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Entry: 2O01
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HEADER    PHOTOSYNTHESIS                          27-NOV-06   2O01              
TITLE     THE STRUCTURE OF A PLANT PHOTOSYSTEM I SUPERCOMPLEX AT 3.4 ANGSTROM   
TITLE    2 RESOLUTION                                                           
CAVEAT     2O01    SEVERAL CHIRALITY ERRORS LOCATED IN CHAIN N AND CHAIN 3      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A1;            
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PSAA, PSI-A;                                                
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A2;            
COMPND   7 CHAIN: B;                                                            
COMPND   8 SYNONYM: PSAB, PSI-B;                                                
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: PHOTOSYSTEM I IRON-SULFUR CENTER;                          
COMPND  11 CHAIN: C;                                                            
COMPND  12 SYNONYM: PHOTOSYSTEM I SUBUNIT VII, 9 KDA POLYPEPTIDE, PSI-C, PSAC;  
COMPND  13 MOL_ID: 4;                                                           
COMPND  14 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT II, CHLOROPLAST;     
COMPND  15 CHAIN: D;                                                            
COMPND  16 SYNONYM: PHOTOSYSTEM I 20 KDA SUBUNIT, PSI-D;                        
COMPND  17 MOL_ID: 5;                                                           
COMPND  18 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT IV A, CHLOROPLAST;   
COMPND  19 CHAIN: E;                                                            
COMPND  20 SYNONYM: PSI-E A;                                                    
COMPND  21 MOL_ID: 6;                                                           
COMPND  22 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT III, CHLOROPLAST;    
COMPND  23 CHAIN: F;                                                            
COMPND  24 SYNONYM: LIGHT-HARVESTING COMPLEX I 17 KDA PROTEIN, PSI-F;           
COMPND  25 MOL_ID: 7;                                                           
COMPND  26 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT V, CHLOROPLAST;      
COMPND  27 CHAIN: G;                                                            
COMPND  28 SYNONYM: PSI-G, PHOTOSYSTEM I 9 KDA PROTEIN;                         
COMPND  29 MOL_ID: 8;                                                           
COMPND  30 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT VI, CHLOROPLAST;     
COMPND  31 CHAIN: H;                                                            
COMPND  32 SYNONYM: PSI- H, LIGHT-HARVESTING COMPLEX I 11 KDA PROTEIN;          
COMPND  33 MOL_ID: 9;                                                           
COMPND  34 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT VIII;                
COMPND  35 CHAIN: I;                                                            
COMPND  36 SYNONYM: PSI-I;                                                      
COMPND  37 MOL_ID: 10;                                                          
COMPND  38 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT IX;                  
COMPND  39 CHAIN: J;                                                            
COMPND  40 SYNONYM: PSI-J;                                                      
COMPND  41 MOL_ID: 11;                                                          
COMPND  42 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT PSAK, CHLOROPLAST;   
COMPND  43 CHAIN: K;                                                            
COMPND  44 MOL_ID: 12;                                                          
COMPND  45 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT XI, CHLOROPLAST;     
COMPND  46 CHAIN: L;                                                            
COMPND  47 SYNONYM: PSI- L, PSI SUBUNIT V;                                      
COMPND  48 MOL_ID: 13;                                                          
COMPND  49 MOLECULE: PHOTOSYSTEM I-N SUBUNIT;                                   
COMPND  50 CHAIN: N;                                                            
COMPND  51 MOL_ID: 14;                                                          
COMPND  52 MOLECULE: AT3G54890;                                                 
COMPND  53 CHAIN: 1;                                                            
COMPND  54 SYNONYM: CHLOROPHYLL A/B-BINDING PROTEIN, AT3G54890/F28P10_130;      
COMPND  55 MOL_ID: 15;                                                          
COMPND  56 MOLECULE: TYPE II CHLOROPHYLL A/B BINDING PROTEIN FROM PHOTOSYSTEM I;
COMPND  57 CHAIN: 2;                                                            
COMPND  58 MOL_ID: 16;                                                          
COMPND  59 MOLECULE: PSI TYPE III CHLOROPHYLL A/B-BINDING PROTEIN;              
COMPND  60 CHAIN: 3;                                                            
COMPND  61 MOL_ID: 17;                                                          
COMPND  62 MOLECULE: PSI LIGHT-HARVESTING ANTENNA CHLOROPHYLL A/B-BINDING       
COMPND  63 PROTEIN;                                                             
COMPND  64 CHAIN: 4                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE   3 ORGANISM_COMMON: PEA;                                                
SOURCE   4 ORGANISM_TAXID: 3888;                                                
SOURCE   5 STRAIN: ALASKA;                                                      
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE   8 ORGANISM_COMMON: PEA;                                                
SOURCE   9 ORGANISM_TAXID: 3888;                                                
SOURCE  10 MOL_ID: 3;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  12 ORGANISM_COMMON: PEA;                                                
SOURCE  13 ORGANISM_TAXID: 3888;                                                
SOURCE  14 MOL_ID: 4;                                                           
SOURCE  15 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;                              
SOURCE  16 ORGANISM_COMMON: SPINACH;                                            
SOURCE  17 ORGANISM_TAXID: 3562;                                                
SOURCE  18 MOL_ID: 5;                                                           
SOURCE  19 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE  20 ORGANISM_COMMON: THALE CRESS;                                        
SOURCE  21 ORGANISM_TAXID: 3702;                                                
SOURCE  22 MOL_ID: 6;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;                              
SOURCE  24 ORGANISM_COMMON: SPINACH;                                            
SOURCE  25 ORGANISM_TAXID: 3562;                                                
SOURCE  26 MOL_ID: 7;                                                           
SOURCE  27 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;                              
SOURCE  28 ORGANISM_COMMON: SPINACH;                                            
SOURCE  29 ORGANISM_TAXID: 3562;                                                
SOURCE  30 MOL_ID: 8;                                                           
SOURCE  31 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;                              
SOURCE  32 ORGANISM_COMMON: SPINACH;                                            
SOURCE  33 ORGANISM_TAXID: 3562;                                                
SOURCE  34 MOL_ID: 9;                                                           
SOURCE  35 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  36 ORGANISM_COMMON: PEA;                                                
SOURCE  37 ORGANISM_TAXID: 3888;                                                
SOURCE  38 MOL_ID: 10;                                                          
SOURCE  39 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;                              
SOURCE  40 ORGANISM_COMMON: SPINACH;                                            
SOURCE  41 ORGANISM_TAXID: 3562;                                                
SOURCE  42 MOL_ID: 11;                                                          
SOURCE  43 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE  44 ORGANISM_COMMON: THALE CRESS;                                        
SOURCE  45 ORGANISM_TAXID: 3702;                                                
SOURCE  46 MOL_ID: 12;                                                          
SOURCE  47 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;                              
SOURCE  48 ORGANISM_COMMON: SPINACH;                                            
SOURCE  49 ORGANISM_TAXID: 3562;                                                
SOURCE  50 MOL_ID: 13;                                                          
SOURCE  51 ORGANISM_SCIENTIFIC: PHASEOLUS VULGARIS;                             
SOURCE  52 ORGANISM_TAXID: 3885;                                                
SOURCE  53 MOL_ID: 14;                                                          
SOURCE  54 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE  55 ORGANISM_COMMON: THALE CRESS;                                        
SOURCE  56 ORGANISM_TAXID: 3702;                                                
SOURCE  57 MOL_ID: 15;                                                          
SOURCE  58 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  59 ORGANISM_COMMON: PEA;                                                
SOURCE  60 ORGANISM_TAXID: 3888;                                                
SOURCE  61 MOL_ID: 16;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE  63 ORGANISM_COMMON: THALE CRESS;                                        
SOURCE  64 ORGANISM_TAXID: 3702;                                                
SOURCE  65 MOL_ID: 17;                                                          
SOURCE  66 ORGANISM_SCIENTIFIC: PISUM SATIVUM;                                  
SOURCE  67 ORGANISM_COMMON: PEA;                                                
SOURCE  68 ORGANISM_TAXID: 3888                                                 
KEYWDS    MEMBRANAL SUPER COMPLEX, PHOTOSYNTHESIS                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.AMUNTS,O.DRORY,N.NELSON                                             
REVDAT   4   25-JUL-12 2O01    1       FORMUL HET    HETATM HETNAM              
REVDAT   4 2                   1       REMARK SITE   VERSN                      
REVDAT   3   24-FEB-09 2O01    1       VERSN                                    
REVDAT   2   20-NOV-07 2O01    1       JRNL                                     
REVDAT   1   08-MAY-07 2O01    0                                                
JRNL        AUTH   A.AMUNTS,O.DRORY,N.NELSON                                    
JRNL        TITL   THE STRUCTURE OF A PLANT PHOTOSYSTEM I SUPERCOMPLEX AT 3.4 A 
JRNL        TITL 2 RESOLUTION.                                                  
JRNL        REF    NATURE                        V. 447    58 2007              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   17476261                                                     
JRNL        DOI    10.1038/NATURE05687                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 3.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 70551                          
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) : 0.348                           
REMARK   3   FREE R VALUE                     : 0.409                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3516                            
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) : 3.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.49                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4106                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 75.93                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2920                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 190                          
REMARK   3   BIN FREE R VALUE                    : 0.4400                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 23599                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6247                                    
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) : 44.13                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.06000                                             
REMARK   3    B22 (A**2) : 0.74000                                              
REMARK   3    B33 (A**2) : 0.82000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.78000                                              
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): 0.975         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.625         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.519        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.778                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.707                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 31845 ; 0.017 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 45477 ; 4.101 ; 2.222       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3024 ;15.284 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1032 ;43.946 ;23.285       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3623 ;27.622 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   103 ;20.588 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3853 ; 0.216 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 31360 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A): 24775 ; 0.388 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 19001 ; 0.334 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1577 ; 0.337 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.113 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   238 ; 0.411 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.210 ; 0.200       
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): 15464 ; 0.563 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 24032 ; 0.878 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 52416 ; 1.334 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 21073 ; 1.697 ; 4.500       
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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2O01 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-DEC-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB040515.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 10                                 
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) : 0.875                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70551                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.400                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.1                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.14000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.4100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.52                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: DM                                                    
REMARK 200 STARTING MODEL: PDB ENTRY 1QZV                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.0, VAPOR DIFFUSION, SITTING DROP,   
REMARK 280  TEMPERATURE 278K                                                    
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       94.39200            
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: HEPTADECAMERIC                    
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,            
REMARK 350                    AND CHAINS: J, K, L, N, 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     SER A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     VAL A    10                                                      
REMARK 465     GLN A    11                                                      
REMARK 465     ILE A    12                                                      
REMARK 465     LEU A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     ASP A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     GLU A    17                                                      
REMARK 465     VAL A    18                                                      
REMARK 465     LYS A    19                                                      
REMARK 465     ILE A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     VAL A    22                                                      
REMARK 465     ASP A    23                                                      
REMARK 465     ARG A    24                                                      
REMARK 465     ASP A    25                                                      
REMARK 465     PRO A    26                                                      
REMARK 465     ILE A    27                                                      
REMARK 465     LYS A    28                                                      
REMARK 465     THR A    29                                                      
REMARK 465     SER A    30                                                      
REMARK 465     UNK K    54                                                      
REMARK 465     PHE 1   128                                                      
REMARK 465     ASP 1   129                                                      
REMARK 465     PRO 1   130                                                      
REMARK 465     LEU 1   131                                                      
REMARK 465     GLY 1   132                                                      
REMARK 465     TYR 1   133                                                      
REMARK 465     SER 1   134                                                      
REMARK 465     LYS 1   135                                                      
REMARK 465     ASP 1   136                                                      
REMARK 465     PRO 1   137                                                      
REMARK 465     LYS 1   138                                                      
REMARK 465     LYS 1   139                                                      
REMARK 465     THR 2   121                                                      
REMARK 465     ASP 2   122                                                      
REMARK 465     PRO 2   123                                                      
REMARK 465     ILE 2   124                                                      
REMARK 465     PHE 2   125                                                      
REMARK 465     PRO 2   126                                                      
REMARK 465     ASN 2   127                                                      
REMARK 465     ASN 2   128                                                      
REMARK 465     LYS 2   129                                                      
REMARK 465     LEU 2   130                                                      
REMARK 465     THR 2   131                                                      
REMARK 465     GLY 2   132                                                      
REMARK 465     THR 2   133                                                      
REMARK 465     ASP 2   134                                                      
REMARK 465     VAL 2   135                                                      
