GenomeNet

Database: PDB
Entry: 5KAI
LinkDB: 5KAI
Original site: 5KAI 
HEADER    ELECTRON TRANSPORT                      01-JUN-16   5KAI              
TITLE     NH3-BOUND RT XFEL STRUCTURE OF PHOTOSYSTEM II 500 MS AFTER THE 2ND    
TITLE    2 ILLUMINATION (2F) AT 2.8 A RESOLUTION                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOTOSYSTEM II PROTEIN D1 1;                               
COMPND   3 CHAIN: A, a;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 1-344;                                        
COMPND   5 SYNONYM: PSII D1 PROTEIN 1,PHOTOSYSTEM II Q(B) PROTEIN 1;            
COMPND   6 EC: 1.10.3.9;                                                        
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PHOTOSYSTEM II CP47 REACTION CENTER PROTEIN;               
COMPND   9 CHAIN: B, b;                                                         
COMPND  10 SYNONYM: PSII 47 KDA PROTEIN,PROTEIN CP-47;                          
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: PHOTOSYSTEM II CP43 REACTION CENTER PROTEIN;               
COMPND  13 CHAIN: C, c;                                                         
COMPND  14 SYNONYM: PSII 43 KDA PROTEIN,PROTEIN CP-43;                          
COMPND  15 MOL_ID: 4;                                                           
COMPND  16 MOLECULE: PHOTOSYSTEM II D2 PROTEIN;                                 
COMPND  17 CHAIN: D, d;                                                         
COMPND  18 SYNONYM: PSII D2 PROTEIN,PHOTOSYSTEM II Q(A) PROTEIN;                
COMPND  19 EC: 1.10.3.9;                                                        
COMPND  20 MOL_ID: 5;                                                           
COMPND  21 MOLECULE: CYTOCHROME B559 SUBUNIT ALPHA;                             
COMPND  22 CHAIN: E, e;                                                         
COMPND  23 SYNONYM: PSII REACTION CENTER SUBUNIT V;                             
COMPND  24 MOL_ID: 6;                                                           
COMPND  25 MOLECULE: CYTOCHROME B559 SUBUNIT BETA;                              
COMPND  26 CHAIN: F, f;                                                         
COMPND  27 SYNONYM: PSII REACTION CENTER SUBUNIT VI;                            
COMPND  28 MOL_ID: 7;                                                           
COMPND  29 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN H;                  
COMPND  30 CHAIN: H, h;                                                         
COMPND  31 SYNONYM: PSII-H;                                                     
COMPND  32 MOL_ID: 8;                                                           
COMPND  33 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN I;                  
COMPND  34 CHAIN: I, i;                                                         
COMPND  35 SYNONYM: PSII-I,PSII 4.4 KDA PROTEIN;                                
COMPND  36 MOL_ID: 9;                                                           
COMPND  37 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN J;                  
COMPND  38 CHAIN: J, j;                                                         
COMPND  39 SYNONYM: PSII-J;                                                     
COMPND  40 MOL_ID: 10;                                                          
COMPND  41 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN K;                  
COMPND  42 CHAIN: K, k;                                                         
COMPND  43 SYNONYM: PSII-K;                                                     
COMPND  44 MOL_ID: 11;                                                          
COMPND  45 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN L;                  
COMPND  46 CHAIN: L, l;                                                         
COMPND  47 SYNONYM: PSII-L;                                                     
COMPND  48 MOL_ID: 12;                                                          
COMPND  49 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN M;                  
COMPND  50 CHAIN: M, m;                                                         
COMPND  51 SYNONYM: PSII-M;                                                     
COMPND  52 MOL_ID: 13;                                                          
COMPND  53 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;          
COMPND  54 CHAIN: O, o;                                                         
COMPND  55 SYNONYM: MSP;                                                        
COMPND  56 MOL_ID: 14;                                                          
COMPND  57 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN T;                  
COMPND  58 CHAIN: T, t;                                                         
COMPND  59 SYNONYM: PSII-TC;                                                    
COMPND  60 MOL_ID: 15;                                                          
COMPND  61 MOLECULE: PHOTOSYSTEM II 12 KDA EXTRINSIC PROTEIN;                   
COMPND  62 CHAIN: U, u;                                                         
COMPND  63 SYNONYM: PS II COMPLEX 12 KDA EXTRINSIC PROTEIN,PSII-U;              
COMPND  64 MOL_ID: 16;                                                          
COMPND  65 MOLECULE: CYTOCHROME C-550;                                          
COMPND  66 CHAIN: V, v;                                                         
COMPND  67 SYNONYM: CYTOCHROME C-549,CYTOCHROME C550,LOW-POTENTIAL CYTOCHROME C;
COMPND  68 MOL_ID: 17;                                                          
COMPND  69 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN YCF12;              
COMPND  70 CHAIN: Y, y;                                                         
COMPND  71 MOL_ID: 18;                                                          
COMPND  72 MOLECULE: PHOTOSYSTEM II REACTION CENTER X PROTEIN;                  
COMPND  73 CHAIN: X, x;                                                         
COMPND  74 MOL_ID: 19;                                                          
COMPND  75 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Z;                  
COMPND  76 CHAIN: Z, z;                                                         
COMPND  77 SYNONYM: PSII-Z;                                                     
COMPND  78 MOL_ID: 20;                                                          
COMPND  79 MOLECULE: PHOTOSYSTEM II PROTEIN Y;                                  
COMPND  80 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    PHOTOSYSTEMS, TRANSMEMBRANE, ROOM TEMPERATURE, ELECTRON TRANSPORT     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.D.YOUNG,M.IBRAHIM,R.CHATTERJEE,S.GUL,S.KOROIDOV,A.S.BREWSTER,       
AUTHOR   2 R.TRAN,R.ALONSO-MORI,F.FULLER,T.KROLL,T.MICHELS-CLARK,H.LAKSMONO,    
AUTHOR   3 R.G.SIERRA,C.A.STAN,C.SARACINI,M.A.BEAN,I.SEUFFERT,D.SOKARAS,T.-     
AUTHOR   4 C.WENG,M.S.HUNTER,A.AQUILA,J.E.KOGLIN,J.ROBINSON,M.LIANG,S.BOUTET,   
AUTHOR   5 A.Y.LYUBIMOV,M.UERVIROJNANGKOORN,N.W.MORIARTY,D.LIEBSCHNER,          
AUTHOR   6 P.V.AFONINE,D.G.WATERMAN,G.EVANS,H.DOBBEK,W.I.WEIS,A.T.BRUNGER,      
AUTHOR   7 P.H.ZWART,P.D.ADAMS,A.ZOUNI,J.MESSINGER,U.BERGMANN,N.K.SAUTER,       
AUTHOR   8 J.KERN,V.K.YACHANDRA,J.YANO                                          
REVDAT   5   20-NOV-19 5KAI    1       REMARK                                   
REVDAT   4   27-SEP-17 5KAI    1       REMARK                                   
REVDAT   3   28-DEC-16 5KAI    1       JRNL                                     
REVDAT   2   14-DEC-16 5KAI    1       JRNL                                     
REVDAT   1   23-NOV-16 5KAI    0                                                
JRNL        AUTH   I.D.YOUNG,M.IBRAHIM,R.CHATTERJEE,S.GUL,F.D.FULLER,           
JRNL        AUTH 2 S.KOROIDOV,A.S.BREWSTER,R.TRAN,R.ALONSO-MORI,T.KROLL,        
JRNL        AUTH 3 T.MICHELS-CLARK,H.LAKSMONO,R.G.SIERRA,C.A.STAN,R.HUSSEIN,    
JRNL        AUTH 4 M.ZHANG,L.DOUTHIT,M.KUBIN,C.DE LICHTENBERG,L.VO PHAM,        
JRNL        AUTH 5 H.NILSSON,M.H.CHEAH,D.SHEVELA,C.SARACINI,M.A.BEAN,           
JRNL        AUTH 6 I.SEUFFERT,D.SOKARAS,T.C.WENG,E.PASTOR,C.WENINGER,           
JRNL        AUTH 7 T.FRANSSON,L.LASSALLE,P.BRAUER,P.ALLER,P.T.DOCKER,B.ANDI,    
JRNL        AUTH 8 A.M.ORVILLE,J.M.GLOWNIA,S.NELSON,M.SIKORSKI,D.ZHU,           
JRNL        AUTH 9 M.S.HUNTER,T.J.LANE,A.AQUILA,J.E.KOGLIN,J.ROBINSON,M.LIANG,  
JRNL        AUTH10 S.BOUTET,A.Y.LYUBIMOV,M.UERVIROJNANGKOORN,N.W.MORIARTY,      
JRNL        AUTH11 D.LIEBSCHNER,P.V.AFONINE,D.G.WATERMAN,G.EVANS,P.WERNET,      
JRNL        AUTH12 H.DOBBEK,W.I.WEIS,A.T.BRUNGER,P.H.ZWART,P.D.ADAMS,A.ZOUNI,   
JRNL        AUTH13 J.MESSINGER,U.BERGMANN,N.K.SAUTER,J.KERN,V.K.YACHANDRA,      
JRNL        AUTH14 J.YANO                                                       
JRNL        TITL   STRUCTURE OF PHOTOSYSTEM II AND SUBSTRATE BINDING AT ROOM    
JRNL        TITL 2 TEMPERATURE.                                                 
JRNL        REF    NATURE                        V. 540   453 2016              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   27871088                                                     
JRNL        DOI    10.1038/NATURE20161                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   P.V.AFONINE,R.W.GROSSE-KUNSTLEVE,N.ECHOLS,J.J.HEADD,         
REMARK   1  AUTH 2 N.W.MORIARTY,M.MUSTYAKIMOV,T.C.TERWILLIGER,A.URZHUMTSEV,     
REMARK   1  AUTH 3 P.H.ZWART,P.D.ADAMS                                          
REMARK   1  TITL   TOWARDS AUTOMATED CRYSTALLOGRAPHIC STRUCTURE REFINEMENT WITH 
REMARK   1  TITL 2 PHENIX.REFINE.                                               
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  68   352 2012              
REMARK   1  REFN                   ESSN 1399-0047                               
REMARK   1  PMID   22505256                                                     
REMARK   1  DOI    10.1107/S0907444912001308                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   P.D.ADAMS,P.V.AFONINE,G.BUNKOCZI,V.B.CHEN,I.W.DAVIS,         
REMARK   1  AUTH 2 N.ECHOLS,J.J.HEADD,L.W.HUNG,G.J.KAPRAL,R.W.GROSSE-KUNSTLEVE, 
REMARK   1  AUTH 3 A.J.MCCOY,N.W.MORIARTY,R.OEFFNER,R.J.READ,D.C.RICHARDSON,    
REMARK   1  AUTH 4 J.S.RICHARDSON,T.C.TERWILLIGER,P.H.ZWART                     
REMARK   1  TITL   PHENIX: A COMPREHENSIVE PYTHON-BASED SYSTEM FOR              
REMARK   1  TITL 2 MACROMOLECULAR STRUCTURE SOLUTION.                           
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  66   213 2010              
REMARK   1  REFN                   ESSN 1399-0047                               
REMARK   1  PMID   20124702                                                     
REMARK   1  DOI    10.1107/S0907444909052925                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX DEV_2411                                      
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.57                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.325                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 211388                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.250                           
REMARK   3   R VALUE            (WORKING SET) : 0.250                           
REMARK   3   FREE R VALUE                     : 0.300                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 0.848                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1792                            
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 43.5751 -  6.5768    1.00    17110   148  0.1961 0.2170        
REMARK   3     2  6.5768 -  5.2230    1.00    16670   143  0.2167 0.2411        
REMARK   3     3  5.2230 -  4.5636    1.00    16511   143  0.1988 0.2573        
REMARK   3     4  4.5636 -  4.1467    1.00    16452   141  0.2128 0.2880        
REMARK   3     5  4.1467 -  3.8497    1.00    16413   141  0.2392 0.2634        
REMARK   3     6  3.8497 -  3.6228    1.00    16371   141  0.2603 0.3420        
REMARK   3     7  3.6228 -  3.4414    1.00    16322   142  0.2908 0.3308        
REMARK   3     8  3.4414 -  3.2917    0.99    16174   136  0.3163 0.3937        
REMARK   3     9  3.2917 -  3.1650    0.98    16075   138  0.3299 0.3666        
REMARK   3    10  3.1650 -  3.0558    0.97    15786   131  0.3473 0.4364        
REMARK   3    11  3.0558 -  2.9603    0.95    15534   128  0.3480 0.4292        
REMARK   3    12  2.9603 -  2.8757    0.94    15221   131  0.3568 0.4172        
REMARK   3    13  2.8757 -  2.8000    0.92    14957   129  0.3581 0.4058        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.504            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.535           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 60.41                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.52                          
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      :  0.003          52003                                  
REMARK   3   ANGLE     :  0.597          71322                                  
REMARK   3   CHIRALITY :  0.040           7052                                  
REMARK   3   PLANARITY :  0.005           8611                                  
REMARK   3   DIHEDRAL  : 21.034          18325                                  
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 5KAI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000221807.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-NOV-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : FREE ELECTRON LASER                
REMARK 200  BEAMLINE                       : CXI                                
REMARK 200  X-RAY GENERATOR MODEL          : SLAC LCLS BEAMLINE CXI             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.7492                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : 1 MICRON KB MIRROR                 
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : CS-PAD CXI-1                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CCTBX.XFEL                         
REMARK 200  DATA SCALING SOFTWARE          : CCTBX.PRIME                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 213400                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.570                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 13.70                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.6200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.17                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.935                              
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: PSII MONOMER COMPOSED OF 4UB6 MONOMER AND            
REMARK 200  ADDITIONAL CHAIN FROM 4PJ0                                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTAL GROWTH WAS AS DESCRIBED IN       
REMARK 280  KERN ET AL. 2005, BIOCHIM. BIOPHYS. ACTA-BIOENERGETICS AND          
REMARK 280  IBRAHIM ET AL. 2015, STRUCT. DYN. 2 (4), 041705, SUBSTITUTING       
REMARK 280  C12E8 FOR BETA-DM AND BETAINE FOR GLYCEROL, PH 7.5, BATCH MODE,     
REMARK 280  TEMPERATURE 293K                                                    
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       58.95550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      165.49800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      112.13400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      165.49800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       58.95550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      112.13400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 40-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, I, J, K,         
REMARK 350                    AND CHAINS: L, M, O, T, U, V, Y, X, Z,            
REMARK 350                    AND CHAINS: R, a, b, c, d, e, f, h, i, j,         
REMARK 350                    AND CHAINS: k, l, m, o, t, u, v, y, x,            
REMARK 350                    AND CHAINS: z, 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 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     MET B     1                                                      
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     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     MET E     1                                                      
REMARK 465     ALA E     2                                                      
REMARK 465     GLY E     3                                                      
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     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     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 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     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     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     MET X     1                                                      
REMARK 465     SER X    40                                                      
REMARK 465     LEU X    41                                                      
REMARK 465     MET R     1                                                      
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 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     MET b     1                                                      
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     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     MET e     1                                                      
REMARK 465     ALA e     2                                                      
