GenomeNet

Database: PDB
Entry: 3LW5
LinkDB: 3LW5
Original site: 3LW5 
HEADER    PHOTOSYNTHESIS                          23-FEB-10   3LW5              
TITLE     IMPROVED MODEL OF PLANT PHOTOSYSTEM I                                 
CAVEAT     3LW5    THE CHIRALITY ERROR AT THE CA CENTER OF TYR H 68.            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A1;            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 21-758;                                           
COMPND   5 SYNONYM: PSAA, PSI-A;                                                
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A2;            
COMPND   8 CHAIN: B;                                                            
COMPND   9 SYNONYM: PSAB, PSI-B;                                                
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: PHOTOSYSTEM I IRON-SULFUR CENTER;                          
COMPND  12 CHAIN: C;                                                            
COMPND  13 SYNONYM: PHOTOSYSTEM I SUBUNIT VII, 9 KDA POLYPEPTIDE, PSI-C, PSAC;  
COMPND  14 MOL_ID: 4;                                                           
COMPND  15 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN;                          
COMPND  16 CHAIN: D;                                                            
COMPND  17 SYNONYM: PHOTOSYSTEM I SUBUNIT PSAD;                                 
COMPND  18 MOL_ID: 5;                                                           
COMPND  19 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN;                          
COMPND  20 CHAIN: E;                                                            
COMPND  21 MOL_ID: 6;                                                           
COMPND  22 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT III, CHLOROPLASTIC;  
COMPND  23 CHAIN: F;                                                            
COMPND  24 SYNONYM: LIGHT-HARVESTING COMPLEX I 17 KDA PROTEIN, PSI-F;           
COMPND  25 MOL_ID: 7;                                                           
COMPND  26 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN;                          
COMPND  27 CHAIN: G;                                                            
COMPND  28 MOL_ID: 8;                                                           
COMPND  29 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN;                          
COMPND  30 CHAIN: H;                                                            
COMPND  31 MOL_ID: 9;                                                           
COMPND  32 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT VIII;                
COMPND  33 CHAIN: I;                                                            
COMPND  34 FRAGMENT: RESIDUES 1-30;                                             
COMPND  35 SYNONYM: PSI-I;                                                      
COMPND  36 MOL_ID: 10;                                                          
COMPND  37 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT IX;                  
COMPND  38 CHAIN: J;                                                            
COMPND  39 SYNONYM: PSI-J;                                                      
COMPND  40 MOL_ID: 11;                                                          
COMPND  41 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT X PSAK;              
COMPND  42 CHAIN: K;                                                            
COMPND  43 MOL_ID: 12;                                                          
COMPND  44 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN;                          
COMPND  45 CHAIN: L;                                                            
COMPND  46 MOL_ID: 13;                                                          
COMPND  47 MOLECULE: PHOTOSYSTEM I-N SUBUNIT;                                   
COMPND  48 CHAIN: N;                                                            
COMPND  49 MOL_ID: 14;                                                          
COMPND  50 MOLECULE: CHAIN R;                                                   
COMPND  51 CHAIN: R;                                                            
COMPND  52 MOL_ID: 15;                                                          
COMPND  53 MOLECULE: AT3G54890;                                                 
COMPND  54 CHAIN: 1;                                                            
COMPND  55 MOL_ID: 16;                                                          
COMPND  56 MOLECULE: TYPE II CHLOROPHYLL A/B BINDING PROTEIN FROM PHOTOSYSTEM I;
COMPND  57 CHAIN: 2;                                                            
COMPND  58 FRAGMENT: RESIDUES 94-269;                                           
COMPND  59 MOL_ID: 17;                                                          
COMPND  60 MOLECULE: CHLOROPHYLL A-B BINDING PROTEIN 3, CHLOROPLASTIC;          
COMPND  61 CHAIN: 3;                                                            
COMPND  62 FRAGMENT: RESIDUES 84-255;                                           
COMPND  63 SYNONYM: LHCII TYPE III CAB-3;                                       
COMPND  64 MOL_ID: 18;                                                          
COMPND  65 MOLECULE: CHLOROPHYLL A-B BINDING PROTEIN P4, CHLOROPLASTIC;         
COMPND  66 CHAIN: 4;                                                            
COMPND  67 FRAGMENT: RESIDUES 81-246;                                           
COMPND  68 SYNONYM: LHCI TYPE III CAB-P4                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE   3 ORGANISM_COMMON: PEA;                                                
SOURCE   4 ORGANISM_TAXID: 3888;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE   7 ORGANISM_COMMON: PEA;                                                
SOURCE   8 ORGANISM_TAXID: 3888;                                                
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  11 ORGANISM_COMMON: PEA;                                                
SOURCE  12 ORGANISM_TAXID: 3888;                                                
SOURCE  13 MOL_ID: 4;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  15 ORGANISM_COMMON: PEA;                                                
SOURCE  16 ORGANISM_TAXID: 3888;                                                
SOURCE  17 MOL_ID: 5;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  19 ORGANISM_COMMON: PEA;                                                
SOURCE  20 ORGANISM_TAXID: 3888;                                                
SOURCE  21 MOL_ID: 6;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  23 ORGANISM_COMMON: PEA;                                                
SOURCE  24 ORGANISM_TAXID: 3888;                                                
SOURCE  25 MOL_ID: 7;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  27 ORGANISM_COMMON: PEA;                                                
SOURCE  28 ORGANISM_TAXID: 3888;                                                
SOURCE  29 MOL_ID: 8;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  31 ORGANISM_COMMON: PEA;                                                
SOURCE  32 ORGANISM_TAXID: 3888;                                                
SOURCE  33 MOL_ID: 9;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  35 ORGANISM_COMMON: PEA;                                                
SOURCE  36 ORGANISM_TAXID: 3888;                                                
SOURCE  37 MOL_ID: 10;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  39 ORGANISM_COMMON: PEA;                                                
SOURCE  40 ORGANISM_TAXID: 3888;                                                
SOURCE  41 MOL_ID: 11;                                                          
SOURCE  42 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  43 ORGANISM_COMMON: PEA;                                                
SOURCE  44 ORGANISM_TAXID: 3888;                                                
SOURCE  45 MOL_ID: 12;                                                          
SOURCE  46 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  47 ORGANISM_COMMON: PEA;                                                
SOURCE  48 ORGANISM_TAXID: 3888;                                                
SOURCE  49 MOL_ID: 13;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  51 ORGANISM_COMMON: PEA;                                                
SOURCE  52 ORGANISM_TAXID: 3888;                                                
SOURCE  53 MOL_ID: 14;                                                          
SOURCE  54 ORGANISM_SCIENTIFIC: UNIDENTIFIED;                                   
SOURCE  55 ORGANISM_TAXID: 32644;                                               
SOURCE  56 MOL_ID: 15;                                                          
SOURCE  57 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  58 ORGANISM_COMMON: PEA;                                                
SOURCE  59 ORGANISM_TAXID: 3888;                                                
SOURCE  60 MOL_ID: 16;                                                          
SOURCE  61 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  62 ORGANISM_COMMON: PEA;                                                
SOURCE  63 ORGANISM_TAXID: 3888;                                                
SOURCE  64 MOL_ID: 17;                                                          
SOURCE  65 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  66 ORGANISM_COMMON: PEA;                                                
SOURCE  67 ORGANISM_TAXID: 3888;                                                
SOURCE  68 MOL_ID: 18;                                                          
SOURCE  69 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  70 ORGANISM_COMMON: PEA;                                                
SOURCE  71 ORGANISM_TAXID: 3888                                                 
KEYWDS    PHOTOSYNTHESIS, ELECTRON TRANSFER, MEMBRANE PROTEINS, LARGE, 2        
KEYWDS   2 COMPLEXES, CHLOROPHYLL, CHLOROPLAST, CHROMOPHORE, ELECTRON           
KEYWDS   3 TRANSPORT, IRON, IRON-SULFUR, MAGNESIUM, MEMBRANE, METAL-BINDING,    
KEYWDS   4 PHOTOSYSTEM I, THYLAKOID, TRANSMEMBRANE, TRANSPORT                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.NELSON,H.TOPORIK                                                    
REVDAT   4   08-NOV-17 3LW5    1       REMARK                                   
REVDAT   3   01-AUG-12 3LW5    1       HET    HETATM VERSN                      
REVDAT   2   01-SEP-10 3LW5    1       DBREF  SOURCE                            
REVDAT   1   18-AUG-10 3LW5    0                                                
JRNL        AUTH   A.AMUNTS,H.TOPORIK,A.BOROVIKOVA,N.NELSON                     
JRNL        TITL   STRUCTURE DETERMINATION AND IMPROVED MODEL OF PLANT          
JRNL        TITL 2 PHOTOSYSTEM I                                                
JRNL        REF    J.BIOL.CHEM.                  V. 285  3478 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   19923216                                                     
JRNL        DOI    10.1074/JBC.M109.072645                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 82447                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.351                           
REMARK   3   R VALUE            (WORKING SET) : 0.349                           
REMARK   3   FREE R VALUE                     : 0.383                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4344                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.39                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5893                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.44                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4960                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 276                          
REMARK   3   BIN FREE R VALUE                    : 0.4850                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 24732                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 11638                                   
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.07                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.62000                                             
REMARK   3    B22 (A**2) : -7.81000                                             
REMARK   3    B33 (A**2) : 9.37000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.43000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.857         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.884         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 50.537        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.792                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.743                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 38548 ; 0.023 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 54957 ; 4.757 ; 2.336       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3108 ;26.852 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1085 ;41.197 ;23.438       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3836 ;25.575 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   105 ;22.066 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  5004 ; 0.515 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 35040 ; 0.015 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 15697 ; 0.416 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 25009 ; 0.612 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 22362 ; 3.568 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 28722 ; 4.412 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES: REFINED INDIVIDUALLY                            
REMARK   4                                                                      
REMARK   4 3LW5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-MAR-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000057804.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.873                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 82447                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 2WSC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22.5MM MES BIS-TRIS, 10MM SUCCINIC       
REMARK 280  ACID, 6% PEG6000, 0.015% DTM, VAPOR DIFFUSION, SITTING DROP,        
REMARK 280  TEMPERATURE 277K, PH 6                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       94.54300            
REMARK 290   SMTRY3   2  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: OCTADECAMERIC                     
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, N, R, 1, 2, 3, 4                
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     THR A   319                                                      
REMARK 465     ASN A   320                                                      
REMARK 465     TRP A   321                                                      
REMARK 465     GLY A   322                                                      
REMARK 465     ILE A   323                                                      
REMARK 465     GLY A   324                                                      
REMARK 465     HIS A   325                                                      
REMARK 465     GLY A   326                                                      
REMARK 465     ASN 1   107                                                      
REMARK 465     TRP 1   108                                                      
REMARK 465     VAL 1   109                                                      
REMARK 465     LYS 1   110                                                      
REMARK 465     ALA 1   111                                                      
REMARK 465     ALA 3   116                                                      
REMARK 465     ILE 3   117                                                      
REMARK 465     ALA 3   118                                                      
REMARK 465     PRO 3   119                                                      
REMARK 465     GLU 3   120                                                      
REMARK 465     TYR 3   121                                                      
REMARK 465     PRO 3   143                                                      
REMARK 465     PRO 3   144                                                      
REMARK 465     ALA 3   145                                                      
REMARK 465     GLY 3   146                                                      
REMARK 465     THR 3   147                                                      
REMARK 465     SER 3   219                                                      
REMARK 465     LEU 3   220                                                      
REMARK 465     LYS 3   221                                                      
REMARK 465     GLU 3   222                                                      
REMARK 465     LEU 3   223                                                      
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     ARG A 220    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     LEU A 272    CG   CD1  CD2                                       
REMARK 470     ARG A 318    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     ASP A 440    CG   OD1  OD2                                       
REMARK 470     ASP B 134    O                                                   
REMARK 470     PHE B 147    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B 456    CG   CD   OE1  OE2                                  
REMARK 470     LYS G 108    CG   CD   CE   NZ                                   
REMARK 470     PHE J  39    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     TYR 1  79    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU 1 134    CG   CD1  CD2                                       
REMARK 470     VAL 1 185    CG1  CG2                                            
REMARK 470     LYS 1 186    CG   CD   CE   NZ                                   
REMARK 470     ARG 2 100    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG 2 111    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU 2 142    CG   CD   OE1  OE2                                  
REMARK 470     VAL 3 114    CG1  CG2                                            
REMARK 470     LEU 3 127    CG   CD1  CD2                                       
REMARK 470     ILE 3 128    CG1  CG2  CD1                                       
REMARK 470     GLU 3 131    CG   CD   OE1  OE2                                  
REMARK 470     LEU 4  81    CG   CD1  CD2                                       
REMARK 470     LEU 4  88    CG   CD1  CD2                                       
REMARK 470     ARG 4 155    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU 4 202    CG   CD   OE1  OE2                                  
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   N    PRO 3   129     C1   CLA 3  1147              0.47            
REMARK 500   OE1  GLN A   197     OG1  THR A   351              0.57            
REMARK 500   CZ   ARG A   102     NE2  HIS 2   253              0.58            
REMARK 500   SD   MET J     1     ND2  ASN 2   102              0.64            
REMARK 500   CE   MET 3   110     C    LEU 3   236              0.66            
REMARK 500   O    CYS N   154     NZ   LYS N   157              0.66            
REMARK 500   CE   LYS 3   184     C3   CLA 3  2009              0.73            
REMARK 500   O    HIS B    89     CG1  VAL B   113              0.76            
REMARK 500   O    ILE 3   128     O1A  CLA 3  1147              0.86            
REMARK 500   NZ   LYS 1   184     O1D  CLA 1  1001              0.87            
REMARK 500   NH1  ARG A   102     NE2  HIS 2   253              0.90            
REMARK 500   CZ   ARG A   102     CD2  HIS 2   253              0.91            
REMARK 500   O    GLU 2   164     CD   ARG 2   167              0.91            
REMARK 500   OD1  ASN A   204     O    MET A   316              0.92            
REMARK 500   CD1  LEU A   520     O2'  LMU A  7044              0.93            
REMARK 500   CD1  ILE A   131     O    PHE B   446              0.94            
REMARK 500   SD   MET 3   110     N    LEU 3   236              0.96            
REMARK 500   NE   ARG B   564     OG   SER C    64              0.97            
REMARK 500   NE2  HIS 2   239     C4C  CLA 2  2003              0.97            
REMARK 500   NE   ARG B   314     CE2  PHE 1    64              0.98            
REMARK 500   CG   ASP 2    95     CB   ASP 3    85              1.01            
REMARK 500   OG   SER 1    82     CAC  CLA 1  1011              1.02            
REMARK 500   NZ   LYS 3   124     CB   ASN 3   149              1.03            
REMARK 500   NZ   LYS 3   184     C5   CLA 3  2009              1.03            
REMARK 500   CB   ILE 3   128     CBA  CLA 3  1147              1.05            
REMARK 500   CE   LYS 3   184     C4   CLA 3  2009              1.05            
REMARK 500   OE1  GLU 1   149    MG    CLA 1  1012              1.05            
REMARK 500   O    LYS B   469     CG2  ILE B   501              1.06            
REMARK 500   CE   MET 3   110     O    LEU 3   236              1.10            
REMARK 500   C    CYS N   154     NZ   LYS N   157              1.10            
REMARK 500   OE1  GLU 2   164     NA   CLA 2  2012              1.10            
REMARK 500   CD   PRO 3   129     C1   CLA 3  1147              1.10            
REMARK 500   C    THR B   293     OE1  GLN G    94              1.12            
REMARK 500   NH2  ARG A   154     OH   TYR A   384              1.12            
REMARK 500   CA   ILE 3   128     CGA  CLA 3  1147              1.12            
REMARK 500   CD1  ILE A   131     C    PHE B   446              1.13            
REMARK 500   CZ   ARG B   564     OG   SER C    64              1.13            
REMARK 500   CE   LYS 4   203     CMD  CLA 4  4002              1.14            
REMARK 500   O    GLU 2   164     CG   ARG 2   167              1.14            
REMARK 500   OG   SER A   104     OE1  GLU A   161              1.14            
REMARK 500   O    SER 1    82     NE2  HIS 1    86              1.14            
REMARK 500   CMC  CLA 1  1006     CMB  CLA 1  1010              1.14            
REMARK 500   NZ   LYS 4   203     CMD  CLA 4  4002              1.15            
REMARK 500   CD   LYS 3   184     C4   CLA 3  2009              1.16            
REMARK 500   OE1  GLU 2   164     C1A  CLA 2  2012              1.16            
REMARK 500   NH1  ARG A   102     CE1  HIS 2   253              1.18            
REMARK 500   CA   ILE 3   128     O2A  CLA 3  1147              1.19            
REMARK 500   CH2  TRP 2   112     NH1  ARG 2   167              1.19            
REMARK 500   CD   GLN A   197     OG1  THR A   351              1.19            
REMARK 500   C    MET D   114     NH1  ARG D   143              1.20            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     579 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OH   TYR 1   173     C    LEU 2   132     2646     0.71            
REMARK 500   CG   PHE F   130     NZ   LYS L   170     2556     0.72            
REMARK 500   OE2  GLU B   205     NH1  ARG K    69     1554     0.79            
REMARK 500   O    THR L   123     CA   GLY 4   180     1455     0.88            
REMARK 500   N    LEU 1   171     N    LEU 2   132     2646     0.98            
REMARK 500   OH   TYR 1   173     CA   LEU 2   132     2646     1.01            
REMARK 500   C    LEU L   203     OH   TYR 4   184     1455     1.02            
REMARK 500   OH   TYR L   205     O    GLU 4   181     1455     1.02            
REMARK 500   OE1  GLU L   124     CE2  PHE 4   172     1455     1.06            
REMARK 500   CD2  LEU 1   171     C    ILE 2   131     2646     1.07            
REMARK 500   CD2  LEU 1   171     O    ILE 2   131     2646     1.08            
REMARK 500   OE1  GLU L   124     CZ   PHE 4   172     1455     1.09            
REMARK 500   CD   GLU L   124     CE2  PHE 4   172     1455     1.11            
REMARK 500   NE2  GLN B   248     C2C  CLA K  3009     1554     1.11            
REMARK 500   CE1  TYR 1   173     O    LEU 2   132     2646     1.13            
REMARK 500   CD   GLU L   124     CZ   PHE 4   172     1455     1.15            
REMARK 500   O    PRO 1   118     CG2  THR 3    89     1554     1.17            
REMARK 500   CD2  PHE F   130     NZ   LYS L   170     2556     1.18            
REMARK 500   CE1  PHE F   130     CE   LYS L   170     2556     1.18            
REMARK 500   OE2  GLU B   205     CZ   ARG K    69     1554     1.19            
REMARK 500   O    PRO 1   170     CB   LEU 2   132     2646     1.20            
