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Database: PDB
Entry: 6FOS
LinkDB: 6FOS
Original site: 6FOS 
HEADER    PHOTOSYNTHESIS                          08-FEB-18   6FOS              
TITLE     CYANIDIOSCHYZON MEROLAE PHOTOSYSTEM I                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIMILAR TO CHLOROPHYLL A/B-BINDING PROTEIN, CP24;          
COMPND   3 CHAIN: 2, 3;                                                         
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: SIMILAR TO LIGHT HARVESTING PROTEIN;                       
COMPND   6 CHAIN: 4;                                                            
COMPND   7 MOL_ID: 3;                                                           
COMPND   8 MOLECULE: PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A1;            
COMPND   9 CHAIN: A;                                                            
COMPND  10 SYNONYM: PSI-A,PSAA;                                                 
COMPND  11 EC: 1.97.1.12;                                                       
COMPND  12 MOL_ID: 4;                                                           
COMPND  13 MOLECULE: PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A2;            
COMPND  14 CHAIN: B;                                                            
COMPND  15 SYNONYM: PSI-B,PSAB;                                                 
COMPND  16 EC: 1.97.1.12;                                                       
COMPND  17 MOL_ID: 5;                                                           
COMPND  18 MOLECULE: PHOTOSYSTEM I IRON-SULFUR CENTER;                          
COMPND  19 CHAIN: C;                                                            
COMPND  20 SYNONYM: 9 KDA POLYPEPTIDE,PSI-C,PHOTOSYSTEM I SUBUNIT VII,PSAC;     
COMPND  21 EC: 1.97.1.12;                                                       
COMPND  22 MOL_ID: 6;                                                           
COMPND  23 MOLECULE: PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A2;            
COMPND  24 CHAIN: D;                                                            
COMPND  25 MOL_ID: 7;                                                           
COMPND  26 MOLECULE: PHOTOSYSTEM I IRON-SULFUR CENTER SUBUNIT VII;              
COMPND  27 CHAIN: E;                                                            
COMPND  28 MOL_ID: 8;                                                           
COMPND  29 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT II;                  
COMPND  30 CHAIN: F;                                                            
COMPND  31 MOL_ID: 9;                                                           
COMPND  32 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT VIII;                
COMPND  33 CHAIN: I;                                                            
COMPND  34 MOL_ID: 10;                                                          
COMPND  35 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT IX;                  
COMPND  36 CHAIN: J;                                                            
COMPND  37 SYNONYM: PSI-J;                                                      
COMPND  38 MOL_ID: 11;                                                          
COMPND  39 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT X;                   
COMPND  40 CHAIN: K;                                                            
COMPND  41 MOL_ID: 12;                                                          
COMPND  42 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT XI;                  
COMPND  43 CHAIN: L;                                                            
COMPND  44 SYNONYM: PSI SUBUNIT V,PSI-L;                                        
COMPND  45 MOL_ID: 13;                                                          
COMPND  46 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT XII;                 
COMPND  47 CHAIN: M;                                                            
COMPND  48 SYNONYM: PSI-M;                                                      
COMPND  49 MOL_ID: 14;                                                          
COMPND  50 MOLECULE: PSAM;                                                      
COMPND  51 CHAIN: O                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CYANIDIOSCHYZON MEROLAE (STRAIN 10D);           
SOURCE   3 ORGANISM_COMMON: RED ALGA;                                           
SOURCE   4 ORGANISM_TAXID: 280699;                                              
SOURCE   5 STRAIN: 10D;                                                         
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: CYANIDIOSCHYZON MEROLAE (STRAIN 10D);           
SOURCE   8 ORGANISM_COMMON: RED ALGA;                                           
SOURCE   9 ORGANISM_TAXID: 280699;                                              
SOURCE  10 STRAIN: 10D;                                                         
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: CYANIDIOSCHYZON MEROLAE (STRAIN 10D);           
SOURCE  13 ORGANISM_COMMON: RED ALGA;                                           
SOURCE  14 ORGANISM_TAXID: 280699;                                              
SOURCE  15 STRAIN: 10D;                                                         
SOURCE  16 MOL_ID: 4;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: CYANIDIOSCHYZON MEROLAE (STRAIN 10D);           
SOURCE  18 ORGANISM_COMMON: RED ALGA;                                           
SOURCE  19 ORGANISM_TAXID: 280699;                                              
SOURCE  20 STRAIN: 10D;                                                         
SOURCE  21 MOL_ID: 5;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: CYANIDIOSCHYZON MEROLAE (STRAIN 10D);           
SOURCE  23 ORGANISM_COMMON: RED ALGA;                                           
SOURCE  24 ORGANISM_TAXID: 280699;                                              
SOURCE  25 STRAIN: 10D;                                                         
SOURCE  26 MOL_ID: 6;                                                           
SOURCE  27 ORGANISM_SCIENTIFIC: CYANIDIOSCHYZON MEROLAE (STRAIN 10D);           
SOURCE  28 ORGANISM_COMMON: RED ALGA;                                           
SOURCE  29 ORGANISM_TAXID: 280699;                                              
SOURCE  30 STRAIN: 10D;                                                         
SOURCE  31 MOL_ID: 7;                                                           
SOURCE  32 ORGANISM_SCIENTIFIC: CYANIDIOSCHYZON MEROLAE (STRAIN 10D);           
SOURCE  33 ORGANISM_COMMON: RED ALGA;                                           
SOURCE  34 ORGANISM_TAXID: 280699;                                              
SOURCE  35 STRAIN: 10D;                                                         
SOURCE  36 MOL_ID: 8;                                                           
SOURCE  37 ORGANISM_SCIENTIFIC: CYANIDIOSCHYZON MEROLAE (STRAIN 10D);           
SOURCE  38 ORGANISM_COMMON: RED ALGA;                                           
SOURCE  39 ORGANISM_TAXID: 280699;                                              
SOURCE  40 STRAIN: 10D;                                                         
SOURCE  41 MOL_ID: 9;                                                           
SOURCE  42 ORGANISM_SCIENTIFIC: CYANIDIOSCHYZON MEROLAE (STRAIN 10D);           
SOURCE  43 ORGANISM_COMMON: RED ALGA;                                           
SOURCE  44 ORGANISM_TAXID: 280699;                                              
SOURCE  45 STRAIN: 10D;                                                         
SOURCE  46 MOL_ID: 10;                                                          
SOURCE  47 ORGANISM_SCIENTIFIC: CYANIDIOSCHYZON MEROLAE (STRAIN 10D);           
SOURCE  48 ORGANISM_COMMON: RED ALGA;                                           
SOURCE  49 ORGANISM_TAXID: 280699;                                              
SOURCE  50 STRAIN: 10D;                                                         
SOURCE  51 MOL_ID: 11;                                                          
SOURCE  52 ORGANISM_SCIENTIFIC: CYANIDIOSCHYZON MEROLAE (STRAIN 10D);           
SOURCE  53 ORGANISM_COMMON: RED ALGA;                                           
SOURCE  54 ORGANISM_TAXID: 280699;                                              
SOURCE  55 STRAIN: 10D;                                                         
SOURCE  56 MOL_ID: 12;                                                          
SOURCE  57 ORGANISM_SCIENTIFIC: CYANIDIOSCHYZON MEROLAE (STRAIN 10D);           
SOURCE  58 ORGANISM_COMMON: RED ALGA;                                           
SOURCE  59 ORGANISM_TAXID: 280699;                                              
SOURCE  60 STRAIN: 10D;                                                         
SOURCE  61 MOL_ID: 13;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: CYANIDIOSCHYZON MEROLAE (STRAIN 10D);           
SOURCE  63 ORGANISM_COMMON: RED ALGA;                                           
SOURCE  64 ORGANISM_TAXID: 280699;                                              
SOURCE  65 STRAIN: 10D;                                                         
SOURCE  66 MOL_ID: 14;                                                          
SOURCE  67 ORGANISM_SCIENTIFIC: CYANIDIOSCHYZON MEROLAE (STRAIN 10D);           
SOURCE  68 ORGANISM_COMMON: RED ALGA;                                           
SOURCE  69 ORGANISM_TAXID: 280699;                                              
SOURCE  70 STRAIN: 10D                                                          
KEYWDS    MEMBRANE PROTEIN, PHOTOSYNTHETIC COMPLEX, REACTION CENTER,            
KEYWDS   2 PHOTOSYSTEM, PHOTOSYNTHESIS                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.NELSON,M.HIPPLER,M.ANTOSHVILI,I.CASPY                               
REVDAT   2   13-FEB-19 6FOS    1       JRNL                                     
REVDAT   1   11-APR-18 6FOS    0                                                
JRNL        AUTH   M.ANTOSHVILI,I.CASPY,M.HIPPLER,N.NELSON                      
JRNL        TITL   STRUCTURE AND FUNCTION OF PHOTOSYSTEM I IN CYANIDIOSCHYZON   
JRNL        TITL 2 MEROLAE.                                                     
JRNL        REF    PHOTOSYN. RES.                V. 139   499 2019              
JRNL        REFN                   ISSN 1573-5079                               
JRNL        PMID   29582227                                                     
JRNL        DOI    10.1007/S11120-018-0501-4                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (DEV_3042: ???)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 4.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.53                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 80.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 41925                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.379                           
REMARK   3   R VALUE            (WORKING SET) : 0.378                           
REMARK   3   FREE R VALUE                     : 0.430                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 842                             
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 48.5339 -  7.2617    1.00     8680   192  0.3704 0.4356        
REMARK   3     2  7.2617 -  5.7669    1.00     8475   181  0.4452 0.4843        
REMARK   3     3  5.7669 -  5.0388    1.00     8425   178  0.3686 0.3824        
REMARK   3     4  5.0388 -  4.5784    0.95     7993   156  0.3359 0.3724        
REMARK   3     5  4.5784 -  4.2505    0.56     4717    83  0.3528 0.4347        
REMARK   3     6  4.2505 -  4.0000    0.33     2793    52  0.4163 0.5679        
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)     : 0.930            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 55.960           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005          27219                                  
REMARK   3   ANGLE     :  1.829          38593                                  
REMARK   3   CHIRALITY :  0.041           3358                                  
REMARK   3   PLANARITY :  0.008           4720                                  
REMARK   3   DIHEDRAL  : 15.086          14575                                  
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 6FOS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-FEB-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200008715.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-JUL-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.999                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS, XSCALE                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41951                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 80.9                               
REMARK 200  DATA REDUNDANCY                : 12.00                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.99                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: MOLREP, PHASER                                        
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 75.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 80MM MGCL2 , 50MM CITRIC ACID, 4-7.5%    
REMARK 280  PEG 4000, 0.025% ALPHA-DM, PH 4.8-5.0 OR 80MM MGCL2 , 50MM          
REMARK 280  CACODYLATE, 4-7.5% PEG 4000, 0.025% ALPHA-DM, PH 5-6, VAPOR         
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      174.79000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      174.79000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       81.56500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      106.76000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       81.56500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      106.76000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      174.79000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       81.56500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      106.76000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      174.79000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       81.56500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      106.76000            
REMARK 290   SMTRY3   8  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: PENTADECAMERIC                    
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTADECAMERIC             
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 37180 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 160290 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -280.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 2, 3, 4, A, B, C, D, E, F, I,         
REMARK 350                    AND CHAINS: J, K, L, M, O                         
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 2    25                                                      
REMARK 465     ALA 2    26                                                      
REMARK 465     PHE 2    27                                                      
REMARK 465     ILE 2    28                                                      
REMARK 465     SER 2    29                                                      
REMARK 465     ALA 2    30                                                      
REMARK 465     LEU 2    31                                                      
REMARK 465     SER 2    32                                                      
REMARK 465     SER 2    33                                                      