REMARK 465     GLY 2   136                                                      
REMARK 465     TYR 2   137                                                      
REMARK 465     PRO 2   138                                                      
REMARK 465     GLY 2   139                                                      
REMARK 465     GLY 2   140                                                      
REMARK 465     ALA 3    90                                                      
REMARK 465     LEU 3    91                                                      
REMARK 465     PRO 3    92                                                      
REMARK 465     TRP 3    93                                                      
REMARK 465     PHE 3    94                                                      
REMARK 465     GLN 3    95                                                      
REMARK 465     THR 3    96                                                      
REMARK 465     GLY 3    97                                                      
REMARK 465     VAL 3    98                                                      
REMARK 465     ILE 3    99                                                      
REMARK 465     PRO 3   100                                                      
REMARK 465     PRO 3   101                                                      
REMARK 465     ALA 3   102                                                      
REMARK 465     GLY 3   103                                                      
REMARK 465     LEU 3   147                                                      
REMARK 465     GLU 3   148                                                      
REMARK 465     LYS 3   149                                                      
REMARK 465     GLY 3   150                                                      
REMARK 465     LEU 3   151                                                      
REMARK 465     ALA 3   152                                                      
REMARK 465     GLY 3   153                                                      
REMARK 465     SER 3   154                                                      
REMARK 465     GLY 3   155                                                      
REMARK 465     ASN 3   156                                                      
REMARK 465     PRO 3   157                                                      
REMARK 465     ALA 3   158                                                      
REMARK 465     TYR 3   159                                                      
REMARK 465     PRO 3   160                                                      
REMARK 465     GLY 3   161                                                      
REMARK 465     GLY 3   162                                                      
REMARK 465     PRO 3   163                                                      
REMARK 465     PHE 3   164                                                      
REMARK 465     PHE 3   165                                                      
REMARK 465     ASN 3   166                                                      
REMARK 465     PRO 3   167                                                      
REMARK 465     LEU 3   168                                                      
REMARK 465     GLY 3   169                                                      
REMARK 465     PHE 3   170                                                      
REMARK 465     GLY 3   171                                                      
REMARK 465     LYS 3   172                                                      
REMARK 465     ASP 3   173                                                      
REMARK 465     GLU 3   174                                                      
REMARK 465     LYS 3   175                                                      
REMARK 465     SER 3   176                                                      
REMARK 465     LEU 3   177                                                      
REMARK 465     LYS 3   178                                                      
REMARK 465     GLU 3   179                                                      
REMARK 465     LEU 3   180                                                      
REMARK 465     LYS 3   181                                                      
REMARK 465     LEU 3   182                                                      
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     ASP B 134    O                                                   
REMARK 470     MET 1   5    CG   SD   CE                                        
REMARK 470     PRO 1   6    CG   CD                                             
REMARK 470     GLU 1   8    CG   CD   OE1  OE2                                  
REMARK 470     PRO 1   9    CG   CD                                             
REMARK 470     ARG 1  10    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO 1  11    CG   CD                                             
REMARK 470     TYR 1  13    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU 1  14    CG   CD1  CD2                                       
REMARK 470     ASP 1  15    CG   OD1  OD2                                       
REMARK 470     SER 1  17    OG                                                  
REMARK 470     PRO 1  19    CG   CD                                             
REMARK 470     ASP 1  21    CG   OD1  OD2                                       
REMARK 470     PHE 1  22    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE 1  24    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP 1  25    CG   OD1  OD2                                       
REMARK 470     PRO 1  26    CG   CD                                             
REMARK 470     LEU 1  27    CG   CD1  CD2                                       
REMARK 470     LEU 1  29    CG   CD1  CD2                                       
REMARK 470     GLU 1  31    CG   CD   OE1  OE2                                  
REMARK 470     VAL 1  32    CG1  CG2                                            
REMARK 470     PRO 1  33    CG   CD                                             
REMARK 470     ASN 1  35    CG   OD1  ND2                                       
REMARK 470     LEU 1  36    CG   CD1  CD2                                       
REMARK 470     GLU 1  37    CG   CD   OE1  OE2                                  
REMARK 470     ARG 1  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR 1  39    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU 1  94    CG   CD1  CD2                                       
REMARK 470     GLU 1 115    CG   CD   OE1  OE2                                  
REMARK 470     LYS 1 116    CG   CD   CE   NZ                                   
REMARK 470     ASP 1 117    CG   OD1  OD2                                       
REMARK 470     PRO 1 118    CG   CD                                             
REMARK 470     GLU 1 119    CG   CD   OE1  OE2                                  
REMARK 470     LYS 1 120    CG   CD   CE   NZ                                   
REMARK 470     LYS 1 121    CG   CD   CE   NZ                                   
REMARK 470     LYS 1 122    CG   CD   CE   NZ                                   
REMARK 470     TYR 1 123    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PRO 1 124    CG   CD                                             
REMARK 470     LEU 1 140    CG   CD1  CD2                                       
REMARK 470     GLU 1 141    CG   CD   OE1  OE2                                  
REMARK 470     GLU 1 142    CG   CD   OE1  OE2                                  
REMARK 470     LEU 1 143    CG   CD1  CD2                                       
REMARK 470     LYS 1 144    CG   CD   CE   NZ                                   
REMARK 470     VAL 1 145    CG1  CG2                                            
REMARK 470     LYS 1 146    CG   CD   CE   NZ                                   
REMARK 470     SER 2  40    OG                                                  
REMARK 470     LEU 2  41    CG   CD1  CD2                                       
REMARK 470     ARG 2  42    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG 2 109    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TRP 2 110    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP 2 110    CZ3  CH2                                            
REMARK 470     ASP 2 112    CG   OD1  OD2                                       
REMARK 470     ILE 2 113    CG1  CG2  CD1                                       
REMARK 470     LEU 2 114    CG   CD1  CD2                                       
REMARK 470     ASN 2 115    CG   OD1  ND2                                       
REMARK 470     PRO 2 116    CG   CD                                             
REMARK 470     CYS 2 118    SG                                                  
REMARK 470     VAL 2 119    CG1  CG2                                            
REMARK 470     ASN 2 120    CG   OD1  ND2                                       
REMARK 470     LEU 3  79    CG   CD1  CD2                                       
REMARK 470     ILE 3  85    CG1  CG2  CD1                                       
REMARK 470     LYS 3 183    CG   CD   CE   NZ                                   
REMARK 470     GLU 3 184    CG   CD   OE1  OE2                                  
REMARK 470     VAL 3 185    CG1  CG2                                            
REMARK 470     LYS 3 186    CG   CD   CE   NZ                                   
REMARK 470     ASN 3 187    CG   OD1  ND2                                       
REMARK 470     ARG 3 189    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU 3 190    CG   CD1  CD2                                       
REMARK 470     MET 3 192    CG   SD   CE                                        
REMARK 470     LEU 3 193    CG   CD1  CD2                                       
REMARK 470     LEU 3 217    CG   CD1  CD2                                       
REMARK 470     PRO 4  34    CG   CD                                             
REMARK 470     GLU 4  35    CG   CD   OE1  OE2                                  
REMARK 470     ASN 4  36    CG   OD1  ND2                                       
REMARK 470     LEU 4  37    CG   CD1  CD2                                       
REMARK 470     ARG 4  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU 4 130    CG   CD   OE1  OE2                                  
REMARK 470     VAL 4 131    CG1  CG2                                            
REMARK 470     TYR 4 133    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PRO 4 134    CG   CD                                             
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   OD2  ASP 2    30     CD   PRO 2    31              1.19            
REMARK 500   OD2  ASP 2    30     N    PRO 2    31              1.22            
REMARK 500   CG   ASP 2    30     CD   PRO 2    31              1.44            
REMARK 500   OD2  ASP 2    30     CG   PRO 2    31              1.52            
REMARK 500   O    ALA F    33     NZ   LYS F    43              1.73            
REMARK 500   O    CYS C    11     O    ILE C    12              1.78            
REMARK 500   CD   PRO L    67     CAB  CLA L  1503              1.78            
REMARK 500   O    GLN A   621     N    ASP A   623              1.78            
REMARK 500   OG1  THR B   720     O1D  CLA B  9010              1.78            
REMARK 500   O    HIS F    79     N    GLY F    81              1.79            
REMARK 500   O    THR A   397     N    MET A   400              1.80            
REMARK 500   CA   SER D    26     O    PRO D    27              1.80            
REMARK 500   CD1  ILE B   344     CBC  CLA B  1225              1.81            
REMARK 500   O    VAL A   173     N    GLY A   176              1.82            
REMARK 500   N    GLY B   287     CMC  CLA B  1218              1.83            
REMARK 500   O    TRP 3   133     CA   GLY 3   137              1.83            
REMARK 500   O    ASN A   650     N    TRP A   652              1.85            
REMARK 500   OG   SER C     4     O    TYR C    68              1.86            
REMARK 500   NE2  HIS C     3     O    CYS C    48              1.86            
REMARK 500   CB   CYS C    11    FE3   SF4 C  3103              1.88            
REMARK 500   O    ASP A   571     ND2  ASN A   574              1.89            
REMARK 500   O    GLN A   374     OG   SER A   378              1.92            
REMARK 500   CA   MET B   290     CBC  CLA B  1218              1.92            
REMARK 500   O    LEU B   305     N    ALA B   307              1.93            
REMARK 500   O    ILE B   304     CB   HIS B   308              1.93            
REMARK 500   O    TYR L    36     N    SER L    38              1.94            
REMARK 500   O    ALA F    39     N    ALA F    41              1.94            
REMARK 500   OD1  ASP A    63     OG   SER A    66              1.94            
REMARK 500   N    MET B   290     CBC  CLA B  1218              1.95            
REMARK 500   CD1  TYR L   165     OBD  CLA L  1503              1.95            
REMARK 500   O    CYS C    51     N    ARG C    53              1.95            
REMARK 500   O    PRO B    99     N    ALA B   103              1.96            
REMARK 500   O    ILE B     5     O    ALA B    13              1.96            
REMARK 500   C    LEU B   289     CBC  CLA B  1218              1.97            
REMARK 500   O    SER B   628     N    GLN B   630              1.97            
REMARK 500   O    GLY A    84     N    ILE A    88              1.97            
REMARK 500   O    THR B    17     N    ARG B    19              1.97            
REMARK 500   O    TRP D    50     OD1  ASN D    73              1.98            
REMARK 500   O    ILE B    37     CD1  PHE D   148              1.98            
REMARK 500   O    LYS A   619     O    GLN A   621              1.99            
REMARK 500   O    GLY B   342     OG1  THR B   345              2.00            
REMARK 500   O    PRO G    95     N    PHE G    97              2.00            
REMARK 500   O    LEU B   289     CBC  CLA B  1218              2.01            
REMARK 500   O    SER B   714     N    ILE B   718              2.01            
REMARK 500   ND2  ASN G    30     O    GLN G    34              2.01            
REMARK 500   O    ILE A   609     O    VAL A   611              2.02            
REMARK 500   OE1  GLN L   129     O    GLN L   131              2.02            
REMARK 500   O    ALA A   744     N    ALA A   748              2.03            
REMARK 500   O    LEU F   105     N    ILE F   108              2.03            
REMARK 500   O    GLY A   454     N    HIS A   456              2.03            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     135 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   O    LEU L   161     O    LEU 4   141     1655     1.55            
REMARK 500   CB   ALA 1    71     OD1  ASP 2    30     1556     1.96            
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    PRO A  48   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    PRO A 118   C   -  N   -  CA  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    PRO A 118   C   -  N   -  CD  ANGL. DEV. = -12.7 DEGREES          
REMARK 500    PRO A 125   C   -  N   -  CA  ANGL. DEV. =  10.7 DEGREES          
REMARK 500    LEU A 216   CA  -  CB  -  CG  ANGL. DEV. =  14.8 DEGREES          
REMARK 500    PRO A 245   C   -  N   -  CA  ANGL. DEV. =  11.3 DEGREES          
REMARK 500    LEU A 250   CA  -  CB  -  CG  ANGL. DEV. =  14.9 DEGREES          
REMARK 500    LEU A 294   CA  -  CB  -  CG  ANGL. DEV. =  17.2 DEGREES          
REMARK 500    PRO A 380   C   -  N   -  CA  ANGL. DEV. =  14.4 DEGREES          
REMARK 500    LEU A 453   CA  -  CB  -  CG  ANGL. DEV. =  17.3 DEGREES          
REMARK 500    PRO A 505   C   -  N   -  CD  ANGL. DEV. = -17.2 DEGREES          
REMARK 500    LEU A 530   CA  -  CB  -  CG  ANGL. DEV. =  17.2 DEGREES          
REMARK 500    LEU A 554   CA  -  CB  -  CG  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    GLY B  24   N   -  CA  -  C   ANGL. DEV. = -19.6 DEGREES          
REMARK 500    LEU B 232   CA  -  CB  -  CG  ANGL. DEV. =  15.9 DEGREES          
REMARK 500    PRO B 391   C   -  N   -  CA  ANGL. DEV. = -14.3 DEGREES          
REMARK 500    PRO B 391   C   -  N   -  CD  ANGL. DEV. =  12.8 DEGREES          
REMARK 500    LEU B 436   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    PRO B 562   C   -  N   -  CA  ANGL. DEV. =  11.2 DEGREES          
REMARK 500    LEU B 631   CA  -  CB  -  CG  ANGL. DEV. =  17.0 DEGREES          
REMARK 500    PRO B 637   C   -  N   -  CA  ANGL. DEV. =  11.6 DEGREES          
REMARK 500    PRO B 697   C   -  N   -  CA  ANGL. DEV. =  12.4 DEGREES          
REMARK 500    LEU B 707   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    PRO C  22   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    PRO D  27   C   -  N   -  CD  ANGL. DEV. = -38.1 DEGREES          
REMARK 500    LEU D  84   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    PRO D 120   C   -  N   -  CD  ANGL. DEV. = -30.7 DEGREES          
REMARK 500    LEU D 156   CA  -  CB  -  CG  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    LEU F   5   CA  -  CB  -  CG  ANGL. DEV. =  15.6 DEGREES          
REMARK 500    LEU F   5   N   -  CA  -  C   ANGL. DEV. = -20.5 DEGREES          
REMARK 500    PRO F   7   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    PRO F  69   C   -  N   -  CA  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    ILE F  72   N   -  CA  -  C   ANGL. DEV. =  16.7 DEGREES          
REMARK 500    PRO G  36   C   -  N   -  CD  ANGL. DEV. = -14.4 DEGREES          
REMARK 500    LEU G  58   N   -  CA  -  C   ANGL. DEV. = -16.8 DEGREES          
REMARK 500    TYR G  84   N   -  CA  -  C   ANGL. DEV. =  16.5 DEGREES          
REMARK 500    GLY G  92   N   -  CA  -  C   ANGL. DEV. = -16.2 DEGREES          
REMARK 500    PRO H  31   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    GLU H  41   N   -  CA  -  C   ANGL. DEV. =  16.3 DEGREES          
REMARK 500    LEU H  54   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    PRO H  87   C   -  N   -  CD  ANGL. DEV. = -15.2 DEGREES          
REMARK 500    LEU I  24   CA  -  CB  -  CG  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    PRO L  18   C   -  N   -  CA  ANGL. DEV. =  11.4 DEGREES          
REMARK 500    PRO L  31   C   -  N   -  CA  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    PRO L  49   C   -  N   -  CA  ANGL. DEV. =  11.2 DEGREES          
REMARK 500    PRO L  73   C   -  N   -  CD  ANGL. DEV. = -29.5 DEGREES          
REMARK 500    PRO 2  31   C   -  N   -  CA  ANGL. DEV. =  11.1 DEGREES          
REMARK 500    PRO 2  38   C   -  N   -  CA  ANGL. DEV. =  20.6 DEGREES          
REMARK 500    PRO 2  38   C   -  N   -  CD  ANGL. DEV. = -15.9 DEGREES          
REMARK 500    LEU 2  41   C   -  N   -  CA  ANGL. DEV. = -31.2 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      52 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    GLU A  32      -84.62    -91.34                                   
REMARK 500    GLN A  33     -142.00   -162.81                                   
REMARK 500    TRP A  34      142.46     88.88                                   
REMARK 500    LYS A  36      168.62     79.82                                   
REMARK 500    HIS A  39      -60.37   -148.81                                   
REMARK 500    PHE A  40      -20.29   -155.87                                   