REMARK 500   O    LEU L   203     CE2  TYR 4   184     1455     1.27            
REMARK 500   O    PRO 1   170     CA   LEU 2   132     2646     1.30            
REMARK 500   CD1  PHE F   130     NZ   LYS L   170     2556     1.32            
REMARK 500   OD2  ASP F   131     CD   LYS L   170     2556     1.32            
REMARK 500   OE2  GLU A   348     OD1  ASN G   147     1556     1.33            
REMARK 500   CZ   TYR 1   173     O    LEU 2   132     2646     1.37            
REMARK 500   OD1  ASP F   131     CG   LYS L   170     2556     1.38            
REMARK 500   CD   GLU B   205     NH1  ARG K    69     1554     1.39            
REMARK 500   CG   ASN D   160     NZ   LYS F   101     2546     1.39            
REMARK 500   O    LEU L   203     CZ   TYR 4   184     1455     1.40            
REMARK 500   NE2  GLN B   248     CMC  CLA K  3009     1554     1.40            
REMARK 500   ND2  ASN L   122     OE1  GLU 4   181     1455     1.46            
REMARK 500   CZ   TYR 1   173     C    LEU 2   132     2646     1.47            
REMARK 500   NE2  GLN B   248     C1C  CLA K  3009     1554     1.49            
REMARK 500   CG   ASP F   131     CD   LYS L   170     2556     1.49            
REMARK 500   O    THR L   123     N    GLY 4   180     1455     1.50            
REMARK 500   OE2  GLU L   124     CZ   PHE 4   172     1455     1.50            
REMARK 500   OG   SER H    81     CZ3  TRP 4   240     2546     1.51            
REMARK 500   OE2  GLU L   124     CE1  PHE 4   172     1455     1.52            
REMARK 500   CZ   PHE F   130     CE   LYS L   170     2556     1.53            
REMARK 500   N    GLU L   124     O    LEU 4   177     1455     1.54            
REMARK 500   CG   LEU 1   171     CA   ILE 2   131     2646     1.55            
REMARK 500   OH   TYR L   205     C    GLU 4   181     1455     1.55            
REMARK 500   CD1  PHE F   130     CE   LYS L   170     2556     1.56            
REMARK 500   O    LEU L   203     OH   TYR 4   184     1455     1.58            
REMARK 500   C    PRO 1   170     N    LEU 2   132     2646     1.58            
REMARK 500   CZ   TYR 1   173     CA   LEU 2   132     2646     1.59            
REMARK 500   CG   ASN L   122     OE1  GLU 4   181     1455     1.60            
REMARK 500   O    PHE L   202     OH   TYR 4   184     1455     1.61            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     130 SYMMETRY CONTACTS                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LEU A  21   C     LEU A  21   O       0.117                       
REMARK 500    PRO A 337   CD    PRO A 337   N      -0.125                       
REMARK 500    PRO B  94   CD    PRO B  94   N      -0.145                       
REMARK 500    PRO B  99   CD    PRO B  99   N      -0.116                       
REMARK 500    PRO B 219   CD    PRO B 219   N      -0.110                       
REMARK 500    GLN B 229   C     GLN B 229   O       0.115                       
REMARK 500    PRO B 457   CD    PRO B 457   N      -0.101                       
REMARK 500    PHE D 188   CB    PHE D 188   CG     -0.106                       
REMARK 500    GLY K 123   C     LEU K 124   N       0.180                       
REMARK 500    PRO L  64   CD    PRO L  64   N      -0.116                       
REMARK 500    LYS N 157   C     LYS N 157   O       0.120                       
REMARK 500    LYS N 157   C     ASP N 158   N       0.159                       
REMARK 500    UNK R   7   C     UNK R   8   N       0.158                       
REMARK 500    GLY 1  60   N     GLY 1  60   CA      0.119                       
REMARK 500    GLY 1  60   CA    GLY 1  60   C      -0.156                       
REMARK 500    GLY 1  63   CA    GLY 1  63   C       0.134                       
REMARK 500    GLY 1  63   C     GLY 1  63   O       0.186                       
REMARK 500    GLY 1 119   N     GLY 1 119   CA      0.207                       
REMARK 500    GLY 1 166   N     GLY 1 166   CA      0.125                       
REMARK 500    LEU 1 171   C     LEU 1 171   O       0.163                       
REMARK 500    GLY 1 172   N     GLY 1 172   CA      0.100                       
REMARK 500    GLY 1 172   CA    GLY 1 172   C       0.116                       
REMARK 500    GLY 1 172   C     GLY 1 172   O       0.204                       
REMARK 500    TYR 1 173   CE2   TYR 1 173   CD2    -0.097                       
REMARK 500    TRP 1 225   CB    TRP 1 225   CG      0.130                       
REMARK 500    TRP 1 225   C     TRP 1 225   O       0.167                       
REMARK 500    TRP 1 225   C     HIS 1 226   N       0.241                       
REMARK 500    GLY 2 130   C     GLY 2 130   O      -0.096                       
REMARK 500    ASN 2 133   C     ASN 2 133   O       0.158                       
REMARK 500    GLY 2 165   C     GLY 2 165   O       0.102                       
REMARK 500    ARG 2 167   CZ    ARG 2 167   NH1     0.088                       
REMARK 500    PRO 2 184   C     ASN 2 185   N       0.154                       
REMARK 500    GLY 2 194   N     GLY 2 194   CA      0.134                       
REMARK 500    PRO 3 129   CD    PRO 3 129   N      -0.089                       
REMARK 500    PHE 3 158   C     PHE 3 158   O       0.137                       
REMARK 500    GLY 3 196   C     GLY 3 196   O       0.096                       
REMARK 500    GLY 3 198   N     GLY 3 198   CA      0.116                       
REMARK 500    ALA 4 129   N     ALA 4 129   CA      0.123                       
REMARK 500    PRO 4 239   CD    PRO 4 239   N      -0.102                       
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    LYS A  28   N   -  CA  -  C   ANGL. DEV. =  17.7 DEGREES          
REMARK 500    GLY A  47   N   -  CA  -  C   ANGL. DEV. = -21.6 DEGREES          
REMARK 500    PRO A  48   C   -  N   -  CA  ANGL. DEV. =  11.1 DEGREES          
REMARK 500    ILE A 116   N   -  CA  -  C   ANGL. DEV. =  17.1 DEGREES          
REMARK 500    PRO A 118   C   -  N   -  CA  ANGL. DEV. =  14.3 DEGREES          
REMARK 500    PRO A 118   C   -  N   -  CD  ANGL. DEV. = -15.1 DEGREES          
REMARK 500    ILE A 158   N   -  CA  -  C   ANGL. DEV. = -16.4 DEGREES          
REMARK 500    PRO A 191   C   -  N   -  CA  ANGL. DEV. =  12.3 DEGREES          
REMARK 500    ASP A 238   N   -  CA  -  C   ANGL. DEV. = -20.3 DEGREES          
REMARK 500    ILE A 242   N   -  CA  -  C   ANGL. DEV. =  19.4 DEGREES          
REMARK 500    HIS A 246   N   -  CA  -  C   ANGL. DEV. =  16.8 DEGREES          
REMARK 500    PRO A 260   C   -  N   -  CA  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    PRO A 260   C   -  N   -  CD  ANGL. DEV. = -14.7 DEGREES          
REMARK 500    GLY A 265   N   -  CA  -  C   ANGL. DEV. =  15.1 DEGREES          
REMARK 500    PRO A 268   C   -  N   -  CD  ANGL. DEV. = -16.1 DEGREES          
REMARK 500    ARG A 284   N   -  CA  -  C   ANGL. DEV. =  23.0 DEGREES          
REMARK 500    LEU A 290   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES          
REMARK 500    TRP A 295   CA  -  C   -  N   ANGL. DEV. = -13.4 DEGREES          
REMARK 500    TRP A 295   O   -  C   -  N   ANGL. DEV. =  10.5 DEGREES          
REMARK 500    PRO A 337   C   -  N   -  CD  ANGL. DEV. = -23.1 DEGREES          
REMARK 500    PRO A 337   CA  -  N   -  CD  ANGL. DEV. =  -8.5 DEGREES          
REMARK 500    GLY A 345   N   -  CA  -  C   ANGL. DEV. = -16.2 DEGREES          
REMARK 500    LEU A 346   CA  -  CB  -  CG  ANGL. DEV. = -16.2 DEGREES          
REMARK 500    GLU A 348   N   -  CA  -  C   ANGL. DEV. = -17.8 DEGREES          
REMARK 500    LEU A 350   CA  -  CB  -  CG  ANGL. DEV. = -16.1 DEGREES          
REMARK 500    SER A 353   N   -  CA  -  C   ANGL. DEV. =  17.0 DEGREES          
REMARK 500    PRO A 424   C   -  N   -  CA  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    PRO A 473   C   -  N   -  CA  ANGL. DEV. =  13.8 DEGREES          
REMARK 500    THR A 503   N   -  CA  -  C   ANGL. DEV. = -16.4 DEGREES          
REMARK 500    PRO A 505   C   -  N   -  CA  ANGL. DEV. =  12.3 DEGREES          
REMARK 500    GLY A 524   N   -  CA  -  C   ANGL. DEV. =  21.8 DEGREES          
REMARK 500    LEU A 530   CA  -  CB  -  CG  ANGL. DEV. =  13.8 DEGREES          
REMARK 500    PRO A 533   C   -  N   -  CD  ANGL. DEV. = -13.8 DEGREES          
REMARK 500    LEU A 534   N   -  CA  -  C   ANGL. DEV. =  18.4 DEGREES          
REMARK 500    PRO A 570   C   -  N   -  CA  ANGL. DEV. =  10.7 DEGREES          
REMARK 500    PRO A 580   C   -  N   -  CA  ANGL. DEV. =  10.4 DEGREES          
REMARK 500    ARG B  19   N   -  CA  -  C   ANGL. DEV. = -16.4 DEGREES          
REMARK 500    GLY B  72   N   -  CA  -  C   ANGL. DEV. = -17.6 DEGREES          
REMARK 500    PRO B  94   C   -  N   -  CA  ANGL. DEV. =  10.8 DEGREES          
REMARK 500    PRO B  94   C   -  N   -  CD  ANGL. DEV. = -14.3 DEGREES          
REMARK 500    PRO B  99   C   -  N   -  CA  ANGL. DEV. =  11.0 DEGREES          
REMARK 500    PRO B  99   CA  -  N   -  CD  ANGL. DEV. =  -9.3 DEGREES          
REMARK 500    PRO B 112   C   -  N   -  CD  ANGL. DEV. = -15.1 DEGREES          
REMARK 500    LEU B 243   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES          
REMARK 500    PRO B 311   C   -  N   -  CD  ANGL. DEV. = -15.1 DEGREES          
REMARK 500    GLY B 321   N   -  CA  -  C   ANGL. DEV. =  15.2 DEGREES          
REMARK 500    PRO B 449   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    TRP B 602   N   -  CA  -  C   ANGL. DEV. =  21.0 DEGREES          
REMARK 500    TRP B 625   N   -  CA  -  C   ANGL. DEV. =  17.3 DEGREES          
REMARK 500    ASN B 633   C   -  N   -  CA  ANGL. DEV. = -16.9 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     147 ANGLE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A  22        1.90     52.13                                   
REMARK 500    LYS A  28       -2.69    118.84                                   
REMARK 500    ALA A  35      153.50    101.78                                   
REMARK 500    LYS A  36      138.34     83.30                                   
REMARK 500    PHE A  40      162.92    176.52                                   
REMARK 500    SER A  41      148.51     39.36                                   
REMARK 500    ALA A  45      134.65    -37.05                                   
REMARK 500    LEU A  57      -40.91     98.86                                   
REMARK 500    HIS A  67      -56.19     88.17                                   
REMARK 500    GLU A  72     -113.95     52.97                                   
REMARK 500    SER A  75      -33.69    -38.04                                   
REMARK 500    ILE A  88      -55.85     77.49                                   
REMARK 500    LEU A  93      -14.73     84.41                                   
REMARK 500    PHE A  98     -119.66    -40.99                                   
REMARK 500    HIS A  99      -63.51     16.12                                   
REMARK 500    ASN A 105      -45.10     59.21                                   
REMARK 500    THR A 114      -11.23     85.29                                   
REMARK 500    TRP A 124      153.47     87.96                                   
REMARK 500    VAL A 127     -132.96     62.09                                   
REMARK 500    GLU A 130       -9.96     99.15                                   
REMARK 500    ASN A 133       76.46   -115.09                                   
REMARK 500    GLN A 151      -32.14   -162.54                                   
REMARK 500    ILE A 158      -59.95    158.56                                   
REMARK 500    THR A 159      175.96     80.98                                   
REMARK 500    SER A 160      149.42    100.41                                   
REMARK 500    GLN A 163      -90.51    -68.69                                   
REMARK 500    LEU A 164      -25.55    -13.88                                   
REMARK 500    PHE A 174       92.25    -64.29                                   
REMARK 500    ALA A 175      130.78    130.64                                   
REMARK 500    MET A 178       44.12    -70.43                                   
REMARK 500    LEU A 179      -11.90   -161.54                                   
REMARK 500    PHE A 184       19.57    -64.70                                   
REMARK 500    HIS A 185     -127.38   -131.13                                   
REMARK 500    TYR A 186      -59.67    -22.13                                   
REMARK 500    ALA A 190      169.33     82.85                                   
REMARK 500    HIS A 205      -87.78    107.98                                   
REMARK 500    HIS A 206      -72.02    -36.15                                   
REMARK 500    LEU A 210      -61.22    173.74                                   
REMARK 500    LEU A 213       11.79    -62.44                                   
REMARK 500    SER A 215      -52.12     92.80                                   
REMARK 500    LEU A 216      -74.06    -64.35                                   
REMARK 500    ARG A 220       76.91    -66.88                                   
REMARK 500    HIS A 221       14.56    136.52                                   
REMARK 500    VAL A 223      -47.47   -151.95                                   
REMARK 500    VAL A 225      -56.53     91.21                                   
REMARK 500    ASN A 230        4.00   -163.01                                   
REMARK 500    ASN A 234       47.98    -65.86                                   
REMARK 500    ALA A 235      -40.75   -150.55                                   
REMARK 500    VAL A 237     -163.07    139.22                                   
REMARK 500    GLU A 247      -37.25     52.65                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     654 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU A   21     VAL A   22                   54.32                    
REMARK 500 VAL A   22     ASP A   23                  118.50                    
REMARK 500 ASP A   23     ARG A   24                 -103.94                    
REMARK 500 ASP A   25     PRO A   26                  -86.43                    
REMARK 500 PRO A   26     ILE A   27                 -137.73                    
REMARK 500 ILE A   27     LYS A   28                 -128.24                    
REMARK 500 LYS A   28     THR A   29                  140.06                    
REMARK 500 LYS A   36     PRO A   37                 -143.11                    
REMARK 500 PRO A   37     GLY A   38                 -125.34                    
REMARK 500 GLY A   38     HIS A   39                 -108.19                    
REMARK 500 HIS A   39     PHE A   40                  135.34                    
REMARK 500 ALA A   45     LYS A   46                 -135.47                    
REMARK 500 LYS A   46     GLY A   47                 -111.76                    
REMARK 500 GLY A   47     PRO A   48                 -146.29                    
REMARK 500 HIS A   62     ASP A   63                  122.57                    
REMARK 500 PHE A   64     ASP A   65                  134.51                    
REMARK 500 SER A   66     HIS A   67                 -147.03                    
REMARK 500 HIS A   67     THR A   68                  148.01                    
REMARK 500 GLU A   73     ILE A   74                 -144.74                    
REMARK 500 LEU A   93     SER A   94                  141.49                    
REMARK 500 PHE A  103     SER A  104                 -143.83                    
REMARK 500 THR A  114     HIS A  115                  146.24                    
REMARK 500 GLY A  117     PRO A  118                 -146.19                    
REMARK 500 SER A  119     ALA A  120                  144.32                    
REMARK 500 VAL A  123     TRP A  124                 -149.54                    
REMARK 500 GLY A  128     GLN A  129                 -147.13                    
REMARK 500 LEU A  132     ASN A  133                 -140.81                    
REMARK 500 GLY A  134     ASP A  135                 -139.88                    
REMARK 500 VAL A  136     GLY A  137                 -108.81                    
REMARK 500 GLY A  142     ILE A  143                  146.27                    
REMARK 500 THR A  146     SER A  147                  144.74                    
REMARK 500 GLY A  148     PHE A  149                  131.82                    
REMARK 500 ALA A  189     ALA A  190                  139.23                    
REMARK 500 GLN A  197     ASP A  198                  130.86                    
REMARK 500 VAL A  199     GLU A  200                 -115.58                    
REMARK 500 SER A  201     MET A  202                 -139.54                    
REMARK 500 LYS A  240     GLU A  241                  125.95                    
REMARK 500 HIS A  246     GLU A  247                  117.48                    
REMARK 500 LEU A  250     ASN A  251                 -147.56                    
REMARK 500 ASN A  251     ARG A  252                 -105.00                    
REMARK 500 GLN A  257     LEU A  258                 -145.69                    
REMARK 500 PHE A  262     ALA A  263                  131.65                    
REMARK 500 ALA A  263     GLU A  264                  120.97                    
REMARK 500 PHE A  270     THR A  271                  120.89                    
REMARK 500 TRP A  274     SER A  275                  146.88                    
REMARK 500 SER A  275     LYS A  276                  149.74                    
REMARK 500 LYS A  276     TYR A  277                  148.00                    
REMARK 500 ASP A  279     PHE A  280                 -139.50                    
REMARK 500 PHE A  280     LEU A  281                  130.74                    
REMARK 500 THR A  282     PHE A  283                  149.16                    
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     536 NON CIS, NON-TRANS OMEGA OUTLIERS.            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    VAL E 126        -11.38                                           
REMARK 500    GLN F  97         11.19                                           
REMARK 500    GLN F 103         20.60                                           
REMARK 500    GLY 1  63        -13.38                                           
REMARK 500    GLY 1  68        -11.38                                           
REMARK 500    LEU 1  69         13.51                                           
REMARK 500    PRO 1 224        -15.12                                           
REMARK 500    TYR 4 175         10.09                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     CLA A 1101                                                       
REMARK 610     CLA A 1102                                                       
REMARK 610     CLA A 1104                                                       
REMARK 610     CLA A 1105                                                       
REMARK 610     CLA A 1107                                                       
REMARK 610     CLA A 1108                                                       
REMARK 610     CLA A 1110                                                       
REMARK 610     CLA A 1111                                                       
REMARK 610     CLA A 1112                                                       
REMARK 610     CLA A 1113                                                       
REMARK 610     CLA A 1116                                                       
REMARK 610     CLA A 1120                                                       
REMARK 610     CLA A 1121                                                       
REMARK 610     CLA A 1122                                                       
REMARK 610     CLA A 1127                                                       
REMARK 610     CLA A 1129                                                       
REMARK 610     CLA A 1133                                                       
REMARK 610     CLA A 1134                                                       
REMARK 610     CLA A 1135                                                       
REMARK 610     CLA A 1137                                                       
REMARK 610     CLA A 1139                                                       
REMARK 610     CLA A 1149                                                       
REMARK 610     CLA A 1151                                                       
REMARK 610     CLA A 1309                                                       
REMARK 610     CLA B 1201                                                       
REMARK 610     CLA B 1208                                                       
REMARK 610     CLA B 1209                                                       
REMARK 610     CLA B 1212                                                       
REMARK 610     CLA B 1213                                                       
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 1221                                                       
REMARK 610     CLA B 1222                                                       
REMARK 610     CLA B 1227                                                       
REMARK 610     CLA B 1228                                                       
REMARK 610     CLA B 1230                                                       
REMARK 610     CLA B 1231                                                       
REMARK 610     CLA B 1232                                                       
REMARK 610     CLA B 1233                                                       
REMARK 610     CLA B 1234                                                       
REMARK 610     CLA B 1236                                                       
REMARK 610     CLA B 1301                                                       
REMARK 610     LMU B 7012                                                       
REMARK 610     LMG B 7101                                                       
REMARK 610     CLA F 1240                                                       
REMARK 610     CLA F 1302                                                       
REMARK 610     CLA F 1305                                                       
REMARK 610     LMU F 7036                                                       
REMARK 610     CLA G 1242                                                       
REMARK 610     CLA H 1241                                                       
REMARK 610     CLA H 1505                                                       
REMARK 610     CLA I 1204                                                       
REMARK 610     CLA J 1308                                                       
REMARK 610     CLA J 1311                                                       
REMARK 610     CLA K 1142                                                       
REMARK 610     CLA K 1143                                                       
REMARK 610     CLA K 1146                                                       
REMARK 610     CLA L 1148                                                       
REMARK 610     CLA L 1501                                                       
REMARK 610     CLA L 1502                                                       
REMARK 610     CLA L 1503                                                       
REMARK 610     CLA L 1504                                                       
REMARK 610     CLA R 1144                                                       
REMARK 610     CLA 1 1001                                                       
REMARK 610     CLA 1 1002                                                       
REMARK 610     CLA 1 1003                                                       
REMARK 610     CLA 1 1005                                                       
REMARK 610     CLA 1 1006                                                       
REMARK 610     CLA 1 1007                                                       
REMARK 610     CLA 1 1008                                                       
REMARK 610     CLA 1 1010                                                       
REMARK 610     CLA 1 1011                                                       
REMARK 610     CLA 1 1012                                                       
REMARK 610     CLA 1 1013                                                       
REMARK 610     CLA 1 1014                                                       
REMARK 610     CLA 1 1015                                                       
REMARK 610     CLA 1 1303                                                       
REMARK 610     CLA 1 1310                                                       
