
HET    CLA  d 401      65                                                       
HET    CLA  d 402      65                                                       
HET    CLA  d 403      65                                                       
HET    BCR  d 404      40                                                       
HET    PL9  d 405      55                                                       
HET    LHG  d 406      49                                                       
HET    LHG  d 407      49                                                       
HET    LFA  d 408      15                                                       
HET    LFA  d 409       9                                                       
HET    LFA  d 410      16                                                       
HET    LHG  e 101      42                                                       
HET    HEM  e 102      43                                                       
HET    LMG  f 101      51                                                       
HET    SQD  f 102      43                                                       
HET    BCR  h 101      40                                                       
HET    DGD  h 102      62                                                       
HET    LFA  i 101      16                                                       
HET    LFA  i 102       7                                                       
HET    LFA  j 101      15                                                       
HET    BCR  k 101      40                                                       
HET    LHG  l 101      49                                                       
HET    LFA  m 101      10                                                       
HET    LFA  m 102      15                                                       
HET    LMG  m 103      51                                                       
HET    LFA  t 101      15                                                       
HET    BCR  t 102      40                                                       
HET    HEM  v 201      43                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     CLA CHLOROPHYLL A                                                    
HETNAM     PHO PHEOPHYTIN A                                                     
HETNAM     BCR BETA-CAROTENE                                                    
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     SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-                      
HETNAM   2 SQD  GLUCOPYRANOSYL]-SN-GLYCEROL                                     
HETNAM     LFA EICOSANE                                                         
HETNAM      FE FE (III) ION                                                     
HETNAM     BCT BICARBONATE ION                                                  
HETNAM     LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE                        
HETNAM     DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)                              
HETNAM     LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE                           
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETSYN     PL9 PLASTOQUINONE 9                                                  
HETSYN     SQD SULFOQUINOVOSYLDIACYLGLYCEROL                                    
HETSYN     LFA LIPID FRAGMENT                                                   
HETSYN     HEM HEME                                                             
FORMUL  41   CL    4(CL 1-)                                                     
FORMUL  43  CLA    70(C55 H72 MG N4 O5 2+)                                      
FORMUL  45  PHO    4(C55 H74 N4 O5)                                             
FORMUL  47  BCR    22(C40 H56)                                                  
FORMUL  48  PL9    4(C53 H80 O2)                                                
FORMUL  49  SQD    8(C41 H78 O12 S)                                             
FORMUL  50  LFA    39(C20 H42)                                                  
FORMUL  54   FE    2(FE 3+)                                                     
FORMUL  55  BCT    2(C H O3 1-)                                                 
FORMUL  74  LMG    12(C45 H86 O10)                                              
FORMUL  00  DGD    8(C51 H96 O15)                                               
FORMUL  11  LHG    10(C38 H75 O10 P)                                            
FORMUL  20  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL  30  HOH   *703(H2 O)                                                    
HELIX    1 AA1 ASN A   12  THR A   22  1                                  11    
HELIX    2 AA2 VAL A   30  ALA A   55  1                                  26    
HELIX    3 AA3 SER A   70  GLY A   74  5                                   5    
HELIX    4 AA4 SER A  101  GLY A  109  1                                   9    
HELIX    5 AA5 GLY A  109  GLY A  138  1                                  30    
HELIX    6 AA6 TRP A  142  LEU A  159  1                                  18    
HELIX    7 AA7 LEU A  159  GLY A  166  1                                   8    
HELIX    8 AA8 SER A  167  GLY A  171  5                                   5    
HELIX    9 AA9 ILE A  176  ASN A  191  1                                  16    
HELIX   10 AB1 ILE A  192  MET A  194  5                                   3    
HELIX   11 AB2 HIS A  195  SER A  222  1                                  28    
HELIX   12 AB3 SER A  232  TYR A  237  5                                   6    
HELIX   13 AB4 ASN A  247  ILE A  259  1                                  13    
HELIX   14 AB5 PHE A  260  SER A  264  5                                   5    
HELIX   15 AB6 ASN A  267  ALA A  294  1                                  28    
HELIX   16 AB7 THR A  316  VAL A  330  1                                  15    
HELIX   17 AB8 PRO B    4  ILE B   13  5                                  10    
HELIX   18 AB9 ASP B   15  PHE B   45  1                                  31    
HELIX   19 AC1 PRO B   54  GLN B   58  5                                   5    
HELIX   20 AC2 VAL B   62  LEU B   69  1                                   8    
HELIX   21 AC3 SER B   92  TYR B  117  1                                  26    
HELIX   22 AC4 LEU B  120  ARG B  124  5                                   5    
HELIX   23 AC5 ASP B  134  PHE B  156  1                                  23    
HELIX   24 AC6 GLY B  186  PHE B  190  5                                   5    
HELIX   25 AC7 ASN B  194  VAL B  219  1                                  26    
HELIX   26 AC8 PRO B  222  LEU B  229  1                                   8    
HELIX   27 AC9 ASN B  233  GLY B  259  1                                  27    
HELIX   28 AD1 PRO B  264  GLY B  269  1                                   6    
HELIX   29 AD2 THR B  271  SER B  277  1                                   7    
HELIX   30 AD3 SER B  278  SER B  294  1                                  17    
HELIX   31 AD4 THR B  297  ALA B  304  1                                   8    
HELIX   32 AD5 PRO B  306  ASP B  313  1                                   8    
HELIX   33 AD6 TYR B  314  ASN B  318  5                                   5    
HELIX   34 AD7 PRO B  329  GLY B  333  5                                   5    
HELIX   35 AD8 SER B  391  GLY B  396  1                                   6    
HELIX   36 AD9 GLY B  403  ASN B  407  5                                   5    
HELIX   37 AE1 ASP B  413  ILE B  425  1                                  13    
HELIX   38 AE2 SER B  446  PHE B  475  1                                  30    
HELIX   39 AE3 ARG B  476  PHE B  479  5                                   4    
HELIX   40 AE4 SER B  487  VAL B  491  5                                   5    
HELIX   41 AE5 GLN C   28  GLY C   32  1                                   5    
HELIX   42 AE6 ALA C   34  ILE C   43  5                                  10    
HELIX   43 AE7 LEU C   45  PHE C   75  1                                  31    
HELIX   44 AE8 PRO C   80  GLN C   84  5                                   5    
HELIX   45 AE9 ILE C   87  LEU C   95  1                                   9    
HELIX   46 AF1 GLY C  100  GLU C  104  5                                   5    
HELIX   47 AF2 THR C  108  ARG C  135  1                                  28    
HELIX   48 AF3 ASP C  153  PHE C  181  1                                  29    
HELIX   49 AF4 ASP C  205  LEU C  213  1                                   9    
HELIX   50 AF5 GLY C  222  VAL C  227  5                                   6    
HELIX   51 AF6 ASN C  229  THR C  254  1                                  26    
HELIX   52 AF7 PHE C  257  ARG C  262  1                                   6    
HELIX   53 AF8 SER C  267  ASN C  293  1                                  27    
HELIX   54 AF9 PRO C  298  GLY C  303  1                                   6    
HELIX   55 AG1 THR C  305  GLY C  325  1                                  21    
HELIX   56 AG2 GLY C  353  TRP C  359  5                                   7    
HELIX   57 AG3 LEU C  366  PRO C  368  5                                   3    
HELIX   58 AG4 ASP C  376  ASP C  383  1                                   8    
HELIX   59 AG5 GLN C  385  THR C  397  1                                  13    
HELIX   60 AG6 SER C  421  GLY C  454  1                                  34    
HELIX   61 AG7 ASP C  460  GLU C  464  5                                   5    
HELIX   62 AG8 PRO C  465  MET C  469  5                                   5    
HELIX   63 AG9 TRP D   14  LYS D   23  1                                  10    
HELIX   64 AH1 TRP D   32  VAL D   55  1                                  24    
HELIX   65 AH2 SER D   66  GLY D   70  5                                   5    
HELIX   66 AH3 ALA D   82  GLY D   86  5                                   5    
HELIX   67 AH4 ASP D  100  LEU D  107  1                                   8    
HELIX   68 AH5 GLY D  108  GLY D  137  1                                  30    
HELIX   69 AH6 PRO D  140  PHE D  146  1                                   7    
HELIX   70 AH7 PHE D  146  LEU D  158  1                                  13    
HELIX   71 AH8 LEU D  158  GLN D  164  1                                   7    
HELIX   72 AH9 SER D  166  ALA D  170  5                                   5    
HELIX   73 AI1 VAL D  175  PHE D  188  1                                  14    
HELIX   74 AI2 ASN D  190  LEU D  193  5                                   4    
HELIX   75 AI3 ASN D  194  ASN D  220  1                                  27    