REMARK 465     ILE 2    34                                                      
REMARK 465     GLY 2    35                                                      
REMARK 465     LEU 2    36                                                      
REMARK 465     LYS 2    37                                                      
REMARK 465     THR 2    38                                                      
REMARK 465     GLY 2    39                                                      
REMARK 465     THR 2    40                                                      
REMARK 465     VAL 2    41                                                      
REMARK 465     THR 2    42                                                      
REMARK 465     ARG 2    43                                                      
REMARK 465     VAL 2    44                                                      
REMARK 465     ALA 2    45                                                      
REMARK 465     CYS 2    46                                                      
REMARK 465     VAL 2    47                                                      
REMARK 465     THR 2    48                                                      
REMARK 465     ARG 2    49                                                      
REMARK 465     VAL 2    50                                                      
REMARK 465     PRO 2    51                                                      
REMARK 465     ALA 2    52                                                      
REMARK 465     ARG 2    53                                                      
REMARK 465     GLY 2    54                                                      
REMARK 465     LEU 2    55                                                      
REMARK 465     ARG 2    56                                                      
REMARK 465     MET 2    57                                                      
REMARK 465     GLN 2    58                                                      
REMARK 465     ALA 2    59                                                      
REMARK 465     PRO 2    60                                                      
REMARK 465     SER 2    61                                                      
REMARK 465     GLY 2    62                                                      
REMARK 465     ALA 2    63                                                      
REMARK 465     THR 2    64                                                      
REMARK 465     MET 2    65                                                      
REMARK 465     PRO 2    66                                                      
REMARK 465     SER 2    67                                                      
REMARK 465     MET 2    68                                                      
REMARK 465     PRO 2    69                                                      
REMARK 465     PHE 2    70                                                      
REMARK 465     LEU 2    71                                                      
REMARK 465     LYS 2    72                                                      
REMARK 465     ARG 2    73                                                      
REMARK 465     PRO 2    74                                                      
REMARK 465     SER 2    75                                                      
REMARK 465     LYS 2    76                                                      
REMARK 465     LEU 2    77                                                      
REMARK 465     ASP 2    78                                                      
REMARK 465     GLY 2    79                                                      
REMARK 465     SER 2    80                                                      
REMARK 465     LEU 2    81                                                      
REMARK 465     PRO 2    82                                                      
REMARK 465     GLY 2    83                                                      
REMARK 465     GLY 2    84                                                      
REMARK 465     GLU 2    85                                                      
REMARK 465     GLY 2    86                                                      
REMARK 465     CYS 2    87                                                      
REMARK 465     PHE 2    88                                                      
REMARK 465     ASP 2    89                                                      
REMARK 465     PRO 2    90                                                      
REMARK 465     LEU 2    91                                                      
REMARK 465     GLY 2    92                                                      
REMARK 465     PHE 2    93                                                      
REMARK 465     ALA 2   238                                                      
REMARK 465     HIS 2   239                                                      
REMARK 465     PHE 2   240                                                      
REMARK 465     ASN 2   241                                                      
REMARK 465     ALA 2   242                                                      
REMARK 465     ILE 2   243                                                      
REMARK 465     LYS 2   244                                                      
REMARK 465     PRO 2   245                                                      
REMARK 465     ASN 2   246                                                      
REMARK 465     MET 3     1                                                      
REMARK 465     ALA 3     2                                                      
REMARK 465     PHE 3     3                                                      
REMARK 465     ILE 3     4                                                      
REMARK 465     SER 3     5                                                      
REMARK 465     ALA 3     6                                                      
REMARK 465     LEU 3     7                                                      
REMARK 465     SER 3     8                                                      
REMARK 465     SER 3     9                                                      
REMARK 465     ILE 3    10                                                      
REMARK 465     GLY 3    11                                                      
REMARK 465     LEU 3    12                                                      
REMARK 465     LYS 3    13                                                      
REMARK 465     THR 3    14                                                      
REMARK 465     GLY 3    15                                                      
REMARK 465     THR 3    16                                                      
REMARK 465     VAL 3    17                                                      
REMARK 465     THR 3    18                                                      
REMARK 465     ARG 3    19                                                      
REMARK 465     VAL 3    20                                                      
REMARK 465     ALA 3    21                                                      
REMARK 465     CYS 3    22                                                      
REMARK 465     VAL 3    23                                                      
REMARK 465     THR 3    24                                                      
REMARK 465     ARG 3    25                                                      
REMARK 465     VAL 3    26                                                      
REMARK 465     PRO 3    27                                                      
REMARK 465     ALA 3    28                                                      
REMARK 465     ARG 3    29                                                      
REMARK 465     GLY 3    30                                                      
REMARK 465     LEU 3    31                                                      
REMARK 465     ARG 3    32                                                      
REMARK 465     MET 3    33                                                      
REMARK 465     GLN 3    34                                                      
REMARK 465     ALA 3    35                                                      
REMARK 465     PRO 3    36                                                      
REMARK 465     SER 3    37                                                      
REMARK 465     GLY 3    38                                                      
REMARK 465     ALA 3    39                                                      
REMARK 465     THR 3    40                                                      
REMARK 465     MET 3    41                                                      
REMARK 465     PRO 3    42                                                      
REMARK 465     SER 3    43                                                      
REMARK 465     MET 3    44                                                      
REMARK 465     PRO 3    45                                                      
REMARK 465     PHE 3    46                                                      
REMARK 465     LEU 3    47                                                      
REMARK 465     LYS 3    48                                                      
REMARK 465     ARG 3    49                                                      
REMARK 465     PRO 3    50                                                      
REMARK 465     SER 3    51                                                      
REMARK 465     LYS 3    52                                                      
REMARK 465     LEU 3    53                                                      
REMARK 465     ASP 3    54                                                      
REMARK 465     GLY 3    55                                                      
REMARK 465     SER 3    56                                                      
REMARK 465     LEU 3    57                                                      
REMARK 465     PRO 3    58                                                      
REMARK 465     GLY 3    59                                                      
REMARK 465     GLY 3    60                                                      
REMARK 465     GLU 3   211                                                      
REMARK 465     GLN 3   212                                                      
REMARK 465     LEU 3   213                                                      
REMARK 465     ALA 3   214                                                      
REMARK 465     HIS 3   215                                                      
REMARK 465     PHE 3   216                                                      
REMARK 465     ASN 3   217                                                      
REMARK 465     ALA 3   218                                                      
REMARK 465     ILE 3   219                                                      
REMARK 465     LYS 3   220                                                      
REMARK 465     PRO 3   221                                                      
REMARK 465     ASN 3   222                                                      
REMARK 465     MET 4    25                                                      
REMARK 465     TYR 4    26                                                      
REMARK 465     ALA 4    27                                                      
REMARK 465     PHE 4    28                                                      
REMARK 465     VAL 4    29                                                      
REMARK 465     SER 4    30                                                      
REMARK 465     PHE 4    31                                                      
REMARK 465     ALA 4    32                                                      
REMARK 465     PRO 4    33                                                      
REMARK 465     LEU 4    34                                                      
REMARK 465     VAL 4    35                                                      
REMARK 465     GLN 4    36                                                      
REMARK 465     ARG 4    37                                                      
REMARK 465     ALA 4    38                                                      
REMARK 465     ASN 4    39                                                      
REMARK 465     THR 4    40                                                      
REMARK 465     VAL 4    41                                                      
REMARK 465     SER 4    42                                                      
REMARK 465     LYS 4    43                                                      
REMARK 465     ALA 4    44                                                      
REMARK 465     THR 4    45                                                      
REMARK 465     GLY 4    46                                                      
REMARK 465     THR 4    47                                                      
REMARK 465     SER 4    48                                                      
REMARK 465     ALA 4    49                                                      
REMARK 465     ILE 4    50                                                      
REMARK 465     ARG 4    51                                                      
REMARK 465     SER 4    52                                                      
REMARK 465     ARG 4    53                                                      
REMARK 465     HIS 4    54                                                      
REMARK 465     ALA 4    55                                                      
REMARK 465     SER 4    56                                                      
REMARK 465     GLY 4    57                                                      
REMARK 465     TYR 4    58                                                      
REMARK 465     ALA 4    59                                                      
REMARK 465     THR 4    60                                                      
REMARK 465     LEU 4    61                                                      
REMARK 465     LYS 4    62                                                      
REMARK 465     MET 4    63                                                      
REMARK 465     GLU 4    64                                                      
REMARK 465     GLN 4    65                                                      
REMARK 465     SER 4    66                                                      
REMARK 465     PRO 4    67                                                      
REMARK 465     ALA 4    68                                                      
REMARK 465     LEU 4    69                                                      
REMARK 465     PRO 4    70                                                      
REMARK 465     PHE 4    71                                                      
REMARK 465     LEU 4    72                                                      
REMARK 465     SER 4    73                                                      
REMARK 465     LYS 4    74                                                      
REMARK 465     PRO 4    75                                                      
REMARK 465     PRO 4    76                                                      