REMARK 610     CLA 2 1307                                                       
REMARK 610     CLA 2 2001                                                       
REMARK 610     CLA 2 2002                                                       
REMARK 610     CLA 2 2003                                                       
REMARK 610     CLA 2 2004                                                       
REMARK 610     CLA 2 2005                                                       
REMARK 610     CLA 2 2008                                                       
REMARK 610     CLA 2 2010                                                       
REMARK 610     CLA 2 2011                                                       
REMARK 610     CLA 2 2012                                                       
REMARK 610     CLA 2 2013                                                       
REMARK 610     CLA 2 2014                                                       
REMARK 610     CLA 3 1118                                                       
REMARK 610     CLA 3 1147                                                       
REMARK 610     CLA 3 2009                                                       
REMARK 610     CLA 3 3001                                                       
REMARK 610     CLA 3 3002                                                       
REMARK 610     CLA 3 3003                                                       
REMARK 610     CLA 3 3004                                                       
REMARK 610     CLA 3 3005                                                       
REMARK 610     CLA 3 3006                                                       
REMARK 610     CLA 3 3007                                                       
REMARK 610     CLA 3 3008                                                       
REMARK 610     CLA 3 3010                                                       
REMARK 610     CLA 3 3012                                                       
REMARK 610     CLA 3 3014                                                       
REMARK 610     CLA 3 3015                                                       
REMARK 610     CLA 3 3017                                                       
REMARK 610     CLA 4 1004                                                       
REMARK 610     CLA 4 1009                                                       
REMARK 610     CLA 4 1306                                                       
REMARK 610     CLA 4 4001                                                       
REMARK 610     CLA 4 4002                                                       
REMARK 610     CLA 4 4003                                                       
REMARK 610     CLA 4 4004                                                       
REMARK 610     CLA 4 4005                                                       
REMARK 610     CLA 4 4006                                                       
REMARK 610     CLA 4 4007                                                       
REMARK 610     CLA 4 4010                                                       
REMARK 610     CLA 4 4011                                                       
REMARK 610     CLA 4 4012                                                       
REMARK 610     CLA 4 4013                                                       
REMARK 610     CLA 4 4014                                                       
REMARK 610     CLA 4 4015                                                       
REMARK 610     LMU 4 7009                                                       
REMARK 610     LMU 4 7053                                                       
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 B1206  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  93   OD2                                                    
REMARK 620 2 CLA B1206   NA   84.2                                              
REMARK 620 3 CLA B1206   NB  100.1  90.6                                        
REMARK 620 4 CLA B1206   NC   95.9 179.6  89.8                                  
REMARK 620 5 CLA B1206   ND   81.2  94.6 174.8  85.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A8001  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 581   SG                                                     
REMARK 620 2 SF4 A8001   S1  138.3                                              
REMARK 620 3 SF4 A8001   S2   97.5 104.3                                        
REMARK 620 4 SF4 A8001   S3   35.1 104.2 104.7                                  
REMARK 620 5 CYS A 590   SG   85.8 132.3  38.9 113.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA L1501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU L 101   OE2                                                    
REMARK 620 2 CLA L1501   NA   95.1                                              
REMARK 620 3 CLA L1501   NB  102.9  92.5                                        
REMARK 620 4 CLA L1501   NC   84.8 177.2  90.2                                  
REMARK 620 5 CLA L1501   ND   77.2  91.8 175.6  85.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C8003  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  58   SG                                                     
REMARK 620 2 SF4 C8003   S2  120.6                                              
REMARK 620 3 SF4 C8003   S3   88.6 104.4                                        
REMARK 620 4 SF4 C8003   S4  127.8 104.8 104.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 44002  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN 4 207   OD1                                                    
REMARK 620 2 CLA 44002   NA  108.2                                              
REMARK 620 3 CLA 44002   NB   66.5  90.8                                        
REMARK 620 4 CLA 44002   NC   73.2 178.5  90.3                                  
REMARK 620 5 CLA 44002   ND  113.1  94.1 174.9  84.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A8001  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 559   SG                                                     
REMARK 620 2 SF4 A8001   S1  141.4                                              
REMARK 620 3 SF4 A8001   S2  106.8 104.5                                        
REMARK 620 4 SF4 A8001   S4   45.3 104.9 104.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C8002  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  51   SG                                                     
REMARK 620 2 SF4 C8002   S1   93.9                                              
REMARK 620 3 SF4 C8002   S2  146.8 104.5                                        
REMARK 620 4 SF4 C8002   S4   44.0 104.9 103.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A8001  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 581   SG                                                     
REMARK 620 2 SF4 A8001   S2   89.1                                              
REMARK 620 3 SF4 A8001   S3   31.2 105.0                                        
REMARK 620 4 SF4 A8001   S4  134.9 104.2 104.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C8003  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PRO C  59   O                                                      
REMARK 620 2 SF4 C8003   S1  135.2                                              
REMARK 620 3 SF4 C8003   S2  106.9 104.6                                        
REMARK 620 4 SF4 C8003   S3   97.3 104.5 104.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 44013  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU 4 145   OE2                                                    
REMARK 620 2 CLA 44013   NA   84.1                                              
REMARK 620 3 CLA 44013   NB   81.4  90.8                                        
REMARK 620 4 CLA 44013   NC   96.7 179.0  90.0                                  
REMARK 620 5 CLA 44013   ND   99.2  92.0 177.2  87.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A1134  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 503   OG1                                                    
REMARK 620 2 CLA A1134   NA   76.7                                              
REMARK 620 3 CLA A1134   NB  117.1  90.8                                        
REMARK 620 4 CLA A1134   NC  102.8 178.7  90.5                                  
REMARK 620 5 CLA A1134   ND   64.2  93.5 175.7  85.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B1232  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CLA B1231   OBD                                                    
REMARK 620 2 CLA B1232   NA   97.0                                              
REMARK 620 3 CLA B1232   NB   74.1  91.7                                        
REMARK 620 4 CLA B1232   NC   83.7 178.6  89.7                                  
REMARK 620 5 CLA B1232   ND  105.6  92.8 175.4  85.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A1109  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CLA A1102   O1A                                                    
REMARK 620 2 CLA A1109   NA   74.9                                              
REMARK 620 3 CLA A1109   NB   97.4  89.6                                        
REMARK 620 4 CLA A1109   NC  105.0 178.4  92.0                                  
REMARK 620 5 CLA A1109   ND   83.5  93.9 176.5  84.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A1121  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 317   OH                                                     
REMARK 620 2 CLA A1121   NA   63.7                                              
REMARK 620 3 CLA A1121   NB   91.9  91.8                                        
REMARK 620 4 CLA A1121   NC  116.4 178.7  89.5                                  
REMARK 620 5 CLA A1121   ND   89.9  92.5 175.7  86.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 22012  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU 2 164   OE1                                                    
REMARK 620 2 CLA 22012   NA   13.5                                              
REMARK 620 3 CLA 22012   NB   93.1  90.9                                        
REMARK 620 4 CLA 22012   NC  166.4 178.5  90.6                                  
REMARK 620 5 CLA 22012   ND   90.4  92.6 176.5  85.9                            
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 1 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 1009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1014                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1015                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1104                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1105                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1106                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1107                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1108                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1109                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1110                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1111                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1112                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1113                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1115                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1116                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1117                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 1118                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1119                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1120                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1121                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1122                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1123                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1124                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1125                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1126                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1127                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1128                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1129                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA L 1130                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1131                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1132                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1133                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1134                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1135                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1136                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1137                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1138                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1139                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1140                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1141                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA K 1142                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA K 1143                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA H 1145                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA K 1146                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 1147                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1149                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA R 1150                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1151                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA I 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1206                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA H 1207                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1208                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1209                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1210                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1211                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1212                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1213                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1214                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1215                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1216                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1217                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1218                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1219                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1220                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1221                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1222                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1223                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1224                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1225                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1226                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1227                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1228                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1229                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1230                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1231                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1232                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1233                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1234                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1235                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1236                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1237                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1238                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1239                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA F 1240                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA H 1241                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA G 1242                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1301                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA F 1302                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1303                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 1304                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA F 1305                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 1306                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA J 1308                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1309                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA J 1311                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA L 1501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA L 1502                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA L 1503                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA L 1504                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA H 1505                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 2002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 2003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 2004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 2005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 2006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 2007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 2009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 2011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 2012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 2013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 2014                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA K 3009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3016                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 4009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4014                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PQN A 5001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PQN B 5002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR A 6002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR A 6003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 6004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 6005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 6006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR A 6007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR A 6008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 6010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR A 6011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR J 6012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR F 6014                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR F 6016                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 6017                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR I 6018                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR L 6019                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 6020                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR I 6021                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR 3 6022                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU K 7001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU 3 7003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU 3 7005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU 2 7006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: TC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU R 7007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU 4 7008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU 4 7009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU A 7010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU H 7011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU B 7012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU H 7017                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU R 7024                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU G 7026                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: UC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU L 7029                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: VC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU H 7030                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: VC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU 4 7034                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: VC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU A 7035                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: VC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU F 7036                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: VC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU B 7038                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: VC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU G 7039                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: VC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU B 7040                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: VC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU K 7041                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: VC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU K 7042                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: WC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU A 7044                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: WC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU A 7045                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: WC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU 2 7046                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: WC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU K 7047                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: WC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU E 7048                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: WC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU D 7050                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: WC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU 4 7052                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: WC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU 4 7053                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: WC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG B 7101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: XC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 8001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: XC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 C 8002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: XC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 C 8003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: XC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 9010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: XC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 9011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: XC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 9012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: XC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 9013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: XC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 9022                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: XC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 9023                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WSC   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 MISSING ALANINE OF THIS POSITION IN CHAIN 4 IS CORRECT BECAUSE IN    
REMARK 999 ALL THE OTHER PLANTS INCLUDING ARABIDOPSIS IT IS MISSING. THE        
REMARK 999 AUTHOR CAN NOT ASSIGN TO THE SEQRES OF CHAIN R. ABOUT CHAIN D, E, F, 
REMARK 999 G, H, J, K, L, N, 1, THE SEQUENCE DATABASE REFERENCE WHICH DERIVES   
REMARK 999 FROM PEA DOES NOT CURRENTLY EXIST.                                   