REMARK 500    ARG A  42      -65.25     29.50                                   
REMARK 500    LYS A  46       18.76     55.09                                   
REMARK 500    PRO A  48     -115.11     -9.33                                   
REMARK 500    ASP A  49      -29.84    133.55                                   
REMARK 500    THR A  51      -86.70    -36.82                                   
REMARK 500    THR A  52       55.30    -49.21                                   
REMARK 500    TRP A  55       11.90   -157.51                                   
REMARK 500    HIS A  58       -9.80    -57.85                                   
REMARK 500    ASP A  60      -87.11   -160.14                                   
REMARK 500    ALA A  61      -61.66     40.54                                   
REMARK 500    HIS A  62      -79.40    -83.65                                   
REMARK 500    ASP A  63      164.22     -1.20                                   
REMARK 500    PHE A  64     -147.38   -120.27                                   
REMARK 500    ASP A  65      -47.36     31.83                                   
REMARK 500    SER A  66       13.90    -68.39                                   
REMARK 500    HIS A  67     -120.32   -128.15                                   
REMARK 500    ASP A  70       74.36    -51.52                                   
REMARK 500    GLU A  72        4.33    -68.36                                   
REMARK 500    GLU A  73       65.01   -151.30                                   
REMARK 500    ILE A  74      -40.89   -163.96                                   
REMARK 500    LYS A  77      -41.21   -146.68                                   
REMARK 500    PHE A  79       55.69    -95.26                                   
REMARK 500    ALA A  81     -128.35    174.21                                   
REMARK 500    HIS A  82      -28.13     74.26                                   
REMARK 500    PHE A  83     -112.35    -79.38                                   
REMARK 500    PHE A  90      -70.54    -57.22                                   
REMARK 500    LEU A  91      -33.00    -30.93                                   
REMARK 500    TRP A  92     -116.79    -68.80                                   
REMARK 500    LEU A  93      -51.43    -13.94                                   
REMARK 500    SER A  94       78.56    -59.36                                   
REMARK 500    PHE A 103       80.87   -157.01                                   
REMARK 500    GLU A 107      -71.27    -62.35                                   
REMARK 500    ALA A 108       60.37    -54.77                                   
REMARK 500    TRP A 109      -60.73    170.65                                   
REMARK 500    LEU A 110      -71.05    -29.39                                   
REMARK 500    ASN A 111      -49.33    -20.09                                   
REMARK 500    PRO A 113     -127.90    -31.72                                   
REMARK 500    THR A 114      -74.36     51.18                                   
REMARK 500    ILE A 116      113.69     97.01                                   
REMARK 500    PRO A 118      158.98    -20.09                                   
REMARK 500    SER A 119      118.73    175.23                                   
REMARK 500    TRP A 124      150.64    -41.33                                   
REMARK 500    PRO A 125       30.10    -88.29                                   
REMARK 500    VAL A 127       19.98     31.49                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS    1344 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 GLN A   33     TRP A   34                  143.09                    
REMARK 500 GLY A   47     PRO A   48                 -142.47                    
REMARK 500 ASP A   65     SER A   66                  148.42                    
REMARK 500 SER A  104     ASN A  105                  147.48                    
REMARK 500 GLY A  117     PRO A  118                 -147.79                    
REMARK 500 HIS A  187     LYS A  188                  145.27                    
REMARK 500 PRO A  191     LYS A  192                  145.69                    
REMARK 500 LEU A  210     LEU A  211                  139.98                    
REMARK 500 PRO A  245     HIS A  246                  149.17                    
REMARK 500 PHE A  269     PHE A  270                  148.68                    
REMARK 500 ALA A  305     ILE A  306                  149.17                    
REMARK 500 ILE A  308     LEU A  309                  147.88                    
REMARK 500 GLY A  314     HIS A  315                  146.37                    
REMARK 500 HIS A  343     LYS A  344                 -149.32                    
REMARK 500 LEU A  346     TYR A  347                 -148.65                    
REMARK 500 GLN A  357     LEU A  358                 -146.40                    
REMARK 500 LEU A  368     THR A  369                  137.79                    
REMARK 500 GLN A  392     LEU A  393                  147.79                    
REMARK 500 ALA A  441     ILE A  442                  141.93                    
REMARK 500 SER A  457     PHE A  458                  146.86                    
REMARK 500 PRO A  486     VAL A  487                   41.08                    
REMARK 500 GLY A  506     ALA A  507                 -145.94                    
REMARK 500 ILE A  569     PRO A  570                 -143.67                    
REMARK 500 SER A  610     VAL A  611                  138.59                    
REMARK 500 ASN A  629     ASP A  630                  147.28                    
REMARK 500 ASP A  630     GLN A  631                  148.65                    
REMARK 500 GLY A  632     VAL A  633                 -147.44                    
REMARK 500 VAL A  685     TRP A  686                  136.57                    
REMARK 500 ILE A  704     GLU A  705                  147.48                    
REMARK 500 ALA A  719     THR A  720                  148.27                    
REMARK 500 GLY A  730     ARG A  731                  146.85                    
REMARK 500 ALA A  756     VAL A  757                 -147.75                    
REMARK 500 PHE B   23     GLY B   24                  147.90                    
REMARK 500 HIS B   50     PHE B   51                  132.87                    
REMARK 500 ASN B   64     LEU B   65                  147.81                    
REMARK 500 ASP B  134     LEU B  135                  144.64                    
REMARK 500 ARG B  208     TRP B  209                  143.00                    
REMARK 500 SER B  238     SER B  239                 -137.85                    
REMARK 500 LEU B  283     PHE B  284                  140.53                    
REMARK 500 LEU B  285     ILE B  286                  147.31                    
REMARK 500 ARG B  292     THR B  293                  132.07                    
REMARK 500 ASN B  294     PHE B  295                  148.79                    
REMARK 500 GLY B  298     HIS B  299                 -143.72                    
REMARK 500 GLY B  313     ARG B  314                  135.41                    
REMARK 500 ALA B  337     LEU B  338                  125.57                    
REMARK 500 THR B  367     GLN B  368                 -130.09                    
REMARK 500 GLN B  368     ALA B  369                 -140.02                    
REMARK 500 GLY B  390     PRO B  391                  147.64                    
REMARK 500 ARG B  396     ASP B  397                  146.74                    
REMARK 500 ASP B  405     ASN B  406                 -147.54                    
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     173 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    SER 2  40         24.11                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR A 114        24.9      L          L   OUTSIDE RANGE           
REMARK 500    TYR A 186        24.8      L          L   OUTSIDE RANGE           
REMARK 500    LYS A 192        24.3      L          L   OUTSIDE RANGE           
REMARK 500    ASP A 253        23.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE A 299        24.0      L          L   OUTSIDE RANGE           
REMARK 500    TYR A 347        23.8      L          L   OUTSIDE RANGE           
REMARK 500    THR A 369        18.9      L          L   OUTSIDE RANGE           
REMARK 500    MET A 379        24.2      L          L   OUTSIDE RANGE           
REMARK 500    THR A 391        20.7      L          L   OUTSIDE RANGE           
REMARK 500    HIS A 438        24.4      L          L   OUTSIDE RANGE           
REMARK 500    PHE A 477        24.3      L          L   OUTSIDE RANGE           
REMARK 500    LEU A 534        25.0      L          L   OUTSIDE RANGE           
REMARK 500    LEU A 557        24.7      L          L   OUTSIDE RANGE           
REMARK 500    ASP A 596        24.6      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 634        24.5      L          L   OUTSIDE RANGE           
REMARK 500    HIS B  50        23.8      L          L   OUTSIDE RANGE           
REMARK 500    GLN B  71        24.8      L          L   OUTSIDE RANGE           
REMARK 500    PHE B  82        24.4      L          L   OUTSIDE RANGE           
REMARK 500    HIS B  83        23.8      L          L   OUTSIDE RANGE           
REMARK 500    HIS B  89        18.9      L          L   OUTSIDE RANGE           
REMARK 500    TRP B 124        21.5      L          L   OUTSIDE RANGE           
REMARK 500    LEU B 129        24.7      L          L   OUTSIDE RANGE           
REMARK 500    HIS B 178        22.8      L          L   OUTSIDE RANGE           
REMARK 500    SER B 240        24.9      L          L   OUTSIDE RANGE           
REMARK 500    TRP B 269        23.2      L          L   OUTSIDE RANGE           
REMARK 500    PHE B 295        24.2      L          L   OUTSIDE RANGE           
REMARK 500    HIS B 299        20.9      L          L   OUTSIDE RANGE           
REMARK 500    LYS B 302        23.0      L          L   OUTSIDE RANGE           
REMARK 500    VAL B 407        24.7      L          L   OUTSIDE RANGE           
REMARK 500    TYR B 472        19.8      L          L   OUTSIDE RANGE           
REMARK 500    LEU B 494        23.6      L          L   OUTSIDE RANGE           
REMARK 500    ILE B 501        24.2      L          L   OUTSIDE RANGE           
REMARK 500    ASN B 504        25.0      L          L   OUTSIDE RANGE           
REMARK 500    LEU B 510        24.9      L          L   OUTSIDE RANGE           
REMARK 500    ILE B 512        24.9      L          L   OUTSIDE RANGE           
REMARK 500    ILE B 523        23.6      L          L   OUTSIDE RANGE           
REMARK 500    LEU B 532        24.6      L          L   OUTSIDE RANGE           
REMARK 500    ASP B 569        21.0      L          L   OUTSIDE RANGE           
REMARK 500    TRP B 589        25.0      L          L   OUTSIDE RANGE           
REMARK 500    ARG B 668        24.1      L          L   OUTSIDE RANGE           
REMARK 500    HIS B 682        22.8      L          L   OUTSIDE RANGE           
REMARK 500    ILE C   7        24.5      L          L   OUTSIDE RANGE           
REMARK 500    TYR C   8        21.1      L          L   OUTSIDE RANGE           
REMARK 500    THR C  10        19.4      L          L   OUTSIDE RANGE           
REMARK 500    VAL C  18        23.3      L          L   OUTSIDE RANGE           
REMARK 500    VAL C  49        24.5      L          L   OUTSIDE RANGE           
REMARK 500    THR C  60        22.1      L          L   OUTSIDE RANGE           
REMARK 500    ASP C  61        24.9      L          L   OUTSIDE RANGE           
REMARK 500    TYR C  68        20.2      L          L   OUTSIDE RANGE           
REMARK 500    ASN D  23        22.2      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     106 CHIRALITY DEVIATIONS.                         
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 1103                                                       
REMARK 610     CLA A 1104                                                       
REMARK 610     CLA A 1105                                                       
REMARK 610     CLA A 1106                                                       
REMARK 610     CLA A 1107                                                       
REMARK 610     CLA A 1108                                                       
REMARK 610     CLA A 1109                                                       
REMARK 610     CLA A 1110                                                       
REMARK 610     CLA A 1111                                                       
REMARK 610     CLA A 1113                                                       
REMARK 610     CLA A 1115                                                       
REMARK 610     CLA A 1116                                                       
REMARK 610     CLA A 1117                                                       
REMARK 610     CLA A 1118                                                       
REMARK 610     CLA A 1119                                                       
REMARK 610     CLA A 1120                                                       
REMARK 610     CLA A 1122                                                       
REMARK 610     CLA A 1123                                                       
REMARK 610     CLA A 1124                                                       
REMARK 610     CLA L 1125                                                       
REMARK 610     CLA A 1126                                                       
REMARK 610     CLA A 1127                                                       
REMARK 610     CLA A 1128                                                       
REMARK 610     CLA A 1129                                                       
REMARK 610     CLA L 1130                                                       
REMARK 610     CLA A 1131                                                       
REMARK 610     CLA A 1132                                                       
REMARK 610     CLA A 1133                                                       
REMARK 610     CLA A 1134                                                       
REMARK 610     CLA A 1135                                                       
REMARK 610     CLA A 1136                                                       
REMARK 610     CLA A 1137                                                       
REMARK 610     CLA B 1138                                                       
REMARK 610     CLA F 1139                                                       
REMARK 610     CLA A 1140                                                       
REMARK 610     CLA K 1141                                                       
REMARK 610     CLA A 1142                                                       
REMARK 610     CLA A 1143                                                       
REMARK 610     CLA A 1144                                                       
REMARK 610     CLA A 1146                                                       
REMARK 610     CLA A 1147                                                       
REMARK 610     CLA A 1148                                                       
REMARK 610     CLA K 1150                                                       
REMARK 610     CLA A 1151                                                       
REMARK 610     CLA A 1152                                                       
REMARK 610     CLA K 1153                                                       
REMARK 610     CLA B 9010                                                       
REMARK 610     CLA A 9011                                                       
REMARK 610     CLA B 9012                                                       
REMARK 610     CLA A 9013                                                       
REMARK 610     CLA B 9022                                                       
REMARK 610     CLA B 9023                                                       
REMARK 610     CLA B 1201                                                       
REMARK 610     CLA B 1202                                                       
REMARK 610     CLA B 1203                                                       
REMARK 610     CLA I 1204                                                       
REMARK 610     CLA B 1205                                                       
REMARK 610     CLA B 1206                                                       
REMARK 610     CLA B 1207                                                       
REMARK 610     CLA B 1208                                                       
REMARK 610     CLA B 1209                                                       
REMARK 610     CLA B 1210                                                       
REMARK 610     CLA B 1211                                                       
REMARK 610     CLA B 1212                                                       
REMARK 610     CLA B 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 1220                                                       
REMARK 610     CLA B 1221                                                       
REMARK 610     CLA B 1223                                                       
REMARK 610     CLA B 1224                                                       
REMARK 610     CLA B 1225                                                       
REMARK 610     CLA B 1226                                                       
REMARK 610     CLA B 1227                                                       
REMARK 610     CLA B 1228                                                       
REMARK 610     CLA B 1229                                                       
REMARK 610     CLA B 1230                                                       
REMARK 610     CLA B 1231                                                       
REMARK 610     CLA B 1232                                                       
REMARK 610     CLA G 1233                                                       
REMARK 610     CLA B 1234                                                       
REMARK 610     CLA B 1235                                                       
REMARK 610     CLA B 1236                                                       
REMARK 610     CLA B 1237                                                       
REMARK 610     CLA B 1238                                                       
REMARK 610     CLA B 1239                                                       
REMARK 610     CLA F 1240                                                       
REMARK 610     CLA B 1241                                                       
REMARK 610     CLA B 1242                                                       
REMARK 610     CLA B 1301                                                       
REMARK 610     CLA F 1302                                                       
REMARK 610     CLA F 1303                                                       
REMARK 610     CLA 4 1304                                                       
REMARK 610     CLA F 1305                                                       
REMARK 610     CLA F 1306                                                       
REMARK 610     CLA J 1307                                                       
REMARK 610     CLA J 1308                                                       
REMARK 610     CLA A 1309                                                       