HELIX   76 AI4 SER D  230  PHE D  235  5                                   6    
HELIX   77 AI5 SER D  245  GLY D  258  1                                  14    
HELIX   78 AI6 ASN D  263  LEU D  291  1                                  29    
HELIX   79 AI7 PHE D  298  ASP D  308  1                                  11    
HELIX   80 AI8 THR D  313  GLN D  334  1                                  22    
HELIX   81 AI9 PRO D  335  ASN D  338  5                                   4    
HELIX   82 AJ1 PRO D  342  LEU D  346  5                                   5    
HELIX   83 AJ2 PRO E    9  SER E   16  1                                   8    
HELIX   84 AJ3 SER E   16  THR E   40  1                                  25    
HELIX   85 AJ4 GLY E   41  GLY E   48  1                                   8    
HELIX   86 AJ5 GLU E   71  GLN E   82  1                                  12    
HELIX   87 AJ6 THR F   17  GLN F   41  1                                  25    
HELIX   88 AJ7 THR H    5  ARG H   12  1                                   8    
HELIX   89 AJ8 PRO H   13  SER H   16  5                                   4    
HELIX   90 AJ9 THR H   27  ASN H   50  1                                  24    
HELIX   91 AK1 GLU I    2  SER I   25  1                                  24    
HELIX   92 AK2 PRO J    9  ALA J   32  1                                  24    
HELIX   93 AK3 PRO K   12  ILE K   17  5                                   6    
HELIX   94 AK4 PHE K   18  LEU K   25  1                                   8    
HELIX   95 AK5 VAL K   27  VAL K   43  1                                  17    
HELIX   96 AK6 ASN L   13  ASN L   37  1                                  25    
HELIX   97 AK7 LEU M    6  SER M   31  1                                  26    
HELIX   98 AK8 THR O    6  VAL O   11  1                                   6    
HELIX   99 AK9 GLY O   14  LYS O   18  5                                   5    
HELIX  100 AL1 LEU O  182  VAL O  187  1                                   6    
HELIX  101 AL2 GLU T    2  PHE T   23  1                                  22    
HELIX  102 AL3 ASN U   11  LEU U   17  1                                   7    
HELIX  103 AL4 GLY U   18  GLU U   23  5                                   6    
HELIX  104 AL5 ASN U   31  TYR U   38  5                                   8    
HELIX  105 AL6 PRO U   43  ASN U   52  1                                  10    
HELIX  106 AL7 SER U   57  ILE U   64  5                                   8    
HELIX  107 AL8 THR U   68  GLU U   77  1                                  10    
HELIX  108 AL9 ASN U   78  GLU U   80  5                                   3    
HELIX  109 AM1 GLU U   88  GLU U   93  1                                   6    
HELIX  110 AM2 GLY U   94  ASP U   96  5                                   3    
HELIX  111 AM3 THR V   22  CYS V   37  1                                  16    
HELIX  112 AM4 CYS V   37  VAL V   42  1                                   6    
HELIX  113 AM5 GLY V   43  ILE V   45  5                                   3    
HELIX  114 AM6 ARG V   55  ALA V   62  1                                   8    
HELIX  115 AM7 ASN V   68  ASN V   78  1                                  11    
HELIX  116 AM8 PHE V  101  ARG V  105  5                                   5    
HELIX  117 AM9 THR V  108  GLY V  127  1                                  20    
HELIX  118 AN1 ASP V  128  TRP V  130  5                                   3    
HELIX  119 AN2 GLY V  132  TYR V  137  5                                   6    
HELIX  120 AN3 MET Y   27  ARG Y   42  1                                  16    
HELIX  121 AN4 THR X    4  ASP X   35  1                                  32    
HELIX  122 AN5 THR Z    2  ALA Z   28  1                                  27    
HELIX  123 AN6 ASP Z   32  ASN Z   58  1                                  27    
HELIX  124 AN7 PHE Z   59  VAL Z   61  5                                   3    
HELIX  125 AN8 LEU a   13  THR a   22  1                                  10    
HELIX  126 AN9 VAL a   30  ALA a   55  1                                  26    
HELIX  127 AO1 SER a   70  GLY a   74  5                                   5    
HELIX  128 AO2 PRO a   95  ALA a   99  5                                   5    
HELIX  129 AO3 SER a  101  ASN a  108  1                                   8    
HELIX  130 AO4 GLY a  109  GLY a  138  1                                  30    
HELIX  131 AO5 TRP a  142  LEU a  159  1                                  18    
HELIX  132 AO6 LEU a  159  GLY a  166  1                                   8    
HELIX  133 AO7 SER a  167  GLY a  171  5                                   5    
HELIX  134 AO8 ILE a  176  ASN a  191  1                                  16    
HELIX  135 AO9 ILE a  192  MET a  194  5                                   3    
HELIX  136 AP1 HIS a  195  SER a  221  1                                  27    
HELIX  137 AP2 SER a  232  TYR a  237  5                                   6    
HELIX  138 AP3 ASN a  247  ILE a  259  1                                  13    
HELIX  139 AP4 PHE a  260  SER a  264  5                                   5    
HELIX  140 AP5 ASN a  267  ALA a  294  1                                  28    
HELIX  141 AP6 THR a  316  VAL a  330  1                                  15    
HELIX  142 AP7 PRO b    4  ILE b   13  5                                  10    
HELIX  143 AP8 ASP b   15  PHE b   45  1                                  31    
HELIX  144 AP9 PRO b   54  GLN b   58  5                                   5    
HELIX  145 AQ1 VAL b   62  LEU b   69  1                                   8    
HELIX  146 AQ2 SER b   92  TYR b  117  1                                  26    
HELIX  147 AQ3 LEU b  120  ARG b  124  5                                   5    
HELIX  148 AQ4 ASP b  134  PHE b  156  1                                  23    
HELIX  149 AQ5 GLY b  186  ASN b  191  5                                   6    
HELIX  150 AQ6 ASN b  194  VAL b  219  1                                  26    
HELIX  151 AQ7 PRO b  222  LEU b  229  1                                   8    
HELIX  152 AQ8 ASN b  233  GLY b  259  1                                  27    
HELIX  153 AQ9 PRO b  264  GLY b  269  1                                   6    
HELIX  154 AR1 THR b  271  SER b  277  1                                   7    
HELIX  155 AR2 SER b  278  GLY b  295  1                                  18    
HELIX  156 AR3 THR b  297  ALA b  304  1                                   8    
HELIX  157 AR4 PRO b  306  ASP b  313  1                                   8    
HELIX  158 AR5 TYR b  314  ASN b  318  5                                   5    
HELIX  159 AR6 PRO b  329  GLY b  333  5                                   5    
HELIX  160 AR7 ASP b  413  ILE b  425  1                                  13    
HELIX  161 AR8 SER b  446  PHE b  475  1                                  30    
HELIX  162 AR9 ARG b  476  PHE b  479  5                                   4    
HELIX  163 AS1 SER b  487  VAL b  491  5                                   5    
HELIX  164 AS2 ASP c   27  GLY c   32  1                                   6    
HELIX  165 AS3 ALA c   34  ILE c   43  5                                  10    
HELIX  166 AS4 LEU c   45  HIS c   74  1                                  30    
HELIX  167 AS5 PRO c   80  GLY c   85  5                                   6    
HELIX  168 AS6 LEU c   88  LEU c   95  1                                   8    
HELIX  169 AS7 GLY c  100  GLU c  104  5                                   5    
HELIX  170 AS8 THR c  108  ARG c  135  1                                  28    
HELIX  171 AS9 ASP c  153  PHE c  182  1                                  30    
HELIX  172 AT1 ASP c  205  LEU c  213  1                                   9    
HELIX  173 AT2 GLY c  222  VAL c  227  5                                   6    
HELIX  174 AT3 ASN c  229  THR c  254  1                                  26    
HELIX  175 AT4 PHE c  257  PHE c  264  1                                   8    
HELIX  176 AT5 SER c  267  ASN c  293  1                                  27    
HELIX  177 AT6 PRO c  298  GLY c  303  1                                   6    
HELIX  178 AT7 THR c  305  GLY c  325  1                                  21    
HELIX  179 AT8 GLY c  353  TRP c  359  5                                   7    
HELIX  180 AT9 LEU c  366  PRO c  368  5                                   3    
HELIX  181 AU1 ASP c  376  ASP c  383  1                                   8    
HELIX  182 AU2 GLN c  385  THR c  397  1                                  13    
HELIX  183 AU3 SER c  421  GLY c  454  1                                  34    
HELIX  184 AU4 ASP c  460  MET c  469  5                                  10    
HELIX  185 AU5 TRP d   14  LYS d   23  1                                  10    
HELIX  186 AU6 SER d   33  VAL d   55  1                                  23    
HELIX  187 AU7 SER d   66  GLY d   70  5                                   5    
HELIX  188 AU8 ALA d   82  GLY d   86  5                                   5    
HELIX  189 AU9 ASP d  100  LEU d  107  1                                   8    
HELIX  190 AV1 GLY d  108  GLY d  137  1                                  30    
HELIX  191 AV2 PRO d  140  PHE d  146  1                                   7    
HELIX  192 AV3 PHE d  146  LEU d  158  1                                  13    
HELIX  193 AV4 LEU d  158  GLN d  164  1                                   7    
HELIX  194 AV5 SER d  166  ALA d  170  5                                   5    
HELIX  195 AV6 GLY d  174  ASN d  190  1                                  17    
HELIX  196 AV7 TRP d  191  LEU d  193  5                                   3    
HELIX  197 AV8 ASN d  194  ASN d  220  1                                  27    
HELIX  198 AV9 SER d  245  GLY d  258  1                                  14    
HELIX  199 AW1 ASN d  263  LEU d  291  1                                  29    
HELIX  200 AW2 PHE d  298  ASP d  308  1                                  11    
HELIX  201 AW3 THR d  313  GLN d  334  1                                  22    
HELIX  202 AW4 PRO d  335  ASN d  338  5                                   4    
HELIX  203 AW5 PRO d  342  LEU d  346  5                                   5    
HELIX  204 AW6 PRO e    9  ILE e   14  1                                   6    
HELIX  205 AW7 SER e   16  THR e   40  1                                  25    
HELIX  206 AW8 GLY e   41  GLY e   48  1                                   8    
HELIX  207 AW9 GLU e   71  GLN e   82  1                                  12    