DBREF  3LW5 A   21   758  UNP    P05310   PSAA_PEA        21    758             
DBREF  3LW5 B    2   734  UNP    P05311   PSAB_PEA         2    734             
DBREF  3LW5 C    1    81  UNP    P10793   PSAC_PEA         1     81             
DBREF  3LW5 D   73   210  PDB    3LW5     3LW5            73    210             
DBREF  3LW5 E   66   129  PDB    3LW5     3LW5            66    129             
DBREF  3LW5 F   78   231  PDB    3LW5     3LW5            78    231             
DBREF  3LW5 G   60   154  PDB    3LW5     3LW5            60    154             
DBREF  3LW5 H   54   122  PDB    3LW5     3LW5            54    122             
DBREF  3LW5 I    1    30  UNP    P17227   PSAI_PEA         1     30             
DBREF  3LW5 J    1    42  PDB    3LW5     3LW5             1     42             
DBREF  3LW5 K   47   130  PDB    3LW5     3LW5            47    130             
DBREF  3LW5 L   51   211  PDB    3LW5     3LW5            51    211             
DBREF  3LW5 N   86   170  PDB    3LW5     3LW5            86    170             
DBREF  3LW5 R    1    53  PDB    3LW5     3LW5             1     53             
DBREF  3LW5 1   57   226  PDB    3LW5     3LW5            57    226             
DBREF  3LW5 2   94   269  UNP    Q41038   Q41038_PEA      94    269             
DBREF  3LW5 3   84   255  UNP    Q32904   CB23_PEA        84    255             
DBREF  3LW5 4   81   246  UNP    Q9SQL2   CB24_PEA        81    247             
SEQADV 3LW5     4       UNP  Q9SQL2    ALA   211 SEE REMARK 999                 
SEQRES   1 A  738  LEU VAL ASP ARG ASP PRO ILE LYS THR SER PHE GLU GLN          
SEQRES   2 A  738  TRP ALA LYS PRO GLY HIS PHE SER ARG THR ILE ALA LYS          
SEQRES   3 A  738  GLY PRO ASP THR THR THR TRP ILE TRP ASN LEU HIS ALA          
SEQRES   4 A  738  ASP ALA HIS ASP PHE ASP SER HIS THR SER ASP LEU GLU          
SEQRES   5 A  738  GLU ILE SER ARG LYS VAL PHE SER ALA HIS PHE GLY GLN          
SEQRES   6 A  738  LEU SER ILE ILE PHE LEU TRP LEU SER GLY MET TYR PHE          
SEQRES   7 A  738  HIS GLY ALA ARG PHE SER ASN TYR GLU ALA TRP LEU ASN          
SEQRES   8 A  738  ASP PRO THR HIS ILE GLY PRO SER ALA GLN VAL VAL TRP          
SEQRES   9 A  738  PRO ILE VAL GLY GLN GLU ILE LEU ASN GLY ASP VAL GLY          
SEQRES  10 A  738  GLY GLY PHE ARG GLY ILE GLN ILE THR SER GLY PHE PHE          
SEQRES  11 A  738  GLN ILE TRP ARG ALA SER GLY ILE THR SER GLU LEU GLN          
SEQRES  12 A  738  LEU TYR CYS THR ALA ILE GLY ALA LEU VAL PHE ALA GLY          
SEQRES  13 A  738  LEU MET LEU PHE ALA GLY TRP PHE HIS TYR HIS LYS ALA          
SEQRES  14 A  738  ALA PRO LYS LEU ALA TRP PHE GLN ASP VAL GLU SER MET          
SEQRES  15 A  738  LEU ASN HIS HIS LEU ALA GLY LEU LEU GLY LEU GLY SER          
SEQRES  16 A  738  LEU SER TRP ALA ARG HIS GLN VAL HIS VAL SER LEU PRO          
SEQRES  17 A  738  ILE ASN GLN PHE LEU ASN ALA GLY VAL ASP PRO LYS GLU          
SEQRES  18 A  738  ILE PRO LEU PRO HIS GLU PHE ILE LEU ASN ARG ASP LEU          
SEQRES  19 A  738  LEU ALA GLN LEU TYR PRO SER PHE ALA GLU GLY ALA THR          
SEQRES  20 A  738  PRO PHE PHE THR LEU ASN TRP SER LYS TYR ALA ASP PHE          
SEQRES  21 A  738  LEU THR PHE ARG GLY GLY LEU ASP PRO LEU THR GLY GLY          
SEQRES  22 A  738  LEU TRP LEU THR ASP ILE ALA HIS HIS HIS LEU ALA ILE          
SEQRES  23 A  738  ALA ILE LEU PHE LEU ILE ALA GLY HIS MET TYR ARG THR          
SEQRES  24 A  738  ASN TRP GLY ILE GLY HIS GLY ILE LYS ASP ILE LEU GLU          
SEQRES  25 A  738  ALA HIS LYS GLY PRO PHE THR GLY GLN GLY HIS LYS GLY          
SEQRES  26 A  738  LEU TYR GLU ILE LEU THR THR SER TRP HIS ALA GLN LEU          
SEQRES  27 A  738  SER ILE ASN LEU ALA MET LEU GLY SER LEU THR ILE VAL          
SEQRES  28 A  738  VAL ALA GLN HIS MET TYR SER MET PRO PRO TYR PRO TYR          
SEQRES  29 A  738  LEU ALA THR ASP TYR ALA THR GLN LEU SER LEU PHE THR          
SEQRES  30 A  738  HIS HIS MET TRP ILE GLY GLY PHE LEU ILE VAL GLY ALA          
SEQRES  31 A  738  ALA ALA HIS ALA ALA ILE PHE MET VAL ARG ASP TYR ASP          
SEQRES  32 A  738  PRO THR THR ARG TYR ASN ASP LEU LEU ASP ARG VAL LEU          
SEQRES  33 A  738  ARG HIS ARG ASP ALA ILE ILE SER HIS LEU ASN TRP VAL          
SEQRES  34 A  738  CYS ILE PHE LEU GLY PHE HIS SER PHE GLY LEU TYR ILE          
SEQRES  35 A  738  HIS ASN ASP THR MET SER ALA LEU GLY ARG PRO GLN ASP          
SEQRES  36 A  738  MET PHE SER ASP THR ALA ILE GLN LEU GLN PRO VAL PHE          
SEQRES  37 A  738  ALA GLN TRP ILE GLN ASN THR HIS ALA LEU ALA PRO GLY          
SEQRES  38 A  738  THR THR ALA PRO GLY ALA THR ALA SER THR SER LEU THR          
SEQRES  39 A  738  TRP GLY GLY GLY ASP LEU VAL ALA VAL GLY ASN LYS VAL          
SEQRES  40 A  738  ALA LEU LEU PRO ILE PRO LEU GLY THR ALA ASP PHE LEU          
SEQRES  41 A  738  VAL HIS HIS ILE HIS ALA PHE THR ILE HIS VAL THR VAL          
SEQRES  42 A  738  LEU ILE LEU LEU LYS GLY VAL LEU PHE ALA ARG SER SER          
SEQRES  43 A  738  ARG LEU ILE PRO ASP LYS ALA ASN LEU GLY PHE ARG PHE          
SEQRES  44 A  738  PRO CYS ASP GLY PRO GLY ARG GLY GLY THR CYS GLN VAL          
SEQRES  45 A  738  SER ALA TRP ASP HIS VAL PHE LEU GLY LEU PHE TRP MET          
SEQRES  46 A  738  TYR ASN SER ILE SER VAL VAL ILE PHE HIS PHE SER TRP          
SEQRES  47 A  738  LYS MET GLN SER ASP VAL TRP GLY THR ILE ASN ASP GLN          
SEQRES  48 A  738  GLY VAL VAL THR HIS ILE THR ALA GLY ASN PHE ALA GLN          
SEQRES  49 A  738  SER SER ILE THR ILE ASN GLY TRP LEU ARG ASP PHE LEU          
SEQRES  50 A  738  TRP ALA GLN ALA SER GLN VAL ILE GLN SER TYR GLY SER          
SEQRES  51 A  738  SER LEU SER ALA TYR GLY LEU PHE PHE LEU GLY ALA HIS          
SEQRES  52 A  738  PHE VAL TRP ALA PHE SER LEU MET PHE LEU PHE SER GLY          
SEQRES  53 A  738  ARG GLY TYR TRP GLN GLU LEU ILE GLU SER ILE VAL TRP          
SEQRES  54 A  738  ALA HIS ASN LYS LEU LYS VAL ALA PRO ALA THR GLN PRO          
SEQRES  55 A  738  ARG ALA LEU SER ILE VAL GLN GLY ARG ALA VAL GLY VAL          
SEQRES  56 A  738  THR HIS TYR LEU LEU GLY GLY ILE ALA THR THR TRP ALA          
SEQRES  57 A  738  PHE PHE LEU ALA ARG ILE ILE ALA VAL GLY                      
SEQRES   1 B  733  ALA LEU ARG ILE PRO ARG PHE SER GLN GLY ILE ALA GLN          
SEQRES   2 B  733  ASP PRO THR THR ARG ARG ILE TRP PHE GLY ILE ALA THR          
SEQRES   3 B  733  ALA HIS ASP PHE GLU SER HIS ASP ASP ILE THR GLU GLY          
SEQRES   4 B  733  ARG LEU TYR GLN ASN ILE PHE ALA SER HIS PHE GLY GLN          
SEQRES   5 B  733  LEU ALA ILE ILE PHE LEU TRP THR SER GLY ASN LEU PHE          
SEQRES   6 B  733  HIS VAL ALA TRP GLN GLY ASN PHE GLU ALA TRP VAL GLN          
SEQRES   7 B  733  ASP PRO PHE HIS VAL ARG PRO ILE ALA HIS ALA ILE TRP          
SEQRES   8 B  733  ASP PRO HIS PHE GLY GLN PRO ALA VAL GLU ALA PHE THR          
SEQRES   9 B  733  ARG GLY GLY ALA LEU GLY PRO VAL ASN ASN ALA TYR SER          
SEQRES  10 B  733  GLY VAL TYR GLN TRP TRP TYR THR ILE GLY LEU ARG THR          
SEQRES  11 B  733  ASN GLU ASP LEU TYR THR GLY ALA ILE PHE LEU LEU PHE          
SEQRES  12 B  733  LEU SER PHE ILE SER LEU LEU ALA GLY TRP LEU HIS LEU          
SEQRES  13 B  733  GLN PRO LYS TRP LYS PRO SER VAL SER TRP PHE LYS ASN          
SEQRES  14 B  733  ALA GLU SER ARG LEU ASN HIS HIS LEU SER GLY LEU PHE          
SEQRES  15 B  733  GLY VAL SER SER LEU ALA TRP ALA GLY HIS LEU VAL HIS          
SEQRES  16 B  733  VAL ALA ILE PRO GLY SER ARG GLY GLU TYR VAL ARG TRP          
SEQRES  17 B  733  ASN ASN PHE LEU ASP VAL LEU PRO TYR PRO GLN GLY LEU          
SEQRES  18 B  733  GLY PRO LEU LEU THR GLY GLN TRP ASN LEU TYR ALA GLN          
SEQRES  19 B  733  ASN PRO SER SER SER ASN HIS LEU PHE GLY THR THR GLN          
SEQRES  20 B  733  GLY ALA GLY THR ALA ILE LEU THR ILE LEU GLY GLY PHE          
SEQRES  21 B  733  HIS PRO GLN THR GLN SER LEU TRP LEU THR ASP VAL ALA          
SEQRES  22 B  733  HIS HIS HIS LEU ALA ILE ALA PHE LEU PHE LEU ILE GLY          
SEQRES  23 B  733  GLY LEU MET TYR ARG THR ASN PHE GLY ILE GLY HIS SER          
SEQRES  24 B  733  ILE LYS TYR ILE LEU GLU ALA HIS ILE PRO PRO GLY GLY          
SEQRES  25 B  733  ARG LEU GLY ARG GLY HIS LYS GLY LEU TYR ASP THR ILE          
SEQRES  26 B  733  ASN ASN SER ILE HIS PHE GLN LEU GLY LEU ALA LEU ALA          
SEQRES  27 B  733  SER LEU GLY VAL ILE THR SER LEU VAL ALA GLN HIS MET          
SEQRES  28 B  733  TYR SER LEU PRO ALA TYR ALA PHE ILE ALA GLN ASP PHE          
SEQRES  29 B  733  THR THR GLN ALA ALA LEU TYR THR HIS HIS GLN TYR ILE          
SEQRES  30 B  733  ALA GLY PHE ILE MET THR GLY ALA PHE ALA HIS GLY PRO          
SEQRES  31 B  733  ILE PHE PHE ILE ARG ASP TYR ASN PRO GLU GLN ASN ALA          
SEQRES  32 B  733  ASP ASN VAL LEU ALA ARG MET LEU GLU HIS LYS GLU ALA          
SEQRES  33 B  733  ILE ILE SER HIS LEU SER TRP ALA SER LEU PHE LEU GLY          
SEQRES  34 B  733  PHE HIS THR LEU GLY LEU TYR VAL HIS ASN ASP VAL MET          
SEQRES  35 B  733  LEU ALA PHE GLY THR PRO GLU LYS GLN ILE LEU ILE GLU          
SEQRES  36 B  733  PRO ILE PHE ALA GLN TRP ILE GLN SER ALA HIS GLY LYS          
SEQRES  37 B  733  THR THR TYR GLY PHE ASP ILE PRO LEU SER SER THR ASN          
SEQRES  38 B  733  GLY PRO ALA LEU ASN ALA GLY ARG ASN ILE TRP LEU PRO          
SEQRES  39 B  733  GLY TRP LEU ASN ALA ILE ASN GLU ASN SER ASN SER LEU          
SEQRES  40 B  733  PHE LEU THR ILE GLY PRO GLY ASP PHE LEU VAL HIS HIS          
SEQRES  41 B  733  ALA ILE ALA LEU GLY LEU HIS THR THR THR LEU ILE LEU          
SEQRES  42 B  733  VAL LYS GLY ALA LEU ASP ALA ARG GLY SER LYS LEU MET          
SEQRES  43 B  733  PRO ASP LYS LYS ASP PHE GLY TYR SER PHE PRO CYS ASP          
SEQRES  44 B  733  GLY PRO GLY ARG GLY GLY THR CYS ASP ILE SER ALA TRP          
SEQRES  45 B  733  ASP ASP PHE TYR LEU ALA VAL PHE TRP MET LEU ASN THR          
SEQRES  46 B  733  ILE GLY TRP VAL THR PHE TYR TRP HIS TRP LYS HIS ILE          
SEQRES  47 B  733  THR LEU TRP ARG GLY ASN VAL SER GLN PHE ASN GLU SER          
SEQRES  48 B  733  SER THR TYR LEU MET GLY TRP LEU ARG ASP TYR LEU TRP          
SEQRES  49 B  733  LEU ASN SER SER GLN LEU ILE ASN GLY ILE THR PRO LEU          
SEQRES  50 B  733  VAL CYS ASN SER LEU SER VAL TRP ALA TRP MET PHE LEU          
SEQRES  51 B  733  PHE GLY HIS LEU VAL TRP ALA THR GLY PHE MET PHE LEU          
SEQRES  52 B  733  ILE SER TRP ARG GLY TYR TRP GLN GLU LEU ILE GLU THR          
SEQRES  53 B  733  LEU ALA TRP ALA HIS GLU ARG THR PRO LEU ALA ASN LEU          
SEQRES  54 B  733  ILE ARG TRP ARG ASP LYS PRO VAL ALA LEU SER ILE VAL          
SEQRES  55 B  733  GLN ALA ARG LEU VAL GLY LEU VAL HIS PHE SER VAL GLY          
SEQRES  56 B  733  TYR ILE PHE THR TYR ALA ALA PHE LEU ILE ALA SER THR          
SEQRES  57 B  733  SER GLY LYS PHE GLY                                          
SEQRES   1 C   81  MET SER HIS SER VAL LYS ILE TYR ASP THR CYS ILE GLY          
SEQRES   2 C   81  CYS THR GLN CYS VAL ARG ALA CYS PRO THR ASP VAL LEU          
SEQRES   3 C   81  GLU MET ILE PRO TRP GLY GLY CYS LYS ALA LYS GLN ILE          
SEQRES   4 C   81  ALA SER ALA PRO ARG THR GLU ASP CYS VAL GLY CYS LYS          
SEQRES   5 C   81  ARG CYS GLU SER ALA CYS PRO THR ASP PHE LEU SER VAL          
SEQRES   6 C   81  ARG VAL TYR LEU TRP HIS GLU THR THR ARG SER MET GLY          
SEQRES   7 C   81  LEU ALA TYR                                                  
SEQRES   1 D  138  GLU LEU ASP PRO ASN THR PRO SER PRO ILE PHE GLY GLY          
SEQRES   2 D  138  SER THR GLY GLY LEU LEU ARG LYS ALA GLN VAL GLU GLU          
SEQRES   3 D  138  PHE TYR VAL ILE THR TRP ASP SER PRO LYS GLU GLN ILE          
SEQRES   4 D  138  PHE GLU MET PRO THR GLY GLY ALA ALA ILE MET ARG GLU          
SEQRES   5 D  138  GLY PRO ASN LEU LEU LYS LEU ALA ARG LYS GLU GLN CYS          
SEQRES   6 D  138  LEU ALA LEU GLY THR ARG LEU ARG SER LYS TYR LYS ILE          
SEQRES   7 D  138  LYS TYR GLN PHE TYR ARG VAL PHE PRO ASN GLY GLU VAL          
SEQRES   8 D  138  GLN TYR LEU HIS PRO LYS ASP GLY VAL TYR PRO GLU LYS          
SEQRES   9 D  138  VAL ASN ALA GLY ARG GLN GLY VAL GLY GLN ASN PHE ARG          
SEQRES  10 D  138  SER ILE GLY LYS ASN VAL SER PRO ILE GLU VAL LYS PHE          
SEQRES  11 D  138  THR GLY LYS GLN PRO TYR ASP LEU                              
SEQRES   1 E   64  ILE GLY PRO LYS ARG GLY ALA LYS VAL LYS ILE LEU ARG          
SEQRES   2 E   64  LYS GLU SER TYR TRP TYR LYS GLY THR GLY SER VAL VAL          
SEQRES   3 E   64  ALA VAL ASP GLN ASP PRO ASN THR ARG TYR PRO VAL VAL          
SEQRES   4 E   64  VAL ARG PHE ASN LYS VAL ASN TYR ALA ASN VAL SER THR          
SEQRES   5 E   64  ASN ASN TYR ALA LEU ASP GLU ILE VAL GLU VAL GLU              
SEQRES   1 F  154  ASP ILE ALA GLY LEU THR PRO CYS LYS GLU SER LYS GLN          
SEQRES   2 F  154  PHE ALA LYS ARG GLU LYS GLN ALA LEU LYS LYS LEU GLN          
SEQRES   3 F  154  ALA SER LEU LYS LEU TYR ALA ASP ASP SER ALA PRO ALA          
SEQRES   4 F  154  LEU ALA ILE LYS ALA THR MET GLU LYS THR LYS LYS ARG          
SEQRES   5 F  154  PHE ASP ASN TYR GLY LYS TYR GLY LEU LEU CYS GLY SER          
SEQRES   6 F  154  ASP GLY LEU PRO HIS LEU ILE VAL SER GLY ASP GLN ARG          
SEQRES   7 F  154  HIS TRP GLY GLU PHE ILE THR PRO GLY ILE LEU PHE LEU          
SEQRES   8 F  154  TYR ILE ALA GLY TRP ILE GLY TRP VAL GLY ARG SER TYR          
SEQRES   9 F  154  LEU ILE ALA ILE ARG ASP GLU LYS LYS PRO THR GLN LYS          
SEQRES  10 F  154  GLU ILE ILE ILE ASP VAL PRO LEU ALA SER SER LEU LEU          
SEQRES  11 F  154  PHE ARG GLY PHE SER TRP PRO VAL ALA ALA TYR ARG GLU          
SEQRES  12 F  154  LEU LEU ASN GLY GLU LEU VAL ASP ASN ASN PHE                  
SEQRES   1 G   95  SER ALA LEU VAL ILE SER LEU SER THR GLY LEU SER LEU          
SEQRES   2 G   95  PHE LEU GLY ARG PHE VAL PHE PHE ASN PHE GLN ARG GLU          
SEQRES   3 G   95  ASN VAL ALA LYS GLN VAL PRO GLU GLN ASN GLY LEU THR          
SEQRES   4 G   95  HIS PHE GLU ALA GLY ASP THR ARG ALA LYS GLU TYR VAL          
SEQRES   5 G   95  SER LEU LEU LYS SER ASN ASP PRO VAL GLY PHE ASN ILE          
SEQRES   6 G   95  VAL ASP VAL LEU ALA TRP GLY SER ILE GLY HIS VAL VAL          
SEQRES   7 G   95  ALA TYR TYR ILE LEU ALA THR THR SER ASN GLY TYR ASP          
SEQRES   8 G   95  PRO ALA PHE PHE                                              
SEQRES   1 H   69  ASP LEU GLU ASP LEU GLY ASN THR THR GLY GLN TRP ASP          
SEQRES   2 H   69  SER TYR GLY SER ASP ALA PRO SER PRO TYR ASN PRO LEU          
SEQRES   3 H   69  GLN SER LYS LEU PHE GLU THR PHE ALA ALA PRO PHE THR          
SEQRES   4 H   69  LYS ARG GLY LEU LEU LEU LYS PHE LEU ILE LEU GLY GLY          
SEQRES   5 H   69  GLY SER THR LEU ALA TYR LEU SER ALA THR ALA SER GLY          
SEQRES   6 H   69  ASP ILE LEU PRO                                              
SEQRES   1 I   30  MET ILE ASN LEU PRO SER LEU PHE VAL PRO LEU VAL GLY          
SEQRES   2 I   30  LEU LEU PHE PRO ALA VAL ALA MET ALA SER LEU PHE LEU          
SEQRES   3 I   30  HIS VAL GLU LYS                                              
SEQRES   1 J   42  MET ARG ASP LEU LYS THR TYR LEU SER VAL ALA PRO VAL          
SEQRES   2 J   42  VAL SER THR LEU TRP PHE GLY ALA LEU ALA GLY LEU LEU          
SEQRES   3 J   42  ILE GLU ILE ASN ARG PHE PHE PRO ASP ALA LEU ILE PHE          
SEQRES   4 J   42  PRO PHE PHE                                                  
SEQRES   1 K   84  ASP PHE ILE GLY SER PRO THR ASN LEU ILE MET VAL THR          
SEQRES   2 K   84  SER THR SER LEU MET LEU PHE ALA GLY ARG PHE GLY LEU          
SEQRES   3 K   84  ALA PRO SER ALA ASN ARG LYS ALA THR ALA GLY LEU LYS          
SEQRES   4 K   84  LEU GLU VAL ARG ASP SER GLY LEU GLN THR GLY ASP PRO          
SEQRES   5 K   84  ALA GLY PHE THR LEU ALA ASP THR LEU ALA CYS GLY VAL          
SEQRES   6 K   84  VAL GLY HIS ILE ILE GLY VAL GLY VAL VAL LEU GLY LEU          
SEQRES   7 K   84  LYS ASN ILE GLY ALA LEU                                      
SEQRES   1 L  161  LYS PRO THR TYR GLN VAL ILE GLN PRO ILE ASN GLY ASP          
SEQRES   2 L  161  PRO PHE ILE GLY SER LEU GLU THR PRO VAL THR SER SER          
SEQRES   3 L  161  PRO LEU ILE ALA TRP TYR LEU SER ASN LEU PRO ALA TYR          
SEQRES   4 L  161  ARG THR ALA VAL SER PRO LEU LEU ARG GLY ILE GLU VAL          
SEQRES   5 L  161  GLY LEU ALA HIS GLY TYR LEU LEU VAL GLY PRO PHE VAL          
SEQRES   6 L  161  LYS ALA GLY PRO LEU ARG ASN THR GLU ILE ALA GLY GLN          
SEQRES   7 L  161  ALA GLY SER LEU ALA ALA GLY GLY LEU VAL VAL ILE LEU          
SEQRES   8 L  161  SER LEU CYS LEU THR ILE TYR GLY ILE SER SER PHE ASN          
SEQRES   9 L  161  GLU GLY ALA PRO SER THR ALA PRO SER LEU THR LEU THR          
SEQRES  10 L  161  GLY ARG LYS LYS GLU PRO ASP GLN LEU GLN THR ALA ASP          
SEQRES  11 L  161  GLY TRP ALA LYS PHE THR GLY GLY PHE PHE PHE GLY GLY          
SEQRES  12 L  161  ILE SER GLY VAL ILE TRP ALA TYR PHE LEU LEU TYR VAL          
SEQRES  13 L  161  LEU ASP LEU PRO TYR                                          
SEQRES   1 N   85  GLY VAL ILE GLU GLU TYR LEU GLU LYS SER LYS THR ASN          
SEQRES   2 N   85  LYS GLU LEU ASN ASP LYS LYS ARG LEU ALA THR THR GLY          
SEQRES   3 N   85  ALA ASN PHE ALA ARG ALA TYR THR VAL GLU PHE GLY SER          
SEQRES   4 N   85  CYS LYS PHE PRO GLU ASN PHE THR GLY CYS GLN ASP LEU          
SEQRES   5 N   85  ALA LYS GLN LYS LYS VAL PRO PHE LEU SER ASP ASP LEU          
SEQRES   6 N   85  ASP LEU GLU CYS GLU GLY LYS ASP LYS TYR LYS CYS GLY          
SEQRES   7 N   85  SER ASN VAL PHE TRP LYS TRP                                  
SEQRES   1 R   53  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 R   53  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   3 R   53  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   4 R   53  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   5 R   53  UNK                                                          
SEQRES   1 1  170  SER ALA PRO GLY ASP PHE GLY PHE ASP PRO LEU GLY LEU          
SEQRES   2 1  170  GLY GLU VAL PRO ALA ASN LEU GLU ARG TYR LYS GLU SER          
SEQRES   3 1  170  GLU LEU ILE HIS CYS ARG TRP ALA MET LEU ALA VAL PRO          
SEQRES   4 1  170  GLY ILE LEU VAL PRO GLU ALA LEU GLY TYR GLY ASN TRP          
SEQRES   5 1  170  VAL LYS ALA GLN GLU TRP ALA ALA LEU PRO GLY GLY GLN          
SEQRES   6 1  170  ALA THR TYR LEU GLY ASN PRO VAL PRO TRP GLY THR LEU          
SEQRES   7 1  170  PRO THR ILE LEU ALA ILE GLU PHE LEU ALA ILE ALA PHE          
SEQRES   8 1  170  VAL GLU HIS GLN ARG SER MET GLU LYS ASP PRO GLU LYS          
SEQRES   9 1  170  LYS LYS TYR PRO GLY GLY ALA PHE ASP PRO LEU GLY TYR          
SEQRES  10 1  170  SER LYS ASP PRO LYS LYS LEU GLU GLU LEU LYS VAL LYS          
SEQRES  11 1  170  GLU ILE LYS ASN GLY ARG LEU ALA LEU LEU ALA PHE VAL          
SEQRES  12 1  170  GLY PHE CYS VAL GLN GLN SER ALA TYR PRO GLY THR GLY          
SEQRES  13 1  170  PRO LEU GLU ASN LEU ALA THR HIS LEU ALA ASP PRO TRP          