REMARK 465     ASN 4    77                                                      
REMARK 465     LEU 4    78                                                      
REMARK 465     SER 4    79                                                      
REMARK 465     PRO 4    80                                                      
REMARK 465     ASP 4    81                                                      
REMARK 465     MET 4    82                                                      
REMARK 465     PRO 4    83                                                      
REMARK 465     GLY 4    84                                                      
REMARK 465     TYR 4    85                                                      
REMARK 465     ARG 4    86                                                      
REMARK 465     GLY 4    87                                                      
REMARK 465     PHE 4    88                                                      
REMARK 465     ASP 4    89                                                      
REMARK 465     PRO 4    90                                                      
REMARK 465     LEU 4    91                                                      
REMARK 465     ARG 4    92                                                      
REMARK 465     PHE 4    93                                                      
REMARK 465     SER 4    94                                                      
REMARK 465     ASP 4    95                                                      
REMARK 465     ALA 4    96                                                      
REMARK 465     PHE 4    97                                                      
REMARK 465     ASP 4    98                                                      
REMARK 465     GLY 4   198                                                      
REMARK 465     ARG 4   199                                                      
REMARK 465     LYS 4   200                                                      
REMARK 465     PRO 4   201                                                      
REMARK 465     GLY 4   202                                                      
REMARK 465     GLU 4   203                                                      
REMARK 465     LEU 4   204                                                      
REMARK 465     GLY 4   205                                                      
REMARK 465     PHE 4   206                                                      
REMARK 465     ASN 4   207                                                      
REMARK 465     PRO 4   208                                                      
REMARK 465     LEU 4   209                                                      
REMARK 465     ASN 4   210                                                      
REMARK 465     LEU 4   211                                                      
REMARK 465     PRO 4   212                                                      
REMARK 465     ASN 4   213                                                      
REMARK 465     ASP 4   214                                                      
REMARK 465     THR 4   251                                                      
REMARK 465     ASN 4   252                                                      
REMARK 465     PHE 4   253                                                      
REMARK 465     GLN 4   254                                                      
REMARK 465     PRO 4   255                                                      
REMARK 465     LEU 4   256                                                      
REMARK 465     GLN 4   257                                                      
REMARK 465     PRO F   184                                                      
REMARK 465     ARG F   185                                                      
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     SER 2 135    OG                                                  
REMARK 470     LYS 2 136    CG   CD   CE   NZ                                   
REMARK 470     LEU 2 137    CG   CD1  CD2                                       
REMARK 470     GLN 2 138    CG   CD   OE1  NE2                                  
REMARK 470     LEU 2 139    CG   CD1  CD2                                       
REMARK 470     SER 2 140    OG                                                  
REMARK 470     ASP 2 142    CG   OD1  OD2                                       
REMARK 470     GLU 2 164    CG   CD   OE1  OE2                                  
REMARK 470     SER B 732    CA   C    O    CB   OG                              
REMARK 470     LEU K  36    CG   CD1  CD2                                       
REMARK 470     MET M   1    CG   SD   CE                                        
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   NE2  HIS B   419     NA   CLA B  1228              1.98            
REMARK 500   NE2  HIS B   419     CHA  CLA B  1228              2.00            
REMARK 500   O    LEU B   339     OG1  THR B   343              2.16            
REMARK 500   O    ASP F   146     OG   SER J     8              2.16            
REMARK 500   NH2  ARG A   459     O    GLN A   634              2.16            
REMARK 500   O    HIS A   346     OH   TYR A   408              2.17            
REMARK 500   OH   TYR L    75     O    TYR L   133              2.17            
REMARK 500   O    TRP A   676     OG   SER A   679              2.18            
REMARK 500   O    PHE B   181     OG   SER B   185              2.18            
REMARK 500   OD1  ASP B   514     OH   TYR B   591              2.19            
REMARK 500   O    LEU B   266     OG1  THR B   269              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU J  36   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR 2 127       25.15   -148.46                                   
REMARK 500    ASP 2 129     -124.03    -85.54                                   
REMARK 500    LYS 2 136       -2.58     72.47                                   
REMARK 500    LEU 2 137     -138.66     57.97                                   
REMARK 500    GLU 2 174      174.15     61.88                                   
REMARK 500    ASN 2 177      -97.92     57.46                                   
REMARK 500    SER 2 198     -122.68     64.79                                   
REMARK 500    GLN 2 200      -35.54   -144.60                                   
REMARK 500    TRP 2 201       85.62     48.87                                   
REMARK 500    THR 2 229      112.96   -160.77                                   
REMARK 500    LYS 2 230      -61.52    -96.07                                   
REMARK 500    ILE 2 233      -65.65     64.88                                   
REMARK 500    PHE 3  64     -116.55   -129.45                                   
REMARK 500    GLU 3  71     -148.78     64.39                                   
REMARK 500    VAL 3  72      137.41     72.45                                   
REMARK 500    ALA 3  98     -178.88     73.33                                   
REMARK 500    THR 3 103     -178.07     60.27                                   
REMARK 500    PHE 3 104     -176.81     59.14                                   
REMARK 500    LYS 3 110     -169.33     67.41                                   
REMARK 500    LEU 3 113      -68.45     12.77                                   
REMARK 500    LEU 3 115      -35.02   -130.38                                   
REMARK 500    PRO 3 117       55.73   -102.50                                   
REMARK 500    LEU 3 119      127.38     68.06                                   
REMARK 500    GLN 3 122       25.88   -149.07                                   
REMARK 500    VAL 3 124      -50.38   -120.24                                   
REMARK 500    ASN 3 126       97.95    -66.29                                   
REMARK 500    LEU 3 145      -29.13   -143.20                                   
REMARK 500    ALA 3 147      -83.84   -155.64                                   
REMARK 500    ASP 3 164       73.20     48.50                                   
REMARK 500    LEU 3 166      -69.43    -98.50                                   
REMARK 500    LYS 3 167     -174.01     73.35                                   
REMARK 500    VAL 3 172      -64.03     19.27                                   
REMARK 500    LYS 3 178       -3.16     73.02                                   
REMARK 500    PHE 3 195      -72.17    -51.70                                   
REMARK 500    LEU 3 204     -162.34    -76.75                                   
REMARK 500    PHE 4 128      -50.42   -121.66                                   
REMARK 500    PHE 4 130       89.40     56.96                                   
REMARK 500    PRO 4 135     -114.57    -75.54                                   
REMARK 500    HIS 4 142       63.56   -154.26                                   
REMARK 500    VAL 4 146     -146.94     53.24                                   
REMARK 500    SER 4 173     -152.71    -77.32                                   
REMARK 500    ASP 4 174      -28.11     68.33                                   
REMARK 500    TRP 4 177     -103.39     55.90                                   
REMARK 500    ASN 4 242      -61.19     61.82                                   
REMARK 500    GLN 4 249     -104.63     56.01                                   
REMARK 500    ASP A  14       78.53   -108.31                                   
REMARK 500    ASP A  16      102.54     63.54                                   
REMARK 500    LEU A  35       42.97   -102.18                                   
REMARK 500    ALA A  36      -45.66   -145.16                                   
REMARK 500    PRO A  39       37.80    -95.19                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     235 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     CLA 2  601                                                       
REMARK 610     CLA 2  602                                                       
REMARK 610     CLA 2  603                                                       
REMARK 610     CLA 2  604                                                       
REMARK 610     CLA 2  605                                                       
REMARK 610     CLA 2  606                                                       
REMARK 610     CLA 2  607                                                       
REMARK 610     CLA 2  608                                                       
REMARK 610     CLA 2  610                                                       
REMARK 610     CLA 2  611                                                       
REMARK 610     CLA 2  612                                                       
REMARK 610     CLA 2  613                                                       
REMARK 610     CLA 2  614                                                       
REMARK 610     CLA 2  615                                                       
REMARK 610     CLA 2  616                                                       
REMARK 610     CLA 3  601                                                       
REMARK 610     CLA 3  602                                                       
REMARK 610     CLA 3  603                                                       
REMARK 610     CLA 3  604                                                       
REMARK 610     CLA 3  606                                                       
REMARK 610     CLA 3  607                                                       
REMARK 610     CLA 3  608                                                       
REMARK 610     CLA 3  610                                                       
REMARK 610     CLA 3  611                                                       
REMARK 610     CLA 3  612                                                       
REMARK 610     CLA 3  614                                                       
REMARK 610     CLA 4  601                                                       
REMARK 610     CLA 4  602                                                       
REMARK 610     CLA 4  603                                                       
REMARK 610     CLA 4  604                                                       
REMARK 610     CLA 4  605                                                       
REMARK 610     CLA 4  606                                                       
REMARK 610     CLA 4  608                                                       
REMARK 610     CLA 4  609                                                       
REMARK 610     CLA 4  610                                                       
REMARK 610     CLA 4  611                                                       
REMARK 610     CLA 4  612                                                       
REMARK 610     CLA 4  615                                                       
REMARK 610     CLA 4  616                                                       
REMARK 610     CLA A 1011                                                       
REMARK 610     CLA A 1012                                                       
REMARK 610     CLA A 1013                                                       
REMARK 610     CLA A 1101                                                       
REMARK 610     CLA A 1102                                                       
REMARK 610     CLA A 1103                                                       
REMARK 610     CLA A 1104                                                       
REMARK 610     CLA A 1105                                                       
REMARK 610     CLA A 1106                                                       
REMARK 610     CLA A 1107                                                       
REMARK 610     CLA A 1108                                                       
REMARK 610     CLA A 1109                                                       
REMARK 610     CLA A 1110                                                       
REMARK 610     CLA A 1111                                                       
REMARK 610     CLA A 1112                                                       
REMARK 610     CLA A 1113                                                       
REMARK 610     CLA A 1114                                                       
REMARK 610     CLA A 1115                                                       
REMARK 610     CLA A 1116                                                       
REMARK 610     CLA A 1117                                                       
REMARK 610     CLA A 1118                                                       
REMARK 610     CLA A 1119                                                       
REMARK 610     CLA A 1120                                                       
REMARK 610     CLA A 1121                                                       
REMARK 610     CLA A 1122                                                       
REMARK 610     CLA A 1123                                                       
REMARK 610     CLA A 1124                                                       
REMARK 610     CLA A 1125                                                       
REMARK 610     CLA A 1126                                                       
REMARK 610     CLA A 1127                                                       
REMARK 610     CLA A 1128                                                       
REMARK 610     CLA A 1129                                                       