HELIX  208 AX1 THR f   17  GLN f   41  1                                  25    
HELIX  209 AX2 THR h    5  ARG h   12  1                                   8    
HELIX  210 AX3 THR h   27  ASN h   50  1                                  24    
HELIX  211 AX4 GLU i    2  SER i   25  1                                  24    
HELIX  212 AX5 GLY i   26  ARG i   30  5                                   5    
HELIX  213 AX6 PRO j    9  ALA j   32  1                                  24    
HELIX  214 AX7 PRO k   12  ILE k   17  5                                   6    
HELIX  215 AX8 PHE k   18  ASP k   23  1                                   6    
HELIX  216 AX9 VAL k   24  PRO k   26  5                                   3    
HELIX  217 AY1 VAL k   27  VAL k   43  1                                  17    
HELIX  218 AY2 ASN l   13  ASN l   37  1                                  25    
HELIX  219 AY3 LEU m    6  SER m   31  1                                  26    
HELIX  220 AY4 THR o    6  VAL o   11  1                                   6    
HELIX  221 AY5 GLY o   14  LYS o   18  5                                   5    
HELIX  222 AY6 LEU o  182  VAL o  187  1                                   6    
HELIX  223 AY7 GLU t    2  PHE t   23  1                                  22    
HELIX  224 AY8 ASN u   11  LEU u   17  1                                   7    
HELIX  225 AY9 GLY u   18  GLU u   23  5                                   6    
HELIX  226 AZ1 ASN u   31  TYR u   38  5                                   8    
HELIX  227 AZ2 PRO u   43  ALA u   53  1                                  11    
HELIX  228 AZ3 SER u   57  ILE u   64  5                                   8    
HELIX  229 AZ4 THR u   68  ASN u   78  1                                  11    
HELIX  230 AZ5 GLU u   88  GLU u   93  1                                   6    
HELIX  231 AZ6 THR v   22  CYS v   37  1                                  16    
HELIX  232 AZ7 CYS v   37  VAL v   42  1                                   6    
HELIX  233 AZ8 GLY v   43  ILE v   45  5                                   3    
HELIX  234 AZ9 ARG v   55  ALA v   60  1                                   6    
HELIX  235 BA1 ASN v   68  ASN v   78  1                                  11    
HELIX  236 BA2 PHE v  101  ARG v  105  5                                   5    
HELIX  237 BA3 THR v  108  GLY v  127  1                                  20    
HELIX  238 BA4 ASP v  128  TRP v  130  5                                   3    
HELIX  239 BA5 GLY v  133  TYR v  137  5                                   5    
HELIX  240 BA6 THR x    4  ASP x   35  1                                  32    
HELIX  241 BA7 TRP R    3  LEU R   35  1                                  33    
HELIX  242 BA8 ARG r    4  LEU r   34  1                                  31    
HELIX  243 BA9 ILE y   25  ARG y   42  1                                  18    
HELIX  244 BB1 THR z    2  SER z   29  1                                  28    
HELIX  245 BB2 ASP z   32  ASN z   58  1                                  27    
HELIX  246 BB3 PHE z   59  VAL z   61  5                                   3    
SHEET    1 AA1 2 ALA A  81  VAL A  82  0                                        
SHEET    2 AA1 2 LEU A 174  GLY A 175 -1  O  LEU A 174   N  VAL A  82           
SHEET    1 AA2 2 LEU A 297  ASN A 298  0                                        
SHEET    2 AA2 2 GLY C 402  SER C 403  1  O  GLY C 402   N  ASN A 298           
SHEET    1 AA3 2 MET B 166  VAL B 168  0                                        
SHEET    2 AA3 2 SER B 177  GLN B 179 -1  O  SER B 177   N  VAL B 168           
SHEET    1 AA4 6 VAL B 377  ASP B 380  0                                        
SHEET    2 AA4 6 ILE B 369  THR B 371 -1  N  LEU B 370   O  ALA B 379           
SHEET    3 AA4 6 GLU B 353  VAL B 356 -1  N  PHE B 355   O  THR B 371           
SHEET    4 AA4 6 ILE B 336  ARG B 347 -1  N  PHE B 346   O  LEU B 354           
SHEET    5 AA4 6 THR B 398  TYR B 402 -1  O  SER B 400   N  VAL B 345           
SHEET    6 AA4 6 THR B 410  PHE B 411 -1  O  PHE B 411   N  VAL B 399           
SHEET    1 AA5 5 VAL B 377  ASP B 380  0                                        
SHEET    2 AA5 5 ILE B 369  THR B 371 -1  N  LEU B 370   O  ALA B 379           
SHEET    3 AA5 5 GLU B 353  VAL B 356 -1  N  PHE B 355   O  THR B 371           
SHEET    4 AA5 5 ILE B 336  ARG B 347 -1  N  PHE B 346   O  LEU B 354           
SHEET    5 AA5 5 ILE B 429  ASP B 433 -1  O  GLU B 431   N  GLN B 338           
SHEET    1 AA6 2 LEU C 185  ASP C 187  0                                        
SHEET    2 AA6 2 ASP C 195  ARG C 197 -1  O  ASP C 195   N  ASP C 187           
SHEET    1 AA7 2 LEU C 341  ARG C 343  0                                        
SHEET    2 AA7 2 ILE C 349  PHE C 351 -1  O  ILE C 350   N  MET C 342           
SHEET    1 AA8 2 ARG C 370  GLY C 371  0                                        
SHEET    2 AA8 2 GLY C 374  LEU C 375 -1  O  GLY C 374   N  GLY C 371           
SHEET    1 AA9 2 ALA D  77  VAL D  78  0                                        
SHEET    2 AA9 2 PHE D 173  GLY D 174 -1  O  PHE D 173   N  VAL D  78           
SHEET    1 AB1 2 TYR O  30  PRO O  31  0                                        
SHEET    2 AB1 2 SER O 135  ILE O 136 -1  O  ILE O 136   N  TYR O  30           
SHEET    1 AB210 PHE O  65  PRO O  67  0                                        
SHEET    2 AB210 TYR O  38  LYS O  53 -1  N  VAL O  52   O  VAL O  66           
SHEET    3 AB210 GLU O 232  GLU O 244 -1  O  LYS O 234   N  LEU O  51           
SHEET    4 AB210 GLU O 210  LEU O 220 -1  N  GLN O 219   O  VAL O 233           
SHEET    5 AB210 LEU O 192  ASP O 205 -1  N  ALA O 202   O  ALA O 212           
SHEET    6 AB210 ASP O 141  PRO O 149 -1  N  PHE O 146   O  GLY O 195           
SHEET    7 AB210 VAL O 126  SER O 128 -1  N  SER O 128   O  LYS O 143           
SHEET    8 AB210 LEU O  93  ILE O 101 -1  N  PHE O  95   O  ALA O 127           
SHEET    9 AB210 LEU O  78  VAL O  87 -1  N  LYS O  86   O  THR O  94           
SHEET   10 AB210 TYR O  38  LYS O  53 -1  N  LEU O  45   O  LEU O  78           
SHEET    1 AB3 3 LYS O  69  LEU O  70  0                                        
SHEET    2 AB3 3 PHE O 103  GLN O 109 -1  O  GLN O 109   N  LYS O  69           
SHEET    3 AB3 3 ARG O 115  THR O 121 -1  O  LEU O 118   N  VAL O 106           
SHEET    1 AB4 2 ILE U  25  ASP U  26  0                                        
SHEET    2 AB4 2 PHE U  82  THR U  83  1  O  THR U  83   N  ILE U  25           
SHEET    1 AB5 2 THR V   9  PRO V  11  0                                        
SHEET    2 AB5 2 THR V  18  THR V  20 -1  O  ILE V  19   N  VAL V  10           
SHEET    1 AB6 2 ALA a  81  VAL a  82  0                                        
SHEET    2 AB6 2 LEU a 174  GLY a 175 -1  O  LEU a 174   N  VAL a  82           
SHEET    1 AB7 2 LEU a 297  ASN a 298  0                                        
SHEET    2 AB7 2 GLY c 402  SER c 403  1  O  GLY c 402   N  ASN a 298           
SHEET    1 AB8 2 MET b 166  VAL b 168  0                                        
SHEET    2 AB8 2 SER b 177  GLN b 179 -1  O  GLN b 179   N  MET b 166           
SHEET    1 AB9 6 VAL b 377  ASP b 380  0                                        
SHEET    2 AB9 6 ILE b 369  THR b 371 -1  N  LEU b 370   O  ALA b 379           
SHEET    3 AB9 6 GLU b 353  VAL b 356 -1  N  PHE b 355   O  THR b 371           
SHEET    4 AB9 6 ILE b 336  ARG b 347 -1  N  PHE b 346   O  LEU b 354           
SHEET    5 AB9 6 THR b 398  TYR b 402 -1  O  SER b 400   N  VAL b 345           
SHEET    6 AB9 6 GLN b 409  PHE b 411 -1  O  GLN b 409   N  PHE b 401           
SHEET    1 AC1 5 VAL b 377  ASP b 380  0                                        
SHEET    2 AC1 5 ILE b 369  THR b 371 -1  N  LEU b 370   O  ALA b 379           
SHEET    3 AC1 5 GLU b 353  VAL b 356 -1  N  PHE b 355   O  THR b 371           
SHEET    4 AC1 5 ILE b 336  ARG b 347 -1  N  PHE b 346   O  LEU b 354           
SHEET    5 AC1 5 ILE b 429  ASP b 433 -1  O  ILE b 429   N  LYS b 341           
SHEET    1 AC2 2 LEU c 185  ASP c 187  0                                        
SHEET    2 AC2 2 ASP c 195  ARG c 197 -1  O  ASP c 195   N  ASP c 187           
SHEET    1 AC3 2 LEU c 341  ARG c 343  0                                        
SHEET    2 AC3 2 ILE c 349  PHE c 351 -1  O  ILE c 350   N  MET c 342           
SHEET    1 AC4 2 ARG c 370  GLY c 371  0                                        
SHEET    2 AC4 2 GLY c 374  LEU c 375 -1  O  GLY c 374   N  GLY c 371           
SHEET    1 AC5 2 TYR o  30  PRO o  31  0                                        
SHEET    2 AC5 2 SER o 135  ILE o 136 -1  O  ILE o 136   N  TYR o  30           
SHEET    1 AC610 PHE o  65  PRO o  67  0                                        
SHEET    2 AC610 TYR o  38  LYS o  53 -1  N  VAL o  52   O  VAL o  66           
SHEET    3 AC610 GLU o 232  GLU o 244 -1  O  GLN o 236   N  THR o  48           
SHEET    4 AC610 GLU o 210  LEU o 220 -1  N  SER o 217   O  ILE o 235           
SHEET    5 AC610 THR o 193  ASP o 205 -1  N  ALA o 202   O  ALA o 212           
SHEET    6 AC610 ASP o 141  VAL o 148 -1  N  VAL o 148   O  THR o 193           
SHEET    7 AC610 VAL o 126  SER o 128 -1  N  SER o 128   O  LYS o 143           
SHEET    8 AC610 LEU o  93  ILE o 101 -1  N  PHE o  95   O  ALA o 127           
SHEET    9 AC610 LEU o  78  VAL o  87 -1  N  LYS o  86   O  THR o  94           
SHEET   10 AC610 TYR o  38  LYS o  53 -1  N  LEU o  45   O  LEU o  78           
SHEET    1 AC7 3 LYS o  69  LEU o  70  0                                        
SHEET    2 AC7 3 PHE o 103  GLN o 109 -1  O  GLN o 109   N  LYS o  69           
SHEET    3 AC7 3 ARG o 115  THR o 121 -1  O  ILE o 116   N  VAL o 108           
SHEET    1 AC8 2 ILE u  25  ASP u  26  0                                        
SHEET    2 AC8 2 PHE u  82  THR u  83  1  O  THR u  83   N  ILE u  25           
SHEET    1 AC9 2 THR v   9  PRO v  11  0                                        
SHEET    2 AC9 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  2.02  
SSBOND   2 CYS o   19    CYS o   44                          1555   1555  2.03  
LINK         NE2 HIS A 215                FE    FE A 414     1555   1555  2.16  
LINK         NE2 HIS A 272                FE    FE A 414     1555   1555  2.50  
LINK         OD1 ASN C  39                MG   CLA C 512     1555   1555  2.16  
LINK         NE2 HIS D 214                FE    FE A 414     1555   1555  2.16  
LINK         NE2 HIS D 268                FE    FE A 414     1555   1555  2.40  
LINK         NE2 HIS E  23                FE   HEM E 102     1555   1555  2.03  