SEQRES  14 1  170  HIS                                                          
SEQRES   1 2  176  SER ASP PRO GLU SER LEU ARG TRP ASN VAL GLN ALA GLU          
SEQRES   2 2  176  LEU VAL HIS SER ARG TRP ALA MET LEU GLY ALA ALA GLY          
SEQRES   3 2  176  ILE PHE ILE PRO GLU PHE LEU THR LYS LEU GLY ILE LEU          
SEQRES   4 2  176  ASN THR PRO SER TRP TYR THR ALA GLY GLU GLN GLU TYR          
SEQRES   5 2  176  PHE THR ASP THR THR THR LEU PHE ILE VAL GLU LEU VAL          
SEQRES   6 2  176  PHE ILE GLY TRP ALA GLU GLY ARG ARG TRP ALA ASP ILE          
SEQRES   7 2  176  LEU ASN PRO GLY CYS VAL ASN THR ASP PRO ILE PHE PRO          
SEQRES   8 2  176  ASN ASN LYS LEU THR GLY THR ASP VAL GLY TYR PRO GLY          
SEQRES   9 2  176  GLY LEU TRP PHE ASP PRO LEU GLY TRP GLY SER ALA SER          
SEQRES  10 2  176  PRO GLN LYS LEU LYS GLU LEU ARG THR LYS GLU ILE LYS          
SEQRES  11 2  176  ASN GLY ARG LEU ALA MET LEU ALA VAL MET GLY ALA TRP          
SEQRES  12 2  176  PHE GLN HIS ILE TYR THR GLY THR GLY PRO ILE ASP ASN          
SEQRES  13 2  176  LEU PHE ALA HIS LEU ALA ASP PRO GLY HIS ALA THR ILE          
SEQRES  14 2  176  PHE ALA ALA PHE THR PRO LYS                                  
SEQRES   1 3  172  SER ASP PRO GLU GLY THR GLY GLY PHE ILE GLU PRO ARG          
SEQRES   2 3  172  TRP LEU ALA TYR GLY GLU VAL ILE ASN GLY ARG PHE ALA          
SEQRES   3 3  172  MET LEU GLY ALA VAL GLY ALA ILE ALA PRO GLU TYR LEU          
SEQRES   4 3  172  GLY LYS VAL GLY LEU ILE PRO GLN GLU THR ALA LEU ALA          
SEQRES   5 3  172  TRP PHE GLN THR GLY VAL ILE PRO PRO ALA GLY THR TYR          
SEQRES   6 3  172  ASN TYR TRP ALA ASP ASN TYR THR LEU PHE VAL LEU GLU          
SEQRES   7 3  172  MET ALA LEU MET GLY PHE ALA GLU HIS ARG ARG PHE GLN          
SEQRES   8 3  172  ASP TRP ALA LYS PRO GLY SER MET GLY LYS GLN TYR PHE          
SEQRES   9 3  172  LEU GLY LEU GLU LYS GLY PHE GLY GLY SER GLY ASN PRO          
SEQRES  10 3  172  ALA TYR PRO GLY GLY PRO PHE PHE ASN PRO LEU GLY PHE          
SEQRES  11 3  172  GLY LYS ASP GLU LYS SER LEU LYS GLU LEU LYS LEU LYS          
SEQRES  12 3  172  GLU VAL LYS ASN GLY ARG LEU ALA MET LEU ALA ILE LEU          
SEQRES  13 3  172  GLY TYR PHE ILE GLN GLY LEU VAL THR GLY VAL GLY PRO          
SEQRES  14 3  172  TYR GLN ASN                                                  
SEQRES   1 4  166  LEU ALA GLU ASP PRO GLU ASN LEU ARG TRP PHE VAL GLN          
SEQRES   2 4  166  ALA GLU LEU VAL ASN GLY ARG TRP ALA MET LEU GLY VAL          
SEQRES   3 4  166  ALA GLY MET LEU LEU PRO GLU VAL PHE THR SER ILE GLY          
SEQRES   4 4  166  ILE ILE ASN VAL PRO LYS TRP TYR ALA ALA GLY LYS GLU          
SEQRES   5 4  166  GLU TYR PHE ALA SER SER SER THR LEU PHE VAL ILE GLU          
SEQRES   6 4  166  PHE ILE LEU SER HIS TYR VAL GLU ILE ARG ARG TRP GLN          
SEQRES   7 4  166  ASP ILE LYS ASN PRO GLY SER VAL ASN GLN ASP PRO ILE          
SEQRES   8 4  166  PHE LYS GLN TYR SER LEU PRO ALA GLY GLU VAL GLY TYR          
SEQRES   9 4  166  PRO GLY GLY ILE PHE ASN PRO LEU ASN PHE ALA PRO THR          
SEQRES  10 4  166  LEU GLU ALA LYS GLU LYS GLU ILE ALA ASN GLY ARG LEU          
SEQRES  11 4  166  MET LEU ALA PHE LEU GLY PHE ILE ILE GLN HIS ASN VAL          
SEQRES  12 4  166  THR GLY LYS GLY PRO PHE ASP ASN LEU LEU GLN HIS ILE          
SEQRES  13 4  166  SER ASP PRO TRP HIS ASN THR ILE VAL GLN                      
HET    CLA  A1101      50                                                       
HET    CLA  A1102      55                                                       
HET    CLA  A1103      65                                                       
HET    CLA  A1104      57                                                       
HET    CLA  A1105      46                                                       
HET    CLA  A1106      65                                                       
HET    CLA  A1107      55                                                       
HET    CLA  A1108      45                                                       
HET    CLA  A1109      65                                                       
HET    CLA  A1110      54                                                       
HET    CLA  A1111      54                                                       
HET    CLA  A1112      45                                                       
HET    CLA  A1113      50                                                       
HET    CLA  A1115      65                                                       
HET    CLA  A1116      52                                                       
HET    CLA  A1117      65                                                       
HET    CLA  A1119      65                                                       
HET    CLA  A1120      51                                                       
HET    CLA  A1121      42                                                       
HET    CLA  A1122      55                                                       
HET    CLA  A1123      65                                                       
HET    CLA  A1124      65                                                       
HET    CLA  A1125      65                                                       
HET    CLA  A1126      65                                                       
HET    CLA  A1127      55                                                       
HET    CLA  A1128      65                                                       
HET    CLA  A1129      50                                                       
HET    CLA  A1131      65                                                       
HET    CLA  A1132      65                                                       
HET    CLA  A1133      50                                                       
HET    CLA  A1134      45                                                       
HET    CLA  A1135      51                                                       
HET    CLA  A1136      65                                                       
HET    CLA  A1137      47                                                       
HET    CLA  A1138      65                                                       
HET    CLA  A1139      51                                                       
HET    CLA  A1140      65                                                       
HET    CLA  A1141      65                                                       
HET    CLA  A1149      46                                                       
HET    CLA  A1151      50                                                       
HET    CLA  A1237      65                                                       
HET    CLA  A1309      25                                                       
HET    PQN  A5001      33                                                       
HET    BCR  A6002      40                                                       
HET    BCR  A6003      40                                                       
HET    BCR  A6007      40                                                       
HET    BCR  A6008      40                                                       
HET    BCR  A6011      40                                                       
HET    LMU  A7010      35                                                       
HET    LMU  A7016      35                                                       
HET    LMU  A7023      35                                                       
HET    LMU  A7035      35                                                       
HET    LMU  A7044      35                                                       
HET    LMU  A7045      35                                                       
HET    SF4  A8001       8                                                       
HET    CLA  A9011      65                                                       
HET    CLA  A9012      65                                                       
HET    CLA  A9013      65                                                       
HET    CLA  A9022      65                                                       
HET    CLA  A9023      65                                                       
HET    CLA  B1201      45                                                       
HET    CLA  B1202      65                                                       
HET    CLA  B1203      65                                                       
HET    CLA  B1205      65                                                       
HET    CLA  B1206      65                                                       
HET    CLA  B1208      54                                                       
HET    CLA  B1209      55                                                       
HET    CLA  B1210      65                                                       
HET    CLA  B1211      65                                                       
HET    CLA  B1212      60                                                       
HET    CLA  B1213      46                                                       
HET    CLA  B1214      59                                                       
HET    CLA  B1215      60                                                       
HET    CLA  B1216      61                                                       
HET    CLA  B1217      50                                                       
HET    CLA  B1218      46                                                       
HET    CLA  B1219      55                                                       
HET    CLA  B1220      65                                                       
HET    CLA  B1221      54                                                       
HET    CLA  B1222      58                                                       
HET    CLA  B1223      65                                                       
HET    CLA  B1224      65                                                       
HET    CLA  B1225      65                                                       
HET    CLA  B1226      65                                                       
HET    CLA  B1227      50                                                       
HET    CLA  B1228      50                                                       
HET    CLA  B1229      65                                                       
HET    CLA  B1230      50                                                       
HET    CLA  B1231      45                                                       
HET    CLA  B1232      45                                                       
HET    CLA  B1233      51                                                       
HET    CLA  B1234      60                                                       
HET    CLA  B1235      65                                                       
HET    CLA  B1236      47                                                       
HET    CLA  B1238      65                                                       
HET    CLA  B1239      65                                                       
HET    CLA  B1301      36                                                       
HET    PQN  B5002      33                                                       
HET    BCR  B6004      40                                                       
HET    BCR  B6005      40                                                       
HET    BCR  B6006      40                                                       
HET    BCR  B6010      40                                                       
HET    BCR  B6017      40                                                       
HET    BCR  B6020      40                                                       
HET    LMU  B7012      25                                                       
HET    LMU  B7038      35                                                       
HET    LMU  B7040      35                                                       
HET    LMG  B7101      49                                                       
HET    CLA  B9010      65                                                       
HET    LMU  C7015      35                                                       
HET    SF4  C8002       8                                                       
HET    SF4  C8003       8                                                       
HET    LMU  D7050      35                                                       
HET    LMU  E7037      35                                                       
HET    LMU  E7048      35                                                       
HET    CLA  F1240      36                                                       
HET    CLA  F1302      41                                                       
HET    CLA  F1305      53                                                       
HET    BCR  F6014      40                                                       
HET    BCR  F6016      40                                                       
HET    LMU  F7036      34                                                       
HET    CLA  G1242      51                                                       
HET    LMU  G7026      35                                                       
HET    LMU  G7039      35                                                       
HET    LMU  G7051      35                                                       
HET    CLA  H1145      65                                                       
HET    CLA  H1207      65                                                       
HET    CLA  H1241      55                                                       
HET    CLA  H1505      55                                                       
HET    LMU  H7002      35                                                       
HET    LMU  H7011      35                                                       
HET    LMU  H7017      35                                                       
HET    LMU  H7028      35                                                       
HET    LMU  H7030      35                                                       
HET    LMU  H7032      35                                                       
HET    LMU  H7043      35                                                       
HET    CLA  I1204      60                                                       
HET    BCR  I6018      40                                                       
HET    BCR  I6021      40                                                       
HET    CLA  J1308      55                                                       
HET    CLA  J1311      61                                                       
HET    BCR  J6012      40                                                       
HET    CLA  K1142      45                                                       
HET    CLA  K1143      50                                                       
HET    CLA  K1146      50                                                       
HET    CLA  K3009      65                                                       
HET    LMU  K7001      35                                                       
HET    LMU  K7041      35                                                       
HET    LMU  K7042      35                                                       
HET    LMU  K7047      35                                                       
HET    CLA  L1130      65                                                       
HET    CLA  L1148      55                                                       
HET    CLA  L1501      50                                                       
HET    CLA  L1502      47                                                       
HET    CLA  L1503      50                                                       
HET    CLA  L1504      55                                                       
HET    BCR  L6019      40                                                       
HET    LMU  L7029      35                                                       
HET    LMU  N7049      35                                                       
HET    CLA  R1144      57                                                       
HET    CLA  R1150      65                                                       
HET    LMU  R7007      35                                                       
HET    LMU  R7014      35                                                       
HET    LMU  R7020      35                                                       
HET    LMU  R7021      35                                                       
HET    LMU  R7022      35                                                       
HET    LMU  R7024      35                                                       
HET    LMU  R7025      35                                                       
HET    CLA  11001      46                                                       
HET    CLA  11002      47                                                       
HET    CLA  11003      47                                                       
HET    CLA  11005      46                                                       
HET    CLA  11006      36                                                       
HET    CLA  11007      61                                                       
HET    CLA  11008      51                                                       
HET    CLA  11010      46                                                       
HET    CLA  11011      36                                                       
HET    CLA  11012      36                                                       
HET    CLA  11013      51                                                       
HET    CLA  11014      61                                                       
HET    CLA  11015      25                                                       
HET    CLA  11303      51                                                       
HET    CLA  11310      25                                                       
HET    BCR  16023      40                                                       
HET    LMU  17004      35                                                       
HET    LMU  17013      35                                                       
HET    CLA  21307      25                                                       
HET    CLA  22001      51                                                       
HET    CLA  22002      56                                                       
HET    CLA  22003      25                                                       