REMARK 610     CLA A 1130                                                       
REMARK 610     CLA A 1131                                                       
REMARK 610     CLA A 1132                                                       
REMARK 610     CLA A 1133                                                       
REMARK 610     CLA A 1134                                                       
REMARK 610     CLA A 1135                                                       
REMARK 610     CLA A 1136                                                       
REMARK 610     CLA A 1137                                                       
REMARK 610     CLA A 1138                                                       
REMARK 610     CLA A 1139                                                       
REMARK 610     CLA A 1140                                                       
REMARK 610     CLA A 1141                                                       
REMARK 610     CLA B 1021                                                       
REMARK 610     CLA B 1022                                                       
REMARK 610     CLA B 1023                                                       
REMARK 610     CLA B 1201                                                       
REMARK 610     CLA B 1202                                                       
REMARK 610     CLA B 1203                                                       
REMARK 610     CLA B 1204                                                       
REMARK 610     CLA B 1205                                                       
REMARK 610     CLA B 1206                                                       
REMARK 610     CLA B 1207                                                       
REMARK 610     CLA B 1208                                                       
REMARK 610     CLA B 1209                                                       
REMARK 610     CLA B 1210                                                       
REMARK 610     CLA B 1211                                                       
REMARK 610     CLA B 1212                                                       
REMARK 610     CLA B 1214                                                       
REMARK 610     CLA B 1215                                                       
REMARK 610     CLA B 1216                                                       
REMARK 610     CLA B 1217                                                       
REMARK 610     CLA B 1218                                                       
REMARK 610     CLA B 1219                                                       
REMARK 610     CLA B 1220                                                       
REMARK 610     CLA B 1221                                                       
REMARK 610     CLA B 1222                                                       
REMARK 610     CLA B 1223                                                       
REMARK 610     CLA B 1224                                                       
REMARK 610     CLA B 1225                                                       
REMARK 610     CLA B 1226                                                       
REMARK 610     CLA B 1227                                                       
REMARK 610     CLA B 1228                                                       
REMARK 610     CLA B 1229                                                       
REMARK 610     CLA B 1230                                                       
REMARK 610     CLA B 1231                                                       
REMARK 610     CLA B 1234                                                       
REMARK 610     CLA B 1235                                                       
REMARK 610     CLA B 1236                                                       
REMARK 610     CLA B 1237                                                       
REMARK 610     CLA B 1238                                                       
REMARK 610     CLA B 1239                                                       
REMARK 610     CLA F 1301                                                       
REMARK 610     CLA F 1302                                                       
REMARK 610     CLA J 1302                                                       
REMARK 610     CLA K 1401                                                       
REMARK 610     CLA K 1402                                                       
REMARK 610     CLA L 1501                                                       
REMARK 610     CLA L 1502                                                       
REMARK 610     CLA L 1503                                                       
REMARK 610     CLA O 1601                                                       
REMARK 610     CLA O 1602                                                       
REMARK 610     CLA O 1603                                                       
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                             CLA A1107  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 120   OE1                                                    
REMARK 620 2 CLA A1107   NA   90.0                                              
REMARK 620 3 CLA A1107   NB   79.1  89.1                                        
REMARK 620 4 CLA A1107   NC   94.4 175.2  93.7                                  
REMARK 620 5 CLA A1107   ND  103.3  93.9 176.2  83.2                            
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 CLA 2 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 2 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 2 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 2 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 2 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 2 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 2 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 2 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 2 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 2 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 2 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 3 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 4 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 4 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 4 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 4 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 4 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 4 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 4 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 4 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 4 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 4 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA 4 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1104                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1105                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1106                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1107                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1108                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1109                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1110                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1111                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1112                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1113                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1114                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1115                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1116                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1117                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1118                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1119                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1120                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1121                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1122                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1123                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1124                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1125                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1126                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1127                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1128                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1129                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1130                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1131                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1132                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1133                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1134                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1135                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1136                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1137                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1138                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1139                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1140                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 1141                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PQN A 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 A 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 4002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 4007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 4008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 4011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 4017                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1021                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1022                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1023                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1206                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1207                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1208                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1209                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1210                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1211                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1212                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1214                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1215                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1217                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1218                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1221                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1222                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1223                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1224                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1225                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1226                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1227                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1228                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1229                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1230                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1234                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1235                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1236                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1237                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1238                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 1239                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PQN B 2002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 4005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 4008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 C 3002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 C 3003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA F 1301                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA F 1302                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR I 4018                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA J 1302                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA K 1401                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA K 1402                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA L 1501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA L 1502                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA L 1503                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA O 1601                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA O 1602                
DBREF  6FOS 2   25   246  UNP    M1UU36   M1UU36_CYAM1     1    222             
DBREF  6FOS 3    1   222  UNP    M1UU36   M1UU36_CYAM1     1    222             
DBREF  6FOS 4   25   257  UNP    M1VKK5   M1VKK5_CYAM1     1    214             
DBREF  6FOS A    9   748  UNP    Q85FY7   PSAA_CYAM1       9    748             
DBREF  6FOS B    8   732  UNP    Q85FY6   PSAB_CYAM1       8    732             
DBREF  6FOS C    2    81  UNP    Q85G47   PSAC_CYAM1       2     81             
DBREF  6FOS D    6   129  UNP    Q85FY0   Q85FY0_CYAM1     6    129             
DBREF  6FOS E    1    69  UNP    Q85FZ1   Q85FZ1_CYAM1     1     69             
DBREF  6FOS F   31   185  UNP    Q85FS9   Q85FS9_CYAM1    31    185             
DBREF  6FOS I    1    32  UNP    Q85FQ6   Q85FQ6_CYAM1     1     32             
DBREF  6FOS J    1    38  UNP    Q85FS8   PSAJ_CYAM1       1     38             
DBREF  6FOS K   15    60  UNP    Q85G51   Q85G51_CYAM1    15     60             
DBREF  6FOS L    1   140  UNP    Q85FP8   PSAL_CYAM1       1    140             
DBREF  6FOS M    1    29  UNP    Q85G73   Q85G73_CYAM1     1     29             
DBREF  6FOS O   51   148  UNP    M1VFJ4   M1VFJ4_CYAM1    51    148             
SEQADV 6FOS MET K   14  UNP  Q85G51              INITIATING METHIONINE          
SEQRES   1 2  222  MET ALA PHE ILE SER ALA LEU SER SER ILE GLY LEU LYS          
SEQRES   2 2  222  THR GLY THR VAL THR ARG VAL ALA CYS VAL THR ARG VAL          
SEQRES   3 2  222  PRO ALA ARG GLY LEU ARG MET GLN ALA PRO SER GLY ALA          
SEQRES   4 2  222  THR MET PRO SER MET PRO PHE LEU LYS ARG PRO SER LYS          
SEQRES   5 2  222  LEU ASP GLY SER LEU PRO GLY GLY GLU GLY CYS PHE ASP          
SEQRES   6 2  222  PRO LEU GLY PHE THR GLU VAL PHE SER LEU GLU TRP LEU          
SEQRES   7 2  222  ARG GLU ALA GLU ILE LYS HIS CYS ARG VAL ALA MET LEU          
SEQRES   8 2  222  ALA VAL LEU GLY VAL ILE ALA GLN GLU PHE GLY THR PHE          
SEQRES   9 2  222  ASP PHE TYR ASN ALA LYS SER LYS LEU GLN LEU SER PRO          
SEQRES  10 2  222  ASP LEU HIS ASN GLN PHE VAL GLN ASN GLY ALA LEU GLN          
SEQRES  11 2  222  GLN ILE LEU LEU PHE VAL CYS ALA TRP GLU PHE ILE VAL          
SEQRES  12 2  222  GLY LEU PRO ALA LEU ILE GLU SER VAL ASN GLY ASN ARG          