REMARK 465     MET f     1                                                      
REMARK 465     THR f     2                                                      
REMARK 465     SER f     3                                                      
REMARK 465     ASN f     4                                                      
REMARK 465     THR f     5                                                      
REMARK 465     PRO f     6                                                      
REMARK 465     ASN f     7                                                      
REMARK 465     GLN f     8                                                      
REMARK 465     GLU f     9                                                      
REMARK 465     PRO f    10                                                      
REMARK 465     VAL f    11                                                      
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     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 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     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     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     MET x     1                                                      
REMARK 465     SER x    40                                                      
REMARK 465     LEU x    41                                                      
REMARK 465     MET r     1                                                      
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS D 336    O                                                   
REMARK 470     GLU b 489    CG   CD   OE1  OE2                                  
REMARK 470     HIS d 336    O                                                   
REMARK 470     THR x   2    OG1  CG2                                            
REMARK 470     LEU r   6    CG   CD1  CD2                                       
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   NH2  ARG H     4     OD2  ASP H     9              1.66            
REMARK 500   OH   TYR d   141     O4   LHG d   406              2.00            
REMARK 500   O    ALA b   155     OG1  THR b   159              2.07            
REMARK 500   O    LEU F    26     OG1  THR F    30              2.12            
REMARK 500   O    GLY B   269     NH2  ARG B   448              2.13            
REMARK 500   NH2  ARG B    18     O8   SQD B   626              2.14            
REMARK 500   O    SER a   217     OG   SER a   221              2.15            
REMARK 500   OG1  THR H     5     OBD  CLA B   617              2.15            
REMARK 500   O    VAL z    25     OG   SER z    29              2.15            
REMARK 500   OD2  ASP b   125     NH1  ARG b   127              2.15            
REMARK 500   OE2  GLU a   333     O    HOH a   801              2.15            
REMARK 500   O3   BCT a   706     O    HOH a   802              2.16            
REMARK 500   O    ARG b   124     NH2  ARG h    12              2.18            
REMARK 500   OH   TYR O    38     O    HOH O   301              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    LYS i  33   CB    LYS i  33   CG     -0.164                       
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      -79.13    -94.54                                   
REMARK 500    LEU A 159      -52.76   -131.86                                   
REMARK 500    ILE A 259      -95.92   -116.29                                   
REMARK 500    ASP B  49       85.86   -165.66                                   
REMARK 500    VAL B  51      -61.39    -95.68                                   
REMARK 500    PRO B  54     -169.75    -78.96                                   
REMARK 500    TYR B 117       67.33   -102.50                                   
REMARK 500    PHE B 162       67.47   -156.92                                   
REMARK 500    TYR B 314      135.12   -174.84                                   
REMARK 500    ASN B 348     -154.35    -85.39                                   
REMARK 500    ASP B 372     -156.62   -112.43                                   
REMARK 500    PHE B 383      -77.15    -89.96                                   
REMARK 500    ASN B 438       73.29     50.15                                   
REMARK 500    PRO B 488       40.07    -58.75                                   
REMARK 500    PHE B 495      -77.72   -103.89                                   
REMARK 500    THR C  24      105.31   -164.91                                   
REMARK 500    ILE C  87      -30.48   -135.25                                   
REMARK 500    GLU C 221      -88.56   -103.45                                   
REMARK 500    TRP C 223     -130.87     55.69                                   
REMARK 500    THR C 295      -66.57    -90.19                                   
REMARK 500    THR C 355        4.09    -69.73                                   
REMARK 500    PRO C 400       53.39    -69.91                                   
REMARK 500    SER C 416      -71.88   -173.99                                   
REMARK 500    SER C 463       53.99   -144.91                                   
REMARK 500    LYS D  23       35.42    -89.80                                   
REMARK 500    VAL D  30      -78.67    -91.41                                   
REMARK 500    SER D  65       23.27   -148.42                                   
REMARK 500    HIS D  87       33.81    -95.73                                   
REMARK 500    PRO D 140       41.91    -86.68                                   
REMARK 500    GLN D 164     -158.74    -94.24                                   
REMARK 500    PHE D 173       89.64    -66.10                                   
REMARK 500    THR D 231       12.49    -69.32                                   
REMARK 500    ALA D 234       30.12    -80.88                                   
REMARK 500    SER D 262       12.24   -141.84                                   
REMARK 500    SER D 295       71.68   -103.36                                   
REMARK 500    ALA D 351      -52.62     63.41                                   
REMARK 500    ARG E  61       16.31   -141.63                                   
REMARK 500    SER H  16      -35.66   -150.48                                   
REMARK 500    GLU H  17       45.82    -78.26                                   
REMARK 500    THR H  27       33.35    -86.17                                   
REMARK 500    LYS H  63       41.91    -75.46                                   
REMARK 500    LYS I  33      -95.23   -117.09                                   
REMARK 500    SER J  39       -2.71     66.26                                   
REMARK 500    ALA K  14      -36.24    140.57                                   
REMARK 500    PRO L   5        2.90    -66.45                                   
REMARK 500    GLN M  32     -126.70    -78.20                                   
REMARK 500    PRO O  56     -155.28    -74.03                                   
REMARK 500    LYS O  57      -69.52   -124.79                                   
REMARK 500    LYS O  59      -26.03     64.71                                   
REMARK 500    ARG O  73     -163.50     56.03                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     141 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 THR o    4     LEU o    5                 -148.09                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     LMG A  603                                                       
REMARK 610     CLA A  609                                                       
REMARK 610     SQD A  612                                                       
REMARK 610     SQD A  614                                                       
REMARK 610     LMG B  621                                                       
REMARK 610     SQD B  623                                                       
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     LMG C  521                                                       
REMARK 610     LMG D  409                                                       
REMARK 610     SQD D  410                                                       
REMARK 610     DGD H  103                                                       
REMARK 610     SQD I  102                                                       
REMARK 610     LMG M  101                                                       
REMARK 610     LMG a  701                                                       
REMARK 610     LMG a  715                                                       
REMARK 610     LHG a  720                                                       
REMARK 610     CLA b  622                                                       
REMARK 610     LMG b  626                                                       
REMARK 610     LMG b  627                                                       
REMARK 610     LMG b  628                                                       
REMARK 610     CLA c  504                                                       
REMARK 610     DGD c  516                                                       
REMARK 610     DGD c  517                                                       
REMARK 610     DGD c  518                                                       
REMARK 610     LMG c  519                                                       
REMARK 610     LMG c  520                                                       
REMARK 610     LMG d  408                                                       
REMARK 610     LHG e  101                                                       
REMARK 610     LMG f  101                                                       
REMARK 610     SQD f  102                                                       
REMARK 610     DGD h  102                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 170   OD1                                                    
REMARK 620 2 OEX A 601   O1  153.3                                              
REMARK 620 3 OEX A 601   O2   87.9  65.9                                        
REMARK 620 4 OEX A 601   O5   98.0  79.6  73.9                                  
REMARK 620 5 GLU A 189   OE1 134.6  72.0 137.3  92.3                            
REMARK 620 6 ALA A 344   O    88.8  78.2  69.5 142.4 108.9                      
REMARK 620 7 HOH A 703   O    94.5 109.8 146.8  73.0  46.9 143.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 170   OD2                                                    
REMARK 620 2 OEX A 601   O5  118.8                                              
REMARK 620 3 OEX A 601   O4   79.8  86.5                                        
REMARK 620 4 GLU A 333   OE2 143.4  91.4  82.2                                  
REMARK 620 5 HOH A 707   O    81.8  87.8 155.2 122.1                            
REMARK 620 6 HOH A 701   O    82.5 156.4  87.4  65.1 106.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 189   OE2                                                    
REMARK 620 2 OEX A 601   O1   76.5                                              
REMARK 620 3 OEX A 601   O5   91.4  91.8                                        
REMARK 620 4 OEX A 601   O3  164.1  91.2  78.7                                  
REMARK 620 5 HIS A 332   NE2 106.5 167.9  99.8  87.5                            
REMARK 620 6 ASP A 342   OD2  97.7  71.2 158.2  87.8  96.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 A 602  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 215   NE2                                                    
REMARK 620 2 HIS A 272   NE2  92.0                                              
REMARK 620 3 HIS D 214   NE2  98.1  92.2                                        
REMARK 620 4 HIS D 268   NE2  82.3 169.8  97.0                                  
REMARK 620 5 BCT A 615   O1  170.8  88.1  91.1  96.1                            
REMARK 620 6 BCT A 615   O2  108.7  90.6 152.9  83.2  62.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 333   OE1                                                    
REMARK 620 2 OEX A 601   O2  153.3                                              
REMARK 620 3 OEX A 601   O3   89.8  90.2                                        
REMARK 620 4 OEX A 601   O4   93.8  85.3 175.4                                  
REMARK 620 5 OEX A 601   O5  107.3  99.4  88.4  93.4                            
REMARK 620 6 GLU C 354   OE2  80.8  72.5  87.1  90.6 170.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 342   OD1                                                    
REMARK 620 2 OEX A 601   O1   91.2                                              
REMARK 620 3 OEX A 601   O2  159.5 104.0                                        
REMARK 620 4 OEX A 601   O3  101.3  86.1  93.5                                  
REMARK 620 5 ALA A 344   OXT  84.2  91.0  81.9 173.8                            
REMARK 620 6 GLU C 354   OE1  81.1 168.4  81.6 103.8  79.7                      
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  106.7                                              
REMARK 620 3 CLA C 512   NB   95.4  91.2                                        
REMARK 620 4 CLA C 512   NC   80.9 171.9  90.9                                  
REMARK 620 5 CLA C 512   ND   91.9  90.2 171.8  86.7                            
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   94.8                                              
REMARK 620 3 HEM E 102   NB  104.1  88.5                                        
REMARK 620 4 HEM E 102   NC   89.5 175.5  91.5                                  
REMARK 620 5 HEM E 102   ND   72.6  91.8 176.8  88.4                            
REMARK 620 6 HIS F  24   NE2 165.1  73.1  84.7 102.4  98.5                      
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  103.3                                              
REMARK 620 3 HEM V 201   NB   93.7  89.6                                        
REMARK 620 4 HEM V 201   NC   72.8 176.2  90.6                                  
REMARK 620 5 HEM V 201   ND   80.0  90.0 173.4  89.4                            
REMARK 620 6 HIS V  92   NE2 163.6  91.5  93.5  92.3  93.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 702  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 170   OD1                                                    
REMARK 620 2 OEX a 702   O1  153.0                                              
REMARK 620 3 OEX a 702   O2   92.1  65.9                                        
REMARK 620 4 OEX a 702   O5  110.2  79.6  73.9                                  
REMARK 620 5 GLU a 189   OE1 148.7  52.7 118.1  87.6                            
REMARK 620 6 ALA a 344   O    82.8  76.4  73.7 145.4  97.2                      
REMARK 620 7 HOH a 808   O   100.9 105.6 153.7  80.2  55.6 130.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 702  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 170   OD2                                                    
REMARK 620 2 OEX a 702   O5  103.0                                              
REMARK 620 3 OEX a 702   O4   80.1  86.6                                        
REMARK 620 4 GLU a 333   OE2 152.3  91.7  77.5                                  
REMARK 620 5 HOH a 801   O   130.5 111.7 134.5  61.4                            
REMARK 620 6 HOH a 807   O    90.0 158.7  79.1  70.1  69.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 702  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 189   OE2                                                    
REMARK 620 2 OEX a 702   O1   86.5                                              
REMARK 620 3 OEX a 702   O5  126.8  91.8                                        
REMARK 620 4 OEX a 702   O3  154.4  91.3  78.7                                  
REMARK 620 5 HIS a 332   NE2  94.2 165.5  99.3  81.8                            
REMARK 620 6 ASP a 342   OD2  73.4  76.3 156.5  81.3  90.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 a 703  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS a 215   NE2                                                    
REMARK 620 2 HIS a 272   NE2  91.9                                              
REMARK 620 3 HIS d 214   NE2  96.7  86.5                                        
REMARK 620 4 HIS d 268   NE2  91.7 175.7  95.3                                  
REMARK 620 5 BCT a 706   O1  164.3  91.5  98.8  84.3                            
REMARK 620 6 BCT a 706   O2  100.5  93.4 162.7  83.7  63.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 702  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 333   OE1                                                    
REMARK 620 2 OEX a 702   O2  146.6                                              
REMARK 620 3 OEX a 702   O3   91.9  90.2                                        
REMARK 620 4 OEX a 702   O4   91.3  85.3 175.3                                  
REMARK 620 5 OEX a 702   O5  114.1  99.3  88.4  93.4                            
REMARK 620 6 GLU c 354   OE2  71.0  76.5  80.6  97.2 168.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 702  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 342   OD1                                                    
REMARK 620 2 OEX a 702   O1   92.6                                              
REMARK 620 3 OEX a 702   O2  158.8 104.0                                        
REMARK 620 4 OEX a 702   O3  100.8  86.1  93.5                                  
REMARK 620 5 ALA a 344   OXT  84.4  87.8  83.2 172.1                            