REMARK 610     CLA G 1248                                                       
REMARK 610     CLA F 4015                                                       
REMARK 610     CLA H 1501                                                       
REMARK 610     CLA L 1502                                                       
REMARK 610     CLA L 1503                                                       
REMARK 610     CLA L 1504                                                       
REMARK 610     CLA H 1505                                                       
REMARK 610     CLA J 2107                                                       
REMARK 610     CLA 1 1004                                                       
REMARK 610     CLA 1 1005                                                       
REMARK 610     CLA 1 1006                                                       
REMARK 610     CLA 4 1009                                                       
REMARK 610     CLA 1 1013                                                       
REMARK 610     CLA 1 1010                                                       
REMARK 610     CLA 1 1011                                                       
REMARK 610     CLA 1 1012                                                       
REMARK 610     CLA 1 1001                                                       
REMARK 610     CLA 1 1007                                                       
REMARK 610     CLA 1 1002                                                       
REMARK 610     CLA 1 1003                                                       
REMARK 610     CLA 1 1008                                                       
REMARK 610     CLA 1 1014                                                       
REMARK 610     CLA 3 2009                                                       
REMARK 610     CLA 2 2004                                                       
REMARK 610     CLA 2 2005                                                       
REMARK 610     CLA 2 2006                                                       
REMARK 610     CLA 2 2010                                                       
REMARK 610     CLA 2 2013                                                       
REMARK 610     CLA 2 2001                                                       
REMARK 610     CLA 2 2011                                                       
REMARK 610     CLA 2 2012                                                       
REMARK 610     CLA 2 2015                                                       
REMARK 610     CLA 2 2007                                                       
REMARK 610     CLA 2 2002                                                       
REMARK 610     CLA 2 2003                                                       
REMARK 610     CLA 2 2008                                                       
REMARK 610     CLA 3 3009                                                       
REMARK 610     CLA 3 3004                                                       
REMARK 610     CLA 3 3005                                                       
REMARK 610     CLA 3 3012                                                       
REMARK 610     CLA 3 3006                                                       
REMARK 610     CLA 3 3013                                                       
REMARK 610     CLA 3 3010                                                       
REMARK 610     CLA 3 3001                                                       
REMARK 610     CLA 3 3011                                                       
REMARK 610     CLA 3 3002                                                       
REMARK 610     CLA 3 3007                                                       
REMARK 610     CLA 3 3015                                                       
REMARK 610     CLA 3 3003                                                       
REMARK 610     CLA 3 3008                                                       
REMARK 610     CLA 4 4009                                                       
REMARK 610     CLA 4 4004                                                       
REMARK 610     CLA 4 4005                                                       
REMARK 610     CLA 4 4006                                                       
REMARK 610     CLA 4 4013                                                       
REMARK 610     CLA 4 4010                                                       
REMARK 610     CLA 4 4011                                                       
REMARK 610     CLA 4 4012                                                       
REMARK 610     CLA 4 4001                                                       
REMARK 610     CLA 4 4007                                                       
REMARK 610     CLA 4 4002                                                       
REMARK 610     CLA 4 4003                                                       
REMARK 610     CLA 4 4008                                                       
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 A1103  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  82   NE2                                                    
REMARK 620 2 CLA A1103   NA   76.1                                              
REMARK 620 3 CLA A1103   NB  107.1  90.5                                        
REMARK 620 4 CLA A1103   NC  104.0 179.3  90.1                                  
REMARK 620 5 CLA A1103   ND   74.2  94.0 175.5  85.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A1104  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A  85   OE1                                                    
REMARK 620 2 CLA A1104   NA   91.9                                              
REMARK 620 3 CLA A1104   NB  107.9  89.9                                        
REMARK 620 4 CLA A1104   NC   87.7 179.4  89.8                                  
REMARK 620 5 CLA A1104   ND   72.0  93.0 177.1  87.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A1105  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  99   NE2                                                    
REMARK 620 2 CLA A1105   NA   76.9                                              
REMARK 620 3 CLA A1105   NB   78.0  90.7                                        
REMARK 620 4 CLA A1105   NC  103.1 179.7  89.5                                  
REMARK 620 5 CLA A1105   ND  102.8  92.2 177.0  87.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A1107  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 129   NE2                                                    
REMARK 620 2 CLA A1107   NA   97.2                                              
REMARK 620 3 CLA A1107   NB   82.9  92.2                                        
REMARK 620 4 CLA A1107   NC   82.8 178.1  89.6                                  
REMARK 620 5 CLA A1107   ND   96.5  91.1 176.7  87.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A1126  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 398   ND1                                                    
REMARK 620 2 CLA A1126   NA   98.2                                              
REMARK 620 3 CLA A1126   NB   92.6  91.5                                        
REMARK 620 4 CLA A1126   NC   82.8 177.9  90.3                                  
REMARK 620 5 CLA A1126   ND   88.6  91.2 176.9  87.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A1127  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 399   NE2                                                    
REMARK 620 2 CLA A1127   NA   91.9                                              
REMARK 620 3 CLA A1127   NB  118.0  91.0                                        
REMARK 620 4 CLA A1127   NC   88.3 179.8  89.0                                  
REMARK 620 5 CLA A1127   ND   62.0  92.0 177.0  88.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B3101  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 590   SG                                                     
REMARK 620 2 SF4 B3101   S1   55.6                                              
REMARK 620 3 SF4 B3101   S2  128.1 111.1                                        
REMARK 620 4 SF4 B3101   S3  127.3 101.7 103.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B1211  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 193   ND1                                                    
REMARK 620 2 CLA B1211   NA  103.6                                              
REMARK 620 3 CLA B1211   NB  100.2  92.1                                        
REMARK 620 4 CLA B1211   NC   76.3 179.1  88.8                                  
REMARK 620 5 CLA B1211   ND   79.5  90.7 177.2  88.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B1213  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 275   NE2                                                    
REMARK 620 2 CLA B1213   NA   88.4                                              
REMARK 620 3 CLA B1213   NB   80.8  90.8                                        
REMARK 620 4 CLA B1213   NC   92.0 179.3  89.8                                  
REMARK 620 5 CLA B1213   ND   99.8  92.3 176.9  87.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B1215  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 277   NE2                                                    
REMARK 620 2 CLA B1215   NA   76.0                                              
REMARK 620 3 CLA B1215   NB   76.6  91.6                                        
REMARK 620 4 CLA B1215   NC  103.8 179.2  89.1                                  
REMARK 620 5 CLA B1215   ND  104.7  93.0 175.5  86.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B1219  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 308   NE2                                                    
REMARK 620 2 CLA B1219   NA  103.1                                              
REMARK 620 3 CLA B1219   NB   87.5  92.3                                        
REMARK 620 4 CLA B1219   NC   76.9 179.2  88.5                                  
REMARK 620 5 CLA B1219   ND   91.9  91.2 176.4  87.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B1227  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 414   NE2                                                    
REMARK 620 2 CLA B1227   NA   62.2                                              
REMARK 620 3 CLA B1227   NB   85.3  93.0                                        
REMARK 620 4 CLA B1227   NC  118.2 178.6  88.4                                  
REMARK 620 5 CLA B1227   ND   97.7  92.7 174.3  85.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B3101  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 559   SG                                                     
REMARK 620 2 SF4 B3101   S2   88.5                                              
REMARK 620 3 SF4 B3101   S3   71.9 103.0                                        
REMARK 620 4 SF4 B3101   S4  166.9 103.1 110.6                                  
REMARK 620 5 ASP B 560   N    71.9 115.5 125.3  97.3                            
REMARK 620 6 GLY B 561   N   116.0  72.4 170.2  63.1  64.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B3101  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 568   SG                                                     
REMARK 620 2 SF4 B3101   S1  163.6                                              
REMARK 620 3 SF4 B3101   S3   90.7 101.9                                        
REMARK 620 4 SF4 B3101   S4   84.2 100.7 110.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B9010  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 654   NE2                                                    
REMARK 620 2 CLA B9010   NA   87.1                                              
REMARK 620 3 CLA B9010   NB   81.7  91.6                                        
REMARK 620 4 CLA B9010   NC   93.2 178.6  89.7                                  
REMARK 620 5 CLA B9010   ND   98.5  93.0 175.4  85.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C3103  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE C  12   N                                                      
REMARK 620 2 SF4 C3103   S1  139.4                                              
REMARK 620 3 SF4 C3103   S2  103.2 105.3                                        
REMARK 620 4 SF4 C3103   S4   94.3 104.7 106.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C3102  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  48   SG                                                     
REMARK 620 2 SF4 C3102   S2   81.7                                              
REMARK 620 3 SF4 C3102   S3   70.6 110.0                                        
REMARK 620 4 SF4 C3102   S4  170.0 108.2 103.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C3102  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL C  49   O                                                      
REMARK 620 2 SF4 C3102   S1  148.8                                              
REMARK 620 3 SF4 C3102   S2  108.6 102.5                                        
REMARK 620 4 SF4 C3102   S3   67.0 104.3 110.7                                  
REMARK 620 5 CYS C  51   N    52.0  96.9 159.1  71.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C3102  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  54   SG                                                     
REMARK 620 2 SF4 C3102   S1   88.0                                              
REMARK 620 3 SF4 C3102   S2  166.2 104.6                                        
REMARK 620 4 SF4 C3102   S4   63.2 107.6 106.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA L1502  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS L  60   NE2                                                    
REMARK 620 2 CLA L1502   NA   93.7                                              
REMARK 620 3 CLA L1502   NB   99.3  89.1                                        
REMARK 620 4 CLA L1502   NC   86.3 179.3  91.7                                  
REMARK 620 5 CLA L1502   ND   80.3  94.7 176.3  84.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 33006  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU 3  77   OE2                                                    
REMARK 620 2 CLA 33006   NA  105.8                                              
REMARK 620 3 CLA 33006   NB   70.6  91.4                                        
REMARK 620 4 CLA 33006   NC   74.3 179.1  89.4                                  
REMARK 620 5 CLA 33006   ND  108.6  91.3 177.3  87.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA H1505  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN H  36   OE1                                                    
REMARK 620 2 CLA H1505   NA   86.5                                              
REMARK 620 3 CLA H1505   NB   84.5  90.6                                        
REMARK 620 4 CLA H1505   NC   93.3 179.5  89.8                                  
REMARK 620 5 CLA H1505   ND   95.4  92.3 177.1  87.3                            
REMARK 620 N                    1     2     3     4                             
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   56.8                                              
REMARK 620 3 CLA B1206   NB  110.3  90.2                                        
REMARK 620 4 CLA B1206   NC  123.4 179.8  89.8                                  
REMARK 620 5 CLA B1206   ND   71.6  92.4 177.4  87.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA 11011  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU 1 109   OE1                                                    
REMARK 620 2 CLA 11011   NA   65.0                                              
REMARK 620 3 CLA 11011   NB   99.0  90.8                                        
REMARK 620 4 CLA 11011   NC  114.9 179.3  89.8                                  
REMARK 620 5 CLA 11011   ND   82.5  92.5 176.7  86.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B1226  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CLA B1203   O2A                                                    
REMARK 620 2 CLA B1226   NA   71.8                                              
REMARK 620 3 CLA B1226   NB   64.3  90.9                                        
REMARK 620 4 CLA B1226   NC  107.9 179.3  89.6                                  
REMARK 620 5 CLA B1226   ND  115.9  91.5 177.5  88.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED                              
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED                              
REMARK 750                                                                      
REMARK 750 TURN                                                                 