HET    CLA  22004      50                                                       
HET    CLA  22005      25                                                       
HET    CLA  22006      65                                                       
HET    CLA  22007      65                                                       
HET    CLA  22008      25                                                       
HET    CLA  22010      25                                                       
HET    CLA  22011      25                                                       
HET    CLA  22012      50                                                       
HET    CLA  22013      50                                                       
HET    CLA  22014      61                                                       
HET    CLA  24009      65                                                       
HET    LMU  27006      35                                                       
HET    LMU  27027      35                                                       
HET    LMU  27031      35                                                       
HET    LMU  27046      35                                                       
HET    CLA  31118      36                                                       
HET    CLA  31147      46                                                       
HET    CLA  32009      56                                                       
HET    CLA  33001      25                                                       
HET    CLA  33002      25                                                       
HET    CLA  33003      36                                                       
HET    CLA  33004      25                                                       
HET    CLA  33005      25                                                       
HET    CLA  33006      25                                                       
HET    CLA  33007      42                                                       
HET    CLA  33008      50                                                       
HET    CLA  33010      25                                                       
HET    CLA  33011      65                                                       
HET    CLA  33012      25                                                       
HET    CLA  33013      65                                                       
HET    CLA  33014      25                                                       
HET    CLA  33015      25                                                       
HET    CLA  33016      65                                                       
HET    CLA  33017      50                                                       
HET    BCR  36022      40                                                       
HET    LMU  37003      35                                                       
HET    LMU  37005      35                                                       
HET    CLA  41004      55                                                       
HET    CLA  41009      36                                                       
HET    CLA  41304      65                                                       
HET    CLA  41306      55                                                       
HET    CLA  44001      50                                                       
HET    CLA  44002      52                                                       
HET    CLA  44003      55                                                       
HET    CLA  44004      25                                                       
HET    CLA  44005      25                                                       
HET    CLA  44006      55                                                       
HET    CLA  44007      52                                                       
HET    CLA  44010      25                                                       
HET    CLA  44011      25                                                       
HET    CLA  44012      36                                                       
HET    CLA  44013      25                                                       
HET    CLA  44014      47                                                       
HET    CLA  44015      46                                                       
HET    LMU  47008      35                                                       
HET    LMU  47009      34                                                       
HET    LMU  47018      35                                                       
HET    LMU  47019      35                                                       
HET    LMU  47033      35                                                       
HET    LMU  47034      35                                                       
HET    LMU  47052      35                                                       
HET    LMU  47053      34                                                       
HETNAM     CLA CHLOROPHYLL A                                                    
HETNAM     PQN PHYLLOQUINONE                                                    
HETNAM     BCR BETA-CAROTENE                                                    
HETNAM     LMU DODECYL-ALPHA-D-MALTOSIDE                                        
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE                        
HETSYN     PQN VITAMIN K1; 2-METHYL-3-PHYTYL-1,4-NAPHTHOQUINONE                 
FORMUL  19  CLA    174(C55 H72 MG N4 O5 2+)                                     
FORMUL  61  PQN    2(C31 H46 O2)                                                
FORMUL  62  BCR    19(C40 H56)                                                  
FORMUL  67  LMU    53(C24 H46 O11)                                              
FORMUL  73  SF4    3(FE4 S4)                                                    
FORMUL  26  LMG    C45 H86 O10                                                  
HELIX    1   1 THR A   51  ASN A   56  1                                   6    
HELIX    2   2 GLU A   73  PHE A   90  1                                  18    
HELIX    3   3 PHE A   90  ALA A  101  1                                  12    
HELIX    4   4 ASN A  105  ASP A  112  1                                   8    
HELIX    5   5 ILE A  152  SER A  156  5                                   5    
HELIX    6   6 SER A  160  TYR A  165  1                                   6    
HELIX    7   7 CYS A  166  PHE A  174  1                                   9    
HELIX    8   8 LEU A  193  ASP A  198  1                                   6    
HELIX    9   9 MET A  202  LEU A  207  1                                   6    
HELIX   10  10 SER A  215  ARG A  220  1                                   6    
HELIX   11  11 LEU A  227  GLN A  231  5                                   5    
HELIX   12  12 THR A  297  LEU A  311  1                                  15    
HELIX   13  13 ILE A  327  GLU A  332  1                                   6    
HELIX   14  14 GLY A  340  LYS A  344  5                                   5    
HELIX   15  15 GLU A  348  SER A  353  5                                   6    
HELIX   16  16 HIS A  355  LEU A  368  1                                  14    
HELIX   17  17 VAL A  371  SER A  378  1                                   8    
HELIX   18  18 ASP A  388  GLN A  392  5                                   5    
HELIX   19  19 LEU A  393  HIS A  399  1                                   7    
HELIX   20  20 TRP A  401  LEU A  406  1                                   6    
HELIX   21  21 VAL A  408  ARG A  420  1                                  13    
HELIX   22  22 ASP A  430  HIS A  438  1                                   9    
HELIX   23  23 LEU A  446  HIS A  456  1                                  11    
HELIX   24  24 PHE A  458  ALA A  469  1                                  12    
HELIX   25  25 ILE A  492  ALA A  497  1                                   6    
HELIX   26  26 LEU A  540  PHE A  562  1                                  23    
HELIX   27  27 PHE A  599  ASP A  623  1                                  25    
HELIX   28  28 ASN A  629  VAL A  633  5                                   5    
HELIX   29  29 ASN A  641  SER A  645  5                                   5    
HELIX   30  30 ASN A  650  ASP A  655  1                                   6    
HELIX   31  31 VAL A  685  ALA A  687  5                                   3    
HELIX   32  32 PHE A  688  PHE A  694  1                                   7    
HELIX   33  33 ARG A  697  LEU A  714  1                                  18    
HELIX   34  34 ILE A  727  VAL A  733  1                                   7    
HELIX   35  35 VAL A  735  LEU A  751  1                                  17    
HELIX   36  36 GLN B   10  ASP B   15  1                                   6    
HELIX   37  37 THR B   18  ILE B   25  1                                   8    
HELIX   38  38 THR B   38  ALA B   48  1                                  11    
HELIX   39  39 PHE B   51  HIS B   67  1                                  17    
HELIX   40  40 VAL B  120  TYR B  125  1                                   6    
HELIX   41  41 GLY B  138  PHE B  147  1                                  10    
HELIX   42  42 PHE B  147  HIS B  156  1                                  10    
HELIX   43  43 VAL B  165  ASN B  170  5                                   6    
HELIX   44  44 HIS B  177  LEU B  182  1                                   6    
HELIX   45  45 LEU B  182  VAL B  197  1                                  16    
HELIX   46  46 ALA B  198  ARG B  203  1                                   6    
HELIX   47  47 GLY B  223  THR B  227  5                                   5    
HELIX   48  48 THR B  271  GLY B  288  1                                  18    
HELIX   49  49 GLY B  321  ASN B  328  1                                   8    
HELIX   50  50 PHE B  332  ALA B  337  1                                   6    
HELIX   51  51 SER B  340  MET B  352  1                                  13    
HELIX   52  52 GLY B  380  GLY B  390  1                                  11    
HELIX   53  53 ASN B  399  ALA B  404  1                                   6    
HELIX   54  54 HIS B  414  ILE B  419  1                                   6    
HELIX   55  55 LEU B  422  LEU B  444  1                                  23    
HELIX   56  56 PRO B  457  ILE B  463  1                                   7    
HELIX   57  57 GLY B  515  ILE B  523  1                                   9    
HELIX   58  58 LEU B  525  ASP B  540  1                                  16    
HELIX   59  59 ALA B  572  VAL B  580  1                                   9    
HELIX   60  60 ASN B  585  TRP B  594  1                                  10    
HELIX   61  61 HIS B  598  ARG B  603  1                                   6    
HELIX   62  62 VAL B  606  SER B  613  1                                   8    
HELIX   63  63 SER B  628  ASN B  633  5                                   6    
HELIX   64  64 SER B  644  THR B  659  1                                  16    
HELIX   65  65 PHE B  661  SER B  666  1                                   6    
HELIX   66  66 ARG B  668  ALA B  679  1                                  12    
HELIX   67  67 ALA B  681  THR B  685  5                                   5    
HELIX   68  68 VAL B  703  GLY B  709  1                                   7    
HELIX   69  69 HIS B  712  ALA B  727  1                                  16    
HELIX   70  70 LYS D  134  ARG D  143  1                                  10    
HELIX   71  71 LEU D  144  SER D  146  5                                   3    
HELIX   72  72 SER F   88  ALA F  104  1                                  17    
HELIX   73  73 MET F  123  LYS F  128  1                                   6    
HELIX   74  74 ILE F  161  ALA F  171  1                                  11    
HELIX   75  75 GLN F  193  ILE F  197  5                                   5    
HELIX   76  76 VAL F  200  GLY F  210  5                                  11    
HELIX   77  77 ALA F  216  LEU F  221  1                                   6    
HELIX   78  78 LEU G   62  LEU G   74  1                                  13    
HELIX   79  79 ASP G  118  GLY G  121  5                                   4    
HELIX   80  80 PHE G  122  ALA G  129  1                                   8    
HELIX   81  81 PHE H  100  ALA H  114  1                                  15    
HELIX   82  82 LEU I   14  LEU I   24  1                                  11    
HELIX   83  83 VAL J   14  TRP J   18  5                                   5    
HELIX   84  84 ALA J   21  LEU J   25  5                                   5    
HELIX   85  85 ASP K   47  GLY K   50  5                                   4    
HELIX   86  86 SER K   51  ALA K   73  1                                  23    
HELIX   87  87 ALA K   99  VAL K  118  1                                  20    
HELIX   88  88 SER L   76  TYR L   82  1                                   7    
HELIX   89  89 SER L   94  LEU L   96  5                                   3    
HELIX   90  90 LEU L   97  HIS L  106  1                                  10    
HELIX   91  91 SER L  131  LEU L  145  1                                  15    
HELIX   92  92 THR L  146  GLY L  149  5                                   4    
HELIX   93  93 THR L  178  ILE L  194  1                                  17    
HELIX   94  94 VAL L  197  PHE L  202  1                                   6    
HELIX   95  95 UNK R    7  UNK R   27  1                                  21    
HELIX   96  96 GLY 1   70  ILE 1   97  1                                  28    
HELIX   97  97 THR 1  133  MET 1  154  1                                  22    
HELIX   98  98 LYS 1  186  VAL 1  199  1                                  14    
HELIX   99  99 GLY 1  200  GLN 1  205  1                                   6    
HELIX  100 100 VAL 2  103  THR 2  127  1                                  25    
HELIX  101 101 LYS 2  128  GLY 2  130  5                                   3    
HELIX  102 102 THR 2  150  ASN 2  173  1                                  24    
HELIX  103 103 LEU 2  217  THR 2  242  1                                  26    
HELIX  104 104 ARG 3   96  LEU 3  111  1                                  16    
HELIX  105 105 LEU 3  160  TRP 3  176  1                                  17    
HELIX  106 106 LYS 3  226  ALA 3  234  1                                   9    
HELIX  107 107 MET 3  235  ILE 3  243  1                                   9    
HELIX  108 108 LEU 4   88  MET 4  109  1                                  22    
HELIX  109 109 THR 4  140  ASN 4  162  1                                  23    
HELIX  110 110 ALA 4  179  TYR 4  184  1                                   6    
HELIX  111 111 GLU 4  202  ASN 4  222  1                                  21    
SHEET    1   A 2 SER A 119  GLN A 121  0                                        
SHEET    2   A 2 ILE A 143  GLN A 144 -1  O  ILE A 143   N  GLN A 121           
SHEET    1   B 2 ILE D 102  THR D 103  0                                        
SHEET    2   B 2 GLN D 153  PHE D 154 -1  O  GLN D 153   N  THR D 103           
SHEET    1   C 2 ILE D 111  PHE D 112  0                                        
SHEET    2   C 2 ALA D 120  ILE D 121 -1  O  ALA D 120   N  PHE D 112           
SHEET    1   D 2 SER E  89  VAL E  90  0                                        
SHEET    2   D 2 VAL E 105  ARG E 106 -1  O  ARG E 106   N  SER E  89           
LINK         OD2 ASP B  93                MG   CLA B1206     1555   1555  2.04  
LINK         SG  CYS A 581                FE4  SF4 A8001     1555   1555  2.28  
LINK         OE2 GLU L 101                MG   CLA L1501     1555   1555  2.29  
LINK         SG  CYS C  58                FE1  SF4 C8003     1555   1555  2.30  
LINK         OD1 ASN 4 207                MG   CLA 44002     1555   1555  2.31  
LINK         SG  CYS B 559                FE3  SF4 A8001     1555   1555  2.49  
LINK         SG  CYS A 590                FE4  SF4 A8001     1555   1555  2.50  
LINK         SG  CYS C  51                FE3  SF4 C8002     1555   1555  2.52  
LINK         SG  CYS A 581                FE1  SF4 A8001     1555   1555  2.57  
LINK         O   PRO C  59                FE4  SF4 C8003     1555   1555  2.63  
LINK         OE2 GLU 4 145                MG   CLA 44013     1555   1555  2.66  
LINK         OG1 THR A 503                MG   CLA A1134     1555   1555  2.89  
LINK         OBD CLA B1231                MG   CLA B1232     1555   1555  2.90  
LINK         O1A CLA A1102                MG   CLA A1109     1555   1555  2.93  
LINK         OH  TYR A 317                MG   CLA A1121     1555   1555  2.95  
LINK         OE1 GLU 2 164                MG   CLA 22012     1555   1555  2.97  
CISPEP   1 ASP E  123    GLU E  124          0       -28.01                     
CISPEP   2 UNK R   39    UNK R   40          0        10.87                     
CISPEP   3 UNK R   41    UNK R   42          0        24.22                     
SITE     1 AC1  3 GLU 1 182  LEU 1 183  LYS 1 184                               
SITE     1 AC2  2 ASN 1 190  CLA 11007                                          
SITE     1 AC3  5 GLY 1 200  PHE 1 201  GLN 1 204  LEU 1 221                    
SITE     2 AC3  5 CLA 11008                                                     
SITE     1 AC4  4 TRP 4 157  GLN 4 158  ASP 4 159  CLA 41009                    
SITE     1 AC5  2 CLA 11012  CLA 11015                                          
SITE     1 AC6  5 ALA 1  93  GLY 1  96  ILE 1  97  CLA 11010                    
SITE     2 AC6  5 CLA 11013                                                     
SITE     1 AC7  4 LYS 1 189  CLA 11002  CLA 41009  LMU 47008                    
SITE     1 AC8  2 CLA 11003  CLA K1142                                          
SITE     1 AC9  4 CLA 11007  ILE 4 154  CLA 41004  CLA 41304                    
SITE     1 BC1  1 CLA 11006                                                     
SITE     1 BC2  4 ARG 1  78  SER 1  82  HIS 1  86  GLN 1 151                    
SITE     1 BC3  4 TYR 1  79  ALA 1 146  GLU 1 149  CLA 11005                    
SITE     1 BC4  4 GLU 1 113  ILE 1 137  CLA 11006  CLA 11014                    
SITE     1 BC5  1 CLA 11013                                                     
SITE     1 BC6  9 ALA 1  58  PRO 1  59  PHE 1  62  GLY 1  63                    
SITE     2 BC6  9 GLY 1  68  VAL 1  72  GLU 1  77  LYS 1  80                    
SITE     3 BC6  9 CLA 11005                                                     
SITE     1 BC7  8 ILE A  54  HIS A  58  CLA A1102  CLA A1109                    
SITE     2 BC7  8 CLA A1140  PQN A5001  CLA A9013  VAL J  13                    