LINK         NE2 HIS F  24                FE   HEM E 102     1555   1555  2.06  
LINK         SG  CYS V  37                 CAB HEM V 201     1555   1555  1.77  
LINK         SG  CYS V  40                 CAC HEM V 201     1555   1555  1.81  
LINK         NE2 HIS V  41                FE   HEM V 201     1555   1555  1.88  
LINK         NE2 HIS V  92                FE   HEM V 201     1555   1555  2.09  
LINK         NE2 HIS a 215                FE    FE a 401     1555   1555  2.16  
LINK         NE2 HIS a 272                FE    FE a 401     1555   1555  2.44  
LINK         OD1 ASN c  39                MG   CLA c 512     1555   1555  2.13  
LINK         NE2 HIS d 214                FE    FE a 401     1555   1555  2.07  
LINK         NE2 HIS d 268                FE    FE a 401     1555   1555  2.39  
LINK         NE2 HIS e  23                FE   HEM e 102     1555   1555  1.85  
LINK         NE2 HIS f  24                FE   HEM e 102     1555   1555  2.19  
LINK         SG  CYS v  37                 CAB HEM v 201     1555   1555  1.77  
LINK         SG  CYS v  40                 CAC HEM v 201     1555   1555  1.83  
LINK         NE2 HIS v  41                FE   HEM v 201     1555   1555  1.89  
LINK         NE2 HIS v  92                FE   HEM v 201     1555   1555  2.06  
LINK        MG   CLA A 404                 O   HOH A 531     1555   1555  2.13  
LINK        MG   CLA A 412                 O   HOH A 540     1555   1555  2.13  
LINK        FE    FE A 414                 O1  BCT A 415     1555   1555  2.05  
LINK        FE    FE A 414                 O2  BCT A 415     1555   1555  2.04  
LINK        MG   CLA B 606                 O   HOH B 762     1555   1555  2.16  
LINK        MG   CLA B 609                 O   HOH B 748     1555   1555  2.14  
LINK        MG   CLA C 505                 O   HOH C 649     1555   1555  2.14  
LINK        MG   CLA C 508                 O   HOH C 604     1555   1555  2.14  
LINK        MG   CLA H 101                 O   HOH B 755     1555   1555  2.14  
LINK        FE    FE a 401                 O1  BCT a 413     1555   1555  2.05  
LINK        FE    FE a 401                 O2  BCT a 413     1555   1555  2.03  
LINK        MG   CLA a 405                 O   HOH a 544     1555   1555  2.12  
LINK        MG   CLA b 603                 O   HOH b 734     1555   1555  2.13  
LINK        MG   CLA b 609                 O   HOH b 756     1555   1555  2.17  
LINK        MG   CLA b 612                 O   HOH b 723     1555   1555  2.14  
LINK        MG   CLA c 505                 O   HOH c 655     1555   1555  2.14  
LINK        MG   CLA c 508                 O   HOH c 637     1555   1555  2.13  
LINK        MG   CLA d 401                 O   HOH d 542     1555   1555  2.13  
CISPEP   1 TYR U   42    PRO U   43          0         0.53                     
CISPEP   2 ALA U   53    PRO U   54          0         1.08                     
CISPEP   3 THR V   63    PRO V   64          0        -9.47                     
CISPEP   4 TYR u   42    PRO u   43          0         8.72                     
CISPEP   5 ALA u   53    PRO u   54          0         6.48                     
CISPEP   6 THR v   63    PRO v   64          0        -5.62                     
SITE     1 AC1  3 ASN A 181  HIS A 332  GLU A 333                               
SITE     1 AC2  4 HIS A 337  ASN A 338  PHE A 339  GLU C 354                    
SITE     1 AC3 18 PRO A 150  SER A 153  VAL A 157  MET A 183                    
SITE     2 AC3 18 PHE A 186  GLN A 187  LEU A 193  HIS A 198                    
SITE     3 AC3 18 GLY A 201  THR A 286  ALA A 287  ILE A 290                    
SITE     4 AC3 18 CLA A 404  CLA A 412  PHO D 401  CLA D 402                    
SITE     5 AC3 18 LHG D 407  PHE T  17                                          
SITE     1 AC4 16 GLN A 199  VAL A 202  ALA A 203  GLY A 207                    
SITE     2 AC4 16 TRP A 278  CLA A 403  PHO A 405  PL9 A 408                    
SITE     3 AC4 16 HOH A 531  VAL D 175  ILE D 178  PHE D 179                    
SITE     4 AC4 16 PHE D 181  LEU D 182  CLA D 402  LMG D 409                    
SITE     1 AC5 19 ALA A 209  LEU A 210  MET A 214  CLA A 404                    
SITE     2 AC5 19 PL9 A 408  ALA D  41  TRP D  48  ILE D 114                    
SITE     3 AC5 19 GLY D 121  LEU D 122  PHE D 125  GLN D 129                    
SITE     4 AC5 19 ASN D 142  PHE D 146  PHE D 153  GLY D 174                    
SITE     5 AC5 19 PRO D 275  LEU D 279  CLA D 402                               
SITE     1 AC6 18 THR A  40  PHE A  93  PRO A  95  ILE A  96                    
SITE     2 AC6 18 TRP A  97  LEU A 114  HIS A 118  LMG C 501                    
SITE     3 AC6 18 CLA C 506  CLA C 507  BCR C 516  DGD C 517                    
SITE     4 AC6 18 VAL I   8  TYR I   9  VAL I  11  VAL I  12                    
SITE     5 AC6 18 THR I  13  PHE I  15                                          
SITE     1 AC7  6 ALA A  43  TRP A 105  LEU A 106  PHE I  15                    
SITE     2 AC7  6 LFA I 101  LFA b 622                                          
SITE     1 AC8 20 PHE A 211  HIS A 215  LEU A 218  ILE A 248                    
SITE     2 AC8 20 HIS A 252  PHE A 255  SER A 264  PHE A 265                    
SITE     3 AC8 20 LEU A 271  LEU A 275  CLA A 404  PHO A 405                    
SITE     4 AC8 20 PHE D  38  PRO D  39  LEU D  45  SQD D 411                    
SITE     5 AC8 20 LHG E 101  THR F  25  LEU F  26  THR X  24                    
SITE     1 AC9 10 LEU A 200  ASN A 267  SER A 270  GLN C  28                    
SITE     2 AC9 10 ALA C  34  TRP C  36  CLA C 509  PHE D 232                    
SITE     3 AC9 10 LHG D 408  PHE K  37                                          
SITE     1 AD1  1 TRP A  20                                                     
SITE     1 AD2 12 TRP A  20  ASN A  26  ARG A  27  LEU A  28                    
SITE     2 AD2 12 ILE A  38  LEU A  42  CLA A 412  PHE T  22                    
SITE     3 AD2 12 BCR T 101  TRP b 113  TYR b 117  BCR b 621                    
SITE     1 AD3 17 MET A 172  ILE A 176  THR A 179  PHE A 180                    
SITE     2 AD3 17 MET A 183  CLA A 403  SQD A 411  HOH A 504                    
SITE     3 AD3 17 HOH A 540  MET D 198  VAL D 201  ALA D 202                    
SITE     4 AD3 17 LEU D 205  GLY D 206  PHO D 401  PL9 D 405                    
SITE     5 AD3 17 LHG D 407                                                     
SITE     1 AD4  4 LEU A 102  ASP A 103  TRP b  75  ASP b  87                    
SITE     1 AD5  5 HIS A 215  HIS A 272  BCT A 415  HIS D 214                    
SITE     2 AD5  5 HIS D 268                                                     
SITE     1 AD6  8 HIS A 215  TYR A 246  HIS A 272   FE A 414                    
SITE     2 AD6  8 HIS D 214  TYR D 244  LYS D 264  HIS D 268                    
SITE     1 AD7 15 GLY B 189  PHE B 190  GLY B 197  HIS B 201                    
SITE     2 AD7 15 VAL B 208  PHE B 247  PHE B 250  CLA B 602                    
SITE     3 AD7 15 CLA B 608  LEU D 162  PHE H  38  ILE H  45                    
SITE     4 AD7 15 TYR H  49  CLA H 101  DGD H 103                               
SITE     1 AD8 17 ARG B  68  LEU B  69  ALA B 146  CYS B 150                    
SITE     2 AD8 17 HIS B 201  HIS B 202  PHE B 247  VAL B 252                    
SITE     3 AD8 17 THR B 262  CLA B 601  CLA B 603  CLA B 604                    
SITE     4 AD8 17 CLA B 605  CLA B 607  CLA B 608  HOH B 725                    
SITE     5 AD8 17 MET H  35                                                     
SITE     1 AD9 19 TRP B  33  PHE B  61  PHE B  65  ARG B  68                    
SITE     2 AD9 19 LEU B 149  VAL B 245  ALA B 248  ALA B 249                    
SITE     3 AD9 19 VAL B 252  PHE B 451  HIS B 455  PHE B 458                    
SITE     4 AD9 19 PHE B 462  CLA B 602  CLA B 604  CLA B 606                    
SITE     5 AD9 19 CLA B 611  CLA B 612  CLA B 614                               
SITE     1 AE1 20 THR B  27  VAL B  30  ALA B  31  ALA B  34                    
SITE     2 AE1 20 VAL B  62  MET B  66  ARG B  68  LEU B  69                    
SITE     3 AE1 20 VAL B  96  HIS B 100  LEU B 103  LEU B 143                    
SITE     4 AE1 20 ALA B 146  ALA B 205  CLA B 602  CLA B 603                    
SITE     5 AE1 20 CLA B 605  CLA B 609  CLA B 611  HOH B 707                    
SITE     1 AE2 15 LEU B  69  TRP B  91  VAL B  96  ALA B  99                    
SITE     2 AE2 15 LEU B 149  GLY B 152  PHE B 156  HIS B 157                    
SITE     3 AE2 15 PHE B 162  PRO B 164  CLA B 602  CLA B 604                    
SITE     4 AE2 15 BCR B 618  LFA B 622  HOH B 777                               
SITE     1 AE3 18 TRP B  33  MET B  37  TYR B  40  GLN B  58                    
SITE     2 AE3 18 GLY B  59  PHE B  61  LEU B 324  THR B 327                    
SITE     3 AE3 18 GLY B 328  PRO B 329  TRP B 450  CLA B 603                    
SITE     4 AE3 18 CLA B 612  BCR B 617  LMG B 619  HOH B 762                    
SITE     5 AE3 18 LHG D 406  BCR t 102                                          
SITE     1 AE4 19 THR B 236  SER B 239  SER B 240  ALA B 243                    
SITE     2 AE4 19 PHE B 463  HIS B 466  ILE B 467  LEU B 474                    
SITE     3 AE4 19 CLA B 602  CLA B 608  CLA B 609  LFA B 625                    
SITE     4 AE4 19 PHE D 120  ILE D 123  MET D 126  LEU D 127                    
SITE     5 AE4 19 PHE D 130  CLA D 403  LEU H  46                               
SITE     1 AE5 17 PHE B 139  ALA B 212  PHE B 215  HIS B 216                    
SITE     2 AE5 17 VAL B 219  PRO B 221  PRO B 222  LEU B 225                    
SITE     3 AE5 17 LEU B 229  CLA B 601  CLA B 602  CLA B 607                    
SITE     4 AE5 17 CLA B 609  THR H  27  MET H  31  PHE H  34                    
SITE     5 AE5 17 BCR H 102                                                     
SITE     1 AE6 14 LEU B 135  PHE B 139  HIS B 142  LEU B 143                    
SITE     2 AE6 14 MET B 231  VAL B 237  SER B 240  SER B 241                    
SITE     3 AE6 14 CLA B 604  CLA B 607  CLA B 608  CLA B 611                    
SITE     4 AE6 14 CLA B 614  HOH B 748                                          
SITE     1 AE7 18 TRP B   5  TYR B   6  ARG B   7  VAL B   8                    
SITE     2 AE7 18 HIS B   9  THR B  10  LEU B 238  LEU B 461                    
SITE     3 AE7 18 PHE B 462  GLY B 465  TRP B 468  HIS B 469                    
SITE     4 AE7 18 ARG B 472  CLA B 611  CLA B 612  CLA B 613                    
SITE     5 AE7 18 HOH B 729  LHG D 406                                          