REMARK 750 DETERMINATION METHOD: AUTHOR DETERMINED                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1104                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1105                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1106                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1107                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1108                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1109                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1110                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1111                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1113                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1115                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1116                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1117                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1118                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1119                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1120                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1122                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1123                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1124                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1126                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1127                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1128                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1129                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA L 1130                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1131                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1132                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1133                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1134                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1135                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1136                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1137                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1138                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA F 1139                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1140                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA K 1141                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1143                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1146                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1147                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1148                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA K 1153                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 9010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 9011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 9012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 9013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 9022                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 9023                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA I 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1206                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1207                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1208                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1209                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1210                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1211                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1212                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1213                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1214                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1215                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1216                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1217                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1218                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1219                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1220                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1221                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1222                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1223                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1224                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1225                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1226                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1227                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1228                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1229                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1230                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1231                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1232                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA G 1233                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1234                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1235                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1236                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1237                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1238                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1239                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA F 1240                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1241                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1242                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1301                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA F 1302                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA F 1303                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 1304                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA F 1305                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA F 1306                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA J 1307                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA J 1308                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA G 1248                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA F 4015                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA H 1501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA L 1502                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA L 1503                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA L 1504                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA H 1505                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA J 2107                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 1009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 1 1008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 2009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 2004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 2005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 2006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 2013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 2011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 2012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 2007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 2002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 2003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 2 2008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: OC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 3 3003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: PC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA 4 4008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: QC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 3101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 C 3102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 C 3103                
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 6011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR F 6016                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 6017                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR I 6018                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: RC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR L 6020                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1QZV   RELATED DB: PDB                                   
REMARK 900 PLANT PSI AT 4.4A RESOLUTIONS                                        
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SEQUENCE FOR CHAIN K WAS MODELED AS ALA DUE TO POOR                  
REMARK 999 ELECTRON DENSITY, THEREFORE ALIGNMENT IS UNCLEAR AND                 
REMARK 999 RESIDUES IN COORDINATES WERE LABELED AS UNK. PROPER                  
REMARK 999 SEQUENCE IS                                                          
REMARK 999 LGAKCDFIGSSTNLIMVTSTTLMLFAGRFGLAPSANRKATAGLRLEARDSGLQ                
REMARK 999 TGDPAGFTLADTLACGTVGHIIGVGVVLGLKNIGAI                                 
DBREF  2O01 A    5   758  UNP    P05310   PSAA_PEA         5    758             
DBREF  2O01 B    2   733  UNP    P05311   PSAB_PEA         2    733             
DBREF  2O01 C    2    81  UNP    P10793   PSAC_PEA         1     80             
DBREF  2O01 D   19   156  UNP    P12353   PSAD_SPIOL      75    212             
DBREF  2O01 E   30    91  UNP    Q9S831   PSAE1_ARATH     81    142             
DBREF  2O01 F    1   154  UNP    P12355   PSAF_SPIOL      78    231             
DBREF  2O01 G    4    98  UNP    P12357   PSAG_SPIOL      73    167             
DBREF  2O01 H   21    95  UNP    P22179   PSAH_SPIOL      70    144             
DBREF  2O01 I    1    30  UNP    P17227   PSAI_PEA         1     30             
DBREF  2O01 J    1    42  UNP    P17230   PSAJ_SPIOL       1     42             
DBREF  2O01 L    5   168  UNP    Q41385   PSAL_SPIOL      53    216             
DBREF  2O01 N    1    85  UNP    Q84U30   Q84U30_PHAVU    86    170             
DBREF  2O01 1    5   191  UNP    Q01667   Q01667_ARATH    49    235             
DBREF  2O01 2   16   201  UNP    Q41038   Q41038_PEA      74    259             
DBREF  2O01 3   54   218  UNP    Q9SY97   Q9SY97_ARATH    95    259             
DBREF  2O01 4   34   198  UNP    Q9SQL2   Q9SQL2_PEA      85    249             
DBREF  2O01 K   54    18  PDB    2O01     2O01            54     18             
SEQADV 2O01 GLY A  220  UNP  P05310    ARG   220 CONFLICT                       
SEQADV 2O01 ALA B  147  UNP  P05311    PHE   147 CONFLICT                       
SEQADV 2O01 GLU 2   17  UNP  Q41038    PRO    75 CONFLICT                       
SEQADV 2O01 SER 2   35  UNP  Q41038    GLY    93 CONFLICT                       
SEQRES   1 A  754  SER PRO GLU PRO LYS VAL GLN ILE LEU ALA ASP PRO GLU          
SEQRES   2 A  754  VAL LYS ILE LEU VAL ASP ARG ASP PRO ILE LYS THR SER          
SEQRES   3 A  754  PHE GLU GLN TRP ALA LYS PRO GLY HIS PHE SER ARG THR          
SEQRES   4 A  754  ILE ALA LYS GLY PRO ASP THR THR THR TRP ILE TRP ASN          
SEQRES   5 A  754  LEU HIS ALA ASP ALA HIS ASP PHE ASP SER HIS THR SER          
SEQRES   6 A  754  ASP LEU GLU GLU ILE SER ARG LYS VAL PHE SER ALA HIS          
SEQRES   7 A  754  PHE GLY GLN LEU SER ILE ILE PHE LEU TRP LEU SER GLY          
SEQRES   8 A  754  MET TYR PHE HIS GLY ALA ARG PHE SER ASN TYR GLU ALA          
SEQRES   9 A  754  TRP LEU ASN ASP PRO THR HIS ILE GLY PRO SER ALA GLN          
SEQRES  10 A  754  VAL VAL TRP PRO ILE VAL GLY GLN GLU ILE LEU ASN GLY          
SEQRES  11 A  754  ASP VAL GLY GLY GLY PHE ARG GLY ILE GLN ILE THR SER          
SEQRES  12 A  754  GLY PHE PHE GLN ILE TRP ARG ALA SER GLY ILE THR SER          
SEQRES  13 A  754  GLU LEU GLN LEU TYR CYS THR ALA ILE GLY ALA LEU VAL          
SEQRES  14 A  754  PHE ALA GLY LEU MET LEU PHE ALA GLY TRP PHE HIS TYR          
SEQRES  15 A  754  HIS LYS ALA ALA PRO LYS LEU ALA TRP PHE GLN ASP VAL          
SEQRES  16 A  754  GLU SER MET LEU ASN HIS HIS LEU ALA GLY LEU LEU GLY          
SEQRES  17 A  754  LEU GLY SER LEU SER TRP ALA GLY HIS GLN VAL HIS VAL          
SEQRES  18 A  754  SER LEU PRO ILE ASN GLN PHE LEU ASN ALA GLY VAL ASP          
SEQRES  19 A  754  PRO LYS GLU ILE PRO LEU PRO HIS GLU PHE ILE LEU ASN          
SEQRES  20 A  754  ARG ASP LEU LEU ALA GLN LEU TYR PRO SER PHE ALA GLU          
SEQRES  21 A  754  GLY ALA THR PRO PHE PHE THR LEU ASN TRP SER LYS TYR          
SEQRES  22 A  754  ALA ASP PHE LEU THR PHE ARG GLY GLY LEU ASP PRO LEU          
SEQRES  23 A  754  THR GLY GLY LEU TRP LEU THR ASP ILE ALA HIS HIS HIS          
SEQRES  24 A  754  LEU ALA ILE ALA ILE LEU PHE LEU ILE ALA GLY HIS MET          
SEQRES  25 A  754  TYR ARG THR ASN TRP GLY ILE GLY HIS GLY ILE LYS ASP          
SEQRES  26 A  754  ILE LEU GLU ALA HIS LYS GLY PRO PHE THR GLY GLN GLY          
SEQRES  27 A  754  HIS LYS GLY LEU TYR GLU ILE LEU THR THR SER TRP HIS          
SEQRES  28 A  754  ALA GLN LEU SER ILE ASN LEU ALA MET LEU GLY SER LEU          
SEQRES  29 A  754  THR ILE VAL VAL ALA GLN HIS MET TYR SER MET PRO PRO          
SEQRES  30 A  754  TYR PRO TYR LEU ALA THR ASP TYR ALA THR GLN LEU SER          
SEQRES  31 A  754  LEU PHE THR HIS HIS MET TRP ILE GLY GLY PHE LEU ILE          
SEQRES  32 A  754  VAL GLY ALA ALA ALA HIS ALA ALA ILE PHE MET VAL ARG          
SEQRES  33 A  754  ASP TYR ASP PRO THR THR ARG TYR ASN ASP LEU LEU ASP          
SEQRES  34 A  754  ARG VAL LEU ARG HIS ARG ASP ALA ILE ILE SER HIS LEU          
SEQRES  35 A  754  ASN TRP VAL CYS ILE PHE LEU GLY PHE HIS SER PHE GLY          
SEQRES  36 A  754  LEU TYR ILE HIS ASN ASP THR MET SER ALA LEU GLY ARG          
SEQRES  37 A  754  PRO GLN ASP MET PHE SER ASP THR ALA ILE GLN LEU GLN          
SEQRES  38 A  754  PRO VAL PHE ALA GLN TRP ILE GLN ASN THR HIS ALA LEU          
SEQRES  39 A  754  ALA PRO GLY THR THR ALA PRO GLY ALA THR ALA SER THR          
SEQRES  40 A  754  SER LEU THR TRP GLY GLY GLY ASP LEU VAL ALA VAL GLY          
SEQRES  41 A  754  ASN LYS VAL ALA LEU LEU PRO ILE PRO LEU GLY THR ALA          
SEQRES  42 A  754  ASP PHE LEU VAL HIS HIS ILE HIS ALA PHE THR ILE HIS          
SEQRES  43 A  754  VAL THR VAL LEU ILE LEU LEU LYS GLY VAL LEU PHE ALA          
SEQRES  44 A  754  ARG SER SER ARG LEU ILE PRO ASP LYS ALA ASN LEU GLY          
SEQRES  45 A  754  PHE ARG PHE PRO CYS ASP GLY PRO GLY ARG GLY GLY THR          
SEQRES  46 A  754  CYS GLN VAL SER ALA TRP ASP HIS VAL PHE LEU GLY LEU          
SEQRES  47 A  754  PHE TRP MET TYR ASN SER ILE SER VAL VAL ILE PHE HIS          
SEQRES  48 A  754  PHE SER TRP LYS MET GLN SER ASP VAL TRP GLY THR ILE          
SEQRES  49 A  754  ASN ASP GLN GLY VAL VAL THR HIS ILE THR ALA GLY ASN          
SEQRES  50 A  754  PHE ALA GLN SER SER ILE THR ILE ASN GLY TRP LEU ARG          
SEQRES  51 A  754  ASP PHE LEU TRP ALA GLN ALA SER GLN VAL ILE GLN SER          
SEQRES  52 A  754  TYR GLY SER SER LEU SER ALA TYR GLY LEU PHE PHE LEU          
SEQRES  53 A  754  GLY ALA HIS PHE VAL TRP ALA PHE SER LEU MET PHE LEU          
SEQRES  54 A  754  PHE SER GLY ARG GLY TYR TRP GLN GLU LEU ILE GLU SER          
SEQRES  55 A  754  ILE VAL TRP ALA HIS ASN LYS LEU LYS VAL ALA PRO ALA          
SEQRES  56 A  754  THR GLN PRO ARG ALA LEU SER ILE VAL GLN GLY ARG ALA          
SEQRES  57 A  754  VAL GLY VAL THR HIS TYR LEU LEU GLY GLY ILE ALA THR          
SEQRES  58 A  754  THR TRP ALA PHE PHE LEU ALA ARG ILE ILE ALA VAL GLY          
SEQRES   1 B  732  ALA LEU ARG ILE PRO ARG PHE SER GLN GLY ILE ALA GLN          
SEQRES   2 B  732  ASP PRO THR THR ARG ARG ILE TRP PHE GLY ILE ALA THR          
SEQRES   3 B  732  ALA HIS ASP PHE GLU SER HIS ASP ASP ILE THR GLU GLY          
SEQRES   4 B  732  ARG LEU TYR GLN ASN ILE PHE ALA SER HIS PHE GLY GLN          
SEQRES   5 B  732  LEU ALA ILE ILE PHE LEU TRP THR SER GLY ASN LEU PHE          
SEQRES   6 B  732  HIS VAL ALA TRP GLN GLY ASN PHE GLU ALA TRP VAL GLN          
SEQRES   7 B  732  ASP PRO PHE HIS VAL ARG PRO ILE ALA HIS ALA ILE TRP          
SEQRES   8 B  732  ASP PRO HIS PHE GLY GLN PRO ALA VAL GLU ALA PHE THR          
SEQRES   9 B  732  ARG GLY GLY ALA LEU GLY PRO VAL ASN ASN ALA TYR SER          
SEQRES  10 B  732  GLY VAL TYR GLN TRP TRP TYR THR ILE GLY LEU ARG THR          
SEQRES  11 B  732  ASN GLU ASP LEU TYR THR GLY ALA ILE PHE LEU LEU PHE          
SEQRES  12 B  732  LEU SER ALA ILE SER LEU LEU ALA GLY TRP LEU HIS LEU          
SEQRES  13 B  732  GLN PRO LYS TRP LYS PRO SER VAL SER TRP PHE LYS ASN          
SEQRES  14 B  732  ALA GLU SER ARG LEU ASN HIS HIS LEU SER GLY LEU PHE          
SEQRES  15 B  732  GLY VAL SER SER LEU ALA TRP ALA GLY HIS LEU VAL HIS          
SEQRES  16 B  732  VAL ALA ILE PRO GLY SER ARG GLY GLU TYR VAL ARG TRP          
SEQRES  17 B  732  ASN ASN PHE LEU ASP VAL LEU PRO TYR PRO GLN GLY LEU          
SEQRES  18 B  732  GLY PRO LEU LEU THR GLY GLN TRP ASN LEU TYR ALA GLN          
SEQRES  19 B  732  ASN PRO SER SER SER ASN HIS LEU PHE GLY THR THR GLN          
SEQRES  20 B  732  GLY ALA GLY THR ALA ILE LEU THR ILE LEU GLY GLY PHE          
SEQRES  21 B  732  HIS PRO GLN THR GLN SER LEU TRP LEU THR ASP VAL ALA          
SEQRES  22 B  732  HIS HIS HIS LEU ALA ILE ALA PHE LEU PHE LEU ILE GLY          
SEQRES  23 B  732  GLY LEU MET TYR ARG THR ASN PHE GLY ILE GLY HIS SER          
SEQRES  24 B  732  ILE LYS TYR ILE LEU GLU ALA HIS ILE PRO PRO GLY GLY          
SEQRES  25 B  732  ARG LEU GLY ARG GLY HIS LYS GLY LEU TYR ASP THR ILE          
SEQRES  26 B  732  ASN ASN SER ILE HIS PHE GLN LEU GLY LEU ALA LEU ALA          
SEQRES  27 B  732  SER LEU GLY VAL ILE THR SER LEU VAL ALA GLN HIS MET          
SEQRES  28 B  732  TYR SER LEU PRO ALA TYR ALA PHE ILE ALA GLN ASP PHE          
SEQRES  29 B  732  THR THR GLN ALA ALA LEU TYR THR HIS HIS GLN TYR ILE          
SEQRES  30 B  732  ALA GLY PHE ILE MET THR GLY ALA PHE ALA HIS GLY PRO          
SEQRES  31 B  732  ILE PHE PHE ILE ARG ASP TYR ASN PRO GLU GLN ASN ALA          
SEQRES  32 B  732  ASP ASN VAL LEU ALA ARG MET LEU GLU HIS LYS GLU ALA          
SEQRES  33 B  732  ILE ILE SER HIS LEU SER TRP ALA SER LEU PHE LEU GLY          
SEQRES  34 B  732  PHE HIS THR LEU GLY LEU TYR VAL HIS ASN ASP VAL MET          
SEQRES  35 B  732  LEU ALA PHE GLY THR PRO GLU LYS GLN ILE LEU ILE GLU          
SEQRES  36 B  732  PRO ILE PHE ALA GLN TRP ILE GLN SER ALA HIS GLY LYS          
SEQRES  37 B  732  THR THR TYR GLY PHE ASP ILE PRO LEU SER SER THR ASN          
SEQRES  38 B  732  GLY PRO ALA LEU ASN ALA GLY ARG ASN ILE TRP LEU PRO          
SEQRES  39 B  732  GLY TRP LEU ASN ALA ILE ASN GLU ASN SER ASN SER LEU          
SEQRES  40 B  732  PHE LEU THR ILE GLY PRO GLY ASP PHE LEU VAL HIS HIS          
SEQRES  41 B  732  ALA ILE ALA LEU GLY LEU HIS THR THR THR LEU ILE LEU          
SEQRES  42 B  732  VAL LYS GLY ALA LEU ASP ALA ARG GLY SER LYS LEU MET          
SEQRES  43 B  732  PRO ASP LYS LYS ASP PHE GLY TYR SER PHE PRO CYS ASP          
SEQRES  44 B  732  GLY PRO GLY ARG GLY GLY THR CYS ASP ILE SER ALA TRP          
SEQRES  45 B  732  ASP ASP PHE TYR LEU ALA VAL PHE TRP MET LEU ASN THR          
SEQRES  46 B  732  ILE GLY TRP VAL THR PHE TYR TRP HIS TRP LYS HIS ILE          
SEQRES  47 B  732  THR LEU TRP ARG GLY ASN VAL SER GLN PHE ASN GLU SER          
SEQRES  48 B  732  SER THR TYR LEU MET GLY TRP LEU ARG ASP TYR LEU TRP          
SEQRES  49 B  732  LEU ASN SER SER GLN LEU ILE ASN GLY ILE THR PRO LEU          
SEQRES  50 B  732  VAL CYS ASN SER LEU SER VAL TRP ALA TRP MET PHE LEU          
SEQRES  51 B  732  PHE GLY HIS LEU VAL TRP ALA THR GLY PHE MET PHE LEU          
SEQRES  52 B  732  ILE SER TRP ARG GLY TYR TRP GLN GLU LEU ILE GLU THR          
SEQRES  53 B  732  LEU ALA TRP ALA HIS GLU ARG THR PRO LEU ALA ASN LEU          
SEQRES  54 B  732  ILE ARG TRP ARG ASP LYS PRO VAL ALA LEU SER ILE VAL          
SEQRES  55 B  732  GLN ALA ARG LEU VAL GLY LEU VAL HIS PHE SER VAL GLY          
SEQRES  56 B  732  TYR ILE PHE THR TYR ALA ALA PHE LEU ILE ALA SER THR          
SEQRES  57 B  732  SER GLY LYS PHE                                              
SEQRES   1 C   80  SER HIS SER VAL LYS ILE TYR ASP THR CYS ILE GLY CYS          
SEQRES   2 C   80  THR GLN CYS VAL ARG ALA CYS PRO THR ASP VAL LEU GLU          
SEQRES   3 C   80  MET ILE PRO TRP GLY GLY CYS LYS ALA LYS GLN ILE ALA          
SEQRES   4 C   80  SER ALA PRO ARG THR GLU ASP CYS VAL GLY CYS LYS ARG          
SEQRES   5 C   80  CYS GLU SER ALA CYS PRO THR ASP PHE LEU SER VAL ARG          
SEQRES   6 C   80  VAL TYR LEU TRP HIS GLU THR THR ARG SER MET GLY LEU          
SEQRES   7 C   80  ALA TYR                                                      
SEQRES   1 D  138  GLU LEU ASP PRO ASN THR PRO SER PRO ILE PHE ALA 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 GLU 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 SER 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 PRO GLY ARG GLN GLY VAL GLY LEU ASN MET 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   62  PRO LYS ARG GLY SER LYS VAL LYS ILE LEU ARG ARG GLU          
SEQRES   2 E   62  SER TYR TRP PHE LYS ASN VAL GLY SER VAL VAL ALA VAL          
SEQRES   3 E   62  ASP GLN ASP PRO LYS THR ARG TYR PRO VAL VAL VAL ARG          
SEQRES   4 E   62  PHE ALA LYS VAL ASN TYR ALA ASN ILE SER THR ASN ASN          
SEQRES   5 E   62  TYR ALA LEU ASP GLU VAL GLU GLU VAL ALA                      
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  PRO SER 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 MET ALA LYS GLN VAL PRO GLU GLN ASN GLY MET SER          
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 ILE VAL          
SEQRES   7 G   95  ALA TYR TYR ILE LEU ALA THR ALA SER ASN GLY TYR ASP          
SEQRES   8 G   95  PRO SER PHE PHE                                              
SEQRES   1 H   75  TRP ASP VAL TYR GLY SER ASP ALA PRO SER PRO TYR ASN          
SEQRES   2 H   75  SER LEU GLN SER LYS PHE PHE GLU THR PHE ALA ALA PRO          
SEQRES   3 H   75  PHE THR LYS ARG GLY LEU LEU LEU LYS PHE LEU ILE LEU          