SEQRES  13 2  222  GLU PRO GLY TYR PHE GLY PHE ASP PRO LEU LYS LEU GLY          
SEQRES  14 2  222  GLY THR VAL GLY SER ALA GLN TRP LYS ARG MET GLN ALA          
SEQRES  15 2  222  GLY GLU LEU ARG ASN GLY ARG LEU ALA MET ILE ALA PHE          
SEQRES  16 2  222  GLY GLY PHE PHE HIS GLN GLN LEU LEU THR LYS GLN GLY          
SEQRES  17 2  222  ILE ILE GLU GLN LEU ALA HIS PHE ASN ALA ILE LYS PRO          
SEQRES  18 2  222  ASN                                                          
SEQRES   1 3  222  MET ALA PHE ILE SER ALA LEU SER SER ILE GLY LEU LYS          
SEQRES   2 3  222  THR GLY THR VAL THR ARG VAL ALA CYS VAL THR ARG VAL          
SEQRES   3 3  222  PRO ALA ARG GLY LEU ARG MET GLN ALA PRO SER GLY ALA          
SEQRES   4 3  222  THR MET PRO SER MET PRO PHE LEU LYS ARG PRO SER LYS          
SEQRES   5 3  222  LEU ASP GLY SER LEU PRO GLY GLY GLU GLY CYS PHE ASP          
SEQRES   6 3  222  PRO LEU GLY PHE THR GLU VAL PHE SER LEU GLU TRP LEU          
SEQRES   7 3  222  ARG GLU ALA GLU ILE LYS HIS CYS ARG VAL ALA MET LEU          
SEQRES   8 3  222  ALA VAL LEU GLY VAL ILE ALA GLN GLU PHE GLY THR PHE          
SEQRES   9 3  222  ASP PHE TYR ASN ALA LYS SER LYS LEU GLN LEU SER PRO          
SEQRES  10 3  222  ASP LEU HIS ASN GLN PHE VAL GLN ASN GLY ALA LEU GLN          
SEQRES  11 3  222  GLN ILE LEU LEU PHE VAL CYS ALA TRP GLU PHE ILE VAL          
SEQRES  12 3  222  GLY LEU PRO ALA LEU ILE GLU SER VAL ASN GLY ASN ARG          
SEQRES  13 3  222  GLU PRO GLY TYR PHE GLY PHE ASP PRO LEU LYS LEU GLY          
SEQRES  14 3  222  GLY THR VAL GLY SER ALA GLN TRP LYS ARG MET GLN ALA          
SEQRES  15 3  222  GLY GLU LEU ARG ASN GLY ARG LEU ALA MET ILE ALA PHE          
SEQRES  16 3  222  GLY GLY PHE PHE HIS GLN GLN LEU LEU THR LYS GLN GLY          
SEQRES  17 3  222  ILE ILE GLU GLN LEU ALA HIS PHE ASN ALA ILE LYS PRO          
SEQRES  18 3  222  ASN                                                          
SEQRES   1 4  214  MET TYR ALA PHE VAL SER PHE ALA PRO LEU VAL GLN ARG          
SEQRES   2 4  214  ALA ASN THR VAL SER LYS ALA THR GLY THR SER ALA ILE          
SEQRES   3 4  214  ARG SER ARG HIS ALA SER GLY TYR ALA THR LEU LYS MET          
SEQRES   4 4  214  GLU GLN SER PRO ALA LEU PRO PHE LEU SER LYS PRO PRO          
SEQRES   5 4  214  ASN LEU SER PRO ASP MET PRO GLY TYR ARG GLY PHE ASP          
SEQRES   6 4  214  PRO LEU ARG PHE SER ASP ALA PHE ASP VAL ASN TRP LEU          
SEQRES   7 4  214  GLN GLU GLY GLU ILE LYS ASN GLY ARG VAL ALA MET LEU          
SEQRES   8 4  214  ALA CYS LEU HIS PHE PHE VAL THR GLU PHE TYR GLN PHE          
SEQRES   9 4  214  PRO PHE PHE ALA GLY ALA PRO LYS LEU ALA GLY PRO ALA          
SEQRES  10 4  214  HIS ASP TYR PHE VAL LYS SER GLY ALA MET ILE GLN ILE          
SEQRES  11 4  214  LEU ALA PHE ILE GLY PHE LEU GLU PHE LEU LEU HIS ARG          
SEQRES  12 4  214  GLY LYS VAL LEU TYR SER ASP MET GLU TRP LYS GLY ARG          
SEQRES  13 4  214  LYS PRO GLY GLU LEU GLY PHE ASN PRO LEU ASN LEU PRO          
SEQRES  14 4  214  ASN ASP LYS ALA MET ARG ASP ARG GLU VAL ASN ASN GLY          
SEQRES  15 4  214  ARG LEU ALA MET LEU GLY PHE ALA GLY ILE ILE HIS GLY          
SEQRES  16 4  214  GLU PHE LEU ASN GLY LYS MET PRO PHE GLU GLN ILE THR          
SEQRES  17 4  214  ASN PHE GLN PRO LEU GLN                                      
SEQRES   1 A  740  VAL LYS VAL VAL VAL ASP ARG ASP VAL VAL PRO THR SER          
SEQRES   2 A  740  PHE GLU LYS TRP ALA LYS PRO GLY HIS PHE SER ARG SER          
SEQRES   3 A  740  LEU ALA LYS GLY PRO LYS THR THR THR TRP ILE TRP ASN          
SEQRES   4 A  740  LEU HIS ALA ASP ALA HIS ASP PHE ASP SER HIS THR SER          
SEQRES   5 A  740  SER LEU GLU GLU VAL SER ARG LYS ILE PHE SER ALA HIS          
SEQRES   6 A  740  PHE GLY GLN LEU ALA ILE ILE PHE ILE TRP LEU SER GLY          
SEQRES   7 A  740  MET TYR PHE HIS GLY ALA ARG PHE SER ASN TYR VAL ALA          
SEQRES   8 A  740  TRP LEU SER ASN PRO THR GLY ILE LYS PRO SER ALA GLN          
SEQRES   9 A  740  VAL VAL TRP PRO ILE VAL GLY GLN GLN ILE LEU ASN ALA          
SEQRES  10 A  740  ASP VAL GLY GLY GLY MET GLN GLY ILE GLN ILE THR SER          
SEQRES  11 A  740  GLY LEU PHE GLN LEU TRP ARG ALA SER GLY ILE VAL ASN          
SEQRES  12 A  740  GLU LEU GLN LEU TYR VAL THR ALA LEU GLY GLY LEU GLY          
SEQRES  13 A  740  MET ALA GLY LEU MET ILE PHE ALA GLY TRP PHE HIS TYR          
SEQRES  14 A  740  HIS LYS ALA ALA PRO LYS LEU GLU TRP PHE GLN ASN VAL          
SEQRES  15 A  740  GLU SER MET LEU ASN HIS HIS LEU ALA GLY LEU LEU GLY          
SEQRES  16 A  740  LEU GLY SER LEU SER TRP ALA GLY HIS GLN ILE HIS VAL          
SEQRES  17 A  740  SER LEU PRO ILE ASN LYS LEU LEU ASP ALA GLY VAL ALA          
SEQRES  18 A  740  PRO SER SER ILE PRO LEU PRO HIS GLU PHE ILE LEU ASN          
SEQRES  19 A  740  ARG ASN LEU MET ALA GLU LEU TYR PRO SER PHE GLN GLN          
SEQRES  20 A  740  GLY LEU VAL PRO PHE PHE THR LEU ASN TRP LYS GLN TYR          
SEQRES  21 A  740  SER ASP ILE LEU THR PHE LYS GLY GLY LEU SER PRO VAL          
SEQRES  22 A  740  THR GLY GLY LEU TRP LEU THR ASP VAL ALA HIS HIS HIS          
SEQRES  23 A  740  LEU ALA ILE ALA VAL LEU PHE LEU VAL ALA GLY HIS MET          
SEQRES  24 A  740  TYR ARG THR ASN TRP GLY ILE GLY HIS SER ILE LYS GLN          
SEQRES  25 A  740  ILE LEU GLU ALA HIS LYS GLY PRO LEU THR GLY GLU GLY          
SEQRES  26 A  740  HIS LYS GLY LEU TYR GLU ILE LEU THR THR SER TRP HIS          
SEQRES  27 A  740  ALA ASN LEU ALA ILE ASN LEU ALA MET LEU GLY SER LEU          
SEQRES  28 A  740  SER ILE ILE VAL ALA HIS HIS MET TYR ALA MET PRO PRO          
SEQRES  29 A  740  TYR PRO TYR LEU ALA THR ASP TYR PRO THR GLN LEU SER          
SEQRES  30 A  740  LEU PHE THR HIS HIS MET TRP ILE GLY GLY PHE CYS ILE          
SEQRES  31 A  740  VAL GLY ALA GLY ALA HIS ALA ALA ILE TYR MET VAL ARG          
SEQRES  32 A  740  ASP TYR SER PRO THR VAL ASN PHE ASN ASN VAL LEU ASP          
SEQRES  33 A  740  ARG MET ILE ARG HIS ARG ASP ALA ILE ILE SER HIS LEU          
SEQRES  34 A  740  ASN TRP VAL CYS ILE PHE LEU GLY MET HIS SER PHE GLY          
SEQRES  35 A  740  LEU TYR ILE HIS ASN ASP THR MET ARG ALA LEU GLY ARG          
SEQRES  36 A  740  ALA GLN ASP MET PHE SER ASP THR ALA ILE GLN LEU GLN          
SEQRES  37 A  740  PRO VAL PHE ALA GLN TRP ILE GLN GLN ILE HIS THR LEU          
SEQRES  38 A  740  ALA PRO GLY ASN THR ALA VAL ASN ALA LEU ALA THR ALA          
SEQRES  39 A  740  SER TYR ALA PHE GLY ALA ASP THR VAL THR VAL GLY SER          
SEQRES  40 A  740  LYS ILE ALA MET MET PRO ILE LYS LEU GLY THR ALA ASP          
SEQRES  41 A  740  PHE MET VAL HIS HIS ILE HIS ALA PHE THR ILE HIS VAL          
SEQRES  42 A  740  THR THR LEU ILE LEU LEU LYS GLY VAL LEU TYR ALA ARG          
SEQRES  43 A  740  ASN SER ARG LEU ILE PRO ASP LYS ALA ASN LEU GLY PHE          
SEQRES  44 A  740  ARG PHE PRO CYS ASP GLY PRO GLY ARG GLY GLY THR CYS          
SEQRES  45 A  740  GLN VAL SER ALA TRP ASP HIS VAL PHE LEU GLY LEU PHE          
SEQRES  46 A  740  TRP MET TYR ASN ALA LEU SER ILE VAL ILE PHE HIS PHE          
SEQRES  47 A  740  SER TRP LYS MET GLN SER ASP VAL TRP GLY THR VAL THR          
SEQRES  48 A  740  SER ASN GLY ALA ILE SER HIS ILE THR GLY GLY ASN PHE          
SEQRES  49 A  740  ALA GLN SER ALA ILE THR ILE ASN GLY TRP LEU ARG ASP          
SEQRES  50 A  740  PHE LEU TRP ALA GLN ALA SER GLN VAL ILE GLN SER TYR          
SEQRES  51 A  740  GLY SER SER LEU SER ALA TYR GLY LEU MET PHE LEU GLY          
SEQRES  52 A  740  ALA HIS PHE VAL TRP ALA PHE SER LEU MET PHE LEU PHE          
SEQRES  53 A  740  SER GLY ARG GLY TYR TRP GLN GLU LEU ILE GLU SER ILE          
SEQRES  54 A  740  VAL TRP ALA HIS ASN LYS LEU LYS VAL ALA PRO ALA ILE          
SEQRES  55 A  740  ALA PRO ARG ALA LEU SER ILE THR GLN GLY ARG ALA VAL          
SEQRES  56 A  740  GLY VAL ALA HIS TYR LEU LEU GLY GLY ILE ALA THR THR          
SEQRES  57 A  740  TRP ALA PHE PHE LEU ALA ARG ILE ILE ALA VAL GLY              
SEQRES   1 B  725  PHE SER GLN ALA LEU ALA SER ASP PRO THR THR ARG ARG          
SEQRES   2 B  725  ILE TRP TYR GLY ILE ALA THR ALA HIS ASP PHE GLU SER          
SEQRES   3 B  725  HIS ASP GLY MET THR GLU GLU ASN LEU TYR GLN LYS ILE          
SEQRES   4 B  725  PHE ALA SER HIS PHE GLY HIS LEU ALA ILE ILE PHE LEU          
SEQRES   5 B  725  TRP THR SER GLY ASN LEU PHE HIS VAL ALA TRP GLN GLY          
SEQRES   6 B  725  ASN PHE GLU GLN TRP VAL ALA ASN PRO LEU LYS THR LYS          
SEQRES   7 B  725  PRO LEU ALA HIS ALA ILE TRP ASP PRO HIS PHE GLY GLN          
SEQRES   8 B  725  ALA ALA LEU LYS ALA PHE THR ARG GLY ASP THR VAL ALA          
SEQRES   9 B  725  ASN ILE SER TYR SER GLY VAL TYR HIS TRP TRP TYR THR          
SEQRES  10 B  725  ILE GLY ILE ARG ASN ASN VAL GLU LEU TYR THR GLY ALA          
SEQRES  11 B  725  LEU GLY LEU LEU VAL LEU SER ALA VAL PHE LEU LEU ALA          
SEQRES  12 B  725  GLY TRP LEU HIS ILE GLN PRO LYS PHE LYS PRO SER LEU          
SEQRES  13 B  725  SER TRP PHE LYS ASN ASN GLU SER ARG LEU ASN HIS HIS          
SEQRES  14 B  725  LEU ALA GLY LEU PHE GLY VAL SER SER LEU ALA TRP THR          
SEQRES  15 B  725  GLY HIS LEU VAL HIS VAL ALA ILE PRO ALA SER ARG GLY          
SEQRES  16 B  725  GLN HIS VAL GLY TRP ASP ASN PHE ILE MET THR PRO PRO          
SEQRES  17 B  725  HIS PRO ALA GLY LEU GLN PRO PHE PHE THR GLY ASN TRP          
SEQRES  18 B  725  SER VAL TYR ALA GLN SER PRO ASP SER MET GLN HIS VAL          
SEQRES  19 B  725  PHE GLY THR SER GLN GLY ALA GLY THR ALA ILE LEU THR          
SEQRES  20 B  725  PHE LEU GLY GLY PHE HIS PRO GLN THR GLN SER LEU TRP          
SEQRES  21 B  725  LEU THR ASP MET ALA HIS HIS HIS LEU ALA ILE ALA VAL          
SEQRES  22 B  725  ILE PHE ILE VAL ALA GLY HIS MET TYR ARG THR ASN PHE          
SEQRES  23 B  725  GLY ILE GLY HIS ASN LEU LYS THR ILE LEU GLU ALA HIS          
SEQRES  24 B  725  ARG PRO PRO SER GLY ARG LEU GLY LYS GLY HIS ILE GLY          
SEQRES  25 B  725  ILE TYR GLN THR LEU THR ASN SER LEU HIS PHE GLN LEU          
SEQRES  26 B  725  GLY LEU ALA LEU ALA SER LEU SER VAL VAL THR SER LEU          
SEQRES  27 B  725  VAL ALA GLN HIS MET TYR ALA MET PRO PRO TYR ALA TYR          
SEQRES  28 B  725  MET ALA PHE ASP TYR VAL THR GLN SER ALA LEU TYR THR          
SEQRES  29 B  725  HIS HIS GLN TYR ILE ALA GLY LEU LEU ILE VAL GLY ALA          
SEQRES  30 B  725  PHE ALA HIS GLY ALA ILE PHE PHE ILE ARG ASP TYR ASP          
SEQRES  31 B  725  PRO GLU GLN ASN GLN ASP ASN VAL LEU ALA ARG MET LEU          
SEQRES  32 B  725  ALA HIS LYS GLU ALA VAL ILE SER HIS LEU SER TRP VAL          
SEQRES  33 B  725  SER LEU PHE LEU GLY PHE HIS THR LEU GLY LEU TYR VAL          
SEQRES  34 B  725  HIS ASN ASP VAL VAL VAL ALA PHE GLY ASN PRO GLU LYS          
SEQRES  35 B  725  GLN ILE LEU ILE GLU PRO ILE PHE ALA GLN TRP ILE GLN          
SEQRES  36 B  725  ALA THR SER GLY LYS MET LEU TYR GLY PHE GLN VAL LEU          
SEQRES  37 B  725  LEU SER SER SER THR SER ASN ALA SER VAL ALA ALA GLN          
SEQRES  38 B  725  GLN LEU TRP LEU PRO GLY TRP LEU GLU ALA VAL ASN ASN          
SEQRES  39 B  725  GLU SER ASN SER LEU PHE LEU THR ILE GLY PRO GLY ASP          
SEQRES  40 B  725  PHE LEU VAL HIS HIS ALA ILE ALA LEU GLY LEU HIS THR          
SEQRES  41 B  725  THR THR LEU ILE LEU VAL LYS GLY ALA LEU ASP ALA ARG          
SEQRES  42 B  725  GLY SER LYS LEU MET PRO ASP LYS LYS ASP PHE GLY TYR          
SEQRES  43 B  725  SER PHE PRO CYS ASP GLY PRO GLY ARG GLY GLY THR CYS          
SEQRES  44 B  725  ASP ILE SER ALA TRP ASP ALA PHE TYR LEU ALA MET PHE          
SEQRES  45 B  725  TRP MET LEU ASN THR ILE GLY TRP VAL THR PHE TYR TRP          
SEQRES  46 B  725  HIS TRP LYS HIS LEU SER LEU TRP GLN GLY ASN VAL ALA          
SEQRES  47 B  725  GLN PHE ASN GLU SER SER THR TYR LEU MET GLY TRP LEU          
SEQRES  48 B  725  ARG ASP TYR LEU TRP LEU ASN SER SER PRO LEU ILE ASN          
SEQRES  49 B  725  GLY TYR ASN PRO TYR GLY MET ASN SER LEU ALA VAL TRP          
SEQRES  50 B  725  SER TRP MET PHE LEU PHE ALA HIS LEU VAL TRP ALA THR          
SEQRES  51 B  725  GLY PHE MET PHE LEU ILE SER TRP ARG GLY TYR TRP GLN          
SEQRES  52 B  725  GLU LEU ILE GLU THR LEU ALA TRP ALA HIS GLU ARG THR          
SEQRES  53 B  725  PRO LEU ALA ASN LEU ILE ARG TRP LYS ASP LYS PRO VAL          
SEQRES  54 B  725  ALA LEU SER ILE VAL GLN ALA ARG LEU VAL GLY LEU VAL          
SEQRES  55 B  725  HIS PHE THR VAL GLY TYR ILE LEU THR TYR ALA ALA PHE          
SEQRES  56 B  725  VAL ILE ALA SER THR ALA GLY LYS PHE SER                      
SEQRES   1 C   80  ALA HIS THR VAL LYS ILE TYR ASP ASN CYS ILE GLY CYS          
SEQRES   2 C   80  THR GLN CYS VAL ARG ALA CYS PRO LEU ASP VAL LEU GLU          
SEQRES   3 C   80  MET VAL PRO TRP ASP GLY CYS LYS ALA GLY GLN MET ALA          
SEQRES   4 C   80  SER ALA PRO ARG THR GLU ASP CYS VAL GLY CYS LYS ARG          
SEQRES   5 C   80  CYS GLU THR ALA CYS PRO THR ASP PHE LEU SER ILE ARG          
SEQRES   6 C   80  VAL TYR LEU GLY GLY GLU THR THR ARG SER MET GLY LEU          
SEQRES   7 C   80  ALA TYR                                                      
SEQRES   1 D  124  MET PRO SER PRO SER PHE LEU GLY SER THR GLY GLY TRP          
SEQRES   2 D  124  LEU ARG CYS ALA GLU THR GLU GLU LYS TYR ALA MET THR          
SEQRES   3 D  124  TRP SER SER ASP GLN GLN HIS ILE PHE GLU MET PRO THR          
SEQRES   4 D  124  GLY GLY ALA ALA VAL MET ASN SER GLY ASP ASN LEU LEU          
SEQRES   5 D  124  TYR LEU ALA ARG LYS GLU GLN ALA LEU ALA LEU ALA THR          
SEQRES   6 D  124  GLN LEU ARG THR GLN PHE LYS ILE GLN ASP TYR LYS ILE          
SEQRES   7 D  124  TYR ARG ILE PHE PRO SER GLY GLU VAL GLN TYR LEU HIS          
SEQRES   8 D  124  PRO LYS ASP GLY VAL LEU PRO TYR GLN VAL ASN LYS GLY          
SEQRES   9 D  124  ARG GLU GLN VAL GLY ARG VAL LYS SER THR ILE GLY LYS          
SEQRES  10 D  124  ASN VAL ASN PRO ALA GLN VAL                                  
SEQRES   1 E   69  MET ILE LYS LYS GLY SER LEU VAL LYS ILE LEU ARG PRO          
SEQRES   2 E   69  GLU SER PHE TRP TYR ASN GLU VAL GLY THR VAL VAL ASN          
SEQRES   3 E   69  VAL GLU THR SER LYS VAL LEU TYR PRO VAL LEU VAL ARG          
SEQRES   4 E   69  PHE ASP LYS VAL ASN TYR SER GLY LEU ASN SER THR ASN          
SEQRES   5 E   69  PHE SER LEU ASP GLU LEU VAL GLU ILE LYS VAL GLU ILE          
SEQRES   6 E   69  LYS SER ASP THR                                              
SEQRES   1 F  155  LEU THR PRO CYS GLN GLN SER GLU ALA PHE HIS LYS ARG          
SEQRES   2 F  155  GLU ILE ASN GLU VAL ARG THR LEU GLU ASN ARG GLN ALA          
SEQRES   3 F  155  ASN TYR GLU ALA ASN SER PRO SER TYR LEU ALA LEU GLN          
SEQRES   4 F  155  SER GLN ILE ASP GLN VAL HIS LYS ARG PHE ASP LYS TYR          
SEQRES   5 F  155  GLY THR LEU LEU CYS GLY GLN ASP GLY LEU PRO HIS LEU          
SEQRES   6 F  155  ILE THR ASP GLY ASP TRP ARG HIS ALA ARG GLU PHE THR          
SEQRES   7 F  155  ILE PRO ALA LEU LEU PHE LEU TYR ILE THR GLY TRP ILE          
SEQRES   8 F  155  GLY TRP VAL GLY ARG SER TYR LEU LYS TYR THR LYS GLU          
SEQRES   9 F  155  THR LYS ASN PRO THR GLU GLN GLU ILE ILE LEU ASP VAL          
SEQRES  10 F  155  PRO MET ALA LEU LYS TYR MET LEU SER GLY PHE LEU TRP          
SEQRES  11 F  155  PRO LEU SER ALA TRP GLN GLU TYR ARG SER GLY GLN LEU          
SEQRES  12 F  155  LEU ALA LYS GLU ASP GLU ILE THR VAL SER PRO ARG              
SEQRES   1 I   32  MET SER ALA SER TYR LEU PRO SER ILE LEU VAL PRO THR          
SEQRES   2 I   32  VAL GLY LEU ILE LEU PRO PHE ALA SER MET ALA ILE LEU          
SEQRES   3 I   32  PHE ILE ALA ILE GLU LYS                                      
SEQRES   1 J   38  MET ASN LEU LYS LYS TYR LEU SER THR ALA PRO VAL VAL          