SITE     1 AE8 17 HIS B   9  LEU B  19  HIS B  23  HIS B  26                    
SITE     2 AE8 17 THR B  27  VAL B 237  LEU B 238  SER B 241                    
SITE     3 AE8 17 VAL B 245  CLA B 603  CLA B 604  CLA B 609                    
SITE     4 AE8 17 CLA B 610  CLA B 612  CLA B 613  CLA B 614                    
SITE     5 AE8 17 HOH B 738                                                     
SITE     1 AE9 10 HIS B   9  HIS B  26  PHE B 462  CLA B 603                    
SITE     2 AE9 10 CLA B 606  CLA B 610  CLA B 611  CLA B 613                    
SITE     3 AE9 10 BCR B 616  LMG B 619                                          
SITE     1 AF1 12 VAL B   8  HIS B   9  TRP B 115  CLA B 610                    
SITE     2 AF1 12 CLA B 611  CLA B 612  BCR B 616  LMG B 619                    
SITE     3 AF1 12 VAL L  10  PHE M  21  LFA M 102  LFA m 101                    
SITE     1 AF2 11 HIS B  23  MET B 138  ILE B 141  HIS B 142                    
SITE     2 AF2 11 LEU B 145  CLA B 603  CLA B 609  CLA B 611                    
SITE     3 AF2 11 CLA B 615  LEU H  11  LEU H  14                               
SITE     1 AF3  6 LEU B  24  TRP B 113  HIS B 114  CLA B 614                    
SITE     2 AF3  6 BCR B 618  THR H   5                                          
SITE     1 AF4  8 MET B  25  LEU B  29  CLA B 612  CLA B 613                    
SITE     2 AF4  8 BCR B 617  LMG B 619  SQD L 101  BCR t 102                    
SITE     1 AF5  7 LEU B  29  GLY B  32  TRP B  33  SER B  36                    
SITE     2 AF5  7 CLA B 606  BCR B 616  BCR t 102                               
SITE     1 AF6  5 LEU B 109  TRP B 113  CLA B 605  CLA B 615                    
SITE     2 AF6  5 LFA B 622                                                     
SITE     1 AF7 15 TYR B  40  THR B 327  PRO B 329  LYS B 332                    
SITE     2 AF7 15 CLA B 606  CLA B 612  CLA B 613  BCR B 616                    
SITE     3 AF7 15 HOH B 710  HOH B 732  LHG L 102  ASN M   4                    
SITE     4 AF7 15 LEU M   6  HOH M 203  LFA t 101                               
SITE     1 AF8  5 TRP B  75  LEU B  98  LFA B 623  LEU a 102                    
SITE     2 AF8  5 SQD a 412                                                     
SITE     1 AF9 10 PRO B 183  GLU B 184  TRP B 185  ILE B 207                    
SITE     2 AF9 10 MET C 180  PHE C 181  THR C 200  LEU C 204                    
SITE     3 AF9 10 ILE C 238  CLA H 101                                          
SITE     1 AG1  4 TRP B  91  LEU B 149  CLA B 605  BCR B 618                    
SITE     1 AG2  5 TRP B  75  LFA B 620  LFA B 627  LEU a 102                    
SITE     2 AG2  5 ASP a 103                                                     
SITE     1 AG3  5 ARG B 224  ALA B 228  LFA B 625  PHE D  15                    
SITE     2 AG3  5 LFA D 412                                                     
SITE     1 AG4  4 ALA B 228  CLA B 607  LFA B 624  LFA D 412                    
SITE     1 AG5  1 LEU B  98                                                     
SITE     1 AG6  5 LEU B  39  LEU B  42  LFA B 623  LEU a  72                    
SITE     2 AG6  5 TYR a  73                                                     
SITE     1 AG7  2 LEU a  72  ILE t   4                                          
SITE     1 AG8 15 TRP A  97  GLU A  98  PHE A 117  CLA A 406                    
SITE     2 AG8 15 LEU C 214  LYS C 215  PRO C 217  PHE C 218                    
SITE     3 AG8 15 GLU C 221  TRP C 223  MET C 281  CLA C 506                    
SITE     4 AG8 15 DGD C 517  LYS I   5  TYR I   9                               
SITE     1 AG9 18 THR C  94  LEU C  95  LEU C 168  GLY C 171                    
SITE     2 AG9 18 ALA C 172  LEU C 175  VAL C 233  HIS C 237                    
SITE     3 AG9 18 ILE C 240  ALA C 278  MET C 282  PHE C 289                    
SITE     4 AG9 18 VAL C 296  TYR C 297  CLA C 503  CLA C 504                    
SITE     5 AG9 18 CLA C 508  BCR C 516                                          
SITE     1 AH1 19 TRP C  63  HIS C  91  LEU C  95  GLY C 171                    
SITE     2 AH1 19 LEU C 174  PHE C 182  LEU C 279  MET C 282                    
SITE     3 AH1 19 ALA C 286  VAL C 290  TYR C 297  LEU C 426                    
SITE     4 AH1 19 HIS C 430  LEU C 433  PHE C 437  CLA C 502                    
SITE     5 AH1 19 CLA C 504  CLA C 511  CLA C 513                               
SITE     1 AH2 16 ILE C  60  VAL C  61  THR C  68  LEU C  88                    
SITE     2 AH2 16 HIS C  91  VAL C 114  HIS C 118  LEU C 279                    
SITE     3 AH2 16 CLA C 502  CLA C 503  CLA C 508  CLA C 510                    
SITE     4 AH2 16 CLA C 511  CLA C 513  CLA C 514  LFA C 521                    
SITE     1 AH3 15 TRP C  63  PHE C  70  GLN C  84  GLY C  85                    
SITE     2 AH3 15 ILE C  87  TRP C 425  SER C 429  PHE C 436                    
SITE     3 AH3 15 DGD C 518  DGD C 519  LMG C 520  HOH C 649                    
SITE     4 AH3 15 LHG D 408  PRO K  26  VAL K  30                               
SITE     1 AH4 15 PHE A  33  LEU A 121  TRP A 131  CLA A 406                    
SITE     2 AH4 15 PHE C 264  TYR C 274  GLY C 277  HIS C 441                    
SITE     3 AH4 15 ALA C 445  ARG C 449  LMG C 501  CLA C 508                    
SITE     4 AH4 15 BCR C 516  VAL I  16  PHE I  23                               
SITE     1 AH5 15 CLA A 406  LEU C 165  LEU C 213  ILE C 243                    
SITE     2 AH5 15 GLY C 247  TRP C 250  HIS C 251  THR C 255                    
SITE     3 AH5 15 PRO C 256  PHE C 257  TRP C 259  PHE C 264                    
SITE     4 AH5 15 CLA C 508  BCR C 516  DGD C 517                               
SITE     1 AH6 17 MET C 157  LEU C 161  HIS C 164  LEU C 165                    
SITE     2 AH6 17 LEU C 168  TRP C 266  TYR C 271  TYR C 274                    
SITE     3 AH6 17 SER C 275  MET C 282  CLA C 502  CLA C 504                    
SITE     4 AH6 17 CLA C 506  CLA C 507  CLA C 510  BCR C 516                    
SITE     5 AH6 17 HOH C 604                                                     
SITE     1 AH7 19 SQD A 409  PHE C  33  TRP C  36  ALA C  37                    
SITE     2 AH7 19 GLY C  38  ASN C  39  LEU C 272  LEU C 276                    
SITE     3 AH7 19 PHE C 436  GLY C 440  TRP C 443  HIS C 444                    
SITE     4 AH7 19 ARG C 447  CLA C 510  CLA C 511  CLA C 512                    
SITE     5 AH7 19 DGD C 518  DGD C 519  LHG D 408                               
SITE     1 AH8 18 ASN C  39  LEU C  42  LEU C  49  ALA C  52                    
SITE     2 AH8 18 HIS C  53  HIS C  56  TYR C 149  GLY C 268                    
SITE     3 AH8 18 TYR C 271  LEU C 272  SER C 275  LEU C 279                    
SITE     4 AH8 18 CLA C 504  CLA C 508  CLA C 509  CLA C 511                    
SITE     5 AH8 18 CLA C 512  CLA C 513                                          
SITE     1 AH9 16 ASN C  39  HIS C  56  TRP C  63  LEU C 279                    
SITE     2 AH9 16 PHE C 436  PHE C 437  CLA C 503  CLA C 504                    
SITE     3 AH9 16 CLA C 509  CLA C 510  CLA C 512  LMG C 520                    
SITE     4 AH9 16 LHG D 408  PRO K  29  VAL K  30  LEU K  33                    
SITE     1 AI1 20 TRP C  35  GLY C  38  ASN C  39  ARG C  41                    
SITE     2 AI1 20 LEU C  42  LEU C  45  LYS C  48  PHE C 127                    
SITE     3 AI1 20 ILE C 134  CLA C 509  CLA C 510  CLA C 511                    
SITE     4 AI1 20 PHE K  32  TRP K  39  GLN K  40  BCR K 102                    
SITE     5 AI1 20 LEU Y  39  ASN Y  45  VAL Z  20  ALA Z  28                    
SITE     1 AI2 12 LEU C  50  HIS C  53  LEU C 125  PHE C 147                    
SITE     2 AI2 12 PHE C 163  HIS C 164  ILE C 166  VAL C 167                    
SITE     3 AI2 12 CLA C 503  CLA C 504  CLA C 510  CLA C 514                    
SITE     1 AI3 10 LEU C  50  VAL C 124  GLY C 128  TYR C 131                    
SITE     2 AI3 10 HIS C 132  TYR C 143  CLA C 504  CLA C 513                    
SITE     3 AI3 10 BCR C 515  LFA C 521                                          
SITE     1 AI4  5 PHE C 112  SER C 121  CLA C 514  TYR K  15                    
SITE     2 AI4  5 GLY Z  55                                                     
SITE     1 AI5 12 CLA A 406  ILE C 209  LEU C 213  ASP C 232                    
SITE     2 AI5 12 GLY C 236  ILE C 240  PHE C 264  CLA C 502                    
SITE     3 AI5 12 CLA C 506  CLA C 507  CLA C 508  LEU I  24                    
SITE     1 AI6 20 PHE A 155  ILE A 163  CLA A 406  PRO C 217                    
SITE     2 AI6 20 GLY C 219  GLY C 220  GLU C 221  GLY C 222                    
SITE     3 AI6 20 TRP C 223  CYS C 288  ASN C 293  ASN C 294                    
SITE     4 AI6 20 THR C 295  ASP C 360  PHE C 361  ARG C 362                    
SITE     5 AI6 20 LEU C 438  LMG C 501  CLA C 507  HOH C 653                    
SITE     1 AI7 16 PHE A 197  GLU C  83  GLN C  84  GLY C  85                    
SITE     2 AI7 16 SER C 406  ASN C 418  PHE C 419  VAL C 420                    
SITE     3 AI7 16 TRP C 425  THR C 428  CLA C 505  CLA C 509                    
SITE     4 AI7 16 DGD C 519  LMG C 520  TYR J  33  LFA J 101                    
SITE     1 AI8 19 GLN A 199  PHE A 300  SER A 305  ASN C 405                    
SITE     2 AI8 19 ASN C 415  SER C 416  ASN C 418  CLA C 505                    
SITE     3 AI8 19 CLA C 509  DGD C 518  HOH C 637  LHG D 408                    
SITE     4 AI8 19 PHE J  29  ALA J  32  TYR J  33  GLY J  37                    
SITE     5 AI8 19 SER J  38  SER J  39  GLN V  34                               
SITE     1 AI9  6 HIS C  74  CLA C 505  CLA C 511  DGD C 518                    
SITE     2 AI9  6 LFA J 101  ASP K  23                                          
SITE     1 AJ1  5 TRP C  97  VAL C 117  HIS C 118  CLA C 504                    
SITE     2 AJ1  5 CLA C 514                                                     
SITE     1 AJ2  7 THR B 159  LEU B 161  ALA B 182  PRO B 183                    
SITE     2 AJ2  7 TRP B 185  LEU C 204  PRO C 206                               
SITE     1 AJ3 16 LEU A  41  THR A  45  TYR A 126  GLN A 130                    
SITE     2 AJ3 16 TYR A 147  GLY A 175  VAL A 283  CLA A 403                    
SITE     3 AJ3 16 CLA A 412  ALA D 208  LEU D 209  ILE D 213                    
SITE     4 AJ3 16 TRP D 253  PHE D 257  PL9 D 405  LHG D 407                    
SITE     1 AJ4 19 PHE A 206  CLA A 403  CLA A 404  PHO A 405                    
SITE     2 AJ4 19 PRO D 149  VAL D 152  VAL D 156  PHE D 181                    
SITE     3 AJ4 19 LEU D 182  PHE D 185  GLN D 186  TRP D 191                    