SEQRES   4 H   75  GLY GLY GLY SER LEU LEU THR TYR VAL SER ALA ASN ALA          
SEQRES   5 H   75  PRO GLN ASP VAL LEU PRO ILE THR ARG GLY PRO GLN GLN          
SEQRES   6 H   75  PRO PRO LYS LEU GLY PRO ARG GLY LYS ILE                      
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 PHE LYS THR TYR LEU SER VAL ALA PRO VAL          
SEQRES   2 J   42  LEU SER THR LEU TRP PHE GLY SER LEU ALA GLY LEU LEU          
SEQRES   3 J   42  ILE GLU ILE ASN ARG PHE PHE PRO ASP ALA LEU THR PHE          
SEQRES   4 J   42  PRO PHE PHE                                                  
SEQRES   1 K   38  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 K   38  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   3 K   38  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK              
SEQRES   1 L  164  LYS PRO THR TYR GLN VAL ILE GLN PRO LEU ASN GLY ASP          
SEQRES   2 L  164  PRO PHE ILE GLY GLY LEU GLU THR PRO VAL THR SER SER          
SEQRES   3 L  164  PRO LEU ILE ALA TRP TYR LEU SER ASN LEU PRO ALA TYR          
SEQRES   4 L  164  ARG THR ALA VAL ASN PRO LEU LEU ARG GLY VAL GLU VAL          
SEQRES   5 L  164  GLY LEU ALA HIS GLY PHE LEU LEU VAL GLY PRO PHE VAL          
SEQRES   6 L  164  LYS ALA GLY PRO LEU ARG ASN THR GLU TYR ALA GLY ALA          
SEQRES   7 L  164  ALA GLY SER LEU ALA ALA ALA GLY LEU VAL VAL ILE LEU          
SEQRES   8 L  164  SER MET CYS LEU THR MET TYR GLY ILE ALA SER PHE LYS          
SEQRES   9 L  164  GLU GLY GLU PRO SER ILE ALA PRO ALA LEU THR LEU THR          
SEQRES  10 L  164  GLY ARG LYS LYS GLN PRO ASP GLN LEU GLN SER ALA ASP          
SEQRES  11 L  164  GLY TRP ALA LYS PHE THR GLY GLY PHE PHE PHE GLY GLY          
SEQRES  12 L  164  VAL SER GLY VAL THR TRP ALA CYS PHE LEU MET TYR VAL          
SEQRES  13 L  164  LEU ASP LEU PRO TYR TYR PHE LYS                              
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 1  187  MET PRO GLY GLU PRO ARG PRO ALA TYR LEU ASP GLY SER          
SEQRES   2 1  187  ALA PRO GLY ASP PHE GLY PHE ASP PRO LEU GLY LEU GLY          
SEQRES   3 1  187  GLU VAL PRO ALA ASN LEU GLU ARG TYR LYS GLU SER GLU          
SEQRES   4 1  187  LEU ILE HIS CYS ARG TRP ALA MET LEU ALA VAL PRO GLY          
SEQRES   5 1  187  ILE LEU VAL PRO GLU ALA LEU GLY TYR GLY ASN TRP VAL          
SEQRES   6 1  187  LYS ALA GLN GLU TRP ALA ALA LEU PRO GLY GLY GLN ALA          
SEQRES   7 1  187  THR TYR LEU GLY ASN PRO VAL PRO TRP GLY THR LEU PRO          
SEQRES   8 1  187  THR ILE LEU ALA ILE GLU PHE LEU ALA ILE ALA PHE VAL          
SEQRES   9 1  187  GLU HIS GLN ARG SER MET GLU LYS ASP PRO GLU LYS LYS          
SEQRES  10 1  187  LYS TYR PRO GLY GLY ALA PHE ASP PRO LEU GLY TYR SER          
SEQRES  11 1  187  LYS ASP PRO LYS LYS LEU GLU GLU LEU LYS VAL LYS GLU          
SEQRES  12 1  187  ILE LYS ASN GLY ARG LEU ALA LEU LEU ALA PHE VAL GLY          
SEQRES  13 1  187  PHE CYS VAL GLN GLN SER ALA TYR PRO GLY THR GLY PRO          
SEQRES  14 1  187  LEU GLU ASN LEU ALA THR HIS LEU ALA ASP PRO TRP HIS          
SEQRES  15 1  187  ASN ASN ILE GLY ASP                                          
SEQRES   1 2  186  PRO GLU TRP LEU ASP GLY SER LEU PRO GLY ASP PHE GLY          
SEQRES   2 2  186  PHE ASP PRO LEU GLY LEU SER SER ASP PRO GLU SER LEU          
SEQRES   3 2  186  ARG TRP ASN VAL GLN ALA GLU LEU VAL HIS SER ARG TRP          
SEQRES   4 2  186  ALA MET LEU GLY ALA ALA GLY ILE PHE ILE PRO GLU PHE          
SEQRES   5 2  186  LEU THR LYS LEU GLY ILE LEU ASN THR PRO SER TRP TYR          
SEQRES   6 2  186  THR ALA GLY GLU GLN GLU TYR PHE THR ASP THR THR THR          
SEQRES   7 2  186  LEU PHE ILE VAL GLU LEU VAL PHE ILE GLY TRP ALA GLU          
SEQRES   8 2  186  GLY ARG ARG TRP ALA ASP ILE LEU ASN PRO GLY CYS VAL          
SEQRES   9 2  186  ASN THR ASP PRO ILE PHE PRO ASN ASN LYS LEU THR GLY          
SEQRES  10 2  186  THR ASP VAL GLY TYR PRO GLY GLY LEU TRP PHE ASP PRO          
SEQRES  11 2  186  LEU GLY TRP GLY SER ALA SER PRO GLN LYS LEU LYS GLU          
SEQRES  12 2  186  LEU ARG THR LYS GLU ILE LYS ASN GLY ARG LEU ALA MET          
SEQRES  13 2  186  LEU ALA VAL MET GLY ALA TRP PHE GLN HIS ILE TYR THR          
SEQRES  14 2  186  GLY THR GLY PRO ILE ASP ASN LEU PHE ALA HIS LEU ALA          
SEQRES  15 2  186  ASP PRO GLY HIS                                              
SEQRES   1 3  165  TRP LEU ALA TYR GLY GLU ILE ILE ASN GLY ARG PHE ALA          
SEQRES   2 3  165  MET LEU GLY ALA ALA GLY ALA ILE ALA PRO GLU ILE LEU          
SEQRES   3 3  165  GLY LYS ALA GLY LEU ILE PRO ALA GLU THR ALA LEU PRO          
SEQRES   4 3  165  TRP PHE GLN THR GLY VAL ILE PRO PRO ALA GLY THR TYR          
SEQRES   5 3  165  THR TYR TRP ALA ASP ASN TYR THR LEU PHE VAL LEU GLU          
SEQRES   6 3  165  MET ALA LEU MET GLY PHE ALA GLU HIS ARG ARG LEU GLN          
SEQRES   7 3  165  ASP TRP TYR ASN PRO GLY SER MET GLY LYS GLN TYR PHE          
SEQRES   8 3  165  LEU GLY LEU GLU LYS GLY LEU ALA GLY SER GLY ASN PRO          
SEQRES   9 3  165  ALA TYR PRO GLY GLY PRO PHE PHE ASN PRO LEU GLY PHE          
SEQRES  10 3  165  GLY LYS ASP GLU LYS SER LEU LYS GLU LEU LYS LEU LYS          
SEQRES  11 3  165  GLU VAL LYS ASN GLY ARG LEU ALA MET LEU ALA ILE LEU          
SEQRES  12 3  165  GLY TYR PHE ILE GLN GLY LEU VAL THR GLY VAL GLY PRO          
SEQRES  13 3  165  TYR GLN ASN LEU LEU ASP HIS LEU ALA                          
SEQRES   1 4  165  PRO GLU ASN LEU ARG TRP PHE VAL GLN ALA GLU LEU VAL          
SEQRES   2 4  165  ASN GLY ARG TRP ALA MET LEU GLY VAL ALA GLY MET LEU          
SEQRES   3 4  165  LEU PRO GLU VAL PHE THR SER ILE GLY ILE ILE ASN VAL          
SEQRES   4 4  165  PRO LYS TRP TYR ALA ALA GLY LYS GLU GLU TYR PHE ALA          
SEQRES   5 4  165  SER SER SER THR LEU PHE VAL ILE GLU PHE ILE LEU SER          
SEQRES   6 4  165  HIS TYR VAL GLU ILE ARG ARG TRP GLN ASP ILE LYS ASN          
SEQRES   7 4  165  PRO GLY SER VAL ASN GLN ASP PRO ILE PHE LYS GLN TYR          
SEQRES   8 4  165  SER LEU PRO ALA GLY GLU VAL GLY TYR PRO GLY GLY ILE          
SEQRES   9 4  165  PHE ASN PRO LEU ASN PHE ALA PRO THR LEU GLU ALA LYS          
SEQRES  10 4  165  GLU LYS GLU ILE ALA ASN GLY ARG LEU ALA MET LEU ALA          
SEQRES  11 4  165  PHE LEU GLY PHE ILE ILE GLN HIS ASN VAL THR GLY LYS          
SEQRES  12 4  165  GLY PRO PHE ASP ASN LEU LEU GLN HIS ILE SER ASP PRO          
SEQRES  13 4  165  TRP HIS ASN THR ILE VAL GLN THR LEU                          
HET    CLA  A1101      25                                                       
HET    CLA  A1102      25                                                       
HET    CLA  A1103      47                                                       
HET    CLA  A1104      25                                                       
HET    CLA  A1105      25                                                       
HET    CLA  A1106      41                                                       
HET    CLA  A1107      57                                                       
HET    CLA  A1108      50                                                       
HET    CLA  A1109      24                                                       
HET    CLA  A1110      25                                                       
HET    CLA  A1111      25                                                       
HET    CLA  A1113      50                                                       
HET    CLA  A1115      47                                                       
HET    CLA  A1116      25                                                       
HET    CLA  A1117      25                                                       
HET    CLA  A1118      25                                                       
HET    CLA  A1119      55                                                       
HET    CLA  A1120      25                                                       
HET    CLA  A1122      55                                                       
HET    CLA  A1123      55                                                       
HET    CLA  A1124      25                                                       
HET    CLA  L1125      25                                                       
HET    CLA  A1126      55                                                       
HET    CLA  A1127      25                                                       
HET    CLA  A1128      55                                                       
HET    CLA  A1129      55                                                       
HET    CLA  L1130      50                                                       
HET    CLA  A1131      44                                                       
HET    CLA  A1132      25                                                       
HET    CLA  A1133      25                                                       
HET    CLA  A1134      25                                                       
HET    CLA  A1135      45                                                       
HET    CLA  A1136      55                                                       
HET    CLA  A1137      55                                                       
HET    CLA  B1138      56                                                       
HET    CLA  F1139      44                                                       
HET    CLA  A1140      55                                                       
HET    CLA  K1141      25                                                       
HET    CLA  A1142      25                                                       
HET    CLA  A1143      25                                                       
HET    CLA  A1144      25                                                       
HET    CLA  A1146      25                                                       
HET    CLA  A1147      25                                                       
HET    CLA  A1148      25                                                       
HET    CLA  K1150      25                                                       
HET    CLA  A1151      25                                                       
HET    CLA  A1152      25                                                       
HET    CLA  K1153      25                                                       
HET    CLA  B9010      47                                                       
HET    CLA  A9011      55                                                       
HET    CLA  B9012      55                                                       
HET    CLA  A9013      46                                                       
HET    CLA  B9022      54                                                       
HET    CLA  B9023      47                                                       
HET    CLA  B1201      25                                                       
HET    CLA  B1202      50                                                       
HET    CLA  B1203      48                                                       
HET    CLA  I1204      55                                                       
HET    CLA  B1205      55                                                       
HET    CLA  B1206      25                                                       
HET    CLA  B1207      55                                                       
HET    CLA  B1208      55                                                       
HET    CLA  B1209      55                                                       
HET    CLA  B1210      25                                                       
HET    CLA  B1211      25                                                       
HET    CLA  B1212      60                                                       
HET    CLA  B1213      25                                                       
HET    CLA  B1214      49                                                       
HET    CLA  B1215      52                                                       
HET    CLA  B1216      56                                                       
HET    CLA  B1217      50                                                       
HET    CLA  B1218      51                                                       
HET    CLA  B1219      51                                                       
HET    CLA  B1220      60                                                       
HET    CLA  B1221      48                                                       
HET    CLA  B1222      65                                                       
HET    CLA  B1223      25                                                       
HET    CLA  B1224      51                                                       
HET    CLA  B1225      45                                                       
HET    CLA  B1226      25                                                       
HET    CLA  B1227      50                                                       
HET    CLA  B1228      55                                                       
HET    CLA  B1229      49                                                       
HET    CLA  B1230      25                                                       
HET    CLA  B1231      46                                                       
HET    CLA  B1232      55                                                       
HET    CLA  G1233      51                                                       
HET    CLA  B1234      50                                                       
HET    CLA  B1235      55                                                       
HET    CLA  B1236      46                                                       
HET    CLA  B1237      51                                                       
HET    CLA  B1238      54                                                       
HET    CLA  B1239      55                                                       
HET    CLA  F1240      25                                                       
HET    CLA  B1241      25                                                       
HET    CLA  B1242      47                                                       
HET    CLA  B1301      25                                                       
HET    CLA  F1302      55                                                       
HET    CLA  F1303      25                                                       
HET    CLA  41304      55                                                       
HET    CLA  F1305      25                                                       
HET    CLA  F1306      25                                                       
HET    CLA  J1307      25                                                       
HET    CLA  J1308      25                                                       
HET    CLA  A1309      25                                                       
HET    CLA  G1248      25                                                       
HET    CLA  F4015      25                                                       
HET    CLA  H1501      55                                                       
HET    CLA  L1502      51                                                       
HET    CLA  L1503      46                                                       
HET    CLA  L1504      55                                                       
HET    CLA  H1505      25                                                       
HET    CLA  J2107      61                                                       
HET    CLA  11004      25                                                       
HET    CLA  11005      25                                                       
HET    CLA  11006      25                                                       
HET    CLA  41009      25                                                       
HET    CLA  11013      25                                                       
HET    CLA  11010      25                                                       
HET    CLA  11011      25                                                       
HET    CLA  11012      25                                                       
HET    CLA  11001      25                                                       
HET    CLA  11007      25                                                       
HET    CLA  11002      25                                                       
HET    CLA  11003      25                                                       
HET    CLA  11008      25                                                       
HET    CLA  11014      25                                                       
HET    CLA  32009      25                                                       
HET    CLA  22004      25                                                       
HET    CLA  22005      25                                                       
HET    CLA  22006      25                                                       
HET    CLA  22010      25                                                       
HET    CLA  22013      25                                                       
HET    CLA  22001      25                                                       
HET    CLA  22011      25                                                       
HET    CLA  22012      25                                                       
HET    CLA  22015      25                                                       
HET    CLA  22007      25                                                       
HET    CLA  22002      25                                                       
HET    CLA  22003      25                                                       
HET    CLA  22008      25                                                       
HET    CLA  33009      25                                                       
HET    CLA  33004      25                                                       
HET    CLA  33005      25                                                       
HET    CLA  33012      25                                                       
HET    CLA  33006      25                                                       
HET    CLA  33013      25                                                       
HET    CLA  33010      25                                                       
HET    CLA  33001      25                                                       
HET    CLA  33011      25                                                       
HET    CLA  33002      25                                                       
HET    CLA  33007      25                                                       
HET    CLA  33015      25                                                       
HET    CLA  33003      25                                                       
HET    CLA  33008      25                                                       
HET    CLA  44009      25                                                       
HET    CLA  44004      25                                                       
HET    CLA  44005      25                                                       
HET    CLA  44006      25                                                       
HET    CLA  44013      25                                                       
HET    CLA  44010      25                                                       
HET    CLA  44011      25                                                       
HET    CLA  44012      25                                                       
HET    CLA  44001      25                                                       