SEQRES   2 J   38  ALA THR LEU TRP LEU PHE LEU THR ALA GLY ILE LEU ILE          
SEQRES   3 J   38  GLU LEU ASN ARG PHE PHE PRO ASP SER LEU PHE TYR              
SEQRES   1 K   47  MET ILE SER ASN LEU VAL GLY VAL ALA VAL GLY ARG TYR          
SEQRES   2 K   47  ALA LEU GLY ARG SER ASP LEU THR GLN LEU ILE ALA SER          
SEQRES   3 K   47  MET CYS PHE GLY HIS ILE ILE GLY VAL GLY ILE VAL LEU          
SEQRES   4 K   47  GLY LEU SER ASN MET GLY VAL ILE                              
SEQRES   1 L  140  MET THR ASP TYR ILE LYS PRO TYR ASN ASN ASP PRO PHE          
SEQRES   2 L  140  VAL GLY HIS LEU ALA THR PRO ILE ASN SER SER SER LEU          
SEQRES   3 L  140  THR ARG ALA TYR LEU SER GLN LEU PRO ILE TYR ARG ARG          
SEQRES   4 L  140  GLY VAL SER PRO PHE LEU ARG GLY LEU GLU ILE GLY MET          
SEQRES   5 L  140  ALA HIS GLY TYR PHE LEU ILE GLY PRO PHE VAL GLN LEU          
SEQRES   6 L  140  GLY PRO LEU ARG ASN THR ASP ILE LYS TYR LEU ALA GLY          
SEQRES   7 L  140  LEU LEU SER ALA ILE GLY LEU ILE VAL ILE LEU THR LEU          
SEQRES   8 L  140  GLY MET LEU LEU TYR GLY ALA VAL SER PHE THR ASN ASP          
SEQRES   9 L  140  SER GLN ASP LEU GLU SER VAL ASP GLY TRP ARG GLN LEU          
SEQRES  10 L  140  ALA SER GLY PHE LEU LEU GLY ALA VAL GLY GLY ALA GLY          
SEQRES  11 L  140  PHE ALA TYR LEU LEU LEU THR LEU PHE SER                      
SEQRES   1 M   29  MET ILE THR ASP ASN GLN VAL PHE VAL ALA LEU ILE MET          
SEQRES   2 M   29  ALA LEU VAL CYS GLY TYR LEU ALA VAL LYS LEU ALA LYS          
SEQRES   3 M   29  GLN LEU ALA                                                  
SEQRES   1 O   98  SER SER LEU ARG MET PHE GLU VAL SER ASP GLY GLU PRO          
SEQRES   2 O   98  TYR PRO LEU ASN PRO ALA VAL ILE PHE ILE ALA LEU ILE          
SEQRES   3 O   98  GLY TRP SER ALA VAL ALA ALA ILE PRO SER ASN ILE PRO          
SEQRES   4 O   98  VAL LEU GLY GLY THR GLY LEU THR GLN ALA PHE LEU ALA          
SEQRES   5 O   98  SER ILE GLN ARG LEU LEU ALA GLN TYR PRO THR GLY PRO          
SEQRES   6 O   98  LYS LEU ASP ASP PRO PHE TRP PHE TYR LEU ILE VAL TYR          
SEQRES   7 O   98  HIS VAL GLY LEU PHE ALA LEU LEU ILE PHE GLY GLN ILE          
SEQRES   8 O   98  GLY TYR ALA GLY TYR ALA LYS                                  
HET    CLA  2 601      25                                                       
HET    CLA  2 602      25                                                       
HET    CLA  2 603      25                                                       
HET    CLA  2 604      25                                                       
HET    CLA  2 605      25                                                       
HET    CLA  2 606      25                                                       
HET    CLA  2 607      25                                                       
HET    CLA  2 608      25                                                       
HET    CLA  2 610      25                                                       
HET    CLA  2 611      25                                                       
HET    CLA  2 612      25                                                       
HET    CLA  2 613      25                                                       
HET    CLA  2 614      25                                                       
HET    CLA  2 615      25                                                       
HET    CLA  2 616      25                                                       
HET    CLA  3 601      25                                                       
HET    CLA  3 602      25                                                       
HET    CLA  3 603      25                                                       
HET    CLA  3 604      25                                                       
HET    CLA  3 606      25                                                       
HET    CLA  3 607      25                                                       
HET    CLA  3 608      25                                                       
HET    CLA  3 610      25                                                       
HET    CLA  3 611      25                                                       
HET    CLA  3 612      25                                                       
HET    CLA  3 614      25                                                       
HET    CLA  4 601      25                                                       
HET    CLA  4 602      25                                                       
HET    CLA  4 603      25                                                       
HET    CLA  4 604      25                                                       
HET    CLA  4 605      25                                                       
HET    CLA  4 606      25                                                       
HET    CLA  4 608      25                                                       
HET    CLA  4 609      25                                                       
HET    CLA  4 610      25                                                       
HET    CLA  4 611      25                                                       
HET    CLA  4 612      25                                                       
HET    CLA  4 615      25                                                       
HET    CLA  4 616      25                                                       
HET    CLA  A1011      50                                                       
HET    CLA  A1012      55                                                       
HET    CLA  A1013      55                                                       
HET    CLA  A1101      45                                                       
HET    CLA  A1102      25                                                       
HET    CLA  A1103      55                                                       
HET    CLA  A1104      55                                                       
HET    CLA  A1105      55                                                       
HET    CLA  A1106      55                                                       
HET    CLA  A1107      55                                                       
HET    CLA  A1108      25                                                       
HET    CLA  A1109      25                                                       
HET    CLA  A1110      25                                                       
HET    CLA  A1111      25                                                       
HET    CLA  A1112      25                                                       
HET    CLA  A1113      25                                                       
HET    CLA  A1114      46                                                       
HET    CLA  A1115      55                                                       
HET    CLA  A1116      55                                                       
HET    CLA  A1117      55                                                       
HET    CLA  A1118      25                                                       
HET    CLA  A1119      25                                                       
HET    CLA  A1120      25                                                       
HET    CLA  A1121      25                                                       
HET    CLA  A1122      25                                                       
HET    CLA  A1123      25                                                       
HET    CLA  A1124      25                                                       
HET    CLA  A1125      25                                                       
HET    CLA  A1126      55                                                       
HET    CLA  A1127      25                                                       
HET    CLA  A1128      25                                                       
HET    CLA  A1129      25                                                       
HET    CLA  A1130      55                                                       
HET    CLA  A1131      45                                                       
HET    CLA  A1132      25                                                       
HET    CLA  A1133      25                                                       
HET    CLA  A1134      25                                                       
HET    CLA  A1135      25                                                       
HET    CLA  A1136      25                                                       
HET    CLA  A1137      25                                                       
HET    CLA  A1138      25                                                       
HET    CLA  A1139      25                                                       
HET    CLA  A1140      25                                                       
HET    CLA  A1141      25                                                       
HET    PQN  A2001      33                                                       
HET    SF4  A3001       8                                                       
HET    BCR  A4002      40                                                       
HET    BCR  A4007      40                                                       
HET    BCR  A4008      40                                                       
HET    BCR  A4011      40                                                       
HET    BCR  A4017      40                                                       
HET    CLA  B1021      45                                                       
HET    CLA  B1022      25                                                       
HET    CLA  B1023      50                                                       
HET    CLA  B1201      25                                                       
HET    CLA  B1202      25                                                       
HET    CLA  B1203      25                                                       
HET    CLA  B1204      25                                                       
HET    CLA  B1205      25                                                       
HET    CLA  B1206      25                                                       
HET    CLA  B1207      25                                                       
HET    CLA  B1208      25                                                       
HET    CLA  B1209      25                                                       
HET    CLA  B1210      25                                                       
HET    CLA  B1211      25                                                       
HET    CLA  B1212      25                                                       
HET    CLA  B1214      25                                                       
HET    CLA  B1215      25                                                       
HET    CLA  B1216      25                                                       
HET    CLA  B1217      25                                                       
HET    CLA  B1218      25                                                       
HET    CLA  B1219      25                                                       
HET    CLA  B1220      25                                                       
HET    CLA  B1221      25                                                       
HET    CLA  B1222      25                                                       
HET    CLA  B1223      25                                                       
HET    CLA  B1224      55                                                       
HET    CLA  B1225      50                                                       
HET    CLA  B1226      55                                                       
HET    CLA  B1227      25                                                       
HET    CLA  B1228      25                                                       
HET    CLA  B1229      50                                                       
HET    CLA  B1230      47                                                       
HET    CLA  B1231      25                                                       
HET    CLA  B1232      65                                                       
HET    CLA  B1234      25                                                       
HET    CLA  B1235      25                                                       
HET    CLA  B1236      45                                                       
HET    CLA  B1237      55                                                       
HET    CLA  B1238      25                                                       
HET    CLA  B1239      25                                                       
HET    PQN  B2002      33                                                       
HET    BCR  B4005      40                                                       
HET    BCR  B4008      40                                                       
HET    SF4  C3002       8                                                       
HET    SF4  C3003       8                                                       
HET    CLA  F1301      45                                                       
HET    CLA  F1302      25                                                       
HET    BCR  I4018      40                                                       
HET    CLA  J1302      50                                                       
HET    CLA  K1401      25                                                       
HET    CLA  K1402      25                                                       
HET    CLA  L1501      25                                                       
HET    CLA  L1502      25                                                       
HET    CLA  L1503      25                                                       
HET    CLA  O1601      25                                                       
HET    CLA  O1602      25                                                       
HET    CLA  O1603      25                                                       
HETNAM     CLA CHLOROPHYLL A                                                    
HETNAM     PQN PHYLLOQUINONE                                                    
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     BCR BETA-CAROTENE                                                    
HETSYN     PQN VITAMIN K1; 2-METHYL-3-PHYTYL-1,4-NAPHTHOQUINONE                 
FORMUL  16  CLA    134(C55 H72 MG N4 O5 2+)                                     
FORMUL  99  PQN    2(C31 H46 O2)                                                
FORMUL  00  SF4    3(FE4 S4)                                                    
FORMUL  01  BCR    8(C40 H56)                                                   
HELIX    1 AA1 GLU 2   95  ARG 2  111  1                                  17    
HELIX    2 AA2 ARG 2  111  ALA 2  116  1                                   6    
HELIX    3 AA3 ALA 2  116  GLU 2  124  1                                   9    
HELIX    4 AA4 ASN 2  132  LEU 2  137  1                                   6    
HELIX    5 AA5 GLN 2  138  HIS 2  144  5                                   7    
HELIX    6 AA6 PHE 2  147  ILE 2  173  1                                  27    
HELIX    7 AA7 ASN 2  179  GLY 2  197  1                                  19    
HELIX    8 AA8 LYS 2  202  GLU 2  208  1                                   7    
HELIX    9 AA9 GLU 2  208  GLN 2  226  1                                  19    
HELIX   10 AB1 LYS 3   84  ALA 3   89  1                                   6    