REMARK 620 6 GLU c 354   OE1  77.0 167.9  84.8 101.9  84.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c 511  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN c  39   OD1                                                    
REMARK 620 2 CLA c 511   NA  103.3                                              
REMARK 620 3 CLA c 511   NB  104.4  91.3                                        
REMARK 620 4 CLA c 511   NC   83.1 172.6  90.8                                  
REMARK 620 5 CLA c 511   ND   82.8  90.3 172.0  86.7                            
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  103.2                                              
REMARK 620 3 HEM e 102   NB  105.1  88.5                                        
REMARK 620 4 HEM e 102   NC   84.3 172.3  91.0                                  
REMARK 620 5 HEM e 102   ND   74.1  91.2 179.0  89.5                            
REMARK 620 6 HIS f  24   NE2 165.9  82.9  87.6  89.4  93.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM v 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS v  41   NE2                                                    
REMARK 620 2 HEM v 201   NA  100.1                                              
REMARK 620 3 HEM v 201   NB   94.2  89.6                                        
REMARK 620 4 HEM v 201   NC   80.0 179.9  90.2                                  
REMARK 620 5 HEM v 201   ND   83.2  89.9 177.3  90.2                            
REMARK 620 6 HIS v  92   NE2 160.1  94.7  99.2  85.2  83.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A 607  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 712   O                                                      
REMARK 620 2 CLA A 607   NA   93.4                                              
REMARK 620 3 CLA A 607   NB   94.5  91.4                                        
REMARK 620 4 CLA A 607   NC   91.4 174.3  91.2                                  
REMARK 620 5 CLA A 607   ND   91.3  90.7 173.7  86.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 602  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 705   O                                                      
REMARK 620 2 CLA B 602   NA   86.9                                              
REMARK 620 3 CLA B 602   NB   86.6  91.4                                        
REMARK 620 4 CLA B 602   NC   98.7 174.0  91.1                                  
REMARK 620 5 CLA B 602   ND   99.4  90.6 173.8  86.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 608  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 704   O                                                      
REMARK 620 2 CLA B 608   NA   92.1                                              
REMARK 620 3 CLA B 608   NB   80.6  91.6                                        
REMARK 620 4 CLA B 608   NC   93.7 173.9  91.0                                  
REMARK 620 5 CLA B 608   ND  105.5  90.5 173.4  86.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 611  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 702   O                                                      
REMARK 620 2 CLA B 611   NA   85.3                                              
REMARK 620 3 CLA B 611   NB   78.2  91.5                                        
REMARK 620 4 CLA B 611   NC  100.8 173.7  91.2                                  
REMARK 620 5 CLA B 611   ND  107.7  90.4 174.0  86.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 505  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 601   O                                                      
REMARK 620 2 CLA C 505   NA   89.5                                              
REMARK 620 3 CLA C 505   NB   85.1  91.5                                        
REMARK 620 4 CLA C 505   NC   96.1 174.1  91.1                                  
REMARK 620 5 CLA C 505   ND  101.1  90.6 173.5  86.2                            
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 602   O                                                      
REMARK 620 2 CLA C 508   NA   94.1                                              
REMARK 620 3 CLA C 508   NB   90.1  91.6                                        
REMARK 620 4 CLA C 508   NC   91.5 173.8  90.9                                  
REMARK 620 5 CLA C 508   ND   95.8  90.6 173.5  86.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA D 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D 504   O                                                      
REMARK 620 2 CLA D 402   NA   87.0                                              
REMARK 620 3 CLA D 402   NB   88.9  91.5                                        
REMARK 620 4 CLA D 402   NC   97.7 174.6  91.2                                  
REMARK 620 5 CLA D 402   ND   96.8  90.8 174.0  86.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA a 708  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH a 810   O                                                      
REMARK 620 2 CLA a 708   NA   89.3                                              
REMARK 620 3 CLA a 708   NB   87.7  91.5                                        
REMARK 620 4 CLA a 708   NC   95.5 174.6  91.2                                  
REMARK 620 5 CLA a 708   ND   98.0  90.7 173.9  86.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA a 719  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH a 809   O                                                      
REMARK 620 2 CLA a 719   NA   91.0                                              
REMARK 620 3 CLA a 719   NB   98.7  91.6                                        
REMARK 620 4 CLA a 719   NC   93.5 174.3  91.2                                  
REMARK 620 5 CLA a 719   ND   87.0  90.6 173.8  86.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b 607  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH b 709   O                                                      
REMARK 620 2 CLA b 607   NA   94.8                                              
REMARK 620 3 CLA b 607   NB   86.7  91.5                                        
REMARK 620 4 CLA b 607   NC   91.8 173.1  90.9                                  
REMARK 620 5 CLA b 607   ND   99.8  90.4 173.1  86.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b 613  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH b 711   O                                                      
REMARK 620 2 CLA b 613   NA   85.5                                              
REMARK 620 3 CLA b 613   NB  101.4  91.5                                        
REMARK 620 4 CLA b 613   NC  100.0 173.4  91.0                                  
REMARK 620 5 CLA b 613   ND   85.2  90.5 173.3  86.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b 616  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH b 704   O                                                      
REMARK 620 2 CLA b 616   NA   84.7                                              
REMARK 620 3 CLA b 616   NB   83.3  91.5                                        
REMARK 620 4 CLA b 616   NC  101.2 173.7  91.1                                  
REMARK 620 5 CLA b 616   ND  102.6  90.2 173.9  86.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c 504  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH c 604   O                                                      
REMARK 620 2 CLA c 504   NA   92.5                                              
REMARK 620 3 CLA c 504   NB   76.8  91.6                                        
REMARK 620 4 CLA c 504   NC   93.3 174.0  91.0                                  
REMARK 620 5 CLA c 504   ND  109.1  90.5 173.6  86.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c 507  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH c 606   O                                                      
REMARK 620 2 CLA c 507   NA   84.9                                              
REMARK 620 3 CLA c 507   NB   86.2  91.6                                        
REMARK 620 4 CLA c 507   NC  100.8 174.0  90.9                                  
REMARK 620 5 CLA c 507   ND  100.1  90.7 173.5  86.3                            
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 OEX A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE2 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 605                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 A 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT A 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD B 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG B 625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD B 626                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR D 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 D 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG D 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD D 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG E 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM E 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR H 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD H 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD I 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR K 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG L 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG M 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM V 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR Y 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG a 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OEX a 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE2 a 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 704                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 705                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT a 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 707                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 708                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO a 709                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO a 710                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 711                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR a 712                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 a 713                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 714                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG a 715                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 719                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG a 720                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD b 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 626                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 627                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 628                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG b 629                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR d 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 d 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG d 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG e 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM e 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG f 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD f 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR h 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD h 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR k 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR k 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR t 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HEM v 201 and CYS v    
REMARK 800  37                                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT5                                                 
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: AT6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HEM v 201 and CYS v    
REMARK 800  37                                                                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5KAF   RELATED DB: PDB                                   
REMARK 900 CORRESPONDING DARK STATE RT STRUCTURE OF PHOTOSYSTEM II              
REMARK 900 RELATED ID: 5TIS   RELATED DB: PDB                                   
DBREF  5KAI A    1   344  UNP    P0A444   PSBA1_THEEB      1    344             
DBREF  5KAI B    1   510  UNP    Q8DIQ1   PSBB_THEEB       1    510             
DBREF  5KAI C   13   473  UNP    Q8DIF8   PSBC_THEEB       1    461             
DBREF  5KAI D    1   352  UNP    Q8CM25   PSBD_THEEB       1    352             
DBREF  5KAI E    1    84  UNP    Q8DIP0   PSBE_THEEB       1     84             
DBREF  5KAI F    1    45  UNP    Q8DIN9   PSBF_THEEB       1     45             
DBREF  5KAI H    2    64  UNP    Q8DJ43   PSBH_THEEB       2     64             
DBREF  5KAI I    2    38  UNP    Q8DJZ6   PSBI_THEEB       2     38             
DBREF  5KAI J    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  5KAI K    1    46  UNP    Q9F1K9   PSBK_THEEB       1     46             
DBREF  5KAI L    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  5KAI M    2    36  UNP    Q8DHA7   PSBM_THEEB       2     36             
DBREF  5KAI O  -25   246  UNP    P0A431   PSBO_THEEB       1    272             
DBREF  5KAI T    2    32  UNP    Q8DIQ0   PSBT_THEEB       2     32             
DBREF  5KAI U  -29   104  UNP    Q9F1L5   PSBU_THEEB       1    134             
DBREF  5KAI V  -25   137  UNP    P0A386   CY550_THEEB      1    163             
DBREF  5KAI Y    1    46  UNP    Q8DJI1   YCF12_THEEB      1     46             
DBREF  5KAI X    1    41  UNP    Q9F1R6   PSBX_THEEB       1     41             
DBREF  5KAI Z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
DBREF  5KAI R    1    41  UNP    Q8DKM3   PSBY_THEEB       1     41             
DBREF  5KAI a    1   344  UNP    P0A444   PSBA1_THEEB      1    344             
DBREF  5KAI b    1   510  UNP    Q8DIQ1   PSBB_THEEB       1    510             
DBREF  5KAI c   13   473  UNP    Q8DIF8   PSBC_THEEB       1    461             
DBREF  5KAI d    1   352  UNP    Q8CM25   PSBD_THEEB       1    352             
DBREF  5KAI e    1    84  UNP    Q8DIP0   PSBE_THEEB       1     84             
DBREF  5KAI f    1    45  UNP    Q8DIN9   PSBF_THEEB       1     45             
DBREF  5KAI h    2    64  UNP    Q8DJ43   PSBH_THEEB       2     64             
DBREF  5KAI i    2    38  UNP    Q8DJZ6   PSBI_THEEB       2     38             
DBREF  5KAI j    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  5KAI k    1    46  UNP    Q9F1K9   PSBK_THEEB       1     46             
DBREF  5KAI l    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  5KAI m    2    36  UNP    Q8DHA7   PSBM_THEEB       2     36             
DBREF  5KAI o  -25   246  UNP    P0A431   PSBO_THEEB       1    272             
DBREF  5KAI t    2    32  UNP    Q8DIQ0   PSBT_THEEB       2     32             
DBREF  5KAI u  -29   104  UNP    Q9F1L5   PSBU_THEEB       1    134             
DBREF  5KAI v  -25   137  UNP    P0A386   CY550_THEEB      1    163             
DBREF  5KAI y    1    46  UNP    Q8DJI1   YCF12_THEEB      1     46             
DBREF  5KAI x    1    41  UNP    Q9F1R6   PSBX_THEEB       1     41             
DBREF  5KAI z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
DBREF  5KAI r    1    41  UNP    Q8DKM3   PSBY_THEEB       1     41             
SEQADV 5KAI FME I    1  UNP  Q8DJZ6              EXPRESSION TAG                 
SEQADV 5KAI FME M    1  UNP  Q8DHA7              EXPRESSION TAG                 
SEQADV 5KAI FME T    1  UNP  Q8DIQ0              EXPRESSION TAG                 
SEQADV 5KAI FME i    1  UNP  Q8DJZ6              EXPRESSION TAG                 
SEQADV 5KAI FME m    1  UNP  Q8DHA7              EXPRESSION TAG                 
SEQADV 5KAI FME t    1  UNP  Q8DIQ0              EXPRESSION TAG                 
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   63  ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO LEU          
SEQRES   2 H   63  ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY THR          
SEQRES   3 H   63  THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU VAL          
SEQRES   4 H   63  PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR LEU          
SEQRES   5 H   63  ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA                  
SEQRES   1 I   38  FME 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  FME 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  FME 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 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 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   63  ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO LEU          
SEQRES   2 h   63  ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY THR          
SEQRES   3 h   63  THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU VAL          
SEQRES   4 h   63  PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR LEU          
SEQRES   5 h   63  ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA                  
SEQRES   1 i   38  FME 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  FME 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  FME 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 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                                                      
MODRES 5KAI FME I    1  MET  MODIFIED RESIDUE                                   
MODRES 5KAI FME M    1  MET  MODIFIED RESIDUE                                   
MODRES 5KAI FME T    1  MET  MODIFIED RESIDUE                                   