HET    CLA  44007      25                                                       
HET    CLA  44002      25                                                       
HET    CLA  44003      25                                                       
HET    CLA  44008      25                                                       
HET    SF4  B3101       8                                                       
HET    SF4  C3102       8                                                       
HET    SF4  C3103       8                                                       
HET    PQN  A5001      33                                                       
HET    PQN  B5002      33                                                       
HET    BCR  A6011      40                                                       
HET    BCR  F6016      40                                                       
HET    BCR  B6017      40                                                       
HET    BCR  I6018      40                                                       
HET    BCR  L6020      40                                                       
HETNAM     CLA CHLOROPHYLL A                                                    
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     PQN PHYLLOQUINONE                                                    
HETNAM     BCR BETA-CAROTENE                                                    
HETSYN     PQN VITAMIN K1; 2-METHYL-3-PHYTYL-1,4-NAPHTHOQUINONE                 
FORMUL  18  CLA    168(C55 H72 MG N4 O5 2+)                                     
FORMUL  86  SF4    3(FE4 S4)                                                    
FORMUL  89  PQN    2(C31 H46 O2)                                                
FORMUL  91  BCR    5(C40 H56)                                                   
HELIX    1  HA THR A   51  ALA A   61  1                                  11    
HELIX    2  HB LEU A   71  ARG A  102  1                                  32    
HELIX    3  HC TYR A  106  ASP A  112  1                                   7    
HELIX    4  HD PHE A  149  ALA A  155  1                                   7    
HELIX    5  HE GLU A  161  LYS A  188  1                                  28    
HELIX    6  HF VAL A  199  VAL A  225  1                                  27    
HELIX    7  HG LEU A  227  ASN A  234  1                                   8    
HELIX    8  HH ARG A  252  LEU A  258  1                                   7    
HELIX    9  HI ASN A  273  ALA A  278  1                                   6    
HELIX   10  HJ LEU A  296  MET A  316  1                                  21    
HELIX   11  HK ASP A  329  ALA A  333  1                                   5    
HELIX   12  HL ALA A  356  SER A  378  1                                  23    
HELIX   13  HM ALA A  390  ARG A  420  1                                  31    
HELIX   14  HN LEU A  431  HIS A  438  1                                   8    
HELIX   15  HO ASP A  440  SER A  468  1                                  29    
HELIX   16  HP ILE A  492  ALA A  499  1                                   8    
HELIX   17  HQ THR A  536  ALA A  563  1                                  28    
HELIX   18  HR TRP A  595  GLN A  621  1                                  27    
HELIX   19  HS PHE A  642  ILE A  647  1                                   6    
HELIX   20  HT ASN A  650  GLN A  660  1                                  11    
HELIX   21  HU SER A  662  SER A  667  1                                   6    
HELIX   22  HV LEU A  672  SER A  695  1                                  24    
HELIX   23  HW TYR A  699  LEU A  714  1                                  16    
HELIX   24  HX VAL A  728  VAL A  757  1                                  30    
HELIX   25  HA ARG B   19  ALA B   28  1                                  10    
HELIX   26  HB GLY B   40  TRP B   70  1                                  31    
HELIX   27  HC ASN B   73  GLN B   79  1                                   7    
HELIX   28  HD VAL B  120  ILE B  127  1                                   8    
HELIX   29  HE ASN B  132  LEU B  157  1                                  26    
HELIX   30  HF ALA B  171  ARG B  203  1                                  33    
HELIX   31  HG GLY B  223  THR B  227  1                                   5    
HELIX   32  HH ASN B  231  GLN B  235  1                                   5    
HELIX   33  HI THR B  271  MET B  290  1                                  20    
HELIX   34  HJ ILE B  301  ILE B  309  1                                   9    
HELIX   35  HK TYR B  323  ASN B  328  1                                   6    
HELIX   36  HL ILE B  330  LEU B  355  1                                  26    
HELIX   37  HM PHE B  365  ILE B  395  1                                  31    
HELIX   38  HN VAL B  407  HIS B  414  1                                   8    
HELIX   39  HO GLU B  416  PHE B  446  1                                  31    
HELIX   40  HP ILE B  458  HIS B  467  1                                  10    
HELIX   41  HQ TRP B  493  ILE B  501  1                                   9    
HELIX   42  HR ASP B  516  ALA B  541  1                                  26    
HELIX   43  HS ALA B  572  TRP B  602  1                                  31    
HELIX   44  HT LEU B  616  ASN B  633  1                                  18    
HELIX   45  HU SER B  644  SER B  666  1                                  23    
HELIX   46  HV GLY B  669  THR B  685  1                                  17    
HELIX   47  HW ILE B  702  GLY B  731  1                                  30    
HELIX   48  HA LYS D   80  LYS D   93  1                                  14    
HELIX   49  HA GLN F   13  ALA F   27  1                                  15    
HELIX   50  HB ALA F   44  LYS F   58  1                                  15    
HELIX   51  HC ILE F   84  ARG F  109  1                                  26    
HELIX   52  HD THR F  115  ILE F  121  1                                   7    
HELIX   53  HF ARG F  142  ASN F  146  1                                   5    
HELIX   54  HA ILE G    8  VAL G   22  1                                  15    
HELIX   55  HB SER G   60  TRP G   74  1                                  15    
HELIX   56  HA GLN H   36  PHE H   43  1                                   8    
HELIX   57  HB GLY H   51  ASN H   71  1                                  21    
HELIX   58  HA SER I    6  PHE I   25  1                                  20    
HELIX   59  HA VAL J   13  PHE J   33  1                                  21    
HELIX   60  HA UNK K    8  UNK K   16  1                                   9    
HELIX   61  HB UNK K   56  UNK K   73  1                                  18    
HELIX   62  HA ALA L   34  LEU L   40  1                                   7    
HELIX   63  HB LEU L   50  ALA L   71  1                                  22    
HELIX   64  HC LEU L   86  TYR L  102  1                                  17    
HELIX   65  HD SER L  132  PHE L  156  1                                  25    
HELIX   66  HA GLU N   15  LYS N   20  1                                   6    
HELIX   67  HB THR N   24  THR N   34  1                                  11    
HELIX   68  HA SER 1   42  VAL 1   59  1                                  18    
HELIX   69  HB LEU 1   94  SER 1  113  1                                  20    
HELIX   70  HC VAL 1  145  SER 1  166  1                                  22    
HELIX   71  HA GLN 2   46  LYS 2   70  1                                  25    
HELIX   72  HB PHE 2   95  ALA 2  111  1                                  17    
HELIX   73  HC LEU 2  156  TRP 2  178  1                                  23    
HELIX   74  HA GLY 3   58  ALA 3   75  1                                  18    
HELIX   75  HB PHE 3  115  TRP 3  133  1                                  19    
HELIX   76  HC LYS 3  183  THR 3  205  1                                  23    
HELIX   77  HA GLN 4   42  LEU 4   60  1                                  19    
HELIX   78  HB LEU 4   90  ASN 4  111  1                                  22    
HELIX   79  HC GLU 4  153  VAL 4  173  1                                  21    
SHEET    1 BS1 4 ASN D  73  LEU D  77  0                                        
SHEET    2 BS1 4 PHE D  45  GLU D  51 -1  O  TRP D  50   O  ASN D  73           
SHEET    3 BS1 4 LYS D  97  PHE D 104 -1  O  GLN D  99   N  THR D  49           
SHEET    4 BS1 4 GLY D 107  LEU D 112 -1  N  VAL D 109   O  ARG D 102           
SHEET    1 BS2 2 VAL E  65  PHE E  69  0                                        
SHEET    2 BS2 2 THR E  79  TYR E  82  0                                        
LINK         NE2 HIS A  82                MG   CLA A1103     1555   1555  2.26  
LINK         OE1 GLN A  85                MG   CLA A1104     1555   1555  2.27  
LINK         NE2 HIS A  99                MG   CLA A1105     1555   1555  2.48  
LINK         NE2 GLN A 129                MG   CLA A1107     1555   1555  2.02  
LINK         ND1 HIS A 398                MG   CLA A1126     1555   1555  2.35  
LINK         NE2 HIS A 399                MG   CLA A1127     1555   1555  2.34  
LINK         SG  CYS A 590                 S1  SF4 B3101     1555   1555  2.08  
LINK         SG  CYS A 590                FE4  SF4 B3101     1555   1555  2.16  
LINK         ND1 HIS B 193                MG   CLA B1211     1555   1555  2.17  
LINK         NE2 HIS B 275                MG   CLA B1213     1555   1555  2.39  
LINK         NE2 HIS B 277                MG   CLA B1215     1555   1555  2.41  
LINK         NE2 HIS B 308                MG   CLA B1219     1555   1555  2.11  
LINK         NE2 HIS B 414                MG   CLA B1227     1555   1555  2.26  
LINK         SG  CYS B 559                FE1  SF4 B3101     1555   1555  2.30  
LINK         SG  CYS B 568                FE2  SF4 B3101     1555   1555  2.47  
LINK         NE2 HIS B 654                MG   CLA B9010     1555   1555  2.48  
LINK         CB  CYS C  11                 S1  SF4 C3103     1555   1555  1.93  
LINK         SG  CYS C  11                 S1  SF4 C3103     1555   1555  2.16  
LINK         N   ILE C  12                FE3  SF4 C3103     1555   1555  1.84  
LINK         SG  CYS C  48                FE1  SF4 C3102     1555   1555  2.49  
LINK         O   VAL C  49                FE4  SF4 C3102     1555   1555  2.22  
LINK         SG  CYS C  54                FE3  SF4 C3102     1555   1555  2.49  
LINK         OE1 GLU F 143                 OE1 GLU F 148     1555   1555  1.38  
LINK         NE2 HIS L  60                MG   CLA L1502     1555   1555  2.45  
LINK         N   CYS C  51                FE4  SF4 C3102     1555   1555  2.63  
LINK         N   ASP B 560                FE1  SF4 B3101     1555   1555  2.74  
LINK         N   GLY B 561                FE1  SF4 B3101     1555   1555  2.75  
LINK         OE2 GLU 3  77                MG   CLA 33006     1555   1555  2.78  
LINK         OE1 GLN H  36                MG   CLA H1505     1555   1555  2.83  
LINK         OD2 ASP B  93                MG   CLA B1206     1555   1555  2.83  
LINK         OE1 GLU 1 109                MG   CLA 11011     1555   1555  2.84  
LINK         O2A CLA B1203                MG   CLA B1226     1555   1555  3.00  
CISPEP   1 PHE A   31    GLU A   32          0        -0.16                     
CISPEP   2 GLU A   32    GLN A   33          0        -0.30                     
CISPEP   3 ALA A   35    LYS A   36          0         8.52                     
CISPEP   4 SER A   80    ALA A   81          0        21.62                     
CISPEP   5 ALA A   81    HIS A   82          0        -9.18                     
CISPEP   6 GLN A  483    LEU A  484          0        -0.95                     
CISPEP   7 VAL A  487    PHE A  488          0         5.76                     
CISPEP   8 ALA A  489    GLN A  490          0        14.87                     
CISPEP   9 GLN A  490    TRP A  491          0        -3.03                     
CISPEP  10 TRP A  491    ILE A  492          0       -10.82                     
CISPEP  11 ILE A  492    GLN A  493          0         5.20                     
CISPEP  12 ILE A  555    LEU A  556          0        17.52                     
CISPEP  13 ILE B    5    PRO B    6          0       -11.40                     
CISPEP  14 TRP B   70    GLN B   71          0        -8.57                     
CISPEP  15 GLN B   71    GLY B   72          0         1.72                     
CISPEP  16 HIS B   83    VAL B   84          0        -5.17                     
CISPEP  17 PRO B  310    PRO B  311          0         7.56                     
CISPEP  18 SER C    4    VAL C    5          0        -8.30                     
CISPEP  19 ILE C   12    GLY C   13          0         0.23                     
CISPEP  20 CYS C   48    VAL C   49          0       -12.33                     
CISPEP  21 GLU D   19    LEU D   20          0        -3.78                     
CISPEP  22 ASP D   21    PRO D   22          0         1.61                     
CISPEP  23 SER D   26    PRO D   27          0        -2.03                     
CISPEP  24 PRO D   72    ASN D   73          0        -7.22                     
CISPEP  25 ARG D  102    VAL D  103          0       -12.55                     
CISPEP  26 PRO D  105    SER D  106          0         3.18                     
CISPEP  27 VAL D  109    GLN D  110          0       -28.93                     
CISPEP  28 HIS D  113    PRO D  114          0       -28.51                     
CISPEP  29 GLY D  150    LYS D  151          0        -0.88                     
CISPEP  30 TYR D  154    ASP D  155          0         5.97                     
CISPEP  31 ASP D  155    LEU D  156          0        18.45                     
CISPEP  32 TRP E   45    PHE E   46          0        24.01                     
CISPEP  33 GLY F    4    LEU F    5          0        11.50                     
CISPEP  34 ALA F   37    PRO F   38          0        28.93                     
CISPEP  35 GLY F   57    LYS F   58          0        -8.90                     
CISPEP  36 LEU F  149    VAL F  150          0         6.20                     
CISPEP  37 VAL F  150    ASP F  151          0        23.54                     
CISPEP  38 ASP F  151    ASN F  152          0         6.77                     
CISPEP  39 ALA G   32    LYS G   33          0        -0.90                     
CISPEP  40 LYS G   33    GLN G   34          0         2.10                     
CISPEP  41 ARG G   50    ALA G   51          0        -2.66                     
CISPEP  42 ALA G   82    TYR G   83          0        29.76                     
CISPEP  43 TYR G   83    TYR G   84          0        11.83                     
CISPEP  44 ILE G   85    LEU G   86          0        -8.30                     
CISPEP  45 THR G   88    ALA G   89          0         0.44                     
CISPEP  46 ALA G   89    SER G   90          0        -5.28                     
CISPEP  47 PHE G   97    PHE G   98          0         0.47                     
CISPEP  48 TYR H   24    GLY H   25          0         2.35                     
CISPEP  49 GLY H   25    SER H   26          0        23.09                     
CISPEP  50 SER H   26    ASP H   27          0         6.24                     
CISPEP  51 GLU H   41    THR H   42          0         8.04                     
CISPEP  52 THR H   42    PHE H   43          0       -18.01                     
CISPEP  53 PHE H   43    ALA H   44          0         3.71                     
CISPEP  54 ALA H   44    ALA H   45          0         0.46                     
CISPEP  55 PRO H   73    GLN H   74          0       -14.11                     
CISPEP  56 GLN H   74    ASP H   75          0         5.28                     
CISPEP  57 GLY H   90    PRO H   91          0        -9.70                     
CISPEP  58 PRO H   91    ARG H   92          0         5.37                     
CISPEP  59 ARG H   92    GLY H   93          0        -4.57                     
CISPEP  60 GLY H   93    LYS H   94          0       -18.04                     
CISPEP  61 PHE I   25    LEU I   26          0        19.30                     
CISPEP  62 ARG J    2    ASP J    3          0        27.70                     
CISPEP  63 PHE J    4    LYS J    5          0       -18.38                     
CISPEP  64 LYS J    5    THR J    6          0       -20.02                     
CISPEP  65 TYR L   79    ALA L   80          0        -6.72                     
CISPEP  66 PRO L  112    SER L  113          0         9.63                     
CISPEP  67 SER L  113    ILE L  114          0       -12.80                     
CISPEP  68 ALA L  115    PRO L  116          0        -9.16                     
CISPEP  69 LEU L  118    THR L  119          0       -13.12                     
CISPEP  70 THR L  119    LEU L  120          0        -2.70                     
CISPEP  71 TYR L  166    PHE L  167          0        20.95                     
CISPEP  72 PHE L  167    LYS L  168          0       -10.33                     
CISPEP  73 VAL N    2    ILE N    3          0        24.62                     
CISPEP  74 GLU N   36    PHE N   37          0         7.26                     
CISPEP  75 GLY N   38    SER N   39          0       -14.55                     
CISPEP  76 SER N   39    CYS N   40          0        16.81                     
CISPEP  77 PRO N   43    GLU N   44          0       -27.19                     
CISPEP  78 GLU N   44    ASN N   45          0       -28.38                     
CISPEP  79 THR N   47    GLY N   48          0         5.51                     
CISPEP  80 GLY N   48    CYS N   49          0         7.08                     
CISPEP  81 LYS N   54    GLN N   55          0        12.04                     
CISPEP  82 LEU N   61    SER N   62          0         3.93                     
CISPEP  83 ASP N   63    ASP N   64          0       -26.54                     
CISPEP  84 GLU N   70    GLY N   71          0        25.37                     
CISPEP  85 LYS N   74    TYR N   75          0       -22.23                     
CISPEP  86 CYS N   77    GLY N   78          0         6.10                     
CISPEP  87 SER N   79    ASN N   80          0        -1.59                     
CISPEP  88 PHE N   82    TRP N   83          0       -12.02                     
CISPEP  89 GLY 1    7    GLU 1    8          0        15.60                     
CISPEP  90 ARG 1   10    PRO 1   11          0        -5.28                     
CISPEP  91 GLY 1   16    SER 1   17          0        -3.21                     
CISPEP  92 SER 1   17    ALA 1   18          0        25.69                     
CISPEP  93 PRO 1   19    GLY 1   20          0         2.01                     
CISPEP  94 PHE 1   22    GLY 1   23          0        -2.37                     
CISPEP  95 GLY 1   23    PHE 1   24          0        -3.42                     
CISPEP  96 LEU 1   27    GLY 1   28          0        -0.88                     
CISPEP  97 ARG 1   38    TYR 1   39          0       -22.80                     
CISPEP  98 TRP 1   68    VAL 1   69          0        -9.10                     
CISPEP  99 GLN 1   81    ALA 1   82          0        -2.30                     
CISPEP 100 ALA 1   82    THR 1   83          0       -25.90                     
CISPEP 101 TYR 1   84    LEU 1   85          0       -28.53                     
CISPEP 102 GLY 1   86    ASN 1   87          0       -20.53                     
CISPEP 103 ASN 1   87    PRO 1   88          0       -23.28                     
CISPEP 104 TRP 1   91    GLY 1   92          0        20.25                     
CISPEP 105 PRO 1  118    GLU 1  119          0         4.30                     