HELIX   11 AB2 VAL 3   93  ALA 3   98  1                                   6    
HELIX   12 AB3 LYS 3  110  LEU 3  115  5                                   6    
HELIX   13 AB4 GLY 3  127  ILE 3  142  1                                  16    
HELIX   14 AB5 LYS 3  178  HIS 3  200  1                                  23    
HELIX   15 AB6 GLN 3  201  LEU 3  204  5                                   4    
HELIX   16 AB7 ASN 4  100  PHE 4  125  1                                  26    
HELIX   17 AB8 GLY 4  149  SER 4  173  1                                  25    
HELIX   18 AB9 ALA 4  216  PHE 4  240  1                                  25    
HELIX   19 AC1 PHE A   22  LYS A   27  1                                   6    
HELIX   20 AC2 SER A   32  ALA A   36  5                                   5    
HELIX   21 AC3 THR A   41  ASP A   51  1                                  11    
HELIX   22 AC4 ASP A   54  HIS A   58  5                                   5    
HELIX   23 AC5 SER A   61  GLY A   91  1                                  31    
HELIX   24 AC6 ASN A   96  ASN A  103  1                                   8    
HELIX   25 AC7 GLY A  119  ASN A  124  5                                   6    
HELIX   26 AC8 GLY A  139  SER A  147  1                                   9    
HELIX   27 AC9 GLU A  152  TRP A  174  1                                  23    
HELIX   28 AD1 LYS A  183  PHE A  187  5                                   5    
HELIX   29 AD2 ASN A  189  LEU A  198  1                                  10    
HELIX   30 AD3 LEU A  201  TRP A  209  1                                   9    
HELIX   31 AD4 LEU A  235  ASN A  242  1                                   8    
HELIX   32 AD5 ASN A  242  TYR A  250  1                                   9    
HELIX   33 AD6 VAL A  258  LEU A  263  1                                   6    
HELIX   34 AD7 ASN A  264  SER A  269  5                                   6    
HELIX   35 AD8 TRP A  286  GLY A  305  1                                  20    
HELIX   36 AD9 SER A  317  GLU A  323  1                                   7    
HELIX   37 AE1 GLY A  336  THR A  342  1                                   7    
HELIX   38 AE2 SER A  344  MET A  370  1                                  27    
HELIX   39 AE3 ASP A  379  ASP A  412  1                                  34    
HELIX   40 AE4 ASN A  420  HIS A  429  1                                  10    
HELIX   41 AE5 HIS A  429  HIS A  447  1                                  19    
HELIX   42 AE6 HIS A  447  GLY A  462  1                                  16    
HELIX   43 AE7 ARG A  463  PHE A  468  1                                   6    
HELIX   44 AE8 PHE A  468  GLN A  474  1                                   7    
HELIX   45 AE9 ALA A  480  LEU A  489  1                                  10    
HELIX   46 AF1 ALA A  527  TYR A  552  1                                  26    
HELIX   47 AF2 SER A  583  VAL A  614  1                                  32    
HELIX   48 AF3 ASN A  640  ASP A  645  1                                   6    
HELIX   49 AF4 GLN A  650  ILE A  655  1                                   6    
HELIX   50 AF5 SER A  663  LEU A  683  1                                  21    
HELIX   51 AF6 GLY A  686  LEU A  704  1                                  19    
HELIX   52 AF7 SER A  716  GLY A  731  1                                  16    
HELIX   53 AF8 ILE A  733  LEU A  741  1                                   9    
HELIX   54 AF9 ALA A  742  VAL A  747  1                                   6    
HELIX   55 AG1 SER B    9  SER B   14  1                                   6    
HELIX   56 AG2 THR B   18  THR B   27  1                                  10    
HELIX   57 AG3 ASP B   30  HIS B   34  5                                   5    
HELIX   58 AG4 THR B   38  GLN B   71  1                                  34    
HELIX   59 AG5 ASN B   73  ASN B   80  1                                   8    
HELIX   60 AG6 GLY B   97  THR B  105  1                                   9    
HELIX   61 AG7 GLU B  132  GLN B  156  1                                  25    
HELIX   62 AG8 SER B  162  PHE B  166  5                                   5    
HELIX   63 AG9 SER B  171  HIS B  176  1                                   6    
HELIX   64 AH1 GLY B  182  HIS B  191  1                                  10    
HELIX   65 AH2 ALA B  196  ARG B  201  1                                   6    
HELIX   66 AH3 LEU B  220  THR B  225  1                                   6    
HELIX   67 AH4 LEU B  268  GLY B  286  1                                  19    
HELIX   68 AH5 HIS B  287  GLY B  294  1                                   8    
HELIX   69 AH6 TYR B  321  SER B  327  1                                   7    
HELIX   70 AH7 SER B  327  HIS B  349  1                                  23    
HELIX   71 AH8 THR B  365  ASP B  395  1                                  31    
HELIX   72 AH9 VAL B  405  LEU B  410  1                                   6    
HELIX   73 AI1 HIS B  412  PHE B  444  1                                  33    
HELIX   74 AI2 PRO B  455  THR B  464  1                                  10    
HELIX   75 AI3 SER B  481  ALA B  486  1                                   6    
HELIX   76 AI4 TRP B  491  ASN B  500  1                                  10    
HELIX   77 AI5 GLY B  511  ASP B  538  1                                  28    
HELIX   78 AI6 MET B  545  PHE B  551  5                                   7    
HELIX   79 AI7 SER B  569  HIS B  593  1                                  25    
HELIX   80 AI8 HIS B  593  GLN B  601  1                                   9    
HELIX   81 AI9 ASN B  603  ALA B  605  5                                   3    
HELIX   82 AJ1 GLN B  606  SER B  611  1                                   6    
HELIX   83 AJ2 TYR B  613  ASP B  620  1                                   8    
HELIX   84 AJ3 SER B  626  ASN B  631  1                                   6    
HELIX   85 AJ4 GLY B  632  ASN B  634  5                                   3    
HELIX   86 AJ5 LEU B  641  SER B  664  1                                  24    
HELIX   87 AJ6 ARG B  666  THR B  683  1                                  18    
HELIX   88 AJ7 LEU B  685  ILE B  689  5                                   5    
HELIX   89 AJ8 SER B  699  PHE B  731  1                                  33    
HELIX   90 AJ9 THR C   15  CYS C   21  1                                   7    
HELIX   91 AK1 ARG C   44  CYS C   48  5                                   5    
HELIX   92 AK2 ARG C   53  CYS C   58  1                                   6    
HELIX   93 AK3 THR C   73  GLY C   78  1                                   6    
HELIX   94 AK4 LEU D   19  GLU D   25  1                                   7    
HELIX   95 AK5 ARG D   61  PHE D   76  1                                  16    
HELIX   96 AK6 SER F   37  ASN F   57  1                                  21    
HELIX   97 AK7 SER F   62  TYR F   65  5                                   4    
HELIX   98 AK8 LEU F   66  LEU F   85  1                                  20    
HELIX   99 AK9 ASP F  100  ALA F  104  5                                   5    
HELIX  100 AL1 ILE F  109  THR F  132  1                                  24    
HELIX  101 AL2 PRO F  138  ILE F  144  1                                   7    
HELIX  102 AL3 VAL F  147  MET F  154  1                                   8    
HELIX  103 AL4 LEU F  155  GLY F  157  5                                   3    
HELIX  104 AL5 TRP F  160  LYS F  176  1                                  17    
HELIX  105 AL6 LEU I    6  ILE I    9  5                                   4    
HELIX  106 AL7 LEU I   10  LYS I   32  1                                  23    
HELIX  107 AL8 ASN J    2  SER J    8  1                                   7    
HELIX  108 AL9 THR J    9  ASN J   29  1                                  21    
HELIX  109 AM1 ILE K   15  ALA K   27  1                                  13    
HELIX  110 AM2 ARG K   30  GLN K   35  5                                   6    
HELIX  111 AM3 LEU K   36  SER K   55  1                                  20    
HELIX  112 AM4 TYR L    4  ASP L   11  1                                   8    
HELIX  113 AM5 SER L   24  LEU L   34  1                                  11    
HELIX  114 AM6 PRO L   35  ARG L   38  5                                   4    
HELIX  115 AM7 LEU L   48  LEU L   58  1                                  11    
HELIX  116 AM8 ILE L   59  LEU L   65  1                                   7    
HELIX  117 AM9 ILE L   73  SER L  100  1                                  28    
HELIX  118 AN1 VAL L  111  ALA L  132  1                                  22    
HELIX  119 AN2 THR M    3  GLN M   27  1                                  25    
HELIX  120 AN3 VAL O   58  GLU O   62  5                                   5    
HELIX  121 AN4 LEU O   66  ALA O   82  1                                  17    
HELIX  122 AN5 ASN O   87  GLY O   92  1                                   6    
HELIX  123 AN6 GLN O  110  THR O  113  5                                   4    
HELIX  124 AN7 GLY O  114  PHE O  133  1                                  20    
SHEET    1 AA1 2 THR A 512  VAL A 513  0                                        
SHEET    2 AA1 2 ILE A 517  MET A 519 -1  O  ALA A 518   N  THR A 512           
SHEET    1 AA2 2 GLY A 616  VAL A 618  0                                        
SHEET    2 AA2 2 ILE A 624  HIS A 626 -1  O  SER A 625   N  THR A 617           
SHEET    1 AA3 2 LEU B  87  ALA B  90  0                                        
SHEET    2 AA3 2 ILE B 113  TYR B 115 -1  O  SER B 114   N  HIS B  89           
SHEET    1 AA4 2 THR C   4  ILE C   7  0                                        
SHEET    2 AA4 2 ILE C  65  TYR C  68 -1  O  ARG C  66   N  LYS C   6           
SHEET    1 AA5 2 MET C  28  PRO C  30  0                                        
SHEET    2 AA5 2 GLN C  38  ALA C  40 -1  O  MET C  39   N  VAL C  29           
SHEET    1 AA6 3 TYR D  28  TRP D  32  0                                        
SHEET    2 AA6 3 ASP D  80  ARG D  85 -1  O  ILE D  83   N  ALA D  29           
SHEET    3 AA6 3 GLU D  91  VAL D  92 -1  O  VAL D  92   N  TYR D  84           
SHEET    1 AA7 2 HIS D  38  GLU D  41  0                                        
SHEET    2 AA7 2 ALA D  47  MET D  50 -1  O  ALA D  48   N  PHE D  40           
SHEET    1 AA8 4 LEU E   7  VAL E   8  0                                        
SHEET    2 AA8 4 GLY E  22  VAL E  24 -1  O  GLY E  22   N  VAL E   8           
SHEET    3 AA8 4 VAL E  36  ARG E  39 -1  O  ARG E  39   N  THR E  23           
SHEET    4 AA8 4 SER E  50  PHE E  53 -1  O  PHE E  53   N  VAL E  36           
SSBOND   1 CYS F   34    CYS F   87                          1555   1555  2.02  
LINK         NH1 ARG 2 210                 CHA CLA 2 607     1555   1555  1.43  
LINK         OE1 GLN A 120                MG   CLA A1107     1555   1555  3.00  
LINK         NE2 HIS B 419                 C1A CLA B1228     1555   1555  1.44  
SITE     1 AC1  1 CLA 2 611                                                     
SITE     1 AC2  3 GLN 2 226  GLN 2 236  LEU 2 237                               
SITE     1 AC3  2 ARG 2 213  TRP 3 139                                          
SITE     1 AC4  4 HIS 2 109  MET 2 216  PHE 2 219  CLA 2 612                    
SITE     1 AC5  4 GLY 2 119  ALA 2 122  GLN 2 123  CLA 2 613                    
SITE     1 AC6  1 ARG 2 210                                                     
SITE     1 AC7  1 GLN 2 154                                                     
SITE     1 AC8  2 ARG 2 111  CLA 2 601                                          
SITE     1 AC9  3 HIS 2 109  LEU 2 158  CLA 2 605                               
SITE     1 AD1  2 CLA 2 606  GLN 4 249                                          
SITE     1 AD2  1 CLA 4 609                                                     
SITE     1 AD3  2 MET 3 180  GLN 3 181                                          
SITE     1 AD4  5 CYS 3  86  ALA 3  89  MET 3  90  GLU 3 184                    
SITE     2 AD4  5 ASN 3 187                                                     
SITE     1 AD5  5 ILE 3 193  GLY 3 197  HIS 3 200  GLN 3 201                    
SITE     2 AD5  5 CLA K1402                                                     
SITE     1 AD6  4 THR 3  70  GLU 3  71  ARG 3 189  CLA 3 607                    
SITE     1 AD7  5 LEU 3  94  ILE 3  97  ALA 3  98  GLN 3  99                    
SITE     2 AD7  5 PHE 3 101                                                     
SITE     1 AD8  3 GLU 3  61  ARG 3 179  CLA 3 604                               
SITE     1 AD9  1 ILE 3 193                                                     
SITE     1 AE1  2 LEU 3 115  ASN 3 126                                          
SITE     1 AE2  2 ARG 3  87  PHE 3 141                                          
SITE     1 AE3  3 GLU 3  80  VAL 3  88  LEU 3 134                               
SITE     1 AE4  1 CLA A1108                                                     
SITE     1 AE5  2 ARG 4 111  CLA 4 616                                          
SITE     1 AE6  2 MET 4 114  CLA 4 608                                          
SITE     1 AE7  1 LEU 4 102                                                     
SITE     1 AE8  3 ASN 4 109  CLA 4 612  PHE F 158                               
SITE     1 AE9  4 HIS 4 119  PHE 4 120  THR 4 123  GLN 4 127                    
SITE     1 AF1  1 CLA 4 602                                                     
SITE     1 AF2  3 CLA 2 614  ARG 4 226  LEU 4 227                               
SITE     1 AF3  1 VAL 4 170                                                     
SITE     1 AF4  4 VAL 4 112  LEU 4 161  LEU 4 164  CLA 4 605                    
SITE     1 AF5  5 GLN 4 103  GLU 4 104  ILE 4 107  ARG 4 218                    
SITE     2 AF5  5 GLU 4 221                                                     
SITE     1 AF6  1 CLA 4 601                                                     
SITE     1 AF7 17 TYR A 596  ASN A 597  ILE A 601  PHE A 604                    
SITE     2 AF7 17 LEU A 647  GLN A 650  PHE A 669  HIS A 673                    
SITE     3 AF7 17 TRP A 676  GLY A 732  THR A 735  THR A 736                    
SITE     4 AF7 17 PHE A 739  CLA A1012  LEU B 622  CLA B1021                    
SITE     5 AF7 17 CLA B1022                                                     
SITE     1 AF8 18 LEU A 670  GLY A 671  HIS A 673  PHE A 674                    
SITE     2 AF8 18 TRP A 676  ALA A 677  CLA A1011  CLA A1013                    
SITE     3 AF8 18 BCR A4011  LEU B 432  VAL B 436  ASP B 439                    
SITE     4 AF8 18 PHE B 579  TRP B 580  ASN B 583  TRP B 587                    
SITE     5 AF8 18 LEU B 614  CLA B1021                                          
SITE     1 AF9 16 PHE A 674  ALA A 677  PHE A 678  LEU A 680                    
SITE     2 AF9 16 MET A 681  TYR A 689  TRP A 690  CLA A1012                    
SITE     3 AF9 16 SER B 424  LEU B 425  GLY B 428  PHE B 429                    
SITE     4 AF9 16 LEU B 523  LEU B 576  TRP B 580  BCR B4005                    
SITE     1 AG1  6 TRP A  44  ILE A  45  HIS A  49  CLA A1102                    
SITE     2 AG1  6 TYR J   6  PRO J  11                                          
SITE     1 AG2  3 ALA A  52  HIS A  53  CLA A1101                               
SITE     1 AG3 13 HIS A  53  PHE A  55  ILE A  69  HIS A  73                    
SITE     2 AG3 13 GLN A  76  ILE A  80  TRP A 345  HIS A 346                    
SITE     3 AG3 13 ASN A 348  LEU A 349  ASN A 352  LEU A 356                    