MODRES 5KAI FME i    1  MET  MODIFIED RESIDUE                                   
MODRES 5KAI FME m    1  MET  MODIFIED RESIDUE                                   
MODRES 5KAI FME t    1  MET  MODIFIED RESIDUE                                   
HET    FME  I   1      10                                                       
HET    FME  M   1      10                                                       
HET    FME  T   1      10                                                       
HET    FME  i   1      10                                                       
HET    FME  m   1      10                                                       
HET    FME  t   1      10                                                       
HET    OEX  A 601      10                                                       
HET    FE2  A 602       1                                                       
HET    LMG  A 603      51                                                       
HET     CL  A 604       1                                                       
HET     CL  A 605       1                                                       
HET    CLA  A 606      65                                                       
HET    CLA  A 607      65                                                       
HET    PHO  A 608      64                                                       
HET    CLA  A 609      54                                                       
HET    BCR  A 610      40                                                       
HET    PL9  A 611      55                                                       
HET    SQD  A 612      52                                                       
HET    UNL  A 613       7                                                       
HET    SQD  A 614      40                                                       
HET    BCT  A 615       4                                                       
HET    UNL  B 601      12                                                       
HET    CLA  B 602      65                                                       
HET    CLA  B 603      65                                                       
HET    CLA  B 604      65                                                       
HET    CLA  B 605      65                                                       
HET    CLA  B 606      65                                                       
HET    CLA  B 607      65                                                       
HET    CLA  B 608      65                                                       
HET    CLA  B 609      65                                                       
HET    CLA  B 610      65                                                       
HET    CLA  B 611      65                                                       
HET    CLA  B 612      65                                                       
HET    CLA  B 613      65                                                       
HET    CLA  B 614      65                                                       
HET    CLA  B 615      65                                                       
HET    CLA  B 616      65                                                       
HET    CLA  B 617      65                                                       
HET    BCR  B 618      40                                                       
HET    BCR  B 619      40                                                       
HET    BCR  B 620      40                                                       
HET    LMG  B 621      51                                                       
HET    UNL  B 622       6                                                       
HET    SQD  B 623      47                                                       
HET    UNL  B 624      11                                                       
HET    LHG  B 625      49                                                       
HET    SQD  B 626      54                                                       
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      62                                                       
HET    DGD  C 519      62                                                       
HET    LMG  C 520      51                                                       
HET    LMG  C 521      51                                                       
HET    PHO  D 401      64                                                       
HET    CLA  D 402      65                                                       
HET    CLA  D 403      65                                                       
HET    CLA  D 404      65                                                       
HET    BCR  D 405      40                                                       
HET    PL9  D 406      55                                                       
HET    LHG  D 407      49                                                       
HET    LHG  D 408      49                                                       
HET    LMG  D 409      51                                                       
HET    SQD  D 410      43                                                       
HET    LHG  E 101      49                                                       
HET    HEM  E 102      43                                                       
HET    UNL  H 101       8                                                       
HET    BCR  H 102      40                                                       
HET    DGD  H 103      62                                                       
HET    UNL  I 101       9                                                       
HET    SQD  I 102      40                                                       
HET    BCR  K 101      40                                                       
HET    LHG  L 101      49                                                       
HET    LMG  M 101      51                                                       
HET    UNL  M 102       6                                                       
HET    UNL  M 103      16                                                       
HET    HEM  V 201      43                                                       
HET    BCR  Y 101      40                                                       
HET    LMG  a 701      51                                                       
HET    OEX  a 702      10                                                       
HET    FE2  a 703       1                                                       
HET     CL  a 704       1                                                       
HET     CL  a 705       1                                                       
HET    BCT  a 706       4                                                       
HET    CLA  a 707      65                                                       
HET    CLA  a 708      65                                                       
HET    PHO  a 709      64                                                       
HET    PHO  a 710      64                                                       
HET    CLA  a 711      65                                                       
HET    BCR  a 712      40                                                       
HET    PL9  a 713      55                                                       
HET    SQD  a 714      54                                                       
HET    LMG  a 715      51                                                       
HET    UNL  a 716       4                                                       
HET    UNL  a 717       7                                                       
HET    UNL  a 718      13                                                       
HET    CLA  a 719      65                                                       
HET    LHG  a 720      39                                                       
HET    SQD  b 601      54                                                       
HET    BCR  b 602      40                                                       
HET    UNL  b 603      11                                                       
HET    UNL  b 604      11                                                       
HET    UNL  b 605      13                                                       
HET    UNL  b 606      13                                                       
HET    CLA  b 607      65                                                       
HET    CLA  b 608      65                                                       
HET    CLA  b 609      65                                                       
HET    CLA  b 610      65                                                       
HET    CLA  b 611      65                                                       
HET    CLA  b 612      65                                                       
HET    CLA  b 613      65                                                       
HET    CLA  b 614      65                                                       
HET    CLA  b 615      65                                                       
HET    CLA  b 616      65                                                       
HET    CLA  b 617      65                                                       
HET    CLA  b 618      65                                                       
HET    CLA  b 619      65                                                       
HET    CLA  b 620      65                                                       
HET    CLA  b 621      65                                                       
HET    CLA  b 622      47                                                       
HET    BCR  b 623      40                                                       
HET    BCR  b 624      40                                                       
HET    BCR  b 625      40                                                       
HET    LMG  b 626      51                                                       
HET    LMG  b 627      51                                                       
HET    LMG  b 628       9                                                       
HET    LHG  b 629      49                                                       
HET    CLA  c 501      65                                                       
HET    CLA  c 502      65                                                       
HET    CLA  c 503      65                                                       
HET    CLA  c 504      58                                                       
HET    CLA  c 505      65                                                       
HET    CLA  c 506      65                                                       
HET    CLA  c 507      65                                                       
HET    CLA  c 508      65                                                       
HET    CLA  c 509      65                                                       
HET    CLA  c 510      65                                                       
HET    CLA  c 511      65                                                       
HET    CLA  c 512      65                                                       
HET    CLA  c 513      65                                                       
HET    BCR  c 514      40                                                       
HET    BCR  c 515      40                                                       
HET    DGD  c 516      62                                                       
HET    DGD  c 517      62                                                       
HET    DGD  c 518      62                                                       
HET    LMG  c 519      51                                                       
HET    LMG  c 520      51                                                       
HET    UNL  d 401      22                                                       
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    LMG  d 408      40                                                       
HET    LHG  e 101      42                                                       
HET    HEM  e 102      43                                                       
HET    LMG  f 101      51                                                       
HET    SQD  f 102      41                                                       
HET    BCR  h 101      40                                                       
HET    DGD  h 102      62                                                       
HET    UNL  i 101      22                                                       
HET    UNL  j 101       9                                                       
HET    BCR  k 101      40                                                       
HET    BCR  k 102      40                                                       
HET    UNL  m 101       5                                                       
HET    UNL  m 102      12                                                       
HET    UNL  t 101      10                                                       
HET    UNL  t 102       5                                                       
HET    BCR  t 103      40                                                       
HET    HEM  v 201      43                                                       
HET    UNL  z 101      11                                                       
HETNAM     FME N-FORMYLMETHIONINE                                               
HETNAM     OEX CA-MN4-O5 CLUSTER                                                
HETNAM     FE2 FE (II) ION                                                      
HETNAM     LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE                        
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     UNL UNKNOWN LIGAND                                                   
HETNAM     BCT BICARBONATE ION                                                  
HETNAM     LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE                           
HETNAM     DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)                              
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETSYN     PL9 PLASTOQUINONE 9                                                  
HETSYN     SQD SULFOQUINOVOSYLDIACYLGLYCEROL                                    
HETSYN     HEM HEME                                                             
FORMUL   8  FME    6(C6 H11 N O3 S)                                             
FORMUL  41  OEX    2(CA MN4 O5)                                                 
FORMUL  42  FE2    2(FE 2+)                                                     
FORMUL  43  LMG    16(C45 H86 O10)                                              
FORMUL  44   CL    4(CL 1-)                                                     
FORMUL  46  CLA    70(C55 H72 MG N4 O5 2+)                                      
FORMUL  48  PHO    4(C55 H74 N4 O5)                                             
FORMUL  50  BCR    22(C40 H56)                                                  
FORMUL  51  PL9    4(C53 H80 O2)                                                
FORMUL  52  SQD    9(C41 H78 O12 S)                                             
FORMUL  55  BCT    2(C H O3 1-)                                                 
FORMUL  80  LHG    10(C38 H75 O10 P)                                            
FORMUL  98  DGD    8(C51 H96 O15)                                               
FORMUL  14  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL  21  HOH   *107(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 PRO A   95  ALA A   99  5                                   5    
HELIX    5 AA5 SER A  101  ASN A  108  1                                   8    
HELIX    6 AA6 GLY A  109  GLY A  138  1                                  30    
HELIX    7 AA7 TRP A  142  LEU A  159  1                                  18    
HELIX    8 AA8 LEU A  159  GLY A  166  1                                   8    
HELIX    9 AA9 SER A  167  GLY A  171  5                                   5    
HELIX   10 AB1 ILE A  176  ASN A  191  1                                  16    
HELIX   11 AB2 ILE A  192  MET A  194  5                                   3    
HELIX   12 AB3 HIS A  195  SER A  222  1                                  28    
HELIX   13 AB4 SER A  232  TYR A  237  5                                   6    
HELIX   14 AB5 ASN A  247  ILE A  259  1                                  13    
HELIX   15 AB6 PHE A  260  SER A  264  5                                   5    
HELIX   16 AB7 ASN A  267  ALA A  294  1                                  28    
HELIX   17 AB8 THR A  316  HIS A  332  1                                  17    
HELIX   18 AB9 PRO B    4  ILE B   13  5                                  10    
HELIX   19 AC1 ASP B   15  PHE B   45  1                                  31    
HELIX   20 AC2 PRO B   54  GLN B   58  5                                   5    
HELIX   21 AC3 VAL B   62  LEU B   69  1                                   8    
HELIX   22 AC4 SER B   92  TYR B  117  1                                  26    
HELIX   23 AC5 LEU B  120  ARG B  124  5                                   5    
HELIX   24 AC6 ASP B  134  PHE B  156  1                                  23    
HELIX   25 AC7 GLY B  186  ASN B  191  5                                   6    
HELIX   26 AC8 ASN B  194  VAL B  219  1                                  26    
HELIX   27 AC9 PRO B  222  LEU B  229  1                                   8    
HELIX   28 AD1 ILE B  234  GLY B  259  1                                  26    