SITE     4 AJ4 19 THR D 192  HIS D 197  GLY D 200  VAL D 204                    
SITE     5 AJ4 19 SER D 282  ALA D 283  VAL D 286                               
SITE     1 AJ5 19 CLA B 607  ILE D  35  CYS D  40  LEU D  43                    
SITE     2 AJ5 19 LEU D  89  LEU D  90  LEU D  91  LEU D  92                    
SITE     3 AJ5 19 TRP D  93  THR D 112  PHE D 113  LEU D 116                    
SITE     4 AJ5 19 HIS D 117  LFA D 413  PHE X  11  GLY X  13                    
SITE     5 AJ5 19 LEU X  14  ALA X  18  VAL X  20                               
SITE     1 AJ6 12 TYR D  42  LEU D  43  GLY D  46  LEU D  49                    
SITE     2 AJ6 12 THR D  50  PHE D 101  LMG D 409  PRO F  29                    
SITE     3 AJ6 12 PHE F  33  LEU F  34  VAL J  21  VAL J  25                    
SITE     1 AJ7 19 ILE A  77  ILE A 176  CLA A 412  MET D 199                    
SITE     2 AJ7 19 ALA D 202  LEU D 210  HIS D 214  THR D 217                    
SITE     3 AJ7 19 MET D 246  TRP D 253  ALA D 260  PHE D 261                    
SITE     4 AJ7 19 LEU D 267  VAL D 274  PHO D 401  VAL L  26                    
SITE     5 AJ7 19 LEU L  29  LHG L 102  PHE T  10                               
SITE     1 AJ8 14 SER A 232  ASN A 234  TYR B   6  ARG B   7                    
SITE     2 AJ8 14 PHE B 464  TRP B 468  CLA B 606  CLA B 610                    
SITE     3 AJ8 14 HOH B 729  TYR D 141  TRP D 266  PHE D 269                    
SITE     4 AJ8 14 LHG L 102  PRO M  18                                          
SITE     1 AJ9 23 MET A  37  CLA A 403  CLA A 412  ILE D 256                    
SITE     2 AJ9 23 PHE D 257  ILE D 259  ALA D 260  PHE D 261                    
SITE     3 AJ9 23 SER D 262  ASN D 263  TRP D 266  PHO D 401                    
SITE     4 AJ9 23 HOH D 538  ASN L  13  THR L  15  SER L  16                    
SITE     5 AJ9 23 TYR L  18  LEU L  19  LHG L 102  HOH L 202                    
SITE     6 AJ9 23 PHE T  17  ALA T  20  ILE T  21                               
SITE     1 AK1 15 ARG A 140  TRP A 142  PHE A 273  SQD A 409                    
SITE     2 AK1 15 TRP C  36  ARG C 447  CLA C 505  CLA C 509                    
SITE     3 AK1 15 CLA C 511  DGD C 519  ASN D 220  ALA D 229                    
SITE     4 AK1 15 SER D 230  THR D 231  PHE D 232                               
SITE     1 AK2 16 CLA A 404  HOH C 637  TYR D  67  GLY D  70                    
SITE     2 AK2 16 ASN D  72  PHE D  73  BCR D 404  HOH D 515                    
SITE     3 AK2 16 ALA F  27  THR F  30  MET F  40  GLN F  41                    
SITE     4 AK2 16 PHE J  28  GLY J  31  ALA J  32  LEU J  36                    
SITE     1 AK3  1 LYS D  23                                                     
SITE     1 AK4 12 PL9 A 408  ARG D  24  ARG D  26  HOH D 522                    
SITE     2 AK4 12 HOH D 548  PHE F  16  THR F  17  VAL F  18                    
SITE     3 AK4 12 VAL F  21  GLN R  30  ILE X  31  ASP X  35                    
SITE     1 AK5  5 LFA B 624  LFA B 625  ASP D  19  LYS D  23                    
SITE     2 AK5  5 TRP D  32                                                     
SITE     1 AK6  3 TRP D  93  CLA D 403  LEU X  21                               
SITE     1 AK7  8 LEU A 258  TYR A 262  ALA A 263  PL9 A 408                    
SITE     2 AK7  8 PRO E   9  PHE E  10  SER E  11  VAL F  23                    
SITE     1 AK8 17 PHE E  10  ILE E  13  ARG E  18  TYR E  19                    
SITE     2 AK8 17 HIS E  23  THR E  26  ILE E  27  LEU E  30                    
SITE     3 AK8 17 ILE F  15  PHE F  16  ARG F  19  TRP F  20                    
SITE     4 AK8 17 HIS F  24  ALA F  27  ILE F  31  ALA R  19                    
SITE     5 AK8 17 ILE R  23                                                     
SITE     1 AK9  8 TRP B 185  GLY B 186  PHE B 190  CLA B 601                    
SITE     2 AK9  8 LMG B 621  HOH B 755  PHE H  41  BCR H 102                    
SITE     1 AL1  6 CLA B 608  PHE H  38  PHE H  41  CLA H 101                    
SITE     2 AL1  6 THR X   2  LEU X   7                                          
SITE     1 AL2 15 TYR B 193  TYR B 258  TYR B 273  GLN B 274                    
SITE     2 AL2 15 SER B 277  PHE B 463  CLA B 601  HOH B 720                    
SITE     3 AL2 15 HIS D  87  LEU D 162  TYR H  49  ASN H  50                    
SITE     4 AL2 15 VAL H  60  SER H  61  TRP H  62                               
SITE     1 AL3  1 BCR A 407                                                     
SITE     1 AL4  2 DGD C 518  LMG C 520                                          
SITE     1 AL5 12 PHE C  62  ALA J  14  THR J  15  LEU K  31                    
SITE     2 AL5 12 ALA K  34  VAL K  38  BCR K 102  ILE Y  28                    
SITE     3 AL5 12 GLY Y  29  GLY Y  32  SER Z  16  PHE Z  17                    
SITE     1 AL6  9 ALA C  55  LEU C  59  ALA C 123  VAL C 130                    
SITE     2 AL6  9 CLA C 512  PHE K  32  BCR K 101  LEU Z  12                    
SITE     3 AL6  9 SER Z  16                                                     
SITE     1 AL7 10 ARG B  18  SER B 104  TRP B 115  BCR B 616                    
SITE     2 AL7 10 ARG L   7  ARG l  14  TYR l  18  TYR m  26                    
SITE     3 AL7 10 PHE t  23  BCR t 102                                          
SITE     1 AL8 17 SER A 232  ASN A 234  PRO B   4  TRP B   5                    
SITE     2 AL8 17 TYR B   6  LMG B 619  TRP D 266  PHE D 273                    
SITE     3 AL8 17 PL9 D 405  LHG D 406  LHG D 407  GLU L  11                    
SITE     4 AL8 17 LEU L  12  ASN L  13  SER L  16  VAL L  26                    
SITE     5 AL8 17 PHE M  21                                                     
SITE     1 AL9  2 SQD b 601  LFA m 102                                          
SITE     1 AM1  4 CLA B 613  ILE M  24  VAL m  27  LFA m 101                    
SITE     1 AM2 12 SQD A 411  ALA T  11  ALA T  15  PHE T  18                    
SITE     2 AM2 12 PHE T  22  SER b  36  TYR b  40  SQD b 601                    
SITE     3 AM2 12 LFA b 602  CLA b 609  BCR b 619  BCR b 620                    
SITE     1 AM3  3 LEU M   8  ALA M  12  CLA b 616                               
SITE     1 AM4 18 ALA V  36  CYS V  37  SER V  39  CYS V  40                    
SITE     2 AM4 18 HIS V  41  THR V  46  THR V  48  LEU V  52                    
SITE     3 AM4 18 ASP V  53  THR V  58  LEU V  59  LEU V  72                    
SITE     4 AM4 18 TYR V  75  MET V  76  TYR V  82  HIS V  92                    
SITE     5 AM4 18 HOH V 301  HOH V 308                                          
SITE     1 AM5  5 HIS a 215  HIS a 272  BCT a 413  HIS d 214                    
SITE     2 AM5  5 HIS d 268                                                     
SITE     1 AM6  2 ASN a 181  GLU a 333                                          
SITE     1 AM7  4 HIS a 337  ASN a 338  PHE a 339  GLU c 354                    
SITE     1 AM8 18 TYR a 147  PRO a 150  SER a 153  VAL a 157                    
SITE     2 AM8 18 MET a 183  PHE a 186  GLN a 187  HIS a 198                    
SITE     3 AM8 18 GLY a 201  VAL a 202  THR a 286  ALA a 287                    
SITE     4 AM8 18 ILE a 290  CLA a 405  PHO a 406  CLA d 401                    
SITE     5 AM8 18 CLA d 402  LHG d 406                                          
SITE     1 AM9 18 PHE a 158  MET a 172  ILE a 176  THR a 179                    
SITE     2 AM9 18 PHE a 180  MET a 183  CLA a 404  PHO a 406                    
SITE     3 AM9 18 HOH a 544  MET d 198  VAL d 201  ALA d 202                    
SITE     4 AM9 18 LEU d 205  GLY d 206  CLA d 402  PL9 d 405                    
SITE     5 AM9 18 LHG l 101  PHE t  10                                          
SITE     1 AN1 16 LEU a  41  ALA a  44  THR a  45  TYR a 126                    
SITE     2 AN1 16 GLN a 130  ALA a 146  TYR a 147  PRO a 150                    
SITE     3 AN1 16 GLY a 175  CLA a 404  CLA a 405  SQD a 412                    
SITE     4 AN1 16 ALA d 208  LEU d 209  ILE d 213  TRP d 253                    
SITE     1 AN2 18 THR a  40  PHE a  93  PRO a  95  ILE a  96                    
SITE     2 AN2 18 TRP a  97  LEU a 114  HIS a 118  LMG c 501                    
SITE     3 AN2 18 CLA c 506  CLA c 507  BCR c 515  DGD c 516                    
SITE     4 AN2 18 VAL i   8  TYR i   9  VAL i  11  VAL i  12                    
SITE     5 AN2 18 THR i  13  PHE i  15                                          
SITE     1 AN3  4 LEU a  42  ALA a  43  ILE a  50  LFA i 101                    
SITE     1 AN4 17 PHE a 211  HIS a 215  LEU a 218  ILE a 248                    
SITE     2 AN4 17 PHE a 255  ILE a 259  SER a 264  PHE a 265                    
SITE     3 AN4 17 LEU a 271  PHO a 414  PHE d  38  PRO d  39                    
SITE     4 AN4 17 CLA d 402  LHG e 101  THR f  25  SQD f 102                    
SITE     5 AN4 17 THR x  24                                                     
SITE     1 AN5 17 LEU a 200  ALA a 203  GLY a 204  ASN a 267                    
SITE     2 AN5 17 SER a 270  PHE a 274  ALA a 277  TRP a 278                    
SITE     3 AN5 17 VAL a 281  GLN c  28  TRP c  36  LMG c 519                    
SITE     4 AN5 17 BCR c 523  PHE d 232  ARG d 233  LHG d 407                    
SITE     5 AN5 17 PHE k  37                                                     
SITE     1 AN6  1 TRP a  20                                                     
SITE     1 AN7  8 TRP B 113  TYR B 117  LFA B 620  ASN a  26                    
SITE     2 AN7  8 ARG a  27  LEU a  28  THR a  45  PHO a 406                    
SITE     1 AN8  8 HIS a 215  GLU a 244  TYR a 246  HIS a 272                    
SITE     2 AN8  8  FE a 401  HIS d 214  TYR d 244  HIS d 268                    
SITE     1 AN9 19 ALA a 209  LEU a 210  MET a 214  LEU a 258                    
SITE     2 AN9 19 PL9 a 409  TRP d  48  ILE d 114  GLY d 121                    
SITE     3 AN9 19 PHE d 125  GLN d 129  ASN d 142  PHE d 146                    
SITE     4 AN9 19 PHE d 153  PHE d 173  GLY d 174  PRO d 275                    
SITE     5 AN9 19 LEU d 279  CLA d 401  CLA d 402                               
SITE     1 AO1 14 ARG L  14  TYR L  18  LEU L  21  TYR M  26                    
SITE     2 AO1 14 LFA M 101  PHE T  23  BCR T 101  ARG b  18                    
SITE     3 AO1 14 SER b 104  PHE b 108  TRP b 115  CLA b 616                    
SITE     4 AO1 14 BCR b 619  ARG l   7                                          
SITE     1 AO2  1 BCR T 101                                                     
SITE     1 AO3  8 TRP b 185  PHE b 190  CLA b 604  LMG b 624                    