SITE     4 AG3 13 CLA A1104                                                     
SITE     1 AG4  6 GLN A  76  ILE A  80  TRP A  83  CLA A1103                    
SITE     2 AG4  6 CLA A1126  CLA A1128                                          
SITE     1 AG5  9 ILE A  82  GLY A  86  PHE A  89  HIS A  90                    
SITE     2 AG5  9 PHE A  94  GLN A 112  TRP A 115  CLA A1106                    
SITE     3 AG5  9 CLA A1107                                                     
SITE     1 AG6 16 TRP A  83  MET A  87  HIS A  90  ALA A 111                    
SITE     2 AG6 16 GLN A 112  GLN A 135  ILE A 136  THR A 137                    
SITE     3 AG6 16 SER A 138  LEU A 140  ALA A 664  TYR A 665                    
SITE     4 AG6 16 CLA A1105  CLA A1107  CLA A1126  BCR A4011                    
SITE     1 AG7 10 GLN A 112  VAL A 113  VAL A 114  TRP A 115                    
SITE     2 AG7 10 GLN A 120  ILE A 134  CLA A1105  CLA A1106                    
SITE     3 AG7 10 CLA B1230  ILE J  26                                          
SITE     1 AG8  4 CLA 3 614  ALA A 172  PHE A 175  HIS A 176                    
SITE     1 AG9  5 SER A  21  LYS A  24  TRP A  25  TRP A 174                    
SITE     2 AG9  5 HIS A 178                                                     
SITE     1 AH1  2 VAL A   9  HIS A 196                                          
SITE     1 AH2  3 PHE A  70  HIS A 196  HIS A 197                               
SITE     1 AH3  4 THR A 158  HIS A 212  CLA A1114  BCR A4002                    
SITE     1 AH4  5 ILE A 214  HIS A 215  PHE A 253  GLY A 256                    
SITE     2 AH4  5 LEU A 257                                                     
SITE     1 AH5  7 ILE 2 233  PHE 3 123  GLN A 154  VAL A 157                    
SITE     2 AH5  7 HIS A 237  LEU A 241  CLA A1112                               
SITE     1 AH6 13 PHE A 260  TRP A 265  TYR A 268  LEU A 272                    
SITE     2 AH6 13 PHE A 274  HIS A 292  LEU A 295  ALA A 296                    
SITE     3 AH6 13 VAL A 299  ASN A 497  CLA A1116  LEU K  52                    
SITE     4 AH6 13 CLA K1401                                                     
SITE     1 AH7 15 THR A 273  PHE A 274  LEU A 285  ASP A 289                    
SITE     2 AH7 15 HIS A 292  HIS A 293  ALA A 296  ILE A 297                    
SITE     3 AH7 15 HIS A 366  MET A 370  ALA A 502  CLA A1115                    
SITE     4 AH7 15 CLA A1117  CLA A1125  CLA A1133                               
SITE     1 AH8 15 LEU A 143  LEU A 202  GLY A 205  SER A 206                    
SITE     2 AH8 15 TRP A 209  GLN A 213  HIS A 293  HIS A 294                    
SITE     3 AH8 15 ILE A 297  PHE A 301  VAL A 363  MET A 367                    
SITE     4 AH8 15 PRO A 372  TYR A 373  CLA A1116                               
SITE     1 AH9  1 HIS A 306                                                     
SITE     1 AI1  4 LEU A 198  ALA A 304  TYR A 308  CLA A1123                    
SITE     1 AI2  2 MET A 307  HIS A 316                                          
SITE     1 AI3  2 HIS A 316  HIS A 325                                          
SITE     1 AI4  4 HIS A 334  LEU A 337  VAL A 422  BCR A4007                    
SITE     1 AI5  7 VAL A 190  LEU A 194  ILE A 318  LEU A 341                    
SITE     2 AI5  7 ILE A 351  ASN A 352  CLA A1119                               
SITE     1 AI6  7 ILE A 361  MET A 391  ILE A 398  ILE A 539                    
SITE     2 AI6  7 THR A 542  THR A 543  BCR A4008                               
SITE     1 AI7  5 HIS A 366  ALA A 369  MET A 370  CLA A1116                    
SITE     2 AI7  5 CLA A1133                                                     
SITE     1 AI8 14 TRP A  83  THR A 137  SER A 138  SER A 385                    
SITE     2 AI8 14 THR A 388  HIS A 389  TRP A 392  PHE A 396                    
SITE     3 AI8 14 ILE A 733  TRP A 737  CLA A1104  CLA A1106                    
SITE     4 AI8 14 CLA A1127  BCR A4011                                          
SITE     1 AI9  5 MET A 367  HIS A 389  HIS A 390  ILE A 393                    
SITE     2 AI9  5 CLA A1126                                                     
SITE     1 AJ1  7 HIS A  53  LEU A 349  PHE A 396  GLY A 400                    
SITE     2 AJ1  7 HIS A 404  TRP A 585  CLA A1104                               
SITE     1 AJ2  8 LEU A 329  VAL A 422  ARG A 425  MET A 426                    
SITE     2 AJ2  8 HIS A 429  ILE A 433  HIS A 436  CLA A1130                    
SITE     1 AJ3  9 ALA A 432  HIS A 436  TRP A 439  CLA A1129                    
SITE     2 AJ3  9 ALA B 679  PRO B 684  PRO L  20  ILE L  21                    
SITE     3 AJ3  9 ASN L  22                                                     
SITE     1 AJ4  8 TRP A 439  ILE A 442  PHE A 443  HIS A 447                    
SITE     2 AJ4  8 CLA A1132  CLA B1237  BCR I4018  LEU L  65                    
SITE     1 AJ5  7 GLY A 450  LEU A 451  ILE A 453  HIS A 454                    
SITE     2 AJ5  7 CLA A1131  BCR I4018  LEU L  65                               
SITE     1 AJ6  6 ILE A 483  ILE A 486  HIS A 487  CLA A1116                    
SITE     2 AJ6  6 CLA A1125  BCR A4008                                          
SITE     1 AJ7  1 THR A 494                                                     
SITE     1 AJ8  5 TYR A 368  HIS A 532  HIS A 535  HIS A 605                    
SITE     2 AJ8  5 PHE A 606                                                     
SITE     1 AJ9  4 LEU A 444  PHE A 479  HIS A 533  CLA A1137                    
SITE     1 AK1  4 LEU A 437  VAL A 440  HIS A 540  CLA A1136                    
SITE     1 AK2  6 ILE A 697  HIS A 701  VAL A 706  CLA A1139                    
SITE     2 AK2  6 CLA B1229  BCR B4005                                          
SITE     1 AK3  7 THR A  42  ILE A  45  HIS A 701  VAL A 706                    
SITE     2 AK3  7 PRO A 708  PRO A 712  CLA A1138                               
SITE     1 AK4  5 TRP A  46  VAL A 675  PHE A 678  VAL A 723                    
SITE     2 AK4  5 HIS A 727                                                     
SITE     1 AK5  2 GLY A 327  PRO A 328                                          
SITE     1 AK6  8 MET A 681  PHE A 682  SER A 685  ARG A 687                    
SITE     2 AK6  8 TRP A 690  ALA A 714  LEU A 715  BCR B4005                    
SITE     1 AK7  6 CYS A 571  CYS A 580  CYS B 557  THR B 565                    
SITE     2 AK7  6 CYS B 566  ARG B 704                                          
SITE     1 AK8  3 GLY A 162  SER A 208  CLA A1112                               
SITE     1 AK9  4 LEU A 337  ILE A 340  TYR A 408  CLA A1122                    
SITE     1 AL1  8 ALA A 354  SER A 358  ALA A 401  LEU A 546                    
SITE     2 AL1  8 LEU A 547  VAL A 550  CLA A1124  CLA A1133                    
SITE     1 AL2 12 PHE A 674  VAL A 675  LEU A 730  ILE A 733                    
SITE     2 AL2 12 ALA A 734  TRP A 737  CLA A1012  CLA A1106                    
SITE     3 AL2 12 CLA A1126  PHE B 429  LEU B 432  CLA B1229                    
SITE     1 AL3 10 TRP B 646  MET B 647  PHE B 650  TRP B 669                    
SITE     2 AL3 10 CLA B1023  CLA B1206  CLA B1224  CLA B1237                    
SITE     3 AL3 10 CLA B1239  PQN B2002                                          
SITE     1 AL4 15 LEU A 647  TRP A 648  CLA A1011  CLA A1012                    
SITE     2 AL4 15 PHE B 590  LEU B 622  SER B 626  ILE B 630                    
SITE     3 AL4 15 HIS B 652  TRP B 655  TYR B 715  THR B 718                    
SITE     4 AL4 15 TYR B 719  PHE B 722  CLA B1022                               
SITE     1 AL5  8 PHE A 449  ASN A 597  TYR A 728  CLA A1011                    
SITE     2 AL5  8 TRP B 655  ALA B 656  CLA B1021  CLA B1023                    
SITE     1 AL6 19 ASN A 438  CYS A 441  ILE A 442  GLY A 445                    
SITE     2 AL6 19 MET A 446  PHE A 449  PHE A 537  ILE A 545                    
SITE     3 AL6 19 PHE A 593  TRP A 594  BCR A4017  ALA B 656                    
SITE     4 AL6 19 PHE B 659  MET B 660  ILE B 663  TYR B 668                    
SITE     5 AL6 19 TRP B 669  LEU B 672  CLA B1022                               
SITE     1 AL7  2 HIS B  29  CLA B1203                                          
SITE     1 AL8  6 ILE B  46  SER B  49  HIS B  50  HIS B  53                    
SITE     2 AL8  6 LEU B 332  CLA B1226                                          
SITE     1 AL9  3 HIS B  53  CLA B1201  CLA B1226                               
SITE     1 AM1  5 LEU B  59  GLY B  63  PHE B  66  HIS B  67                    
SITE     2 AM1  5 BCR I4018                                                     
SITE     1 AM2  6 ASN B  64  GLY B 117  VAL B 118  TRP B 644                    
SITE     2 AM2  6 CLA B1207  CLA B1224                                          
SITE     1 AM3  7 LEU A 461  BCR A4017  ASP B  93  HIS B  95                    
SITE     2 AM3  7 PHE B  96  VAL B 643  CLA B1207                               
SITE     1 AM4  9 HIS B  67  ALA B  88  HIS B  89  SER B 114                    
SITE     2 AM4  9 TYR B 115  SER B 116  GLY B 117  CLA B1205                    
SITE     3 AM4  9 CLA B1206                                                     
SITE     1 AM5  3 HIS B 154  TRP B 165  CLA B1210                               
SITE     1 AM6  2 HIS B 175  CLA B1210                                          
SITE     1 AM7  7 PHE B  47  TRP B 165  ARG B 172  HIS B 176                    
SITE     2 AM7  7 LEU B 180  CLA B1208  CLA B1209                               
SITE     1 AM8  3 HIS B 191  VAL B 195  TRP B 207                               
SITE     1 AM9  4 HIS B  95  LEU I  16  BCR I4018  PRO L  67                    
SITE     1 AN1  3 ASP B 270  HIS B 273  ALA B 277                               
SITE     1 AN2  6 TRP B 121  TRP B 188  ASP B 270  MET B 271                    
SITE     2 AN2  6 HIS B 274  HIS B 275                                          
SITE     1 AN3  5 ASN B 174  HIS B 175  ALA B 178  HIS B 287                    
SITE     2 AN3  5 ARG B 290                                                     
SITE     1 AN4  3 HIS B 287  THR B 291  ASN B 292                               
SITE     1 AN5  2 LEU B 173  SER B 338                                          
SITE     1 AN6  4 SER B 344  ILE B 381  CLA B1236  BCR B4008                    
SITE     1 AN7  2 LEU B 345  HIS B 349                                          
SITE     1 AN8 12 BCR A4017  TRP B  60  VAL B 118  ALA B 368                    
SITE     2 AN8 12 THR B 371  HIS B 372  TYR B 375  ILE B 376                    
SITE     3 AN8 12 ILE B 716  TYR B 719  CLA B1205  CLA B1225                    
SITE     1 AN9 12 TRP B  60  THR B  61  TYR B 119  TRP B 121                    
SITE     2 AN9 12 TRP B 122  THR B 343  TYR B 356  HIS B 372                    
SITE     3 AN9 12 HIS B 373  ILE B 376  LEU B 380  CLA B1224                    
SITE     1 AO1 14 ALA B  26  HIS B  29  ASP B  30  LEU B 336                    
SITE     2 AO1 14 LEU B 379  GLY B 383  HIS B 387  ILE B 390                    
SITE     3 AO1 14 TYR B 553  PHE B 574  MET B 578  VAL B 709                    
SITE     4 AO1 14 CLA B1202  CLA B1203                                          
SITE     1 AO2  4 MET B 409  HIS B 412  HIS B 419  CLA B1228                    
SITE     1 AO3  2 HIS B 419  CLA B1227                                          
SITE     1 AO4 12 CLA A1138  BCR A4011  TRP B 422  PHE B 426                    
SITE     2 AO4 12 PHE B 429  HIS B 430  CLA B1230  BCR B4005                    
SITE     3 AO4 12 PHE F 107  LEU F 115  TYR F 116  TRP F 123                    
SITE     1 AO5 13 VAL A 118  CLA A1107  PHE B 429  GLY B 433                    
SITE     2 AO5 13 VAL B 436  HIS B 437  VAL B 440  LYS B 449                    
SITE     3 AO5 13 CLA B1229  BCR B4005  LEU J  25  LEU J  28                    
SITE     4 AO5 13 ASN J  29                                                     
SITE     1 AO6  6 TYR B 351  ILE B 461  ILE B 510  HIS B 518                    
SITE     2 AO6  6 TYR B 591  TRP B 592                                          
SITE     1 AO7  4 LEU B 427  PHE B 457  PHE B 515  CLA B1236                    
SITE     1 AO8  5 LEU B 420  LEU B 525  HIS B 526  CLA B1222                    
SITE     2 AO8  5 CLA B1235                                                     
SITE     1 AO9  8 SER A 435  TRP A 439  ILE A 442  CLA A1131                    
SITE     2 AO9  8 BCR A4017  LEU B 676  ILE B 689  CLA B1238                    
SITE     1 AP1  3 TRP B 691  PRO B 695  CLA B1237                               
SITE     1 AP2  5 BCR A4017  PHE B 661  VAL B 706  HIS B 710                    
SITE     2 AP2  5 PQN B2002                                                     
SITE     1 AP3 10 BCR A4017  MET B 660  PHE B 661  SER B 664                    
SITE     2 AP3 10 TRP B 665  TRP B 669  ALA B 697  LEU B 698                    
SITE     3 AP3 10 ALA B 703  CLA B1239                                          
SITE     1 AP4  9 CLA A1013  CLA A1138  PQN A2001  CLA B1229                    
SITE     2 AP4  9 CLA B1230  LEU F 115  TRP F 123  CLA F1301                    
SITE     3 AP4  9 LEU J  25                                                     
SITE     1 AP5  6 PHE B 330  ALA B 337  VAL B 341  PHE B 385                    
SITE     2 AP5  6 GLY B 388  CLA B1222                                          
SITE     1 AP6 11 CYS C  21  PRO C  22  VAL C  25  LEU C  26                    
SITE     2 AP6 11 CYS C  48  GLY C  50  CYS C  51  LYS C  52                    
SITE     3 AP6 11 ARG C  53  CYS C  54  VAL C  67                               
SITE     1 AP7 12 CYS C  11  ILE C  12  GLY C  13  CYS C  14                    
SITE     2 AP7 12 THR C  15  GLN C  16  MET C  28  ALA C  40                    
SITE     3 AP7 12 CYS C  58  PRO C  59  SER C  64  ILE C  65                    
SITE     1 AP8  5 BCR B4005  ILE F 121  GLY F 122  TRP J  17                    
SITE     2 AP8  5 LEU J  25                                                     
SITE     1 AP9  3 ASP F  98  GLY F  99  ASP F 100                               
SITE     1 AQ1  6 CLA A1131  CLA A1132  CLA B1204  CLA B1212                    
SITE     2 AQ1  6 PRO I  19  PHE I  20                                          
SITE     1 AQ2  6 TRP A 115  LEU J  20  GLY J  23  ILE J  24                    
SITE     2 AQ2  6 GLU J  27  ARG J  30                                          
SITE     1 AQ3  4 CLA A1115  ILE K  45  GLY K  49  GLY K  53                    
SITE     1 AQ4  6 CLA 3 603  PHE A 261  LEU A 263  LEU K  18                    
SITE     2 AQ4  6 ARG K  25  HIS K  44                                          
SITE     1 AQ5  5 TYR L  30  GLN L  33  LEU L  34  PRO L  35                    
SITE     2 AQ5  5 GLU L  49                                                     
SITE     1 AQ6  4 LEU B 685  ILE L  36  HIS L  54  PHE L  57                    
SITE     1 AQ7  4 TYR L  56  PHE L  57  GLY L  60  LEU L 136                    
SITE     1 AQ8  1 ILE O  71                                                     
SITE     1 AQ9  3 LEU O 125  HIS O 129  PHE O 133                               
CRYST1  163.130  213.520  349.580  90.00  90.00  90.00 C 2 2 21     16          
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      0.006130  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004683  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002861        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system