HELIX   29 AD2 PRO B  264  GLY B  269  1                                   6    
HELIX   30 AD3 ARG B  272  SER B  277  1                                   6    
HELIX   31 AD4 SER B  278  SER B  294  1                                  17    
HELIX   32 AD5 THR B  297  ALA B  304  1                                   8    
HELIX   33 AD6 PRO B  306  ASP B  313  1                                   8    
HELIX   34 AD7 TYR B  314  ASN B  318  5                                   5    
HELIX   35 AD8 PRO B  329  GLY B  333  5                                   5    
HELIX   36 AD9 SER B  391  GLY B  396  1                                   6    
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 ASP C   27  GLY C   32  1                                   6    
HELIX   40 AE4 ALA C   34  ILE C   43  5                                  10    
HELIX   41 AE5 LEU C   45  HIS C   74  1                                  30    
HELIX   42 AE6 PRO C   80  GLY C   85  5                                   6    
HELIX   43 AE7 ILE C   87  LEU C   95  1                                   9    
HELIX   44 AE8 GLY C  100  GLU C  104  5                                   5    
HELIX   45 AE9 THR C  108  ARG C  135  1                                  28    
HELIX   46 AF1 ASP C  153  PHE C  181  1                                  29    
HELIX   47 AF2 ASP C  205  PHE C  210  1                                   6    
HELIX   48 AF3 GLY C  211  LYS C  215  5                                   5    
HELIX   49 AF4 GLY C  222  VAL C  227  5                                   6    
HELIX   50 AF5 ASN C  229  THR C  254  1                                  26    
HELIX   51 AF6 PHE C  257  ARG C  262  1                                   6    
HELIX   52 AF7 SER C  267  ASN C  293  1                                  27    
HELIX   53 AF8 PRO C  298  GLY C  303  1                                   6    
HELIX   54 AF9 THR C  305  LEU C  324  1                                  20    
HELIX   55 AG1 GLY C  353  TRP C  359  5                                   7    
HELIX   56 AG2 LEU C  366  PRO C  368  5                                   3    
HELIX   57 AG3 ASP C  376  ASP C  383  1                                   8    
HELIX   58 AG4 GLN C  385  THR C  397  1                                  13    
HELIX   59 AG5 SER C  421  GLY C  454  1                                  34    
HELIX   60 AG6 ASP C  460  GLU C  464  5                                   5    
HELIX   61 AG7 PRO C  465  MET C  469  5                                   5    
HELIX   62 AG8 GLY D   13  LYS D   23  1                                  11    
HELIX   63 AG9 SER D   33  VAL D   55  1                                  23    
HELIX   64 AH1 ALA D   82  GLY D   86  5                                   5    
HELIX   65 AH2 ASP D  100  LEU D  107  1                                   8    
HELIX   66 AH3 GLY D  108  GLY D  137  1                                  30    
HELIX   67 AH4 PRO D  140  PHE D  146  1                                   7    
HELIX   68 AH5 PHE D  146  LEU D  158  1                                  13    
HELIX   69 AH6 LEU D  158  GLN D  164  1                                   7    
HELIX   70 AH7 SER D  166  ALA D  170  5                                   5    
HELIX   71 AH8 VAL D  175  HIS D  189  1                                  15    
HELIX   72 AH9 ASN D  190  LEU D  193  5                                   4    
HELIX   73 AI1 ASN D  194  ASN D  220  1                                  27    
HELIX   74 AI2 SER D  230  ALA D  234  5                                   5    
HELIX   75 AI3 SER D  245  PHE D  257  1                                  13    
HELIX   76 AI4 ASN D  263  ALA D  290  1                                  28    
HELIX   77 AI5 PHE D  298  ASP D  308  1                                  11    
HELIX   78 AI6 THR D  313  GLN D  334  1                                  22    
HELIX   79 AI7 PRO D  342  LEU D  346  5                                   5    
HELIX   80 AI8 PRO E    9  THR E   15  1                                   7    
HELIX   81 AI9 SER E   16  THR E   40  1                                  25    
HELIX   82 AJ1 GLY E   41  GLY E   48  1                                   8    
HELIX   83 AJ2 GLU E   71  GLU E   81  1                                  11    
HELIX   84 AJ3 GLN E   82  LYS E   84  5                                   3    
HELIX   85 AJ4 THR F   17  GLN F   41  1                                  25    
HELIX   86 AJ5 TRP H    6  LEU H   11  1                                   6    
HELIX   87 AJ6 ARG H   12  ASN H   15  5                                   4    
HELIX   88 AJ7 THR H   27  ASN H   50  1                                  24    
HELIX   89 AJ8 GLU I    2  SER I   25  1                                  24    
HELIX   90 AJ9 PRO J    9  GLY J   31  1                                  23    
HELIX   91 AK1 ALA J   32  ALA J   34  5                                   3    
HELIX   92 AK2 TYR K   15  ILE K   17  5                                   3    
HELIX   93 AK3 PHE K   18  ASP K   23  1                                   6    
HELIX   94 AK4 VAL K   24  PRO K   26  5                                   3    
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 GLY O   14  LYS O   18  5                                   5    
HELIX   99 AK9 LEU O  182  VAL O  187  1                                   6    
HELIX  100 AL1 GLU T    2  PHE T   23  1                                  22    
HELIX  101 AL2 ASN U   11  LEU U   17  1                                   7    
HELIX  102 AL3 GLY U   18  GLU U   23  5                                   6    
HELIX  103 AL4 ASN U   31  GLN U   37  5                                   7    
HELIX  104 AL5 PRO U   43  ASN U   52  1                                  10    
HELIX  105 AL6 SER U   57  ILE U   64  5                                   8    
HELIX  106 AL7 THR U   68  GLU U   77  1                                  10    
HELIX  107 AL8 ASN U   78  GLU U   80  5                                   3    
HELIX  108 AL9 GLU U   88  GLU U   93  1                                   6    
HELIX  109 AM1 GLY U   94  ASP U   96  5                                   3    
HELIX  110 AM2 THR V    4  VAL V    7  5                                   4    
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  LEU V   61  1                                   7    
HELIX  115 AM7 ASN V   68  MET V   76  1                                   9    
HELIX  116 AM8 PHE V  101  ASN V  106  5                                   6    
HELIX  117 AM9 THR V  108  GLU V  122  1                                  15    
HELIX  118 AN1 GLU V  122  GLY V  127  1                                   6    
HELIX  119 AN2 GLY V  133  TYR V  137  5                                   5    
HELIX  120 AN3 GLN Y   21  ARG Y   42  1                                  22    
HELIX  121 AN4 THR X    4  ASP X   35  1                                  32    
HELIX  122 AN5 LEU Z    4  TYR Z   27  1                                  24    
HELIX  123 AN6 SER Z   36  LEU Z   57  1                                  22    
HELIX  124 AN7 ASN Z   58  VAL Z   61  5                                   4    
HELIX  125 AN8 TRP R    3  VAL R    8  1                                   6    
HELIX  126 AN9 LEU R    9  LEU R   35  1                                  27    
HELIX  127 AO1 ASN a   12  THR a   22  1                                  11    
HELIX  128 AO2 VAL a   30  ALA a   55  1                                  26    
HELIX  129 AO3 SER a   70  GLY a   74  5                                   5    
HELIX  130 AO4 PRO a   95  ALA a   99  5                                   5    
HELIX  131 AO5 SER a  101  ASN a  108  1                                   8    
HELIX  132 AO6 GLY a  109  LEU a  137  1                                  29    
HELIX  133 AO7 TRP a  142  LEU a  159  1                                  18    
HELIX  134 AO8 LEU a  159  GLY a  166  1                                   8    
HELIX  135 AO9 SER a  167  GLY a  171  5                                   5    
HELIX  136 AP1 ILE a  176  ASN a  191  1                                  16    
HELIX  137 AP2 ILE a  192  MET a  194  5                                   3    
HELIX  138 AP3 HIS a  195  THR a  220  1                                  26    
HELIX  139 AP4 SER a  232  TYR a  237  5                                   6    
HELIX  140 AP5 ASN a  247  ILE a  259  1                                  13    
HELIX  141 AP6 PHE a  260  SER a  264  5                                   5    
HELIX  142 AP7 ASN a  267  ALA a  294  1                                  28    
HELIX  143 AP8 THR a  316  VAL a  330  1                                  15    
HELIX  144 AP9 PRO b    4  ILE b   13  5                                  10    
HELIX  145 AQ1 ASP b   15  ALA b   43  1                                  29    
HELIX  146 AQ2 VAL b   62  LEU b   69  1                                   8    
HELIX  147 AQ3 SER b   92  TYR b  117  1                                  26    
HELIX  148 AQ4 LEU b  120  ARG b  124  5                                   5    
HELIX  149 AQ5 ASP b  134  HIS b  157  1                                  24    
HELIX  150 AQ6 GLY b  186  ASN b  191  5                                   6    
HELIX  151 AQ7 ASN b  194  VAL b  219  1                                  26    
HELIX  152 AQ8 PRO b  222  LEU b  229  1                                   8    
HELIX  153 AQ9 ILE b  234  GLY b  259  1                                  26    
HELIX  154 AR1 PRO b  264  GLY b  269  1                                   6    
HELIX  155 AR2 THR b  271  SER b  277  1                                   7    
HELIX  156 AR3 SER b  278  SER b  294  1                                  17    
HELIX  157 AR4 THR b  297  ALA b  304  1                                   8    
HELIX  158 AR5 PRO b  306  TYR b  312  1                                   7    
HELIX  159 AR6 ASP b  313  ASN b  318  5                                   6    
HELIX  160 AR7 PRO b  329  GLY b  333  5                                   5    
HELIX  161 AR8 SER b  391  GLY b  396  1                                   6    
HELIX  162 AR9 ASP b  413  ILE b  425  1                                  13    
HELIX  163 AS1 SER b  446  PHE b  475  1                                  30    
HELIX  164 AS2 SER b  487  GLU b  492  1                                   6    
HELIX  165 AS3 ASP c   27  GLY c   32  1                                   6    
HELIX  166 AS4 ALA c   34  ILE c   43  5                                  10    
HELIX  167 AS5 LEU c   45  HIS c   74  1                                  30    
HELIX  168 AS6 PRO c   80  GLN c   84  5                                   5    
HELIX  169 AS7 LEU c   88  LEU c   95  1                                   8    
HELIX  170 AS8 GLY c  100  GLU c  104  5                                   5    
HELIX  171 AS9 THR c  108  ARG c  135  1                                  28    
HELIX  172 AT1 ASP c  153  PHE c  181  1                                  29    
HELIX  173 AT2 ASP c  205  PHE c  210  1                                   6    
HELIX  174 AT3 GLY c  222  VAL c  227  5                                   6    
HELIX  175 AT4 ASN c  229  THR c  254  1                                  26    
HELIX  176 AT5 PHE c  257  ARG c  262  1                                   6    
HELIX  177 AT6 SER c  267  ASN c  293  1                                  27    
HELIX  178 AT7 PRO c  298  GLY c  303  1                                   6    
HELIX  179 AT8 THR c  305  LYS c  323  1                                  19    
HELIX  180 AT9 ASN c  327  ALA c  331  5                                   5    
HELIX  181 AU1 GLY c  353  TRP c  359  5                                   7    
HELIX  182 AU2 LEU c  366  PRO c  368  5                                   3    
HELIX  183 AU3 ASP c  376  ASP c  383  1                                   8    
HELIX  184 AU4 GLN c  385  THR c  397  1                                  13    
HELIX  185 AU5 SER c  421  GLY c  454  1                                  34    
HELIX  186 AU6 GLU c  464  MET c  469  5                                   6    
HELIX  187 AU7 GLY d   13  LYS d   23  1                                  11    
HELIX  188 AU8 VAL d   30  VAL d   55  1                                  26    
HELIX  189 AU9 ALA d   82  GLY d   86  5                                   5    
HELIX  190 AV1 ASP d  100  LEU d  107  1                                   8    
HELIX  191 AV2 GLY d  108  GLY d  137  1                                  30    
HELIX  192 AV3 PRO d  140  PHE d  146  1                                   7    
HELIX  193 AV4 PHE d  146  LEU d  158  1                                  13    
HELIX  194 AV5 LEU d  158  GLN d  164  1                                   7    
HELIX  195 AV6 SER d  166  ALA d  170  5                                   5    
HELIX  196 AV7 VAL d  175  ASN d  190  1                                  16    
HELIX  197 AV8 ASN d  194  ASN d  220  1                                  27    
HELIX  198 AV9 SER d  245  PHE d  257  1                                  13    
HELIX  199 AW1 ASN d  263  ALA d  290  1                                  28    
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  342  LEU d  346  5                                   5    
HELIX  203 AW5 PRO e    9  ILE e   14  1                                   6    
HELIX  204 AW6 SER e   16  THR e   40  1                                  25    
HELIX  205 AW7 GLY e   41  GLY e   48  1                                   8    
HELIX  206 AW8 GLU e   71  LEU e   80  1                                  10    
HELIX  207 AW9 GLU e   81  LYS e   84  5                                   4    
HELIX  208 AX1 THR f   17  GLN f   41  1                                  25    
HELIX  209 AX2 THR h    5  LEU h   11  1                                   7    
HELIX  210 AX3 THR h   27  ASN h   50  1                                  24    
HELIX  211 AX4 GLU i    2  LEU i   24  1                                  23    
HELIX  212 AX5 PRO j    9  ALA j   32  1                                  24    
HELIX  213 AX6 TYR k   15  ILE k   17  5                                   3    
HELIX  214 AX7 PHE k   18  ASP k   23  1                                   6    
HELIX  215 AX8 VAL k   24  PRO k   26  5                                   3    
HELIX  216 AX9 VAL k   27  GLY k   44  1                                  18    
HELIX  217 AY1 ASN l   13  ASN l   37  1                                  25    
HELIX  218 AY2 LEU m    6  SER m   31  1                                  26    
HELIX  219 AY3 GLY o   14  LYS o   18  5                                   5    
HELIX  220 AY4 LEU o  182  VAL o  187  1                                   6    
HELIX  221 AY5 GLU t    2  PHE t   23  1                                  22    
HELIX  222 AY6 ASN u   11  GLY u   18  1                                   8    
HELIX  223 AY7 THR u   19  GLU u   23  5                                   5    
HELIX  224 AY8 ASN u   31  TYR u   38  5                                   8    
HELIX  225 AY9 PRO u   43  ASN u   52  1                                  10    
HELIX  226 AZ1 SER u   57  ILE u   64  5                                   8    
HELIX  227 AZ2 ARG u   70  GLU u   77  1                                   8    
HELIX  228 AZ3 ASN u   78  GLU u   80  5                                   3    
HELIX  229 AZ4 GLU u   88  GLU u   93  1                                   6    
HELIX  230 AZ5 GLY u   94  ASP u   96  5                                   3    
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  LEU v   61  1                                   7    
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  GLU v  122  1                                  15    
HELIX  238 BA4 GLU v  122  GLY v  127  1                                   6    
HELIX  239 BA5 ASP v  128  TRP v  130  5                                   3    
HELIX  240 BA6 GLY v  133  TYR v  137  5                                   5    
HELIX  241 BA7 VAL y   18  ARG y   43  1                                  26    
HELIX  242 BA8 THR x    4  ASP x   35  1                                  32    
HELIX  243 BA9 PHE z    5  ALA z   28  1                                  24    
HELIX  244 BB1 LYS z   37  LEU z   57  1                                  21    
HELIX  245 BB2 ASN z   58  VAL z   61  5                                   4    
HELIX  246 BB3 TRP r    3  ASN r   22  1                                  20    
HELIX  247 BB4 ILE r   23  LEU r   35  1                                  13    
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  GLN B 179   N  MET B 166           
SHEET    1 AA4 6 ALA B 379  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  THR B 398   N  ARG B 347           
SHEET    6 AA4 6 THR B 410  PHE B 411 -1  O  PHE B 411   N  VAL B 399           
SHEET    1 AA5 5 ALA B 379  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  ARG C 197   N  LEU C 185           
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  PRO O 245 -1  O  GLN O 236   N  THR O  48           
SHEET    4 AB210 GLU O 210  LEU O 220 -1  N  GLN O 219   O  VAL O 233           
SHEET    5 AB210 THR O 193  VAL O 204 -1  N  ALA O 202   O  ALA O 212           
SHEET    6 AB210 ASP O 141  VAL O 148 -1  N  VAL O 148   O  THR O 193           
SHEET    7 AB210 LYS O 123  SER O 128 -1  N  LYS O 123   O  ASN O 147           
SHEET    8 AB210 LEU O  93  GLU O  97 -1  N  GLU O  97   O  LEU O 125           
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  ILE O 116   N  VAL O 108           