SITE     2 AO3  8 HOH b 734  PHE h  41  LEU h  55  BCR h 101                    
SITE     1 AO4 16 GLY b 189  PHE b 190  PRO b 192  GLY b 197                    
SITE     2 AO4 16 HIS b 201  PHE b 247  PHE b 250  CLA b 603                    
SITE     3 AO4 16 CLA b 605  CLA b 611  LEU d 162  PHE h  38                    
SITE     4 AO4 16 ILE h  45  TYR h  49  BCR h 101  DGD h 102                    
SITE     1 AO5 17 ARG b  68  LEU b  69  ALA b 146  CYS b 150                    
SITE     2 AO5 17 PHE b 153  HIS b 201  HIS b 202  PHE b 247                    
SITE     3 AO5 17 VAL b 252  THR b 262  CLA b 604  CLA b 606                    
SITE     4 AO5 17 CLA b 607  CLA b 608  CLA b 611  HOH b 713                    
SITE     5 AO5 17 PHE h  38                                                     
SITE     1 AO6 18 TRP b  33  PHE b  61  PHE b  65  ARG b  68                    
SITE     2 AO6 18 LEU b 149  VAL b 245  ALA b 248  ALA b 249                    
SITE     3 AO6 18 VAL b 252  PHE b 451  HIS b 455  PHE b 458                    
SITE     4 AO6 18 PHE b 462  CLA b 605  CLA b 607  CLA b 609                    
SITE     5 AO6 18 CLA b 614  CLA b 615                                          
SITE     1 AO7 16 THR b  27  VAL b  30  TRP b  33  ALA b  34                    
SITE     2 AO7 16 VAL b  62  MET b  66  ARG b  68  VAL b  96                    
SITE     3 AO7 16 HIS b 100  ALA b 205  CLA b 605  CLA b 606                    
SITE     4 AO7 16 CLA b 608  CLA b 611  CLA b 612  CLA b 614                    
SITE     1 AO8 15 LEU b  69  PHE b  90  TRP b  91  VAL b  96                    
SITE     2 AO8 15 ALA b  99  GLY b 152  PHE b 153  HIS b 157                    
SITE     3 AO8 15 PHE b 162  PRO b 164  CLA b 605  CLA b 607                    
SITE     4 AO8 15 LFA b 625  LFA b 627  HOH b 729                               
SITE     1 AO9 17 BCR T 101  TRP b  33  MET b  37  TYR b  40                    
SITE     2 AO9 17 GLN b  58  GLY b  59  PHE b  61  LEU b 324                    
SITE     3 AO9 17 THR b 327  GLY b 328  TRP b 450  CLA b 606                    
SITE     4 AO9 17 BCR b 620  LHG b 628  HOH b 756  MET d 281                    
SITE     5 AO9 17 LMG m 103                                                     
SITE     1 AP1 18 THR b 236  SER b 239  SER b 240  ALA b 243                    
SITE     2 AP1 18 PHE b 463  HIS b 466  THR b 473  LEU b 474                    
SITE     3 AP1 18 CLA b 611  CLA b 612  LFA b 629  LEU d  89                    
SITE     4 AP1 18 PHE d 120  ILE d 123  MET d 126  LEU h  39                    
SITE     5 AP1 18 LEU h  43  DGD h 102                                          
SITE     1 AP2 18 PHE b 139  ALA b 212  PHE b 215  HIS b 216                    
SITE     2 AP2 18 VAL b 219  PRO b 221  PRO b 222  LEU b 229                    
SITE     3 AP2 18 CLA b 604  CLA b 605  CLA b 607  CLA b 610                    
SITE     4 AP2 18 CLA b 612  LFA b 629  THR h  27  MET h  31                    
SITE     5 AP2 18 PHE h  34  BCR h 101                                          
SITE     1 AP3 13 PHE b 139  HIS b 142  LEU b 143  MET b 231                    
SITE     2 AP3 13 VAL b 237  SER b 240  SER b 241  CLA b 607                    
SITE     3 AP3 13 CLA b 610  CLA b 611  CLA b 614  CLA b 617                    
SITE     4 AP3 13 HOH b 723                                                     
SITE     1 AP4 16 TRP b   5  TYR b   6  ARG b   7  VAL b   8                    
SITE     2 AP4 16 HIS b   9  LEU b 461  GLY b 465  TRP b 468                    
SITE     3 AP4 16 HIS b 469  ARG b 472  CLA b 614  CLA b 615                    
SITE     4 AP4 16 CLA b 616  LHG b 628  HOH b 712  LHG l 101                    
SITE     1 AP5 16 HIS b   9  LEU b  19  HIS b  23  HIS b  26                    
SITE     2 AP5 16 THR b  27  VAL b 237  LEU b 238  SER b 241                    
SITE     3 AP5 16 CLA b 606  CLA b 607  CLA b 612  CLA b 613                    
SITE     4 AP5 16 CLA b 615  CLA b 616  CLA b 617  HOH b 753                    
SITE     1 AP6 10 HIS b   9  HIS b  26  PHE b 462  CLA b 606                    
SITE     2 AP6 10 CLA b 613  CLA b 614  CLA b 616  BCR b 619                    
SITE     3 AP6 10 PHE m  14  LMG m 103                                          
SITE     1 AP7 13 PHE T   8  LFA T 102  VAL b   8  HIS b   9                    
SITE     2 AP7 13 SQD b 601  CLA b 613  CLA b 614  CLA b 615                    
SITE     3 AP7 13 BCR b 619  GLN l   8  VAL l  10  PHE m  21                    
SITE     4 AP7 13 LMG m 103                                                     
SITE     1 AP8 11 ILE b  20  HIS b  23  LEU b  24  MET b 138                    
SITE     2 AP8 11 ILE b 141  HIS b 142  LEU b 145  CLA b 612                    
SITE     3 AP8 11 CLA b 614  CLA b 618  LEU h  14                               
SITE     1 AP9 11 ILE b  20  LEU b  24  TRP b 113  HIS b 114                    
SITE     2 AP9 11 LEU b 120  LEU b 122  PHE b 123  CLA b 617                    
SITE     3 AP9 11 BCR b 621  THR h   5  LEU h   7                               
SITE     1 AQ1  9 PHE T  19  BCR T 101  MET b  25  LEU b  29                    
SITE     2 AQ1  9 TRP b 115  SQD b 601  CLA b 615  CLA b 616                    
SITE     3 AQ1  9 BCR b 620                                                     
SITE     1 AQ2  9 BCR T 101  LEU b  29  GLY b  32  TRP b  33                    
SITE     2 AQ2  9 SER b  36  VAL b 102  GLY b 105  CLA b 609                    
SITE     3 AQ2  9 BCR b 619                                                     
SITE     1 AQ3  6 SQD A 411  PHE T  22  LEU b 106  LEU b 109                    
SITE     2 AQ3  6 ALA b 110  CLA b 618                                          
SITE     1 AQ4  4 BCR A 407  TRP b  75  LEU b  98  LFA b 627                    
SITE     1 AQ5  3 LEU A  72  LEU b  39  ALA b  43                               
SITE     1 AQ6  7 GLU b 184  TRP b 185  CLA b 603  ASN c 201                    
SITE     2 AQ6  7 PRO c 202  ILE c 238  LMG c 522                               
SITE     1 AQ7  3 PHE b  90  TRP b  91  CLA b 608                               
SITE     1 AQ8  1 LEU b  98                                                     
SITE     1 AQ9  2 CLA b 608  LFA b 622                                          
SITE     1 AR1 13 ASN a 234  TYR b   6  ARG b   7  PHE b 464                    
SITE     2 AR1 13 TRP b 468  CLA b 609  CLA b 613  HOH b 712                    
SITE     3 AR1 13 TYR d 141  TRP d 266  PHE d 269  PHE d 273                    
SITE     4 AR1 13 LHG l 101                                                     
SITE     1 AR2  3 CLA b 610  CLA b 611  LFA d 409                               
SITE     1 AR3  4 ARG b 224  LEU b 225  ASP d  16  LFA d 409                    
SITE     1 AR4 11 TRP a  97  PHE a 117  CLA a 407  LEU c 214                    
SITE     2 AR4 11 LYS c 215  SER c 216  PHE c 218  TRP c 223                    
SITE     3 AR4 11 CLA c 506  LYS i   5  TYR i   9                               
SITE     1 AR5 16 LEU c  95  LEU c 168  GLY c 171  ALA c 172                    
SITE     2 AR5 16 HIS c 237  ILE c 240  ALA c 278  MET c 282                    
SITE     3 AR5 16 PHE c 289  VAL c 296  TYR c 297  CLA c 503                    
SITE     4 AR5 16 CLA c 504  CLA c 507  CLA c 508  BCR c 515                    
SITE     1 AR6 15 TRP c  63  HIS c  91  LEU c  95  LEU c 174                    
SITE     2 AR6 15 LEU c 279  ALA c 286  VAL c 290  TYR c 297                    
SITE     3 AR6 15 HIS c 430  PHE c 437  CLA c 502  CLA c 504                    
SITE     4 AR6 15 CLA c 511  CLA c 513  HOH c 627                               
SITE     1 AR7 15 VAL c  61  ALA c  64  THR c  68  LEU c  88                    
SITE     2 AR7 15 HIS c  91  HIS c 118  LEU c 279  CLA c 502                    
SITE     3 AR7 15 CLA c 503  CLA c 508  CLA c 510  CLA c 511                    
SITE     4 AR7 15 CLA c 513  CLA c 514  LFA c 521                               
SITE     1 AR8 17 TRP c  63  MET c  67  PHE c  70  GLN c  84                    
SITE     2 AR8 17 GLY c  85  ILE c  87  TRP c 425  SER c 429                    
SITE     3 AR8 17 PHE c 436  CLA c 509  CLA c 511  DGD c 517                    
SITE     4 AR8 17 DGD c 518  LMG c 519  HOH c 655  LHG d 407                    
SITE     5 AR8 17 PRO k  26                                                     
SITE     1 AR9 16 LEU a 121  TRP a 131  CLA a 407  PHE c 264                    
SITE     2 AR9 16 SER c 273  TYR c 274  GLY c 277  MET c 281                    
SITE     3 AR9 16 HIS c 441  LEU c 442  ALA c 445  ARG c 449                    
SITE     4 AR9 16 LMG c 501  CLA c 508  BCR c 515  PHE i  23                    
SITE     1 AS1 15 CLA a 407  LEU c 161  LEU c 165  ILE c 243                    
SITE     2 AS1 15 GLY c 247  TRP c 250  HIS c 251  THR c 255                    
SITE     3 AS1 15 PRO c 256  PHE c 257  TRP c 259  PHE c 264                    
SITE     4 AS1 15 CLA c 502  CLA c 508  BCR c 515                               
SITE     1 AS2 15 LEU c 161  HIS c 164  LEU c 165  LEU c 168                    
SITE     2 AS2 15 TRP c 266  TYR c 271  TYR c 274  MET c 282                    
SITE     3 AS2 15 CLA c 502  CLA c 504  CLA c 506  CLA c 507                    
SITE     4 AS2 15 CLA c 510  BCR c 515  HOH c 637                               
SITE     1 AS3 18 PHE c  33  TRP c  36  ALA c  37  GLY c  38                    
SITE     2 AS3 18 ASN c  39  LEU c 272  LEU c 276  PHE c 436                    
SITE     3 AS3 18 GLY c 440  TRP c 443  HIS c 444  ARG c 447                    
SITE     4 AS3 18 CLA c 505  CLA c 510  CLA c 511  CLA c 512                    
SITE     5 AS3 18 LMG c 519  LHG d 407                                          
SITE     1 AS4 16 ASN c  39  LEU c  49  ALA c  52  HIS c  53                    
SITE     2 AS4 16 HIS c  56  TYR c 149  ILE c 160  LEU c 272                    
SITE     3 AS4 16 SER c 275  LEU c 279  CLA c 504  CLA c 508                    
SITE     4 AS4 16 CLA c 509  CLA c 511  CLA c 512  CLA c 513                    
SITE     1 AS5 15 ASN c  39  HIS c  56  LEU c 433  PHE c 437                    
SITE     2 AS5 15 CLA c 503  CLA c 504  CLA c 505  CLA c 509                    
SITE     3 AS5 15 CLA c 510  CLA c 512  LMG c 519  LHG d 407                    
SITE     4 AS5 15 PRO k  29  VAL k  30  LEU k  33                               
SITE     1 AS6 20 ARG c  26  TRP c  35  GLY c  38  ASN c  39                    
SITE     2 AS6 20 ARG c  41  LEU c  42  LEU c  45  LYS c  48                    
SITE     3 AS6 20 ALA c  52  ILE c 134  CLA c 509  CLA c 510                    