SITE     1 BC8  7 LEU A  57  HIS A  58  LYS A  77  GLN A  85                    
SITE     2 BC8  7 CLA A1101  CLA A1104  CLA A1109                               
SITE     1 BC9 22 HIS A  62  PHE A  64  LYS A  77  VAL A  78                    
SITE     2 BC9 22 ALA A  81  HIS A  82  GLN A  85  LEU A  86                    
SITE     3 BC9 22 ILE A  89  PHE A  90  PHE A 174  TRP A 354                    
SITE     4 BC9 22 GLN A 357  LEU A 358  ASN A 361  LEU A 365                    
SITE     5 BC9 22 CLA A1104  CLA A1111  CLA A1123  CLA A1128                    
SITE     6 BC9 22 BCR A6002  BCR A6003                                          
SITE     1 CC1  6 GLN A  85  TRP A  92  LEU A 406  CLA A1102                    
SITE     2 CC1  6 CLA A1103  CLA A1128                                          
SITE     1 CC2 12 LEU A  91  TRP A  92  SER A  94  GLY A  95                    
SITE     2 CC2 12 PHE A  98  HIS A  99  PHE A 103  GLN A 121                    
SITE     3 CC2 12 VAL A 122  CLA A1106  CLA A1107  BCR J6012                    
SITE     1 CC3 14 MET A  96  ALA A 120  GLN A 121  ILE A 143                    
SITE     2 CC3 14 ILE A 145  THR A 146  SER A 147  TYR A 675                    
SITE     3 CC3 14 CLA A1105  CLA A1107  CLA A1126  CLA A1128                    
SITE     4 CC3 14 BCR A6011  BCR J6012                                          
SITE     1 CC4 12 GLN A 121  VAL A 122  VAL A 123  TRP A 124                    
SITE     2 CC4 12 ILE A 126  VAL A 127  GLN A 129  PHE A 678                    
SITE     3 CC4 12 CLA A1105  CLA A1106  CLA B1230  BCR J6012                    
SITE     1 CC5  7 CLA 31118  LEU A 177  ALA A 181  PHE A 184                    
SITE     2 CC5  7 TRP A 195  CLA A1110  CLA A1111                               
SITE     1 CC6  9 GLU A  32  HIS A  67  LYS A  77  SER A  80                    
SITE     2 CC6  9 GLY A 182  TYR A 186  HIS A 187  CLA A1101                    
SITE     3 CC6  9 CLA A1102                                                     
SITE     1 CC7  7 CLA 31118  TRP A 195  SER A 201  HIS A 205                    
SITE     2 CC7  7 CLA A1108  CLA A1111  BCR A6003                               
SITE     1 CC8 13 PHE A  79  PHE A  83  PHE A 174  TRP A 195                    
SITE     2 CC8 13 SER A 201  MET A 202  HIS A 205  HIS A 206                    
SITE     3 CC8 13 LEU A 210  CLA A1103  CLA A1108  CLA A1110                    
SITE     4 CC8 13 CLA A1123                                                     
SITE     1 CC9 10 CLA 31147  ILE A 158  THR A 167  SER A 217                    
SITE     2 CC9 10 TRP A 218  ARG A 220  HIS A 221  PRO A 245                    
SITE     3 CC9 10 CLA A1113  BCR A6002                                          
SITE     1 DC1  8 LEU A 216  ARG A 220  HIS A 224  ILE A 249                    
SITE     2 DC1  8 LEU A 250  ARG A 252  CLA A1112  BCR A6002                    
SITE     1 DC2  7 LEU A 281  HIS A 301  LEU A 304  ALA A 305                    
SITE     2 DC2  7 ILE A 308  CLA A1116  MET K  64                               
SITE     1 DC3  9 HIS A 301  HIS A 302  HIS A 375  MET A 379                    
SITE     2 DC3  9 THR A 511  CLA A1115  CLA A1117  CLA A1125                    
SITE     3 DC3  9 CLA A1133                                                     
SITE     1 DC4 15 LEU A 211  GLY A 214  TRP A 218  GLN A 222                    
SITE     2 DC4 15 ILE A 299  HIS A 302  HIS A 303  PHE A 310                    
SITE     3 DC4 15 LEU A 368  VAL A 372  PRO A 381  CLA A1116                    
SITE     4 DC4 15 CLA A1125  CLA A1127  BCR A6003                               
SITE     1 DC5  4 CLA A1108  CLA A1110  LEU B 232  GLN B 235                    
SITE     1 DC6 11 LEU A 207  LEU A 309  PHE A 310  ILE A 330                    
SITE     2 DC6 11 CLA A1120  CLA A1121  CLA A1122  CLA A1123                    
SITE     3 DC6 11 CLA A1125  BCR A6007  BCR A6008                               
SITE     1 DC7  9 ASP A 329  ILE A 330  ALA A 333  HIS A 334                    
SITE     2 DC7  9 CLA A1119  CLA A1121  CLA A1122  CLA A1151                    
SITE     3 DC7  9 LYS K  79                                                     
SITE     1 DC8  7 HIS A 315  MET A 316  TYR A 317  ASP A 329                    
SITE     2 DC8  7 CLA A1119  CLA A1120  ARG K  78                               
SITE     1 DC9  7 HIS A 343  LEU A 346  LEU A 431  CLA A1119                    
SITE     2 DC9  7 CLA A1120  CLA A1123  BCR A6007                               
SITE     1 EC1 18 PHE A 196  GLN A 197  MET A 202  LEU A 203                    
SITE     2 EC1 18 LEU A 350  THR A 351  THR A 352  TRP A 354                    
SITE     3 EC1 18 GLN A 357  ILE A 360  ASN A 361  MET A 364                    
SITE     4 EC1 18 LEU A 365  CLA A1103  CLA A1111  CLA A1119                    
SITE     5 EC1 18 CLA A1122  CLA A1125                                          
SITE     1 EC2 11 ILE A 370  VAL A 371  ILE A 407  VAL A 553                    
SITE     2 EC2 11 SER A 608  CLA A1125  CLA A1135  CLA A1136                    
SITE     3 EC2 11 CLA A1137  BCR A6007  BCR A6008                               
SITE     1 EC3 16 MET A 364  LEU A 368  VAL A 371  HIS A 375                    
SITE     2 EC3 16 SER A 378  MET A 379  THR A 511  SER A 512                    
SITE     3 EC3 16 CLA A1116  CLA A1117  CLA A1119  CLA A1123                    
SITE     4 EC3 16 CLA A1124  CLA A1133  CLA A1135  BCR A6008                    
SITE     1 EC4 16 TRP A  92  MET A  96  THR A 146  SER A 147                    
SITE     2 EC4 16 SER A 394  THR A 397  HIS A 398  TRP A 401                    
SITE     3 EC4 16 PHE A 678  ILE A 743  TRP A 747  CLA A1106                    
SITE     4 EC4 16 CLA A1127  BCR A6011  CLA A9012  BCR J6012                    
SITE     1 EC5 11 ILE A 152  THR A 369  MET A 376  TYR A 382                    
SITE     2 EC5 11 LEU A 395  HIS A 398  HIS A 399  ILE A 402                    
SITE     3 EC5 11 CLA A1117  CLA A1126  BCR A6003                               
SITE     1 EC6 19 HIS A  58  ALA A  59  ASP A  60  ALA A  61                    
SITE     2 EC6 19 HIS A  62  ASP A  63  HIS A 355  LEU A 362                    
SITE     3 EC6 19 PHE A 405  GLY A 409  HIS A 413  ILE A 416                    
SITE     4 EC6 19 TRP A 595  THR A 736  CLA A1103  CLA A1104                    
SITE     5 EC6 19 CLA A1106  CLA A1140  BCR A6011                               
SITE     1 EC7  7 PHE A 338  HIS A 438  ILE A 442  HIS A 445                    
SITE     2 EC7  7 CLA A1137  THR L  71  CLA L1130                               
SITE     1 EC8 15 HIS A 445  CLA A1129  CLA A1136  CLA A1137                    
SITE     2 EC8 15 CLA A1237  THR B 685  PRO B 686  SER L  68                    
SITE     3 EC8 15 THR L  71  PRO L  72  VAL L  73  THR L  74                    
SITE     4 EC8 15 ILE L  79  TYR L  82  CLA L1504                               
SITE     1 EC9 14 TRP A 448  ILE A 451  PHE A 452  PHE A 455                    
SITE     2 EC9 14 HIS A 456  CLA A1132  CLA A1136  CLA A1237                    
SITE     3 EC9 14 ILE B  21  TRP B  22  BCR B6017  BCR B6020                    
SITE     4 EC9 14 BCR I6018  BCR L6019                                          
SITE     1 FC1 17 PHE A 455  GLY A 459  ILE A 462  HIS A 463                    
SITE     2 FC1 17 ASP A 475  CLA A1131  CLA A1136  CLA A9022                    
SITE     3 FC1 17 HIS B  95  BCR B6020  CLA H1207  BCR I6018                    
SITE     4 FC1 17 LEU L 110  PRO L 113  PHE L 114  ALA L 117                    
SITE     5 FC1 17 PRO L 119                                                     
SITE     1 FC2  8 ILE A 492  HIS A 496  ALA A 499  THR A 511                    
SITE     2 FC2  8 CLA A1116  CLA A1125  CLA A1134  BCR A6008                    
SITE     1 FC3  5 LMU 27046  THR A 503  CLA A1133  CLA A1141                    
SITE     2 FC3  5 BCR A6008                                                     
SITE     1 FC4 12 GLN A 374  TYR A 377  TRP A 491  ILE A 532                    
SITE     2 FC4 12 LEU A 534  HIS A 542  HIS A 545  HIS A 615                    
SITE     3 FC4 12 CLA A1124  CLA A1125  CLA A1136  CLA A1137                    
SITE     1 FC5 14 TRP A 448  PHE A 452  LEU A 453  TRP A 491                    
SITE     2 FC5 14 HIS A 542  HIS A 543  HIS A 550  CLA A1124                    
SITE     3 FC5 14 CLA A1131  CLA A1132  CLA A1135  CLA A1137                    
SITE     4 FC5 14 CLA L1130  CLA L1504                                          
SITE     1 FC6  8 LEU A 446  VAL A 449  HIS A 550  CLA A1124                    
SITE     2 FC6  8 CLA A1129  CLA A1135  CLA A1136  CLA L1130                    
SITE     1 FC7 14 ILE A 707  ALA A 710  HIS A 711  LEU A 714                    
SITE     2 FC7 14 CLA A1139  PQN A5001  SER B 420  SER B 423                    
SITE     3 FC7 14 TRP B 424  LEU B 427  CLA B1229  TYR F 181                    
SITE     4 FC7 14 CLA F1240  BCR F6014                                          
SITE     1 FC8 16 THR A  51  TRP A  55  ILE A 704  VAL A 708                    
SITE     2 FC8 16 HIS A 711  VAL A 716  ALA A 717  PRO A 722                    
SITE     3 FC8 16 ARG A 723  CLA A1138  TYR F 181  LEU F 182                    
SITE     4 FC8 16 ILE F 198  LEU F 202  PRO J  12  SER J  15                    
SITE     1 FC9 18 TRP A  55  VAL A 685  PHE A 688  PHE A 692                    
SITE     2 FC9 18 LEU A 725  GLN A 729  ALA A 732  VAL A 733                    
SITE     3 FC9 18 THR A 736  HIS A 737  LEU A 740  CLA A1101                    
SITE     4 FC9 18 CLA A1128  PQN A5001  BCR A6011  CLA A9013                    
SITE     5 FC9 18 BCR F6014  PHE J  19                                          
SITE     1 GC1  2 PHE A 270  CLA A1134                                          
SITE     1 GC2  2 CLA 11008  CLA K1143                                          
SITE     1 GC3  4 ALA K 104  ALA K 108  CLA K1142  LMU K7001                    
SITE     1 GC4  1 LMU H7017                                                     
SITE     1 GC5  1 LMU K7001                                                     
SITE     1 GC6  8 LEU 3 127  ILE 3 128  PRO 3 129  GLN 3 130                    
SITE     2 GC6  8 BCR 36022  HIS A 246  CLA A1112  BCR A6002                    
SITE     1 GC7  1 CLA A1151                                                     
SITE     1 GC8  1 LMU R7007                                                     
SITE     1 GC9  7 LYS A 335  GLY A 336  PRO A 337  PHE A 338                    
SITE     2 GC9  7 CLA A1120  CLA A1149  BCR A6007                               
SITE     1 HC1 10 PHE B   8  ALA B  28  HIS B  29  HIS B  34                    
SITE     2 HC1 10 SER B  49  GLN B  53  CLA B1202  CLA B1203                    
SITE     3 HC1 10 CLA B1226  BCR I6021                                          
SITE     1 HC2 15 HIS B  29  PHE B  31  ILE B  46  HIS B  50                    
SITE     2 HC2 15 GLN B  53  ARG B 174  ILE B 330  LEU B 334                    
SITE     3 HC2 15 ALA B 337  CLA B1201  CLA B1203  CLA B1210                    
SITE     4 HC2 15 CLA B1221  CLA B1226  BCR B6005                               
SITE     1 HC3 12 HIS B  29  ILE B  57  TRP B  60  ILE B 382                    
SITE     2 HC3 12 CLA B1201  CLA B1202  CLA B1205  CLA B1224                    
SITE     3 HC3 12 CLA B1225  CLA B1226  BCR B6005  LMG B7101                    
SITE     1 HC4 10 LEU B  59  SER B  62  PHE B  66  HIS B  67                    
SITE     2 HC4 10 ALA B  90  CLA B1205  CLA B1206  PHE I   8                    
SITE     3 HC4 10 VAL I  12  BCR I6018                                          
SITE     1 HC5 16 TRP B  60  ALA B  88  HIS B  89  ASN B 114                    
SITE     2 HC5 16 ASN B 115  TYR B 117  SER B 118  VAL B 645                    
SITE     3 HC5 16 TRP B 646  MET B 649  CLA B1203  CLA B1206                    
SITE     4 HC5 16 CLA B1224  BCR B6017  CLA I1204  BCR I6018                    
SITE     1 HC6 17 THR A 466  ALA A 469  LEU A 470  CLA A9022                    
SITE     2 HC6 17 ILE B  91  TRP B  92  ASP B  93  HIS B  95                    
SITE     3 HC6 17 ASN B 114  SER B 644  VAL B 645  CLA B1205                    
SITE     4 HC6 17 CLA B1239  CLA H1207  PHE I  16  CLA I1204                    
SITE     5 HC6 17 BCR I6018                                                     
SITE     1 HC7 11 CLA A1132  CLA A9022  HIS B  95  CLA B1206                    
SITE     2 HC7 11 BCR B6020  LEU H 109  SER H 113  GLY I  13                    
SITE     3 HC7 11 LEU I  14  BCR I6018  PRO L 119                               
SITE     1 HC8 10 PHE B  51  LEU B 151  ALA B 152  LEU B 155                    
SITE     2 HC8 10 HIS B 156  LYS B 162  TRP B 167  CLA B1209                    
SITE     3 HC8 10 CLA B1210  ASN G  95                                          
SITE     1 HC9  9 TRP B 167  SER B 173  HIS B 177  THR B 293                    
SITE     2 HC9  9 CLA B1208  CLA B1210  CLA B1217  BCR B6005                    
SITE     3 HC9  9 ASN G  95                                                     
SITE     1 IC1 17 PHE B  47  HIS B  50  PHE B  51  LEU B  54                    
SITE     2 IC1 17 TRP B 123  TRP B 167  ARG B 174  HIS B 177                    
SITE     3 IC1 17 HIS B 178  LEU B 182  PHE B 183  CLA B1202                    
SITE     4 IC1 17 CLA B1208  CLA B1209  CLA B1215  CLA B1225                    
SITE     5 IC1 17 BCR B6005                                                     
SITE     1 IC2  9 LEU B 129  THR B 137  PHE B 141  ALA B 189                    
SITE     2 IC2  9 TRP B 190  HIS B 193  HIS B 196  PHE B 212                    
SITE     3 IC2  9 BCR B6006                                                     
SITE     1 IC3 10 LEU B 188  ALA B 191  GLY B 192  VAL B 195                    
SITE     2 IC3 10 HIS B 196  LEU B 216  LEU B 222  BCR B6004                    
SITE     3 IC3 10 BCR B6005  BCR B6006                                          
SITE     1 IC4  8 TRP B 230  TYR B 233  HIS B 275  LEU B 278                    
SITE     2 IC4  8 ALA B 279  PHE B 282  LEU B 283  TRP B 493                    
SITE     1 IC5 13 LEU B 268  ASP B 272  HIS B 275  HIS B 276                    
SITE     2 IC5 13 ILE B 280  LEU B 283  HIS B 351  LEU B 355                    
SITE     3 IC5 13 TRP B 493  CLA B1215  CLA B1223  CLA B1231                    
SITE     4 IC5 13 CLA B1232                                                     
SITE     1 IC6 13 PHE B 183  SER B 186  TRP B 190  HIS B 276                    
SITE     2 IC6 13 HIS B 277  ILE B 280  ILE B 344  LEU B 347                    
SITE     3 IC6 13 VAL B 348  CLA B1210  CLA B1214  CLA B1216                    
SITE     4 IC6 13 CLA B1225                                                     
SITE     1 IC7 11 LEU B 175  LEU B 179  PHE B 284  MET B 290                    
SITE     2 IC7 11 TYR B 291  ILE B 304  CLA B1215  CLA B1218                    
SITE     3 IC7 11 CLA B1219  CLA B1220  CLA B1221                               
SITE     1 IC8 11 VAL B 185  LEU B 285  LEU B 289  ARG B 292                    
SITE     2 IC8 11 THR B 293  PHE B 295  ILE B 297  CLA B1209                    
SITE     3 IC8 11 BCR B6004  LEU G  74  PHE G  77                               
SITE     1 IC9 10 ILE B 286  GLY B 287  LEU B 289  MET B 290                    
SITE     2 IC9 10 GLY B 298  HIS B 299  CLA B1216  CLA B1219                    
SITE     3 IC9 10 BCR B6004  TYR G 110                                          
SITE     1 JC1  9 HIS B 299  TYR B 303  ILE B 304  HIS B 308                    
SITE     2 JC1  9 CLA B1216  CLA B1218  CLA B1220  CLA B1301                    
SITE     3 JC1  9 TYR G 110                                                     
SITE     1 JC2 10 LEU B 305  PRO B 310  VAL B 407  LEU B 408                    
SITE     2 JC2 10 MET B 411  CLA B1216  CLA B1219  CLA B1221                    
SITE     3 JC2 10 CLA B1223  CLA B1227                                          
SITE     1 JC3 12 ARG B 174  LEU B 175  HIS B 178  PHE B 183                    
SITE     2 JC3 12 TYR B 323  LEU B 336  ALA B 337  SER B 340                    
SITE     3 JC3 12 CLA B1202  CLA B1216  CLA B1220  CLA B1223                    
SITE     1 JC4 13 SER B 346  GLN B 350  MET B 383  PHE B 387                    
SITE     2 JC4 13 LEU B 527  THR B 530  THR B 531  ILE B 587                    
SITE     3 JC4 13 CLA B1223  CLA B1234  CLA B1235  CLA B1236                    
SITE     4 JC4 13 BCR B6010                                                     
SITE     1 JC5 14 SER B 340  VAL B 343  LEU B 347  GLN B 350                    
SITE     2 JC5 14 HIS B 351  SER B 354  LEU B 355  CLA B1214                    
SITE     3 JC5 14 CLA B1220  CLA B1221  CLA B1222  CLA B1231                    
SITE     4 JC5 14 CLA B1236  BCR B6010                                          
SITE     1 JC6 12 TRP B  60  ASN B  64  SER B 118  ALA B 370                    
SITE     2 JC6 12 HIS B 374  ILE B 718  PHE B 719  ALA B 722                    
SITE     3 JC6 12 ILE B 726  CLA B1203  CLA B1205  CLA B1225                    
SITE     1 JC7 18 TRP B  60  GLY B 119  TRP B 123  ALA B 189                    
SITE     2 JC7 18 ILE B 344  THR B 345  VAL B 348  MET B 352                    
SITE     3 JC7 18 LEU B 371  HIS B 374  HIS B 375  ILE B 378                    
SITE     4 JC7 18 CLA B1203  CLA B1210  CLA B1215  CLA B1224                    
SITE     5 JC7 18 BCR B6005  BCR B6006                                          
SITE     1 JC8 19 ALA B  26  HIS B  29  ASP B  30  LEU B 334                    
SITE     2 JC8 19 PHE B 381  THR B 384  GLY B 385  HIS B 389                    
SITE     3 JC8 19 ILE B 392  ARG B 396  TRP B 573  PHE B 576                    
SITE     4 JC8 19 LEU B 707  VAL B 711  CLA B1201  CLA B1202                    
SITE     5 JC8 19 CLA B1203  CLA B1239  LMG B7101                               
SITE     1 JC9  8 ARG B 317  ARG B 410  MET B 411  HIS B 414                    
SITE     2 JC9  8 HIS B 421  CLA B1220  CLA B1228  CLA B1236                    
SITE     1 KC1  7 TRP A 709  LEU A 714  HIS B 421  TRP B 424                    
SITE     2 KC1  7 CLA B1227  PHE F 231  BCR F6016                               
SITE     1 KC2 13 CLA A1138  TRP B 424  LEU B 427  PHE B 428                    
SITE     2 KC2 13 PHE B 431  HIS B 432  CLA B1230  CLA B1235                    
SITE     3 KC2 13 PHE F 160  PHE F 167  ILE F 174  BCR F6014                    
SITE     4 KC2 13 BCR F6016                                                     
SITE     1 KC3 15 VAL A 127  CLA A1107  BCR A6011  CLA A9012                    
SITE     2 KC3 15 GLY B 435  VAL B 438  HIS B 439  VAL B 442                    