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  SER b 177   N  VAL b 168           
SHEET    1 AB9 2 ILE b 336  TRP b 340  0                                        
SHEET    2 AB9 2 PHE b 430  ASP b 433 -1  O  GLU b 431   N  ALA b 339           
SHEET    1 AC1 6 VAL b 377  ASP b 380  0                                        
SHEET    2 AC1 6 ILE b 369  THR b 371 -1  N  LEU b 370   O  ALA b 379           
SHEET    3 AC1 6 GLU b 353  VAL b 356 -1  N  PHE b 355   O  THR b 371           
SHEET    4 AC1 6 HIS b 343  ARG b 347 -1  N  PHE b 346   O  LEU b 354           
SHEET    5 AC1 6 THR b 398  TYR b 402 -1  O  THR b 398   N  ARG b 347           
SHEET    6 AC1 6 THR b 410  PHE b 411 -1  O  PHE b 411   N  VAL b 399           
SHEET    1 AC2 2 LEU c 185  ASP c 187  0                                        
SHEET    2 AC2 2 ASP c 195  ARG c 197 -1  O  ARG c 197   N  LEU c 185           
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 ALA d  77  VAL d  78  0                                        
SHEET    2 AC5 2 PHE d 173  GLY d 174 -1  O  PHE d 173   N  VAL d  78           
SHEET    1 AC6 2 TYR o  30  PRO o  31  0                                        
SHEET    2 AC6 2 SER o 135  ILE o 136 -1  O  ILE o 136   N  TYR o  30           
SHEET    1 AC710 VAL o  66  PRO o  67  0                                        
SHEET    2 AC710 TYR o  38  VAL o  52 -1  N  VAL o  52   O  VAL o  66           
SHEET    3 AC710 GLU o 232  PRO o 245 -1  O  LYS o 234   N  LEU o  51           
SHEET    4 AC710 GLU o 210  LEU o 220 -1  N  ILE o 211   O  ALA o 241           
SHEET    5 AC710 LEU o 192  ASP o 205 -1  N  ALA o 202   O  ALA o 212           
SHEET    6 AC710 ASP o 141  PRO o 149 -1  N  PHE o 142   O  LEU o 199           
SHEET    7 AC710 LYS o 123  SER o 128 -1  N  LYS o 123   O  ASN o 147           
SHEET    8 AC710 THR o  94  ILE o 101 -1  N  GLU o  97   O  LEU o 125           
SHEET    9 AC710 LEU o  78  LEU o  85 -1  N  GLU o  84   O  VAL o  96           
SHEET   10 AC710 TYR o  38  VAL o  52 -1  N  ILE o  40   O  GLY o  83           
SHEET    1 AC8 3 LYS o  69  LEU o  70  0                                        
SHEET    2 AC8 3 PHE o 103  GLN o 109 -1  O  GLN o 109   N  LYS o  69           
SHEET    3 AC8 3 ARG o 115  THR o 121 -1  O  ILE o 116   N  VAL o 108           
SHEET    1 AC9 2 ILE u  25  ASP u  26  0                                        
SHEET    2 AC9 2 PHE u  82  THR u  83  1  O  THR u  83   N  ILE u  25           
SHEET    1 AD1 2 THR v   9  PRO v  11  0                                        
SHEET    2 AD1 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  2.03  
SSBOND   2 CYS o   19    CYS o   44                          1555   1555  2.03  
LINK         OD1 ASP A 170                CA1  OEX A 601     1555   1555  2.35  
LINK         OD2 ASP A 170                MN4  OEX A 601     1555   1555  2.05  
LINK         OE1 GLU A 189                CA1  OEX A 601     1555   1555  3.11  
LINK         OE2 GLU A 189                MN1  OEX A 601     1555   1555  1.79  
LINK         NE2 HIS A 215                FE   FE2 A 602     1555   1555  2.18  
LINK         NE2 HIS A 272                FE   FE2 A 602     1555   1555  2.20  
LINK         NE2 HIS A 332                MN1  OEX A 601     1555   1555  2.11  
LINK         OE1 GLU A 333                MN3  OEX A 601     1555   1555  2.05  
LINK         OE2 GLU A 333                MN4  OEX A 601     1555   1555  2.09  
LINK         OD1 ASP A 342                MN2  OEX A 601     1555   1555  2.17  
LINK         OD2 ASP A 342                MN1  OEX A 601     1555   1555  2.21  
LINK         O   ALA A 344                CA1  OEX A 601     1555   1555  2.42  
LINK         OXT ALA A 344                MN2  OEX A 601     1555   1555  1.89  
LINK         OD1 ASN C  39                MG   CLA C 512     1555   1555  2.22  
LINK         OE1 GLU C 354                MN2  OEX A 601     1555   1555  2.11  
LINK         OE2 GLU C 354                MN3  OEX A 601     1555   1555  2.12  
LINK         NE2 HIS D 214                FE   FE2 A 602     1555   1555  2.19  
LINK         NE2 HIS D 268                FE   FE2 A 602     1555   1555  2.20  
LINK         NE2 HIS E  23                FE   HEM E 102     1555   1555  2.18  
LINK         NE2 HIS F  24                FE   HEM E 102     1555   1555  2.18  
LINK         C   FME I   1                 N   GLU I   2     1555   1555  1.33  
LINK         C   FME M   1                 N   GLU M   2     1555   1555  1.33  
LINK         C   FME T   1                 N   GLU T   2     1555   1555  1.33  
LINK         SG  CYS V  37                 CBB HEM V 201     1555   1555  1.76  
LINK         SG  CYS V  37                 CAB HEM V 201     1555   1555  1.68  
LINK         SG  CYS V  40                 CAC HEM V 201     1555   1555  1.86  
LINK         NE2 HIS V  41                FE   HEM V 201     1555   1555  2.16  
LINK         NE2 HIS V  92                FE   HEM V 201     1555   1555  2.17  
LINK         OD1 ASP a 170                CA1  OEX a 702     1555   1555  2.35  
LINK         OD2 ASP a 170                MN4  OEX a 702     1555   1555  2.03  
LINK         OE1 GLU a 189                CA1  OEX a 702     1555   1555  3.10  
LINK         OE2 GLU a 189                MN1  OEX a 702     1555   1555  1.78  
LINK         NE2 HIS a 215                FE   FE2 a 703     1555   1555  2.17  
LINK         NE2 HIS a 272                FE   FE2 a 703     1555   1555  2.19  
LINK         NE2 HIS a 332                MN1  OEX a 702     1555   1555  2.13  
LINK         OE1 GLU a 333                MN3  OEX a 702     1555   1555  2.06  
LINK         OE2 GLU a 333                MN4  OEX a 702     1555   1555  2.09  
LINK         OD1 ASP a 342                MN2  OEX a 702     1555   1555  2.17  
LINK         OD2 ASP a 342                MN1  OEX a 702     1555   1555  2.21  
LINK         O   ALA a 344                CA1  OEX a 702     1555   1555  2.45  
LINK         OXT ALA a 344                MN2  OEX a 702     1555   1555  1.90  
LINK         OD1 ASN c  39                MG   CLA c 511     1555   1555  2.21  
LINK         OE1 GLU c 354                MN2  OEX a 702     1555   1555  2.11  
LINK         OE2 GLU c 354                MN3  OEX a 702     1555   1555  2.13  
LINK         NE2 HIS d 214                FE   FE2 a 703     1555   1555  2.16  
LINK         NE2 HIS d 268                FE   FE2 a 703     1555   1555  2.19  
LINK         NE2 HIS e  23                FE   HEM e 102     1555   1555  2.18  
LINK         NE2 HIS f  24                FE   HEM e 102     1555   1555  2.17  
LINK         C   FME i   1                 N   GLU i   2     1555   1555  1.33  
LINK         C   FME m   1                 N   GLU m   2     1555   1555  1.33  
LINK         C   FME t   1                 N   GLU t   2     1555   1555  1.33  
LINK         SG  CYS v  37                 CAB HEM v 201     1555   1555  1.68  
LINK         SG  CYS v  37                 CBB HEM v 201     1555   1555  1.71  
LINK         SG  CYS v  40                 CAC HEM v 201     1555   1555  1.85  
LINK         NE2 HIS v  41                FE   HEM v 201     1555   1555  2.16  
LINK         NE2 HIS v  92                FE   HEM v 201     1555   1555  2.16  
LINK        CA1  OEX A 601                 O   HOH A 703     1555   1555  2.60  
LINK        MN4  OEX A 601                 O   HOH A 707     1555   1555  2.09  
LINK        MN4  OEX A 601                 O   HOH A 701     1555   1555  2.19  
LINK        FE   FE2 A 602                 O1  BCT A 615     1555   1555  2.16  
LINK        FE   FE2 A 602                 O2  BCT A 615     1555   1555  2.20  
LINK        MG   CLA A 607                 O   HOH A 712     1555   1555  2.15  
LINK        MG   CLA B 602                 O   HOH B 705     1555   1555  2.15  
LINK        MG   CLA B 608                 O   HOH B 704     1555   1555  2.15  
LINK        MG   CLA B 611                 O   HOH B 702     1555   1555  2.15  
LINK        MG   CLA C 505                 O   HOH C 601     1555   1555  2.15  
LINK        MG   CLA C 508                 O   HOH C 602     1555   1555  2.15  
LINK        MG   CLA D 402                 O   HOH D 504     1555   1555  2.15  
LINK        CA1  OEX a 702                 O   HOH a 808     1555   1555  2.89  
LINK        MN4  OEX a 702                 O   HOH a 801     1555   1555  2.13  
LINK        MN4  OEX a 702                 O   HOH a 807     1555   1555  2.29  
LINK        FE   FE2 a 703                 O1  BCT a 706     1555   1555  2.18  
LINK        FE   FE2 a 703                 O2  BCT a 706     1555   1555  2.08  
LINK        MG   CLA a 708                 O   HOH a 810     1555   1555  2.15  
LINK        MG   CLA a 719                 O   HOH a 809     1555   1555  2.15  
LINK        MG   CLA b 607                 O   HOH b 709     1555   1555  2.16  
LINK        MG   CLA b 613                 O   HOH b 711     1555   1555  2.15  
LINK        MG   CLA b 616                 O   HOH b 704     1555   1555  2.15  
LINK        MG   CLA c 504                 O   HOH c 604     1555   1555  2.15  
LINK        MG   CLA c 507                 O   HOH c 606     1555   1555  2.15  
CISPEP   1 TYR U   42    PRO U   43          0        -0.93                     
CISPEP   2 ALA U   53    PRO U   54          0         1.18                     
CISPEP   3 THR V   63    PRO V   64          0        -1.55                     
CISPEP   4 THR Z    2    ILE Z    3          0        18.50                     
CISPEP   5 GLU o   54    GLU o   55          0         6.92                     
CISPEP   6 PRO o   56    LYS o   57          0        26.41                     
CISPEP   7 TYR u   42    PRO u   43          0        -2.34                     
CISPEP   8 ALA u   53    PRO u   54          0        -0.45                     
CISPEP   9 THR v   63    PRO v   64          0        -0.97                     
SITE     1 AC1 12 ASP A 170  GLU A 189  HIS A 332  GLU A 333                    
SITE     2 AC1 12 HIS A 337  ASP A 342  ALA A 344  HOH A 701                    
SITE     3 AC1 12 HOH A 703  HOH A 707  GLU C 354  ARG C 357                    
SITE     1 AC2  5 HIS A 215  HIS A 272  BCT A 615  HIS D 214                    
SITE     2 AC2  5 HIS D 268                                                     
SITE     1 AC3 10 TRP A  20  ASN A  26  ARG A  27  LEU A  28                    
SITE     2 AC3 10 ILE A  38  PHO A 608  PHE T  22  TYR b 117                    
SITE     3 AC3 10 BCR b 602  BCR b 624                                          
SITE     1 AC4  3 HIS A 332  GLU A 333  LYS D 317                               
SITE     1 AC5  3 HIS A 337  ASN A 338  PHE A 339                               
SITE     1 AC6 18 TYR A 147  PRO A 150  SER A 153  VAL A 157                    
SITE     2 AC6 18 MET A 183  PHE A 186  ILE A 192  LEU A 193                    
SITE     3 AC6 18 HIS A 198  GLY A 201  THR A 286  ALA A 287                    
SITE     4 AC6 18 ILE A 290  CLA A 607  PHO A 608  LEU D 205                    
SITE     5 AC6 18 CLA D 402  CLA D 403                                          
SITE     1 AC7 17 GLN A 199  VAL A 202  ALA A 203  PHE A 206                    
SITE     2 AC7 17 GLY A 207  LEU A 210  TRP A 278  CLA A 606                    
SITE     3 AC7 17 PL9 A 611  HOH A 712  PHE D 157  VAL D 175                    
SITE     4 AC7 17 ILE D 178  PHE D 179  LEU D 182  CLA D 403                    
SITE     5 AC7 17 LMG D 409                                                     
SITE     1 AC8 18 LEU A  41  ALA A  44  THR A  45  TYR A 126                    
SITE     2 AC8 18 GLN A 130  TYR A 147  LEU A 174  GLY A 175                    
SITE     3 AC8 18 PRO A 279  VAL A 283  LMG A 603  CLA A 606                    
SITE     4 AC8 18 ALA D 208  LEU D 209  ILE D 213  TRP D 253                    
SITE     5 AC8 18 PHE D 257  CLA D 402                                          
SITE     1 AC9 16 PRO A  39  THR A  40  PHE A  93  PRO A  95                    
SITE     2 AC9 16 ILE A  96  LEU A 114  PHE A 117  HIS A 118                    
SITE     3 AC9 16 BCR A 610  LMG C 501  VAL I   8  VAL I  12                    
SITE     4 AC9 16 THR I  13  PHE I  15  VAL I  16  SQD I 102                    
SITE     1 AD1  5 LEU A  42  ALA A  43  ALA A  54  CLA A 609                    
SITE     2 AD1  5 SQD I 102                                                     
SITE     1 AD2 13 PHE A 211  HIS A 215  LEU A 218  HIS A 252                    
SITE     2 AD2 13 PHE A 255  SER A 264  PHE A 265  LEU A 271                    
SITE     3 AD2 13 LEU A 275  CLA A 607  LEU D  45  PHO D 401                    
SITE     4 AD2 13 THR X  24                                                     
SITE     1 AD3 12 SER A 270  PHE A 274  TRP A 278  GLN C  28                    
SITE     2 AD3 12 TRP C  36  CLA C 509  PHE D 232  ARG D 233                    
SITE     3 AD3 12 LHG D 408  LEU K  33  ALA K  34  PHE K  37                    
SITE     1 AD4  5 LEU A 102  ASP A 103  GLN O 109  TRP b  75                    
SITE     2 AD4  5 GLU b  94                                                     
SITE     1 AD5  8 HIS A 215  TYR A 246  HIS A 272  FE2 A 602                    
SITE     2 AD5  8 HIS D 214  TYR D 244  LYS D 264  HIS D 268                    
SITE     1 AD6  8 PRO B 187  PHE B 190  CLA B 603  LMG B 621                    
SITE     2 AD6  8 HOH B 701  HOH B 705  PHE H  41  BCR H 102                    
SITE     1 AD7 14 GLY B 189  PHE B 190  PRO B 192  HIS B 201                    
SITE     2 AD7 14 PHE B 247  CLA B 602  CLA B 604  CLA B 610                    
SITE     3 AD7 14 PHE H  38  PHE H  41  ILE H  45  TYR H  49                    
SITE     4 AD7 14 BCR H 102  DGD H 103                                          
SITE     1 AD8 15 ARG B  68  LEU B  69  ALA B 146  CYS B 150                    
SITE     2 AD8 15 PHE B 153  HIS B 201  HIS B 202  VAL B 252                    
SITE     3 AD8 15 THR B 262  CLA B 603  CLA B 605  CLA B 606                    
SITE     4 AD8 15 CLA B 607  PHE H  38  BCR H 102                               
SITE     1 AD9 16 TRP B  33  PHE B  61  PHE B  65  ARG B  68                    
SITE     2 AD9 16 VAL B 245  ALA B 248  VAL B 252  PHE B 451                    
SITE     3 AD9 16 HIS B 455  PHE B 458  CLA B 604  CLA B 606                    
SITE     4 AD9 16 CLA B 607  CLA B 608  CLA B 614  CLA B 616                    
SITE     1 AE1 15 THR B  27  VAL B  30  ALA B  31  TRP B  33                    
SITE     2 AE1 15 ALA B  34  VAL B  62  PHE B  65  MET B  66                    
SITE     3 AE1 15 ARG B  68  HIS B 100  ALA B 205  CLA B 604                    
SITE     4 AE1 15 CLA B 605  CLA B 607  CLA B 611                               
SITE     1 AE2 16 LEU B  69  GLY B  70  PHE B  90  TRP B  91                    
SITE     2 AE2 16 VAL B  96  ALA B  99  GLY B 152  PHE B 153                    
SITE     3 AE2 16 PHE B 156  HIS B 157  PHE B 162  PRO B 164                    
SITE     4 AE2 16 CLA B 604  CLA B 605  CLA B 606  BCR B 620                    
SITE     1 AE3 14 TRP B  33  TYR B  40  GLN B  58  GLY B  59                    
SITE     2 AE3 14 PHE B  61  LEU B 324  THR B 327  GLY B 328                    
SITE     3 AE3 14 TRP B 450  CLA B 605  LHG B 625  HOH B 704                    
SITE     4 AE3 14 LMG M 101  BCR t 103                                          
SITE     1 AE4 12 THR B 236  SER B 239  ALA B 243  HIS B 466                    
SITE     2 AE4 12 THR B 473  CLA B 610  CLA B 611  SQD B 623                    
SITE     3 AE4 12 PHE D 120  ILE D 123  MET D 126  LEU D 127                    
SITE     1 AE5 15 PHE B 139  ALA B 212  PHE B 215  HIS B 216                    
SITE     2 AE5 15 PRO B 221  PRO B 222  LEU B 225  LEU B 229                    
SITE     3 AE5 15 CLA B 603  CLA B 609  CLA B 611  THR H  27                    
SITE     4 AE5 15 MET H  31  PHE H  34  BCR H 102                               
SITE     1 AE6 12 PHE B 139  HIS B 142  THR B 236  VAL B 237                    
SITE     2 AE6 12 SER B 240  SER B 241  CLA B 606  CLA B 609                    
SITE     3 AE6 12 CLA B 610  CLA B 613  CLA B 616  HOH B 702                    
SITE     1 AE7 17 TRP B   5  TYR B   6  ARG B   7  VAL B   8                    
SITE     2 AE7 17 HIS B   9  THR B  10  ILE B 242  LEU B 461                    
SITE     3 AE7 17 PHE B 462  GLY B 465  TRP B 468  HIS B 469                    
SITE     4 AE7 17 ARG B 472  CLA B 613  CLA B 614  LHG B 625                    
SITE     5 AE7 17 LHG L 101                                                     
SITE     1 AE8 12 HIS B   9  LEU B  19  HIS B  23  HIS B  26                    
SITE     2 AE8 12 THR B  27  LEU B 238  SER B 241  CLA B 611                    
SITE     3 AE8 12 CLA B 612  CLA B 614  CLA B 615  CLA B 616                    
SITE     1 AE9 10 HIS B   9  HIS B  26  VAL B  30  PHE B 462                    
SITE     2 AE9 10 CLA B 605  CLA B 612  CLA B 613  CLA B 615                    
SITE     3 AE9 10 BCR B 618  LHG B 625                                          
SITE     1 AF1 11 VAL B   8  HIS B   9  LEU B  29  CLA B 613                    
SITE     2 AF1 11 CLA B 614  BCR B 618  SQD B 626  GLN L   8                    
SITE     3 AF1 11 VAL L  10  PHE M  21  LMG M 101                               
SITE     1 AF2 11 HIS B  23  MET B 138  HIS B 142  LEU B 145                    
SITE     2 AF2 11 CLA B 605  CLA B 611  CLA B 613  CLA B 617                    
SITE     3 AF2 11 LEU H   7  LEU H  11  LEU H  14                               
SITE     1 AF3  9 ILE B  20  LEU B  24  TRP B 113  HIS B 114                    
SITE     2 AF3  9 CLA B 616  ARG H   3  THR H   5  LEU H  11                    