SITE     4 AS6 20 CLA c 511  PHE k  32  LEU k  33  TRP k  39                    
SITE     5 AS6 20 GLN k  40  BCR k 101  VAL z  20  ALA z  28                    
SITE     1 AS7 11 HIS c  53  PHE c 147  PHE c 163  HIS c 164                    
SITE     2 AS7 11 VAL c 167  GLY c 171  CLA c 503  CLA c 504                    
SITE     3 AS7 11 CLA c 510  CLA c 514  BCR c 524                               
SITE     1 AS8 10 GLY c 128  TYR c 131  HIS c 132  PRO c 137                    
SITE     2 AS8 10 LEU c 140  TYR c 143  PHE c 147  CLA c 504                    
SITE     3 AS8 10 CLA c 513  BCR c 524                                          
SITE     1 AS9 12 CLA a 407  ILE c 209  LEU c 213  GLY c 236                    
SITE     2 AS9 12 HIS c 237  ILE c 240  PHE c 264  CLA c 502                    
SITE     3 AS9 12 CLA c 506  CLA c 507  CLA c 508  LEU i  24                    
SITE     1 AT1 24 PHE a 155  ILE a 160  ILE a 163  CLA a 407                    
SITE     2 AT1 24 PRO c 217  PHE c 218  GLY c 219  GLY c 220                    
SITE     3 AT1 24 GLU c 221  GLY c 222  VAL c 225  MET c 281                    
SITE     4 AT1 24 PHE c 284  CYS c 288  PHE c 292  ASN c 293                    
SITE     5 AT1 24 ASN c 294  THR c 295  ASP c 360  PHE c 361                    
SITE     6 AT1 24 ARG c 362  HOH c 613  HOH c 644  HOH c 656                    
SITE     1 AT2 19 HIS a 195  PHE a 197  HOH a 507  GLU c  83                    
SITE     2 AT2 19 GLN c  84  GLY c  85  SER c 406  ASN c 418                    
SITE     3 AT2 19 PHE c 419  VAL c 420  TRP c 425  THR c 428                    
SITE     4 AT2 19 SER c 429  CLA c 505  DGD c 518  LMG c 519                    
SITE     5 AT2 19 HOH c 603  TYR j  33  LFA j 101                               
SITE     1 AT3 21 LEU a 200  ALA a 203  PHE a 300  PHE a 302                    
SITE     2 AT3 21 SER a 305  ASN c 405  ASN c 415  SER c 416                    
SITE     3 AT3 21 ASN c 418  CLA c 505  DGD c 517  CLA d 401                    
SITE     4 AT3 21 LHG d 407  LMG f 101  HOH f 202  PHE j  29                    
SITE     5 AT3 21 ALA j  32  TYR j  33  GLY j  37  SER j  38                    
SITE     6 AT3 21 GLN v  34                                                     
SITE     1 AT4 11 SQD a 410  HIS c  74  CLA c 505  CLA c 509                    
SITE     2 AT4 11 CLA c 511  DGD c 517  HOH c 633  ILE j  22                    
SITE     3 AT4 11 LFA j 101  ASP k  23  ILE y  25                               
SITE     1 AT5  2 TRP c  35  PHE k  45                                          
SITE     1 AT6  5 TRP c  97  VAL c 113  VAL c 117  SER c 121                    
SITE     2 AT6  5 CLA c 504                                                     
SITE     1 AT7  9 ALA b 155  THR b 159  LEU b 161  ALA b 182                    
SITE     2 AT7  9 LMG b 624  LEU c 204  ASP c 205  PRO c 206                    
SITE     3 AT7  9 ALA c 246                                                     
SITE     1 AT8 15 SQD a 410  PHE c  62  THR j  15  GLY j  18                    
SITE     2 AT8 15 MET j  19  ILE k  28  LEU k  31  ALA k  34                    
SITE     3 AT8 15 VAL k  38  BCR k 101  GLY y  29  GLY y  32                    
SITE     4 AT8 15 SER z  16  PHE z  17  VAL z  20                               
SITE     1 AT9  7 PHE c 112  VAL c 116  SER c 121  PHE c 147                    
SITE     2 AT9  7 CLA c 513  CLA c 514  TYR k  15                               
SITE     1 AU1 14 GLN a 199  VAL a 202  GLY a 207  TRP a 278                    
SITE     2 AU1 14 CLA a 404  PHO a 414  DGD c 518  VAL d 175                    
SITE     3 AU1 14 ILE d 178  PHE d 179  PHE d 181  CLA d 402                    
SITE     4 AU1 14 HOH d 542  LMG f 101                                          
SITE     1 AU2 20 PHE a 206  CLA a 404  CLA a 405  PL9 a 409                    
SITE     2 AU2 20 PHO a 414  VAL d 152  VAL d 156  LEU d 182                    
SITE     3 AU2 20 PHE d 185  GLN d 186  TRP d 191  THR d 192                    
SITE     4 AU2 20 HIS d 197  GLY d 200  VAL d 204  SER d 282                    
SITE     5 AU2 20 ALA d 283  VAL d 286  CLA d 401  LMG f 101                    
SITE     1 AU3 18 ILE d  35  CYS d  40  LEU d  43  LEU d  89                    
SITE     2 AU3 18 LEU d  90  LEU d  91  LEU d  92  TRP d  93                    
SITE     3 AU3 18 TRP d 104  THR d 112  PHE d 113  LEU d 116                    
SITE     4 AU3 18 HIS d 117  LFA d 410  LEU h  37  VAL h  40                    
SITE     5 AU3 18 LEU x  14  VAL x  20                                          
SITE     1 AU4 12 TYR d  42  LEU d  43  GLY d  46  GLY d  47                    
SITE     2 AU4 12 LEU d  49  THR d  50  PRO f  29  THR f  30                    
SITE     3 AU4 12 PHE f  33  LMG f 101  VAL j  21  VAL j  25                    
SITE     1 AU5 18 ILE a  53  ILE a  77  ILE a 176  CLA a 405                    
SITE     2 AU5 18 MET d 198  MET d 199  HIS d 214  THR d 217                    
SITE     3 AU5 18 MET d 246  TRP d 253  ALA d 260  PHE d 261                    
SITE     4 AU5 18 VAL d 274  LHG d 406  VAL l  26  LEU l  29                    
SITE     5 AU5 18 LHG l 101  PHE t  10                                          
SITE     1 AU6 17 MET a  37  CLA a 404  PHE d 257  PHE d 261                    
SITE     2 AU6 17 SER d 262  ASN d 263  TRP d 266  PL9 d 405                    
SITE     3 AU6 17 ASN l  13  THR l  15  SER l  16  TYR l  18                    
SITE     4 AU6 17 LHG l 101  HOH l 202  PHE t  17  ALA t  20                    
SITE     5 AU6 17 ILE t  21                                                     
SITE     1 AU7 18 ARG a 140  TRP a 142  PHE a 273  TRP a 284                    
SITE     2 AU7 18 SQD a 410  TRP c  36  TRP c 443  ARG c 447                    
SITE     3 AU7 18 CLA c 505  CLA c 509  CLA c 511  DGD c 518                    
SITE     4 AU7 18 GLU d 219  ASN d 220  ALA d 229  SER d 230                    
SITE     5 AU7 18 THR d 231  PHE d 232                                          
SITE     1 AU8  3 LFA b 629  LFA b 630  TRP d  32                               
SITE     1 AU9  6 TRP d  93  GLN d  98  GLY d  99  CLA d 403                    
SITE     2 AU9  6 ILE x  12  SER x  16                                          
SITE     1 AV1  7 TYR a 262  PL9 a 409  LEU d  37  PRO e   9                    
SITE     2 AV1  7 PHE e  10  SER e  11  VAL f  23                               
SITE     1 AV2 15 ILE e  13  ARG e  18  TYR e  19  HIS e  23                    
SITE     2 AV2 15 THR e  26  LEU e  30  HOH e 202  ILE f  15                    
SITE     3 AV2 15 ARG f  19  TRP f  20  HIS f  24  ALA f  27                    
SITE     4 AV2 15 ILE f  31  ALA r  19  ILE r  23                               
SITE     1 AV3 18 DGD c 518  TYR d  67  GLY d  70  CYS d  71                    
SITE     2 AV3 18 ASN d  72  PHE d  73  CLA d 401  CLA d 402                    
SITE     3 AV3 18 BCR d 404  THR f  30  MET f  40  GLN f  41                    
SITE     4 AV3 18 HOH f 201  HOH f 202  PHE j  28  GLY j  31                    
SITE     5 AV3 18 ALA j  32  LEU j  36                                          
SITE     1 AV4 11 PL9 a 409  ARG d  26  PHE f  16  THR f  17                    
SITE     2 AV4 11 VAL f  18  VAL f  21  GLN r  30  LEU r  34                    
SITE     3 AV4 11 THR x  24  VAL x  27  ASP x  35                               
SITE     1 AV5  9 CLA b 603  CLA b 604  CLA b 611  LEU h  37                    
SITE     2 AV5  9 PHE h  38  PHE h  41  LEU h  55  ILE x   3                    
SITE     3 AV5  9 LEU x   7                                                     
SITE     1 AV6 16 TYR b 193  PHE b 250  TYR b 258  TYR b 273                    
SITE     2 AV6 16 TYR b 279  CLA b 604  CLA b 610  HOH b 726                    
SITE     3 AV6 16 HIS d  87  LEU d 162  LEU d 291  TYR h  49                    
SITE     4 AV6 16 ASN h  50  VAL h  60  SER h  61  TRP h  62                    
SITE     1 AV7  1 BCR a 408                                                     
SITE     1 AV8  5 DGD c 517  LMG c 519  GLY j  26  TYR j  30                    
SITE     2 AV8  5 TYR j  33                                                     
SITE     1 AV9  9 ALA c  55  LEU c  59  ALA c 123  CLA c 512                    
SITE     2 AV9  9 BCR c 523  PHE k  32  LEU k  35  VAL z  13                    
SITE     3 AV9  9 SER z  16                                                     
SITE     1 AW1 17 SER a 232  ASN a 234  CLA a 405  PRO b   4                    
SITE     2 AW1 17 TRP b   5  TYR b   6  CLA b 613  LHG b 628                    
SITE     3 AW1 17 TRP d 266  PL9 d 405  LHG d 406  GLU l  11                    
SITE     4 AW1 17 LEU l  12  ASN l  13  SER l  16  PHE m  21                    
SITE     5 AW1 17 LMG m 103                                                     
SITE     1 AW2  3 CLA B 613  LFA M 102  ILE m  23                               
SITE     1 AW3  3 VAL M  27  LFA M 101  GLN m  28                               
SITE     1 AW4 14 THR b 327  GLY b 328  PRO b 329  LYS b 332                    
SITE     2 AW4 14 PHE b 453  CLA b 609  CLA b 615  CLA b 616                    
SITE     3 AW4 14 HOH b 760  PHE l  35  LHG l 101  ASN m   4                    
SITE     4 AW4 14 LEU m   6  ALA m  10                                          
SITE     1 AW5  5 TYR B  40  LMG B 619  ALA m  12  MET t   1                    
SITE     2 AW5  5 PHE t   8                                                     
SITE     1 AW6 12 TYR B  40  CLA B 606  BCR B 616  BCR B 617                    
SITE     2 AW6 12 SQD L 101  LEU a  28  ILE t   4  PHE t   8                    
SITE     3 AW6 12 ALA t  11  ALA t  15  PHE t  18  PHE t  22                    
SITE     1 AW7 16 ALA v  36  CYS v  37  ALA v  38  SER v  39                    
SITE     2 AW7 16 HIS v  41  ILE v  45  THR v  46  LYS v  47                    
SITE     3 AW7 16 THR v  48  ASN v  49  LEU v  52  ASP v  53                    
SITE     4 AW7 16 LEU v  72  TYR v  75  TYR v  82  HIS v  92                    
SITE     1 AW8 15 PHE v  33  ALA v  36  ALA v  38  SER v  39                    
SITE     2 AW8 15 CYS v  40  HIS v  41  THR v  46  THR v  48                    
SITE     3 AW8 15 ASN v  49  LEU v  52  ASP v  53  LEU v  72                    
SITE     4 AW8 15 TYR v  75  TYR v  82  HIS v  92                               
CRYST1  116.326  219.617  304.043  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      0.008597  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004553  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003289        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system