SITE     3 KC3 15 LYS B 451  CLA B1229  BCR F6014  ASN J  30                    
SITE     4 KC3 15 ASP J  35  ALA J  36  BCR J6012                               
SITE     1 KC4  9 TRP B 462  ILE B 463  HIS B 467  LEU B 498                    
SITE     2 KC4  9 CLA B1214  CLA B1223  CLA B1232  CLA B1234                    
SITE     3 KC4  9 BCR B6010                                                     
SITE     1 KC5  8 LEU B 486  GLY B 489  ILE B 492  TRP B 493                    
SITE     2 KC5  8 CLA B1214  CLA B1231  CLA B1233  BCR B6010                    
SITE     1 KC6  3 TRP 3  97  ALA B 488  CLA B1232                               
SITE     1 KC7 16 GLN B 350  TYR B 353  TYR B 372  GLN B 376                    
SITE     2 KC7 16 PHE B 459  ALA B 460  ILE B 463  HIS B 520                    
SITE     3 KC7 16 ILE B 523  VAL B 590  TYR B 593  LYS B 597                    
SITE     4 KC7 16 CLA B1222  CLA B1231  CLA B1235  CLA B1236                    
SITE     1 KC8 16 LEU B 429  PRO B 457  ILE B 458  PHE B 459                    
SITE     2 KC8 16 ALA B 460  ASP B 516  PHE B 517  HIS B 520                    
SITE     3 KC8 16 HIS B 521  CLA B1222  CLA B1229  CLA B1234                    
SITE     4 KC8 16 CLA B1236  PHE F 160  ILE F 161  BCR F6016                    
SITE     1 KC9 11 HIS B 421  LEU B 422  TRP B 424  ALA B 524                    
SITE     2 KC9 11 LEU B 527  HIS B 528  CLA B1222  CLA B1223                    
SITE     3 KC9 11 CLA B1227  CLA B1234  CLA B1235                               
SITE     1 LC1 13 TRP A 448  ILE A 451  CLA A1131  LEU B 678                    
SITE     2 LC1 13 CLA B1238  BCR B6017  BCR B6020  HIS L 106                    
SITE     3 LC1 13 LEU L 110  LEU L 141  CLA L1130  CLA L1502                    
SITE     4 LC1 13 BCR L6019                                                     
SITE     1 LC2 16 CLA A1237  CLA A9023  THR B  18  ILE B  21                    
SITE     2 LC2 16 TRP B  22  ARG B 692  TRP B 693  ARG B 694                    
SITE     3 LC2 16 PRO B 697  CLA B1239  LEU I  14  MET I  21                    
SITE     4 LC2 16 PHE I  25  BCR I6018  TYR L 148  BCR L6019                    
SITE     1 LC3 17 CLA A9023  LEU B 655  VAL B 656  MET B 662                    
SITE     2 LC3 17 VAL B 708  VAL B 711  HIS B 712  CLA B1206                    
SITE     3 LC3 17 CLA B1226  CLA B1238  PQN B5002  BCR B6017                    
SITE     4 LC3 17 LMG B7101  ALA I  18  MET I  21  ALA I  22                    
SITE     5 LC3 17 CYS L 144                                                     
SITE     1 LC4  4 CLA A1138  TRP F 173  ILE F 174  TRP J  18                    
SITE     1 LC5  1 BCR I6021                                                     
SITE     1 LC6  5 GLN G  83  ARG G  84  LYS G 115  PRO G 119                    
SITE     2 LC6  5 LMU G7026                                                     
SITE     1 LC7  6 PRO B 310  PRO B 311  GLY B 312  ARG B 314                    
SITE     2 LC7  6 LEU B 315  CLA B1219                                          
SITE     1 LC8  5 SER F 151  GLY F 152  TRP F 157  CLA F1305                    
SITE     2 LC8  5 BCR F6016                                                     
SITE     1 LC9  3 TRP 1 225  HIS 1 226  CLA 41304                               
SITE     1 MC1  3 CLA 11303  CLA 41009  CLA 44012                               
SITE     1 MC2  4 CLA 41306  CLA 44005  TRP F 157  CLA F1302                    
SITE     1 MC3  5 GLY 4 216  GLN 4 220  CLA 44005  LEU F 166                    
SITE     2 MC3  5 CLA F1305                                                     
SITE     1 MC4  1 CLA 22014                                                     
SITE     1 MC5  1 LEU A 172                                                     
SITE     1 MC6  2 CLA 22014  ARG J  31                                          
SITE     1 MC7  6 PRO H  78  GLN H  80  TYR L  82  GLU L 101                    
SITE     2 MC7  6 LEU L 104  ALA L 105                                          
SITE     1 MC8  7 CLA A1237  BCR B6020  TYR L  82  LEU L  86                    
SITE     2 MC8  7 VAL L 102  HIS L 106  BCR L6019                               
SITE     1 MC9  2 GLY L 112  PRO L 113                                          
SITE     1 NC1  5 CLA A1136  VAL L  73  LEU L  78  ILE L  79                    
SITE     2 NC1  5 CLA L1130                                                     
SITE     1 NC2  1 ILE E  66                                                     
SITE     1 NC3  1 ARG 2 218                                                     
SITE     1 NC4  3 ILE 2 122  GLU 2 221  CLA 22007                               
SITE     1 NC5  3 TRP 2 236  HIS 2 239  THR 2 267                               
SITE     1 NC6  8 GLU 2 106  LEU 2 107  SER 2 110  LYS 2 220                    
SITE     2 NC6  8 ASN 2 224  LEU 2 227  CLA 22007  CLA 32009                    
SITE     1 NC7  1 HIS 2 109                                                     
SITE     1 NC8  1 LEU 2 126                                                     
SITE     1 NC9  4 GLU 2 221  CLA 22002  CLA 22004  CLA 32009                    
SITE     1 OC1  4 CLA 22004  CLA 22007  SER 3 181  LYS 3 184                    
SITE     1 OC2  1 LEU 2 115                                                     
SITE     1 OC3  9 HIS 2 109  TRP 2 112  LEU 2 157  ILE 2 160                    
SITE     2 OC3  9 GLY 2 161  GLU 2 164  ARG 2 167  TRP 2 168                    
SITE     3 OC3  9 CLA 22013                                                     
SITE     1 OC4  2 GLU 2 156  CLA 22012                                          
SITE     1 OC5  2 CLA J1308  CLA J1311                                          
SITE     1 OC6  5 ARG 3  96  GLN B 235  ASN B 236  PRO B 237                    
SITE     2 OC6  5 LEU B 258                                                     
SITE     1 OC7  4 ALA 3 234  ILE 3 238  TYR 3 241  CLA 33016                    
SITE     1 OC8  3 ILE 3 104  TYR 3 202  LEU 3 225                               
SITE     1 OC9  3 GLY 3 126  LEU 3 127  ILE 3 243                               
SITE     1 PC1  2 LEU 3 122  CLA 33013                                          
SITE     1 PC2  1 CLA K3009                                                     
SITE     1 PC3  7 CLA 33007  SER B 239  SER B 240  GLN B 248                    
SITE     2 PC3  7 GLY B 249  PHE B 261  PRO B 263                               
SITE     1 PC4  5 VAL 3 125  LEU 3 127  ILE 3 128  THR 3 156                    
SITE     2 PC4  5 MET 3 162                                                     
SITE     1 PC5  1 CLA 33012                                                     
SITE     1 PC6  3 LEU 3  98  GLU 3 102  CLA 33011                               
SITE     1 PC7  5 PHE 3 108  LEU 3 111  PHE 3 158  MET 3 165                    
SITE     2 PC7  5 CLA 33006                                                     
SITE     1 PC8  1 CLA 33003                                                     
SITE     1 PC9  3 ASP 4 169  GLN 4 174  THR 4 197                               
SITE     1 QC1  5 LYS 4 203  ASN 4 207  LEU 4 210  MET 4 211                    
SITE     2 QC1  5 LMU R7024                                                     
SITE     1 QC2  1 PHE 4 217                                                     
SITE     1 QC3  3 CLA 24009  ILE 4 205  ARG 4 209                               
SITE     1 QC4  4 ILE 4 219  CLA 41306  CLA 44010  CLA F1305                    
SITE     1 QC5  5 LEU 4 111  TRP 4 126  TYR 4 127  LMU 47034                    
SITE     2 QC5  5 LMU 47052                                                     
SITE     1 QC6  3 ARG 2 166  CLA 44004  LMU 47053                               
SITE     1 QC7  3 PHE 4 142  PHE 4 146  CLA 44005                               
SITE     1 QC8  3 ARG 4 100  ARG 4 156  PRO 4 170                               
SITE     1 QC9  7 ALA 4  94  VAL 4  97  HIS 4 150  GLU 4 153                    
SITE     2 QC9  7 ARG 4 156  TRP 4 157  CLA 41304                               
SITE     1 RC1  3 TRP 4 126  GLU 4 145  PHE 4 146                               
SITE     1 RC2  2 ASN 4 167  LMU 47034                                          
SITE     1 RC3 12 TRP A  55  MET A 691  PHE A 692  SER A 695                    
SITE     2 RC3 12 GLY A 696  ARG A 697  TRP A 700  LEU A 725                    
SITE     3 RC3 12 CLA A1101  CLA A1138  CLA A1140  BCR F6014                    
SITE     1 RC4 12 MET B 662  PHE B 663  TRP B 667  ARG B 668                    
SITE     2 RC4 12 TRP B 671  ALA B 699  LEU B 700  ALA B 705                    
SITE     3 RC4 12 CLA B1239  BCR B6017  LMG B7101  BCR L6019                    
SITE     1 RC5  8 CLA 31147  THR A 167  LEU A 216  SER A 217                    
SITE     2 RC5  8 CLA A1103  CLA A1112  CLA A1113  BCR A6003                    
SITE     1 RC6  7 LEU A 213  GLY A 214  CLA A1103  CLA A1110                    
SITE     2 RC6  7 CLA A1117  CLA A1127  BCR A6002                               
SITE     1 RC7  7 PHE B 282  LEU B 285  LEU B 289  CLA B1212                    
SITE     2 RC7  7 CLA B1217  CLA B1218  PHE G  77                               
SITE     1 RC8  8 ILE B  57  VAL B 185  CLA B1202  CLA B1203                    
SITE     2 RC8  8 CLA B1209  CLA B1210  CLA B1212  CLA B1225                    
SITE     1 RC9  6 LEU B  65  PHE B 141  LEU B 142  CLA B1211                    
SITE     2 RC9  6 CLA B1212  CLA B1225                                          
SITE     1 SC1  6 ALA A 356  ILE A 360  CLA A1119  CLA A1122                    
SITE     2 SC1  6 CLA A1124  CLA A1151                                          
SITE     1 SC2 10 SER A 367  ILE A 407  ALA A 410  ALA A 411                    
SITE     2 SC2 10 VAL A 553  CLA A1119  CLA A1124  CLA A1125                    
SITE     3 SC2 10 CLA A1133  CLA A1134                                          
SITE     1 SC3  9 PHE B 332  GLY B 335  PHE B 387  GLY B 390                    
SITE     2 SC3  9 PHE B 394  CLA B1222  CLA B1223  CLA B1231                    
SITE     3 SC3  9 CLA B1232                                                     
SITE     1 SC4 13 PHE A 684  VAL A 685  ALA A 744  TRP A 747                    
SITE     2 SC4 13 CLA A1106  CLA A1126  CLA A1128  CLA A1140                    
SITE     3 SC4 13 CLA A9012  CLA A9013  CLA B1230  BCR F6014                    
SITE     4 SC4 13 BCR J6012                                                     
SITE     1 SC5  7 CLA A1105  CLA A1106  CLA A1107  CLA A1126                    
SITE     2 SC5  7 BCR A6011  CLA B1230  PHE J  19                               
SITE     1 SC6 12 CLA A1138  CLA A1140  PQN A5001  BCR A6011                    
SITE     2 SC6 12 CLA A9013  PHE B 431  CLA B1229  CLA B1230                    
SITE     3 SC6 12 PRO F 163  LEU F 166  PHE F 167  ILE F 170                    
SITE     1 SC7  8 LEU A 714  CLA B1228  CLA B1229  CLA B1235                    
SITE     2 SC7  8 GLY F 172  GLY F 175  TRP F 176  CLA F1302                    
SITE     1 SC8 11 CLA A1131  CLA A1237  CLA A9022  CLA A9023                    
SITE     2 SC8 11 VAL B 645  TRP B 648  MET B 649  PHE B 652                    
SITE     3 SC8 11 CLA B1205  CLA B1239  PQN B5002                               
SITE     1 SC9 10 CLA A1131  CLA A1132  CLA A9023  CLA B1205                    
SITE     2 SC9 10 CLA B1206  CLA B1238  CLA H1207  VAL I  12                    
SITE     3 SC9 10 CLA I1204  BCR I6021                                          
SITE     1 TC1 14 CLA A1131  CLA A1237  ILE B  21  ILE B  25                    
SITE     2 TC1 14 CLA B1238  PQN B5002  MET I  21  LEU I  24                    
SITE     3 TC1 14 BCR I6021  LEU L 141  CYS L 144  LEU L 145                    
SITE     4 TC1 14 TYR L 148  CLA L1502                                          
SITE     1 TC2  6 CLA A1131  CLA A1132  CLA A1237  LEU B 687                    
SITE     2 TC2  6 CLA H1207  CLA L1502                                          
SITE     1 TC3 10 CLA B1201  CLA H1241  LEU I   7  PHE I   8                    
SITE     2 TC3 10 LEU I  11  VAL I  12  PHE I  16  ALA I  20                    
SITE     3 TC3 10 BCR I6018  BCR L6019                                          
SITE     1 TC4  3 GLN 3 130  THR 3 132  CLA 31147                               
SITE     1 TC5  3 SER K  91  CLA K1143  CLA K1146                               
SITE     1 TC6  2 LMU 27006  LMU 37005                                          
SITE     1 TC7  2 LMU 27006  LMU 37003                                          
SITE     1 TC8  2 LMU 37003  LMU 37005                                          
SITE     1 TC9  2 LMU 47009  CLA R1150                                          
SITE     1 UC1  2 CLA 11007  ILE I   2                                          
SITE     1 UC2  1 LMU R7007                                                     
SITE     1 UC3  1 LMU K7047                                                     
SITE     1 UC4  1 LMU H7030                                                     
SITE     1 UC5  1 TRP B 154                                                     
SITE     1 UC6  1 CLA H1145                                                     
SITE     1 UC7  1 CLA 44002                                                     
SITE     1 UC8  1 CLA G1242                                                     
SITE     1 UC9  1 SER L 159                                                     
SITE     1 VC1  1 LMU H7011                                                     
SITE     1 VC2  3 CLA 44006  CLA 44014  LMU 47052                               
SITE     1 VC3  1 ASP A  65                                                     
SITE     1 VC4  1 LMU E7048                                                     
SITE     1 VC5  2 LMU B7040  LMU G7039                                          
SITE     1 VC6  2 LMU B7038  PHE G 100                                          
SITE     1 VC7  1 LMU B7038                                                     
SITE     1 VC8  1 LMU K7042                                                     
SITE     1 VC9  2 LYS K  85  LMU K7041                                          
SITE     1 WC1  3 LEU A 520  GLN A 631  GLY A 632                               
SITE     1 WC2  7 LEU 1 125  THR A  68  GLU A  73  TYR A 186                    
SITE     2 WC2  7 TRP G 130  GLY G 134  HIS G 135                               
SITE     1 WC3  2 TRP 2 206  CLA A1134                                          
SITE     1 WC4  2 LMU A7010  VAL K 118                                          
SITE     1 WC5  1 LMU F7036                                                     
SITE     1 WC6  1 ARG D 123                                                     
SITE     1 WC7  2 CLA 44006  LMU 47034                                          
SITE     1 WC8  2 CLA 24009  ASP L 208                                          
SITE     1 WC9 15 PHE B  23  ALA B  26  ASP B  30  PHE B 381                    
SITE     2 WC9 15 SER B 556  PHE B 576  GLN B 704  LEU B 707                    
SITE     3 WC9 15 VAL B 711  SER B 714  CLA B1203  CLA B1226                    
SITE     4 WC9 15 CLA B1239  PQN B5002  TRP C  70                               
SITE     1 XC1  7 CYS A 581  PRO A 584  CYS A 590  CYS B 559                    
SITE     2 XC1  7 ASP B 560  CYS B 568  ILE B 702                               
SITE     1 XC2  5 CYS C  21  ASP C  24  VAL C  49  CYS C  51                    
SITE     2 XC2  5 CYS C  54                                                     
SITE     1 XC3  6 CYS C  11  ILE C  12  GLY C  13  VAL C  18                    
SITE     2 XC3  6 CYS C  58  PRO C  59                                          
SITE     1 XC4 18 LEU A 657  CLA A9011  CLA A9012  CLA A9022                    
SITE     2 XC4 18 TYR B 437  ALA B 522  TRP B 589  PHE B 592                    
SITE     3 XC4 18 TRP B 619  LEU B 620  LEU B 624  PHE B 650                    
SITE     4 XC4 18 HIS B 654  TRP B 657  TYR B 717  THR B 720                    
SITE     5 XC4 18 TYR B 721  PHE B 724                                          
SITE     1 XC5 23 TYR A 461  ILE A 544  THR A 548  TYR A 606                    
SITE     2 XC5 23 SER A 610  PHE A 614  ILE A 649  TRP A 652                    
SITE     3 XC5 23 LEU A 657  ALA A 661  ILE A 665  PHE A 679                    
SITE     4 XC5 23 HIS A 683  TRP A 686  GLY A 742  THR A 745                    
SITE     5 XC5 23 THR A 746  PHE A 749  CLA A9012  CLA A9022                    
SITE     6 XC5 23 LEU B 624  TRP B 625  CLA B9010                               
SITE     1 XC6 19 LEU A 677  LEU A 680  GLY A 681  HIS A 683                    
SITE     2 XC6 19 PHE A 684  TRP A 686  ALA A 687  CLA A1126                    
SITE     3 XC6 19 BCR A6011  CLA A9011  CLA A9013  PHE B 581                    
SITE     4 XC6 19 TRP B 582  ASN B 585  TRP B 589  LEU B 616                    
SITE     5 XC6 19 TRP B 657  CLA B1230  CLA B9010                               
SITE     1 XC7 21 PHE A 684  ALA A 687  PHE A 688  LEU A 690                    
SITE     2 XC7 21 MET A 691  PHE A 694  TYR A 699  TRP A 700                    
SITE     3 XC7 21 LEU A 703  CLA A1101  CLA A1140  BCR A6011                    
SITE     4 XC7 21 CLA A9012  LEU B 427  GLY B 430  PHE B 431                    
SITE     5 XC7 21 LEU B 525  ILE B 533  PHE B 581  TRP B 582                    
SITE     6 XC7 21 BCR F6014                                                     
SITE     1 XC8 19 PHE A 458  ILE A 462  PHE A 603  TRP A 604                    
SITE     2 XC8 19 ASN A 607  CLA A1132  CLA A9011  CLA A9023                    
SITE     3 XC8 19 TRP B 648  LEU B 651  PHE B 652  HIS B 654                    
SITE     4 XC8 19 LEU B 655  TRP B 657  ALA B 658  CLA B1206                    
SITE     5 XC8 19 BCR B6017  CLA B9010  CLA H1207                               
SITE     1 XC9 21 ASN A 447  CYS A 450  ILE A 451  PHE A 455                    
SITE     2 XC9 21 PHE A 458  PHE A 547  LEU A 554  ILE A 555                    
SITE     3 XC9 21 TRP A 604  CLA A9022  ALA B 658  THR B 659                    
SITE     4 XC9 21 PHE B 661  MET B 662  ILE B 665  TYR B 670                    
SITE     5 XC9 21 TRP B 671  CLA B1238  CLA B1239  BCR B6017                    
SITE     6 XC9 21 BCR I6018                                                     
CRYST1  120.655  189.086  129.388  90.00  91.24  90.00 P 1 21 1      2          
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      0.008288  0.000000  0.000179        0.00000                         
SCALE2      0.000000  0.005289  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007731        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system