SITE     3 AF3  9 LMG a 701                                                     
SITE     1 AF4  9 MET B  25  LEU B  29  TRP B 115  CLA B 614                    
SITE     2 AF4  9 CLA B 615  BCR B 619  SQD B 626  LMG M 101                    
SITE     3 AF4  9 BCR t 103                                                     
SITE     1 AF5  8 LEU B  29  GLY B  32  SER B  36  ILE B 101                    
SITE     2 AF5  8 VAL B 102  GLY B 105  BCR B 618  BCR t 103                    
SITE     1 AF6  6 LEU B 106  LEU B 107  LEU B 109  ALA B 110                    
SITE     2 AF6  6 TRP B 113  CLA B 607                                          
SITE     1 AF7  7 PRO B 183  GLU B 184  TRP B 185  CLA B 602                    
SITE     2 AF7  7 THR C 200  LEU C 204  LMG C 521                               
SITE     1 AF8  4 ALA B 228  CLA B 609  TRP D  32  ARG D 134                    
SITE     1 AF9 13 SER A 232  ASN A 234  TRP B   5  TYR B   6                    
SITE     2 AF9 13 ARG B   7  PHE B 464  TRP B 468  CLA B 608                    
SITE     3 AF9 13 CLA B 612  CLA B 614  TYR D 141  PHE D 269                    
SITE     4 AF9 13 LHG L 101                                                     
SITE     1 AG1 10 ARG B  18  TRP B 115  CLA B 615  BCR B 618                    
SITE     2 AG1 10 ARG L   7  ARG l  14  TYR l  18  LEU t  16                    
SITE     3 AG1 10 PHE t  19  PHE t  23                                          
SITE     1 AG2 13 PHE A  93  TRP A  97  GLU A  98  PHE A 117                    
SITE     2 AG2 13 CLA A 609  LEU C 214  LYS C 215  SER C 216                    
SITE     3 AG2 13 PHE C 218  TRP C 223  MET C 281  CLA C 506                    
SITE     4 AG2 13 TYR I   9                                                     
SITE     1 AG3 14 LEU C  95  LEU C 168  GLY C 171  ALA C 172                    
SITE     2 AG3 14 VAL C 233  HIS C 237  ALA C 278  MET C 282                    
SITE     3 AG3 14 PHE C 289  TYR C 297  CLA C 503  CLA C 504                    
SITE     4 AG3 14 CLA C 507  BCR C 516                                          
SITE     1 AG4 17 TRP C  63  HIS C  91  LEU C 174  PHE C 182                    
SITE     2 AG4 17 LEU C 279  MET C 282  ALA C 286  VAL C 290                    
SITE     3 AG4 17 TYR C 297  LEU C 426  HIS C 430  LEU C 433                    
SITE     4 AG4 17 PHE C 437  CLA C 502  CLA C 504  CLA C 505                    
SITE     5 AG4 17 CLA C 511                                                     
SITE     1 AG5 13 ILE C  60  VAL C  61  ALA C  64  THR C  68                    
SITE     2 AG5 13 LEU C  88  HIS C  91  VAL C 114  HIS C 118                    
SITE     3 AG5 13 LEU C 279  CLA C 502  CLA C 503  CLA C 511                    
SITE     4 AG5 13 CLA C 513                                                     
SITE     1 AG6 14 TRP C  63  PHE C  70  GLN C  84  GLY C  85                    
SITE     2 AG6 14 TRP C 425  SER C 429  PHE C 436  CLA C 503                    
SITE     3 AG6 14 CLA C 511  DGD C 518  LMG C 520  HOH C 601                    
SITE     4 AG6 14 LHG D 408  PRO K  26                                          
SITE     1 AG7 11 PHE A  33  LEU A 121  TRP A 131  PHE C 264                    
SITE     2 AG7 11 SER C 273  TYR C 274  HIS C 441  ARG C 449                    
SITE     3 AG7 11 LMG C 501  CLA C 508  BCR C 516                               
SITE     1 AG8 14 LEU C 161  LEU C 165  ILE C 243  GLY C 247                    
SITE     2 AG8 14 TRP C 250  HIS C 251  THR C 255  PRO C 256                    
SITE     3 AG8 14 PHE C 257  TRP C 259  PHE C 264  CLA C 502                    
SITE     4 AG8 14 CLA C 508  BCR C 516                                          
SITE     1 AG9 13 LEU C 161  HIS C 164  LEU C 168  PHE C 264                    
SITE     2 AG9 13 TRP C 266  TYR C 271  TYR C 274  SER C 275                    
SITE     3 AG9 13 MET C 282  CLA C 506  CLA C 507  CLA C 510                    
SITE     4 AG9 13 HOH C 602                                                     
SITE     1 AH1 20 SQD A 612  TRP C  36  ALA C  37  GLY C  38                    
SITE     2 AH1 20 ASN C  39  ALA C  40  LEU C 272  PHE C 436                    
SITE     3 AH1 20 PHE C 437  GLY C 440  TRP C 443  HIS C 444                    
SITE     4 AH1 20 CLA C 510  CLA C 511  CLA C 512  DGD C 518                    
SITE     5 AH1 20 LMG C 520  LHG D 408  VAL K  30  LEU K  33                    
SITE     1 AH2 16 ASN C  39  LEU C  49  ALA C  52  HIS C  53                    
SITE     2 AH2 16 HIS C  56  TYR C 149  GLY C 268  TYR C 271                    
SITE     3 AH2 16 LEU C 272  SER C 275  LEU C 279  CLA C 508                    
SITE     4 AH2 16 CLA C 509  CLA C 511  CLA C 512  CLA C 513                    
SITE     1 AH3 13 ASN C  39  HIS C  56  LEU C  59  PHE C 436                    
SITE     2 AH3 13 CLA C 503  CLA C 504  CLA C 505  CLA C 509                    
SITE     3 AH3 13 CLA C 510  CLA C 512  LHG D 408  PRO K  29                    
SITE     4 AH3 13 LEU K  33                                                     
SITE     1 AH4 17 ASN C  25  TRP C  35  GLY C  38  ASN C  39                    
SITE     2 AH4 17 ARG C  41  LEU C  42  LEU C  45  LYS C  48                    
SITE     3 AH4 17 CLA C 509  CLA C 510  CLA C 511  TRP K  39                    
SITE     4 AH4 17 GLN K  40  BCR K 101  ASN Y  45  LEU Y  46                    
SITE     5 AH4 17 VAL Z  20                                                     
SITE     1 AH5 11 HIS C  53  ALA C  57  PHE C 147  PHE C 163                    
SITE     2 AH5 11 HIS C 164  VAL C 167  ILE C 170  CLA C 504                    
SITE     3 AH5 11 CLA C 510  CLA C 514  BCR C 515                               
SITE     1 AH6 11 LEU C  50  VAL C  54  VAL C 124  GLY C 128                    
SITE     2 AH6 11 TYR C 131  HIS C 132  LEU C 140  TYR C 143                    
SITE     3 AH6 11 PHE C 147  CLA C 513  BCR C 515                               
SITE     1 AH7  7 PHE C 112  VAL C 116  SER C 121  VAL C 124                    
SITE     2 AH7  7 CLA C 513  CLA C 514  ASN Z  58                               
SITE     1 AH8 10 ILE C 209  LEU C 213  ILE C 224  GLY C 236                    
SITE     2 AH8 10 HIS C 237  ILE C 240  PHE C 264  CLA C 502                    
SITE     3 AH8 10 CLA C 506  CLA C 507                                          
SITE     1 AH9 17 PHE A 155  ILE A 163  PRO C 217  GLY C 219                    
SITE     2 AH9 17 GLY C 220  GLU C 221  GLY C 222  TRP C 223                    
SITE     3 AH9 17 VAL C 227  CYS C 288  PHE C 292  ASN C 293                    
SITE     4 AH9 17 ASN C 294  THR C 295  ASP C 360  PHE C 361                    
SITE     5 AH9 17 ARG C 362                                                     
SITE     1 AI1 15 PHE A 197  GLU C  83  GLN C  84  GLY C  85                    
SITE     2 AI1 15 SER C 406  ASN C 418  PHE C 419  VAL C 420                    
SITE     3 AI1 15 TRP C 425  THR C 428  CLA C 505  CLA C 509                    
SITE     4 AI1 15 DGD C 519  LMG C 520  TYR J  33                               
SITE     1 AI2 15 GLN A 199  TRP A 278  ASN A 301  SER A 305                    
SITE     2 AI2 15 ASN C 405  SER C 406  ASN C 415  SER C 416                    
SITE     3 AI2 15 ASN C 418  DGD C 518  ALA J  32  TYR J  33                    
SITE     4 AI2 15 GLY J  37  SER J  38  SER J  39                               
SITE     1 AI3  9 HIS C  74  CLA C 505  CLA C 509  DGD C 518                    
SITE     2 AI3  9 ASP K  23  VAL K  27  VAL K  30  GLN Y  21                    
SITE     3 AI3  9 ILE Y  25                                                     
SITE     1 AI4  8 THR B 159  LEU B 161  PRO B 183  TRP B 185                    
SITE     2 AI4  8 LMG B 621  LEU C 204  ASP C 205  PRO C 206                    
SITE     1 AI5 16 LEU A 210  MET A 214  PL9 A 611  TRP D  48                    
SITE     2 AI5 16 ILE D 114  GLY D 121  LEU D 122  PHE D 125                    
SITE     3 AI5 16 GLN D 129  ASN D 142  PHE D 146  PHE D 173                    
SITE     4 AI5 16 GLY D 174  VAL D 175  LEU D 279  CLA D 403                    
SITE     1 AI6 17 THR A  45  MET A 172  ILE A 176  THR A 179                    
SITE     2 AI6 17 PHE A 180  MET A 183  CLA A 606  PHO A 608                    
SITE     3 AI6 17 MET D 198  VAL D 201  ALA D 202  GLY D 206                    
SITE     4 AI6 17 CLA D 403  PL9 D 406  LHG D 407  HOH D 504                    
SITE     5 AI6 17 PHE T  10                                                     
SITE     1 AI7 19 MET A 183  CLA A 606  CLA A 607  LEU D  45                    
SITE     2 AI7 19 PRO D 149  VAL D 152  VAL D 156  LEU D 182                    
SITE     3 AI7 19 PHE D 185  GLN D 186  TRP D 191  THR D 192                    
SITE     4 AI7 19 HIS D 197  GLY D 200  VAL D 201  SER D 282                    
SITE     5 AI7 19 ALA D 283  PHO D 401  CLA D 402                               
SITE     1 AI8 16 ILE D  35  PRO D  39  LEU D  43  LEU D  89                    
SITE     2 AI8 16 LEU D  90  LEU D  92  TRP D  93  THR D 112                    
SITE     3 AI8 16 PHE D 113  HIS D 117  LEU H  43  PHE X  11                    
SITE     4 AI8 16 GLY X  13  LEU X  14  LEU X  15  GLY X  17                    
SITE     1 AI9  8 TYR D  42  GLY D  46  LEU D  49  THR D  50                    
SITE     2 AI9  8 LMG D 409  THR F  30  PHE F  33  VAL J  21                    
SITE     1 AJ1 11 VAL A  49  PHE A  52  LEU D 209  HIS D 214                    
SITE     2 AJ1 11 THR D 217  TRP D 253  ALA D 260  PHE D 261                    
SITE     3 AJ1 11 LEU D 267  CLA D 402  LHG L 101                               
SITE     1 AJ2 13 ILE D 256  PHE D 257  ILE D 259  ALA D 260                    
SITE     2 AJ2 13 PHE D 261  SER D 262  ASN D 263  TRP D 266                    
SITE     3 AJ2 13 CLA D 402  ASN L  13  THR L  15  LEU L  19                    
SITE     4 AJ2 13 LHG L 101                                                     
SITE     1 AJ3 16 ARG A 140  TRP A 142  PHE A 273  SQD A 612                    
SITE     2 AJ3 16 TRP C  36  TRP C 443  ARG C 447  CLA C 505                    
SITE     3 AJ3 16 CLA C 509  CLA C 511  GLU D 219  ASN D 220                    
SITE     4 AJ3 16 ALA D 229  SER D 230  THR D 231  PHE D 232                    
SITE     1 AJ4 12 CLA A 607  TYR D  67  GLY D  70  ASN D  72                    
SITE     2 AJ4 12 PHE D  73  BCR D 405  MET F  40  GLN F  41                    
SITE     3 AJ4 12 PHE J  28  GLY J  31  ALA J  32  LEU J  36                    
SITE     1 AJ5 10 ARG D  24  ARG D  26  HOH D 503  GLU E   7                    
SITE     2 AJ5 10 PHE F  16  THR F  17  VAL F  18  LEU R  34                    
SITE     3 AJ5 10 ILE X  31  ASP X  35                                          
SITE     1 AJ6  6 TYR A 262  PHE A 265  PHE D 125  PRO E   9                    
SITE     2 AJ6  6 PHE E  10  SER E  11                                          
SITE     1 AJ7 11 ILE E  13  ARG E  18  TYR E  19  HIS E  23                    
SITE     2 AJ7 11 LEU E  30  ARG F  19  TRP F  20  HIS F  24                    
SITE     3 AJ7 11 ALA F  27  ILE F  31  ALA R  19                               
SITE     1 AJ8  8 CLA B 602  CLA B 603  CLA B 604  CLA B 610                    
SITE     2 AJ8  8 LEU H  37  PHE H  38  PHE H  41  THR X   2                    
SITE     1 AJ9 14 TYR B 193  PHE B 250  TYR B 258  TYR B 273                    
SITE     2 AJ9 14 SER B 277  PHE B 463  CLA B 603  HIS D  87                    
SITE     3 AJ9 14 LEU D 162  TYR H  49  ASN H  50  VAL H  60                    
SITE     4 AJ9 14 SER H  61  TRP H  62                                          
SITE     1 AK1  7 CLA A 609  BCR A 610  FME I   1  THR I   3                    
SITE     2 AK1  7 LEU I   4  THR I   7  PHE I  15                               
SITE     1 AK2  5 SER C 122  ALA C 123  CLA C 512  TYR K  15                    
SITE     2 AK2  5 PHE K  32                                                     
SITE     1 AK3 18 SER A 232  ASN A 234  PRO B   4  TRP B   5                    
SITE     2 AK3 18 TYR B   6  CLA B 612  LHG B 625  TRP D 266                    
SITE     3 AK3 18 PHE D 273  PL9 D 406  LHG D 407  GLU L  11                    
SITE     4 AK3 18 LEU L  12  ASN L  13  SER L  16  GLY L  20                    
SITE     5 AK3 18 PHE M  21  LMG M 101                                          
SITE     1 AK4 10 TYR B  40  THR B 327  PRO B 329  CLA B 608                    
SITE     2 AK4 10 CLA B 615  BCR B 618  LHG L 101  ASN M   4                    
SITE     3 AK4 10 ALA M  10  VAL M  17                                          
SITE     1 AK5 16 ALA V  36  CYS V  37  CYS V  40  HIS V  41                    
SITE     2 AK5 16 THR V  48  LEU V  52  ASP V  53  LEU V  54                    
SITE     3 AK5 16 THR V  58  LEU V  59  TYR V  75  MET V  76                    
SITE     4 AK5 16 TYR V  82  ILE V  88  HIS V  92  HOH V 302                    
SITE     1 AK6 13 PHE C  62  ALA J  14  THR J  15  ILE K  28                    
SITE     2 AK6 13 LEU K  31  ALA K  34  VAL K  38  ILE Y  28                    
SITE     3 AK6 13 GLY Y  29  GLY Y  32  PRO Y  33  SER Z  16                    
SITE     4 AK6 13 PHE Z  17                                                     
SITE     1 AK7  6 TRP B 113  TYR B 117  CLA B 617  LEU a  28                    
SITE     2 AK7  6 THR a  45  PHE t  22                                          
SITE     1 AK8 12 ASP a 170  GLU a 189  HIS a 332  GLU a 333                    
SITE     2 AK8 12 HIS a 337  ASP a 342  ALA a 344  HOH a 801                    
SITE     3 AK8 12 HOH a 807  HOH a 808  GLU c 354  ARG c 357                    
SITE     1 AK9  5 HIS a 215  HIS a 272  BCT a 706  HIS d 214                    
SITE     2 AK9  5 HIS d 268                                                     
SITE     1 AL1  4 ASN a 181  HIS a 332  GLU a 333  LYS d 317                    
SITE     1 AL2  4 HIS a 337  ASN a 338  PHE a 339  GLU c 354                    
SITE     1 AL3  9 HIS a 215  GLU a 244  TYR a 246  HIS a 272                    
SITE     2 AL3  9 FE2 a 703  HOH a 802  HIS d 214  TYR d 244                    
SITE     3 AL3  9 HIS d 268                                                     
SITE     1 AL4 18 TYR a 147  PRO a 150  SER a 153  VAL a 157                    
SITE     2 AL4 18 MET a 183  PHE a 186  ILE a 192  LEU a 193                    
SITE     3 AL4 18 HIS a 198  GLY a 201  PHE a 206  THR a 286                    
SITE     4 AL4 18 ILE a 290  PHO a 709  CLA a 719  LEU d 182                    
SITE     5 AL4 18 CLA d 402  LHG d 407                                          
SITE     1 AL5 15 GLN a 199  VAL a 202  ALA a 203  GLY a 207                    
SITE     2 AL5 15 LEU a 210  TRP a 278  HOH a 810  DGD c 518                    
SITE     3 AL5 15 PHE d 157  VAL d 175  ILE d 178  PHE d 179                    
SITE     4 AL5 15 LEU d 182  CLA d 402  LMG f 101                               
SITE     1 AL6 16 LEU a  41  ALA a  44  THR a  45  PHE a 119                    
SITE     2 AL6 16 TYR a 126  GLN a 130  TYR a 147  PRO a 279                    
SITE     3 AL6 16 VAL a 283  CLA a 707  CLA a 719  ALA d 208                    
SITE     4 AL6 16 LEU d 209  ILE d 213  TRP d 253  PHE d 257                    
SITE     1 AL7 21 PHE a 206  LEU a 210  MET a 214  LEU a 258                    
SITE     2 AL7 21 PL9 a 713  ALA d  41  LEU d  45  TRP d  48                    
SITE     3 AL7 21 GLY d 121  LEU d 122  PHE d 125  GLN d 129                    
SITE     4 AL7 21 ASN d 142  PHE d 146  PRO d 149  PHE d 153                    
SITE     5 AL7 21 GLY d 174  VAL d 175  PRO d 275  LEU d 279                    
SITE     6 AL7 21 CLA d 402                                                     
SITE     1 AL8 12 ILE a  36  PHE a  93  PRO a  95  ILE a  96                    
SITE     2 AL8 12 LEU a 114  HIS a 118  CLA c 505  CLA c 506                    
SITE     3 AL8 12 BCR c 515  VAL i   8  TYR i   9  VAL i  12                    
SITE     1 AL9  2 LEU a  42  ALA a  43                                          
SITE     1 AM1 11 MET a 214  HIS a 215  LEU a 218  PHE a 255                    
SITE     2 AM1 11 SER a 264  PHE a 265  LEU a 271  PHO a 710                    
SITE     3 AM1 11 VAL d  30  LHG e 101  THR x  24                               
SITE     1 AM2 14 LEU a 200  ALA a 203  ASN a 267  SER a 270                    
SITE     2 AM2 14 PHE a 274  TRP a 278  VAL a 281  LHG a 720                    
SITE     3 AM2 14 GLN c  28  TRP c  36  PHE d 232  ARG d 233                    
SITE     4 AM2 14 ALA k  34  PHE k  37                                          
SITE     1 AM3 12 PHE a  93  TRP a  97  GLU a  98  HOH a 811                    
SITE     2 AM3 12 LEU c 213  LEU c 214  LYS c 215  SER c 216                    
SITE     3 AM3 12 TRP c 223  CLA c 505  LYS i   5  TYR i   9                    
SITE     1 AM4 13 MET a 172  ILE a 176  THR a 179  PHE a 180                    
SITE     2 AM4 13 MET a 183  CLA a 707  PHO a 709  HOH a 809                    
SITE     3 AM4 13 MET d 198  VAL d 201  ALA d 202  CLA d 402                    
SITE     4 AM4 13 PL9 d 405                                                     
SITE     1 AM5 12 ARG a 140  TRP a 142  PHE a 273  SQD a 714                    
SITE     2 AM5 12 TRP c  36  TRP c 443  ARG c 447  CLA c 508                    
SITE     3 AM5 12 GLU d 219  ALA d 229  THR d 231  PHE d 232                    
SITE     1 AM6  8 TYR L  18  TYR M  26  PHE T  23  ARG b  18                    
SITE     2 AM6  8 SER b 104  CLA b 620  ASN l   4  ARG l   7                    
SITE     1 AM7 10 LMG A 603  PHE T   8  ALA T  15  PHE T  17                    
SITE     2 AM7 10 PHE T  18  TRP b  33  MET b  37  CLA b 613                    
SITE     3 AM7 10 BCR b 623  BCR b 624                                          
SITE     1 AM8  7 PRO b 187  PHE b 190  LMG b 627  HOH b 709                    
SITE     2 AM8  7 PHE c 181  LEU h  55  BCR h 101                               
SITE     1 AM9 13 TRP b 185  GLY b 189  PHE b 190  PRO b 192                    
SITE     2 AM9 13 GLY b 197  ALA b 200  HIS b 201  ALA b 204                    
SITE     3 AM9 13 PHE b 247  CLA b 609  LEU h  46  TYR h  49                    
SITE     4 AM9 13 DGD h 102                                                     
SITE     1 AN1 17 ARG b  68  LEU b  69  ALA b 146  LEU b 149                    
SITE     2 AN1 17 CYS b 150  PHE b 153  HIS b 201  HIS b 202                    
SITE     3 AN1 17 ALA b 248  VAL b 252  THR b 262  CLA b 608                    
SITE     4 AN1 17 CLA b 610  CLA b 611  CLA b 612  PHE h  38                    
SITE     5 AN1 17 BCR h 101                                                     
SITE     1 AN2 18 TRP b  33  PHE b  61  PHE b  65  ARG b  68                    
SITE     2 AN2 18 LEU b 149  VAL b 245  ALA b 249  VAL b 252                    
SITE     3 AN2 18 PHE b 451  HIS b 455  PHE b 458  PHE b 462                    
SITE     4 AN2 18 CLA b 609  CLA b 611  CLA b 612  CLA b 613                    
SITE     5 AN2 18 CLA b 618  CLA b 619                                          
SITE     1 AN3 14 THR b  27  VAL b  30  ALA b  34  VAL b  62                    
SITE     2 AN3 14 MET b  66  ARG b  68  VAL b  96  HIS b 100                    
SITE     3 AN3 14 LEU b 103  LEU b 143  CLA b 609  CLA b 610                    
SITE     4 AN3 14 CLA b 612  CLA b 616                                          
SITE     1 AN4 18 LEU b  69  GLY b  70  VAL b  71  TRP b  91                    
SITE     2 AN4 18 VAL b  96  ALA b  99  VAL b 102  LEU b 149                    
SITE     3 AN4 18 GLY b 152  PHE b 153  PHE b 156  HIS b 157                    
SITE     4 AN4 18 PHE b 162  PRO b 164  CLA b 609  CLA b 610                    
SITE     5 AN4 18 CLA b 611  BCR b 625                                          
SITE     1 AN5 18 TRP b  33  TYR b  40  GLN b  58  GLY b  59                    
SITE     2 AN5 18 PHE b  61  LEU b 324  THR b 327  GLY b 328                    
SITE     3 AN5 18 TRP b 450  BCR b 602  CLA b 610  CLA b 619                    
SITE     4 AN5 18 BCR b 624  LMG b 626  HOH b 711  LHG d 406                    
SITE     5 AN5 18 LEU l  27  PHE l  31                                          
SITE     1 AN6 14 THR b 236  SER b 239  ALA b 243  PHE b 247                    
SITE     2 AN6 14 PHE b 463  HIS b 466  ILE b 467  LEU b 474                    
SITE     3 AN6 14 CLA b 615  CLA b 616  LMG b 628  PHE d 120                    
SITE     4 AN6 14 MET d 126  LEU h  43                                          
SITE     1 AN7 14 PHE b 139  VAL b 208  ALA b 212  PHE b 215                    
SITE     2 AN7 14 HIS b 216  VAL b 219  PRO b 221  PRO b 222                    
SITE     3 AN7 14 LEU b 229  CLA b 614  CLA b 616  THR h  27                    
SITE     4 AN7 14 MET h  31  BCR h 101                                          
SITE     1 AN8 12 PHE b 139  HIS b 142  THR b 236  VAL b 237                    
SITE     2 AN8 12 SER b 240  SER b 241  CLA b 611  CLA b 614                    
SITE     3 AN8 12 CLA b 615  CLA b 618  CLA b 621  HOH b 704                    
SITE     1 AN9 18 TYR b   6  ARG b   7  VAL b   8  HIS b   9                    
SITE     2 AN9 18 THR b  10  LEU b 238  ILE b 242  PHE b 458                    
SITE     3 AN9 18 LEU b 461  PHE b 462  GLY b 465  TRP b 468                    
SITE     4 AN9 18 HIS b 469  CLA b 618  CLA b 619  CLA b 620                    
SITE     5 AN9 18 LHG b 629  LHG d 406                                          
SITE     1 AO1 14 HIS b   9  ALA b  22  HIS b  23  HIS b  26                    
SITE     2 AO1 14 THR b  27  VAL b 237  LEU b 238  SER b 241                    
SITE     3 AO1 14 CLA b 610  CLA b 616  CLA b 617  CLA b 619                    
SITE     4 AO1 14 CLA b 620  CLA b 621                                          
SITE     1 AO2 10 HIS b   9  HIS b  26  VAL b  30  PHE b 462                    
SITE     2 AO2 10 CLA b 610  CLA b 613  CLA b 617  CLA b 618                    
SITE     3 AO2 10 CLA b 620  BCR b 623                                          
SITE     1 AO3  9 VAL b   8  HIS b   9  SQD b 601  CLA b 617                    
SITE     2 AO3  9 CLA b 618  CLA b 619  BCR b 623  VAL l  10                    
SITE     3 AO3  9 PHE m  21                                                     
SITE     1 AO4 10 ILE b  20  HIS b  23  MET b 138  HIS b 142                    
SITE     2 AO4 10 LEU b 145  CLA b 616  CLA b 618  CLA b 622                    
SITE     3 AO4 10 LEU h  14  ASN h  15                                          
SITE     1 AO5  7 ILE b  20  LEU b  24  TRP b 113  HIS b 114                    
SITE     2 AO5  7 CLA b 621  BCR b 625  THR h   5                               
SITE     1 AO6  7 MET b  25  TRP b 115  BCR b 602  CLA b 619                    
SITE     2 AO6  7 CLA b 620  BCR b 624  LEU m  13                               
SITE     1 AO7  9 LMG A 603  LEU b  29  GLY b  32  TRP b  33                    
SITE     2 AO7  9 VAL b 102  GLY b 105  BCR b 602  CLA b 613                    
SITE     3 AO7  9 BCR b 623                                                     
SITE     1 AO8  6 PHE T  18  LEU b 109  CYS b 112  TRP b 113                    
SITE     2 AO8  6 CLA b 612  CLA b 622                                          
SITE     1 AO9  4 GLY b 328  PRO b 329  CLA b 613  ASN m   4                    
SITE     1 AP1  8 PRO b 183  GLU b 184  TRP b 185  CLA b 607                    
SITE     2 AP1  8 ILE c 170  LEU c 173  ASN c 201  PRO c 202                    
SITE     1 AP2  2 CLA b 614  LMG d 408                                          
SITE     1 AP3 16 SER a 232  ASN a 234  PRO b   4  TRP b   5                    
SITE     2 AP3 16 TYR b   6  CLA b 617  TRP d 266  PHE d 273                    
SITE     3 AP3 16 PL9 d 405  LHG d 406  LHG d 407  GLU l  11                    
SITE     4 AP3 16 LEU l  12  ASN l  13  SER l  16  PHE m  21                    
SITE     1 AP4 16 LEU c  95  LEU c 168  GLY c 171  ALA c 172                    
SITE     2 AP4 16 LEU c 175  ILE c 224  VAL c 233  HIS c 237                    
SITE     3 AP4 16 MET c 282  ILE c 285  TYR c 297  CLA c 502                    
SITE     4 AP4 16 CLA c 503  CLA c 506  CLA c 507  BCR c 515                    
SITE     1 AP5 15 TRP c  63  HIS c  91  LEU c 174  LEU c 279                    
SITE     2 AP5 15 MET c 282  ALA c 286  TYR c 297  HIS c 430                    
SITE     3 AP5 15 LEU c 433  PHE c 437  CLA c 501  CLA c 503                    
SITE     4 AP5 15 CLA c 504  CLA c 510  CLA c 512                               
SITE     1 AP6 12 ILE c  60  VAL c  61  ALA c  64  THR c  68                    
SITE     2 AP6 12 LEU c  88  HIS c  91  ILE c  92  VAL c 114                    
SITE     3 AP6 12 HIS c 118  CLA c 501  CLA c 502  CLA c 507                    
SITE     1 AP7 13 TRP c  63  PHE c  70  GLN c  84  GLY c  85                    
SITE     2 AP7 13 TRP c 425  SER c 429  CLA c 502  CLA c 510                    
SITE     3 AP7 13 DGD c 517  LMG c 519  HOH c 604  PRO k  26                    
SITE     4 AP7 13 VAL k  30                                                     
SITE     1 AP8 16 LEU a 121  TRP a 131  CLA a 711  LMG a 715                    
SITE     2 AP8 16 PHE c 264  SER c 273  TYR c 274  GLY c 277                    
SITE     3 AP8 16 HIS c 441  LEU c 442  ALA c 445  ARG c 449                    
SITE     4 AP8 16 CLA c 507  BCR c 515  DGD c 516  VAL i  16                    
SITE     1 AP9 15 CLA a 711  ILE c 243  GLY c 247  TRP c 250                    
SITE     2 AP9 15 HIS c 251  THR c 255  PRO c 256  PHE c 257                    
SITE     3 AP9 15 TRP c 259  ALA c 260  PHE c 264  CLA c 501                    
SITE     4 AP9 15 CLA c 507  BCR c 515  DGD c 516                               
SITE     1 AQ1 16 MET c 157  LEU c 161  HIS c 164  LEU c 168                    
SITE     2 AQ1 16 TRP c 266  TYR c 271  TYR c 274  SER c 275                    
SITE     3 AQ1 16 MET c 282  CLA c 501  CLA c 503  CLA c 505                    
SITE     4 AQ1 16 CLA c 506  CLA c 509  BCR c 515  HOH c 606                    
SITE     1 AQ2 16 LHG a 720  PHE c  33  TRP c  36  ALA c  37                    
SITE     2 AQ2 16 GLY c  38  ASN c  39  LEU c 276  PHE c 436                    
SITE     3 AQ2 16 PHE c 437  GLY c 440  TRP c 443  HIS c 444                    
SITE     4 AQ2 16 CLA c 509  CLA c 510  DGD c 517  LMG c 519                    
SITE     1 AQ3 15 ASN c  39  LEU c  49  ALA c  52  HIS c  53                    
SITE     2 AQ3 15 HIS c  56  GLY c 268  TYR c 271  LEU c 272                    
SITE     3 AQ3 15 SER c 275  LEU c 279  CLA c 507  CLA c 508                    
SITE     4 AQ3 15 CLA c 510  CLA c 511  CLA c 512                               
SITE     1 AQ4 12 ASN c  39  HIS c  56  LEU c  59  ILE c  60                    
SITE     2 AQ4 12 PHE c 436  PHE c 437  CLA c 502  CLA c 504                    
SITE     3 AQ4 12 CLA c 508  CLA c 509  PRO k  29  LEU k  33                    
SITE     1 AQ5 23 ASN c  25  ARG c  26  TRP c  35  GLY c  38                    
SITE     2 AQ5 23 ASN c  39  ARG c  41  LEU c  42  LEU c  45                    
SITE     3 AQ5 23 LYS c  48  ALA c  52  GLY c 126  PHE c 127                    
SITE     4 AQ5 23 VAL c 130  CLA c 509  PHE k  32  TRP k  39                    
SITE     5 AQ5 23 GLN k  40  BCR k 102  ASN y  45  LEU y  46                    
SITE     6 AQ5 23 VAL z  20  VAL z  23  ALA z  28                               
SITE     1 AQ6 12 HIS c  53  VAL c  54  ALA c  57  LEU c 125                    
SITE     2 AQ6 12 PHE c 147  PHE c 163  HIS c 164  ILE c 170                    
SITE     3 AQ6 12 CLA c 502  CLA c 509  CLA c 513  BCR c 514                    
SITE     1 AQ7  8 LEU c  50  VAL c 124  GLY c 128  TYR c 131                    
SITE     2 AQ7  8 HIS c 132  TYR c 143  CLA c 512  BCR c 514                    
SITE     1 AQ8  8 PHE c 112  SER c 121  VAL c 124  CLA c 512                    
SITE     2 AQ8  8 CLA c 513  TYR k  15  VAL z  51  GLY z  55                    
SITE     1 AQ9 11 CLA a 711  ILE c 209  LEU c 213  GLY c 236                    
SITE     2 AQ9 11 HIS c 237  PHE c 264  CLA c 501  CLA c 505                    
SITE     3 AQ9 11 CLA c 506  CLA c 507  PHE i  23                               
SITE     1 AR1 19 PHE a 155  ILE a 163  PRO c 217  GLY c 219                    
SITE     2 AR1 19 GLY c 220  GLY c 222  TRP c 223  VAL c 225                    
SITE     3 AR1 19 VAL c 227  CYS c 288  PHE c 292  ASN c 293                    
SITE     4 AR1 19 ASN c 294  THR c 295  ASP c 360  PHE c 361                    
SITE     5 AR1 19 ARG c 362  CLA c 505  CLA c 506                               
SITE     1 AR2 16 PHE a 197  GLU c  83  GLN c  84  GLY c  85                    
SITE     2 AR2 16 SER c 406  ASN c 418  PHE c 419  VAL c 420                    
SITE     3 AR2 16 TRP c 425  THR c 428  CLA c 504  CLA c 508                    
SITE     4 AR2 16 DGD c 518  LMG c 519  HOH c 602  TYR j  33                    
SITE     1 AR3 20 GLN a 199  LEU a 200  TRP a 278  PHE a 300                    
SITE     2 AR3 20 ASN a 301  SER a 305  CLA a 708  ASN c 405                    
SITE     3 AR3 20 SER c 406  VAL c 407  ASN c 415  SER c 416                    
SITE     4 AR3 20 ASN c 418  DGD c 517  ASN d  72  ALA j  32                    
SITE     5 AR3 20 TYR j  33  GLY j  37  SER j  38  GLN v  34                    
SITE     1 AR4  6 HIS c  74  CLA c 504  CLA c 508  DGD c 517                    
SITE     2 AR4  6 ASP k  23  GLN y  21                                          
SITE     1 AR5  8 PHE b 151  THR b 159  LEU b 161  ALA b 182                    
SITE     2 AR5  8 PRO b 183  ASP c 205  PRO c 206  TRP c 239                    
SITE     1 AR6 20 MET a 183  CLA a 707  CLA a 708  PHO a 710                    
SITE     2 AR6 20 CLA a 719  LEU d  45  PRO d 149  VAL d 152                    
SITE     3 AR6 20 VAL d 156  PHE d 181  LEU d 182  PHE d 185                    
SITE     4 AR6 20 GLN d 186  TRP d 191  THR d 192  HIS d 197                    
SITE     5 AR6 20 GLY d 200  VAL d 201  SER d 282  VAL d 286                    
SITE     1 AR7 16 ILE d  35  CYS d  40  LEU d  43  LEU d  89                    
SITE     2 AR7 16 LEU d  90  LEU d  91  LEU d  92  TRP d  93                    
SITE     3 AR7 16 THR d 112  PHE d 113  LEU d 116  HIS d 117                    
SITE     4 AR7 16 GLY x  13  LEU x  15  GLY x  17  ALA x  18                    
SITE     1 AR8  9 TYR d  42  GLY d  46  GLY d  47  LEU d  49                    
SITE     2 AR8  9 THR d  50  THR f  30  PHE f  33  LEU f  34                    
SITE     3 AR8  9 LMG f 101                                                     
SITE     1 AR9 12 PHE a  52  CLA a 719  LHG b 629  MET d 199                    
SITE     2 AR9 12 HIS d 214  THR d 217  TRP d 253  ALA d 260                    
SITE     3 AR9 12 PHE d 261  LEU l  23  VAL l  26  PHE t  10                    
SITE     1 AS1 11 SER a 232  ASN a 234  TYR b   6  ARG b   7                    
SITE     2 AS1 11 PHE b 464  TRP b 468  CLA b 613  CLA b 617                    
SITE     3 AS1 11 LHG b 629  TYR d 141  PHE d 269                               
SITE     1 AS2 14 CLA a 707  LHG b 629  PHE d 257  ILE d 259                    
SITE     2 AS2 14 ALA d 260  PHE d 261  SER d 262  ASN d 263                    
SITE     3 AS2 14 TRP d 266  ASN l  13  THR l  15  TYR l  18                    
SITE     4 AS2 14 LEU l  19  PHE t  17                                          
SITE     1 AS3  5 ARG b 224  LMG b 628  ASP d  19  LYS d  23                    
SITE     2 AS3  5 ARG d 134                                                     
SITE     1 AS4  7 LEU a 258  PHE a 260  TYR a 262  PL9 a 713                    
SITE     2 AS4  7 PRO e   9  PHE e  10  SER e  11                               
SITE     1 AS5 13 PHE e  10  ARG e  18  TYR e  19  HIS e  23                    
SITE     2 AS5 13 THR e  26  LEU e  30  ILE f  15  ARG f  19                    
SITE     3 AS5 13 TRP f  20  HIS f  24  ALA f  27  ALA r  19                    
SITE     4 AS5 13 ILE r  23                                                     
SITE     1 AS6 14 CLA a 708  TYR d  67  CYS d  71  ASN d  72                    
SITE     2 AS6 14 PHE d  73  BCR d 404  LEU f  26  THR f  30                    
SITE     3 AS6 14 ILE f  37  MET f  40  GLN f  41  PHE j  28                    
SITE     4 AS6 14 GLY j  31  ALA j  32                                          
SITE     1 AS7  8 ARG d  24  ARG d  26  PHE f  16  THR f  17                    
SITE     2 AS7  8 VAL f  18  GLN r  30  ILE x  31  ASP x  35                    
SITE     1 AS8  6 CLA b 607  CLA b 609  CLA b 615  LEU h  37                    
SITE     2 AS8  6 PHE h  38  ILE h  44                                          
SITE     1 AS9 15 TYR b 193  PHE b 250  GLY b 254  TYR b 258                    
SITE     2 AS9 15 TYR b 273  GLN b 274  TYR b 279  CLA b 608                    
SITE     3 AS9 15 HIS d  87  GLY d 163  TYR h  49  ASN h  50                    
SITE     4 AS9 15 VAL h  60  SER h  61  TRP h  62                               
SITE     1 AT1 16 PHE c  62  ALA j  14  THR j  15  GLY j  18                    
SITE     2 AT1 16 MET j  19  LEU k  25  ILE k  28  LEU k  31                    
SITE     3 AT1 16 ALA k  34  VAL k  38  BCR k 102  ILE y  28                    
SITE     4 AT1 16 GLY y  29  GLY y  32  SER z  16  PHE z  17                    
SITE     1 AT2  7 LEU c  59  SER c 122  CLA c 511  LEU k  21                    
SITE     2 AT2  7 PHE k  32  BCR k 101  SER z  16                               
SITE     1 AT3 10 TRP B  33  SER B  36  CLA B 608  BCR B 618                    
SITE     2 AT3 10 BCR B 619  PHE t   8  ALA t  11  ALA t  15                    
SITE     3 AT3 10 PHE t  18  PHE t  22                                          
SITE     1 AT4 16 PHE v  33  ALA v  36  ALA v  38  SER v  39                    
SITE     2 AT4 16 CYS v  40  HIS v  41  THR v  48  LEU v  52                    
SITE     3 AT4 16 ASP v  53  THR v  58  LEU v  59  TYR v  75                    
SITE     4 AT4 16 MET v  76  TYR v  82  HIS v  92  PRO v  93                    
SITE     1 AT5 19 ALA v  36  CYS v  37  ALA v  38  SER v  39                    
SITE     2 AT5 19 HIS v  41  VAL v  42  ILE v  45  THR v  46                    
SITE     3 AT5 19 LYS v  47  THR v  48  LEU v  52  ASP v  53                    
SITE     4 AT5 19 THR v  58  LEU v  59  TYR v  75  MET v  76                    
SITE     5 AT5 19 TYR v  82  HIS v  92  PRO v  93                               
SITE     1 AT6 16 PHE v  33  ALA v  36  ALA v  38  SER v  39                    
SITE     2 AT6 16 CYS v  40  HIS v  41  THR v  48  LEU v  52                    
SITE     3 AT6 16 ASP v  53  THR v  58  LEU v  59  TYR v  75                    
SITE     4 AT6 16 MET v  76  TYR v  82  HIS v  92  PRO v  93                    
CRYST1  117.911  224.268  330.996  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      0.008481  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004459  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003021        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system