CISPEP 106 LEU 1  181    ALA 1  182          0         1.91                     
CISPEP 107 ASP 1  183    PRO 1  184          0        -0.79                     
CISPEP 108 ASN 1  188    ILE 1  189          0         6.26                     
CISPEP 109 ILE 1  189    GLY 1  190          0        13.18                     
CISPEP 110 LEU 2   19    ASP 2   20          0         8.15                     
CISPEP 111 LEU 2   32    GLY 2   33          0        22.70                     
CISPEP 112 GLY 2   33    LEU 2   34          0        22.79                     
CISPEP 113 THR 2   93    LEU 2   94          0       -27.51                     
CISPEP 114 LEU 2  114    ASN 2  115          0       -21.28                     
CISPEP 115 PRO 2  145    LEU 2  146          0         9.93                     
CISPEP 116 SER 2  152    PRO 2  153          0       -28.37                     
CISPEP 117 PRO 2  153    GLN 2  154          0        22.74                     
CISPEP 118 THR 2  186    GLY 2  187          0        -2.21                     
CISPEP 119 ILE 2  189    ASP 2  190          0        10.41                     
CISPEP 120 ASN 2  191    LEU 2  192          0        11.03                     
CISPEP 121 LEU 2  192    PHE 2  193          0        27.48                     
CISPEP 122 ALA 2  194    HIS 2  195          0       -29.44                     
CISPEP 123 TRP 3   54    LEU 3   55          0        12.30                     
CISPEP 124 LEU 3   55    ALA 3   56          0        -6.79                     
CISPEP 125 ILE 3   78    LEU 3   79          0        20.44                     
CISPEP 126 LYS 3   81    ALA 3   82          0         6.65                     
CISPEP 127 GLY 3   83    LEU 3   84          0        -1.40                     
CISPEP 128 LEU 3   84    ILE 3   85          0        18.57                     
CISPEP 129 GLY 3  140    LYS 3  141          0        29.25                     
CISPEP 130 PRO 3  209    TYR 3  210          0       -17.99                     
CISPEP 131 ASN 3  212    LEU 3  213          0       -20.98                     
CISPEP 132 LEU 3  217    ALA 3  218          0         5.08                     
CISPEP 133 ALA 4   77    ALA 4   78          0         4.61                     
CISPEP 134 ALA 4   85    SER 4   86          0       -10.67                     
CISPEP 135 PRO 4  112    GLY 4  113          0       -19.78                     
CISPEP 136 ASN 4  116    GLN 4  117          0       -22.98                     
CISPEP 137 ILE 4  120    PHE 4  121          0        14.92                     
CISPEP 138 TYR 4  124    SER 4  125          0        24.62                     
CISPEP 139 SER 4  125    LEU 4  126          0       -21.59                     
SITE     1 AC1  3 ILE A  54  HIS A  58  PRO J  12                               
SITE     1 AC2  1 HIS A  62                                                     
SITE     1 AC3 17 HIS A  62  PHE A  64  VAL A  78  ALA A  81                    
SITE     2 AC3 17 HIS A  82  GLN A  85  LEU A  86  TRP A 354                    
SITE     3 AC3 17 HIS A 355  LEU A 358  ASN A 361  LEU A 362                    
SITE     4 AC3 17 LEU A 365  CLA A1104  CLA A1111  CLA A1123                    
SITE     5 AC3 17 CLA A1128                                                     
SITE     1 AC4  4 GLN A  85  ILE A  89  CLA A1103  CLA A1128                    
SITE     1 AC5  5 SER A  94  PHE A  98  HIS A  99  CLA A1106                    
SITE     2 AC5  5 CLA A1107                                                     
SITE     1 AC6  7 ALA A 120  ILE A 145  THR A 146  TYR A 675                    
SITE     2 AC6  7 CLA A1105  CLA A1107  CLA A1126                               
SITE     1 AC7  8 GLN A 121  TRP A 124  GLN A 129  LEU A 132                    
SITE     2 AC7  8 CLA A1105  CLA A1106  PHE B 446  ILE J  27                    
SITE     1 AC8 10 ASN A 204  HIS A 205  LEU A 311  ILE A 312                    
SITE     2 AC8 10 GLY A 314  HIS A 315  TYR A 317  THR A 319                    
SITE     3 AC8 10 ILE A 323  CLA A1110                                          
SITE     1 AC9  6 GLN A  33  LYS A  77  SER A  80  ALA A  81                    
SITE     2 AC9  6 TYR A 186  HIS A 187                                          
SITE     1 BC1  2 CLA A1108  CLA A1146                                          
SITE     1 BC2  4 MET A 202  LEU A 210  CLA A1103  CLA A1123                    
SITE     1 BC3  9 LEU A 216  ALA A 219  GLY A 220  HIS A 224                    
SITE     2 BC3  9 ILE A 249  LEU A 250  ARG A 252  ALA A 263                    
SITE     3 BC3  9 TYR A 277                                                     
SITE     1 BC4  5 TRP A 274  ALA A 278  LEU A 281  ALA A 305                    
SITE     2 BC4  5 CLA K1141                                                     
SITE     1 BC5  5 PHE A 283  ASP A 298  HIS A 302  HIS A 375                    
SITE     2 BC5  5 CLA A1117                                                     
SITE     1 BC6  2 HIS A 302  CLA A1116                                          
SITE     1 BC7  1 TRP A 195                                                     
SITE     1 BC8  5 LEU A 203  MET A 316  TYR A 317  CLA A1122                    
SITE     2 BC8  5 CLA A1123                                                     
SITE     1 BC9  1 HIS A 325                                                     
SITE     1 CC1  8 LEU A 331  HIS A 334  HIS A 343  LEU A 346                    
SITE     2 CC1  8 LEU A 431  CLA A1119  CLA A1123  CLA A1129                    
SITE     1 CC2 12 VAL A 199  MET A 202  LEU A 203  HIS A 206                    
SITE     2 CC2 12 ILE A 360  ASN A 361  MET A 364  LEU A 365                    
SITE     3 CC2 12 CLA A1103  CLA A1111  CLA A1119  CLA A1122                    
SITE     1 CC3  4 ILE A 370  ILE A 407  CLA A1135  CLA A1137                    
SITE     1 CC4 13 TRP A  92  THR A 146  SER A 147  SER A 394                    
SITE     2 CC4 13 THR A 397  HIS A 398  TRP A 401  ILE A 402                    
SITE     3 CC4 13 ILE A 743  TRP A 747  PHE A 750  CLA A1106                    
SITE     4 CC4 13 BCR A6011                                                     
SITE     1 CC5  6 THR A 369  VAL A 372  MET A 376  HIS A 398                    
SITE     2 CC5  6 HIS A 399  ILE A 402                                          
SITE     1 CC6 13 HIS A  58  ALA A  59  ASP A  60  HIS A  62                    
SITE     2 CC6 13 ASP A  63  LEU A 358  GLY A 409  ARG A 420                    
SITE     3 CC6 13 PHE A 577  TRP A 595  CLA A1103  CLA A1104                    
SITE     4 CC6 13 CLA A1140                                                     
SITE     1 CC7 11 PHE A 338  LEU A 431  ARG A 434  HIS A 438                    
SITE     2 CC7 11 ILE A 442  HIS A 445  CLA A1122  CLA A1137                    
SITE     3 CC7 11 THR L  25  PRO L  26  CLA L1130                               
SITE     1 CC8 10 HIS A 445  TRP A 448  CLA A1129  CLA A1137                    
SITE     2 CC8 10 PRO B 686  LEU L  23  THR L  25  VAL L  27                    
SITE     3 CC8 10 LEU L  37  CLA L1504                                          
SITE     1 CC9 10 TRP A 448  ILE A 451  PHE A 452  PHE A 455                    
SITE     2 CC9 10 HIS A 456  CLA A1132  CLA A1136  CLA B1237                    
SITE     3 CC9 10 PRO L  67  BCR L6020                                          
SITE     1 DC1 10 HIS A 456  GLY A 459  LEU A 460  ILE A 462                    
SITE     2 DC1 10 HIS A 463  MET A 467  CLA A1131  CLA B1207                    
SITE     3 DC1 10 ALA L  71  GLY L  72                                          
SITE     1 DC2  2 HIS A 496  CLA A1134                                          
SITE     1 DC3  3 ALA A 504  PRO A 505  CLA A1133                               
SITE     1 DC4 13 ILE A 370  GLN A 374  TYR A 377  PHE A 396                    
SITE     2 DC4 13 TRP A 491  GLN A 493  HIS A 496  ILE A 532                    
SITE     3 DC4 13 HIS A 542  PHE A 616  CLA A1124  CLA A1136                    
SITE     4 DC4 13 CLA A1137                                                     
SITE     1 DC5 10 PHE A 452  LEU A 453  PHE A 488  ASP A 538                    
SITE     2 DC5 10 HIS A 543  ALA A 546  CLA A1131  CLA A1135                    
SITE     3 DC5 10 CLA A1137  CLA L1504                                          
SITE     1 DC6  8 LEU A 446  ILE A 549  HIS A 550  CLA A1124                    
SITE     2 DC6  8 CLA A1129  CLA A1135  CLA A1136  CLA L1130                    
SITE     1 DC7 11 ILE A 707  ALA A 710  PQN A5001  SER B 420                    
SITE     2 DC7 11 SER B 423  TRP B 424  LEU B 427  CLA B1228                    
SITE     3 DC7 11 CLA B1229  CLA F1139  CLA F1240                               
SITE     1 DC8 11 THR A  51  TRP A  55  ILE A 704  HIS A 711                    
SITE     2 DC8 11 PRO A 722  PQN A5001  CLA B1138  TYR F 104                    
SITE     3 DC8 11 LEU F 105  GLU F 118  ILE F 119                               
SITE     1 DC9 12 TRP A  55  PHE A 684  VAL A 685  PHE A 688                    
SITE     2 DC9 12 PHE A 692  LEU A 725  ALA A 732  VAL A 733                    
SITE     3 DC9 12 THR A 736  HIS A 737  CLA A1128  PQN A5001                    
SITE     1 EC1  5 CLA A1115  UNK K  13  UNK K  14  UNK K  17                    
SITE     2 EC1  5 UNK K  18                                                     
SITE     1 EC2  2 PHE A 269  PHE A 270                                          
SITE     1 EC3  3 LEU A 210  LEU A 213  CLA A1110                               
SITE     1 EC4  2 CYS A 166  HIS A 246                                          
SITE     1 EC5  4 SER A 217  TRP A 218  HIS A 221  VAL A 225                    
SITE     1 EC6  1 UNK K  71                                                     
SITE     1 EC7 14 LEU A 653  LEU A 657  CLA A9011  LEU B 624                    
SITE     2 EC7 14 PHE B 650  HIS B 654  TRP B 657  TYR B 717                    
SITE     3 EC7 14 PHE B 719  THR B 720  TYR B 721  PHE B 724                    
SITE     4 EC7 14 CLA B9012  CLA B9022                                          
SITE     1 EC8 16 TYR A 606  ASN A 607  SER A 610  TRP A 652                    
SITE     2 EC8 16 ALA A 661  ILE A 665  HIS A 683  TRP A 686                    
SITE     3 EC8 16 TYR A 738  GLY A 742  THR A 745  THR A 746                    
SITE     4 EC8 16 PHE A 749  LEU B 624  CLA B9010  CLA B9012                    
SITE     1 EC9 13 LEU A 677  LEU A 680  GLY A 681  PHE A 684                    
SITE     2 EC9 13 BCR A6011  CLA A9011  CLA A9013  LEU B 434                    
SITE     3 EC9 13 TRP B 582  ASN B 585  TRP B 589  LEU B 616                    
SITE     4 EC9 13 CLA B9010                                                     
SITE     1 FC1 12 PHE A 684  ALA A 687  PHE A 688  LEU A 690                    
SITE     2 FC1 12 MET A 691  PHE A 694  TRP A 700  LEU B 427                    
SITE     3 FC1 12 GLY B 430  PHE B 581  TRP B 582  CLA B9012                    
SITE     1 FC2 14 PHE A 458  ILE A 462  TRP A 604  ASN A 607                    
SITE     2 FC2 14 ILE A 649  TYR A 738  TRP B 648  LEU B 651                    
SITE     3 FC2 14 PHE B 652  HIS B 654  LEU B 655  ALA B 658                    
SITE     4 FC2 14 CLA B9010  CLA B9023                                          
SITE     1 FC3 16 ASN A 447  CYS A 450  PHE A 455  ILE A 555                    
SITE     2 FC3 16 LEU A 600  PHE A 603  TRP A 604  LEU B 655                    
SITE     3 FC3 16 THR B 659  PHE B 661  MET B 662  TYR B 670                    
SITE     4 FC3 16 LEU B 674  CLA B1239  BCR B6017  CLA B9022                    
SITE     1 FC4  3 ILE B  25  HIS B  29  CLA B1203                               
SITE     1 FC5 13 HIS B  29  ILE B  46  GLN B  53  LEU B  54                    
SITE     2 FC5 13 ILE B 330  HIS B 331  GLN B 333  LEU B 334                    
SITE     3 FC5 13 ALA B 337  LEU B 341  CLA B1203  CLA B1210                    
SITE     4 FC5 13 CLA B1221                                                     
SITE     1 FC6  6 ILE B  57  TRP B  60  CLA B1201  CLA B1202                    
SITE     2 FC6  6 CLA B1225  CLA B1226                                          
SITE     1 FC7  9 LEU B  59  PHE B  66  TRP B  70  ALA B  90                    
SITE     2 FC7  9 CLA B1205  PRO I   5  PHE I   8  VAL I  12                    
SITE     3 FC7  9 BCR I6018                                                     
SITE     1 FC8 12 ALA B  88  HIS B  89  ASN B 114  ASN B 115                    
SITE     2 FC8 12 ALA B 116  TYR B 117  SER B 118  TRP B 646                    
SITE     3 FC8 12 MET B 649  CLA B1224  BCR B6017  CLA I1204                    
SITE     1 FC9  8 THR A 466  LEU A 470  ASP B  93  HIS B  95                    
SITE     2 FC9  8 PHE B  96  VAL B 645  TRP B 648  BCR B6017                    
SITE     1 GC1 14 CLA A1132  PRO B  94  HIS B  95  GLY H  61                    
SITE     2 GC1 14 LEU H  65  VAL I   9  GLY I  13  LEU I  14                    
SITE     3 GC1 14 BCR I6018  PRO L  73  ALA L  87  GLY L  90                    
SITE     4 GC1 14 LEU L  91  BCR L6020                                          
SITE     1 GC2  8 LEU B 151  HIS B 156  TRP B 161  LYS B 162                    
SITE     2 GC2  8 TRP B 167  CLA B1209  CLA B1210  ASN G  39                    
SITE     1 GC3 12 TRP B 167  ASN B 170  SER B 173  HIS B 177                    
SITE     2 GC3 12 THR B 293  ASN B 294  CLA B1208  CLA B1210                    
SITE     3 GC3 12 CLA B1217  GLN G  38  ASN G  39  MET G  41                    
SITE     1 GC4  8 HIS B  50  ARG B 174  HIS B 178  LEU B 182                    
SITE     2 GC4  8 CLA B1202  CLA B1208  CLA B1209  CLA B1241                    
SITE     1 GC5  7 ALA B 189  TRP B 190  HIS B 193  HIS B 196                    
SITE     2 GC5  7 VAL B 197  ARG B 208  PHE B 212                               
SITE     1 GC6  7 HIS B 196  PHE B 212  LEU B 213  LEU B 222                    
SITE     2 GC6  7 LEU B 225  ILE B 254  LEU B 255                               
SITE     1 GC7  7 ASN B 231  LEU B 255  HIS B 275  LEU B 278                    
SITE     2 GC7  7 ALA B 279  TRP B 493  CLA B1214                               
SITE     1 GC8 11 ILE B 257  VAL B 273  HIS B 275  HIS B 276                    
SITE     2 GC8 11 ALA B 279  ILE B 280  HIS B 351  LEU B 355                    
SITE     3 GC8 11 CLA B1213  CLA B1223  CLA B1231                               
SITE     1 GC9 14 TRP B 123  THR B 126  ILE B 127  SER B 186                    
SITE     2 GC9 14 TRP B 190  LEU B 194  VAL B 273  HIS B 276                    
SITE     3 GC9 14 HIS B 277  ILE B 280  LEU B 347  VAL B 348                    
SITE     4 GC9 14 MET B 352  CLA B1225                                          
SITE     1 HC1 11 PHE B 183  LEU B 283  PHE B 284  ILE B 286                    
SITE     2 HC1 11 MET B 290  TYR B 291  ILE B 304  CLA B1218                    
SITE     3 HC1 11 CLA B1220  CLA B1221  CLA B1242                               
SITE     1 HC2  7 HIS B 177  LEU B 289  THR B 293  PHE B 295                    
SITE     2 HC2  7 CLA B1209  LEU G  18  PHE G  21                               
SITE     1 HC3 10 CLA 11012  ILE B 286  GLY B 287  LEU B 289                    
SITE     2 HC3 10 MET B 290  TYR B 291  ILE B 297  HIS B 299                    
SITE     3 HC3 10 CLA B1216  CLA B1219                                          
SITE     1 HC4  7 HIS B 299  TYR B 303  HIS B 308  PRO B 310                    
SITE     2 HC4  7 PRO B 311  CLA B1218  CLA B1220                               
SITE     1 HC5 11 ILE B 304  HIS B 308  PRO B 310  PRO B 311                    
SITE     2 HC5 11 VAL B 407  LEU B 408  CLA B1216  CLA B1219                    
SITE     3 HC5 11 CLA B1221  CLA B1227  CLA B1242                               
SITE     1 HC6 10 ALA B 171  ARG B 174  LEU B 175  HIS B 178                    
SITE     2 HC6 10 PHE B 183  ILE B 326  ASN B 327  CLA B1202                    
SITE     3 HC6 10 CLA B1216  CLA B1220                                          
SITE     1 HC7  9 SER B 346  LEU B 347  GLN B 350  GLN B 376                    
SITE     2 HC7  9 THR B 530  THR B 531  CLA B1234  CLA B1235                    
SITE     3 HC7  9 CLA B1236                                                     
SITE     1 HC8  6 GLN B 350  HIS B 351  SER B 354  LEU B 355                    
SITE     2 HC8  6 CLA B1214  CLA B1231                                          
SITE     1 HC9 12 TRP B  60  TYR B 117  SER B 118  ALA B 370                    
SITE     2 HC9 12 HIS B 374  ILE B 378  ILE B 718  PHE B 719                    
SITE     3 HC9 12 ALA B 722  ILE B 726  CLA B1205  CLA B1225                    
SITE     1 IC1 16 VAL B 120  TRP B 123  LEU B 341  ILE B 344                    
SITE     2 IC1 16 THR B 345  VAL B 348  MET B 352  TYR B 358                    
SITE     3 IC1 16 LEU B 371  HIS B 374  HIS B 375  ILE B 378                    
SITE     4 IC1 16 ILE B 382  CLA B1203  CLA B1215  CLA B1224                    
SITE     1 IC2  7 LEU B 334  LEU B 338  PHE B 381  GLY B 385                    
SITE     2 IC2  7 HIS B 389  PHE B 576  CLA B1203                               
SITE     1 IC3  7 ARG B 317  ARG B 410  MET B 411  HIS B 414                    
SITE     2 IC3  7 CLA B1220  CLA B1228  CLA B1242                               
SITE     1 IC4  7 TRP A 709  HIS B 421  TRP B 424  CLA B1138                    
SITE     2 IC4  7 CLA B1227  CLA B1236  BCR F6016                               
SITE     1 IC5 11 TRP B 424  LEU B 427  PHE B 428  PHE B 431                    
SITE     2 IC5 11 HIS B 432  CLA B1138  CLA B1230  PHE F  90                    
SITE     3 IC5 11 ALA F  94  GLY F  95  GLY F  98                               
SITE     1 IC6  4 GLY B 435  VAL B 438  HIS B 439  CLA B1229                    
SITE     1 IC7  7 ILE B 463  HIS B 467  PHE B 509  CLA B1214                    
SITE     2 IC7  7 CLA B1223  CLA B1232  CLA B1234                               
SITE     1 IC8  8 PRO B 484  ALA B 485  ASN B 487  ALA B 488                    
SITE     2 IC8  8 GLY B 489  TRP B 493  CLA B1231  CLA G1233                    
SITE     1 IC9  4 ALA B 488  CLA B1232  PRO G   4  SER G   5                    
SITE     1 JC1 17 TYR B 353  PHE B 459  ALA B 460  ILE B 463                    
SITE     2 JC1 17 GLN B 464  HIS B 467  PHE B 509  LEU B 510                    
SITE     3 JC1 17 ILE B 512  HIS B 520  VAL B 590  TYR B 593                    
SITE     4 JC1 17 TRP B 594  CLA B1222  CLA B1231  CLA B1235                    
SITE     5 JC1 17 CLA B1236                                                     
SITE     1 JC2 14 LEU B 429  PRO B 457  ILE B 458  PHE B 459                    
SITE     2 JC2 14 ALA B 460  PHE B 517  HIS B 521  ALA B 524                    
SITE     3 JC2 14 HIS B 528  CLA B1222  CLA B1234  CLA B1236                    
SITE     4 JC2 14 PHE F  83  CLA F1302                                          
SITE     1 JC3 10 ILE B 418  HIS B 421  LEU B 422  ALA B 524                    
SITE     2 JC3 10 LEU B 527  HIS B 528  CLA B1222  CLA B1228                    
SITE     3 JC3 10 CLA B1234  CLA B1235                                          
SITE     1 JC4  9 SER A 444  ASN A 447  ILE A 451  CLA A1131                    
SITE     2 JC4  9 LEU B 678  HIS B 682  CLA B1238  BCR B6017                    
SITE     3 JC4  9 BCR L6020                                                     
SITE     1 JC5 12 THR B  18  TRP B  22  ALA B 679  HIS B 682                    
SITE     2 JC5 12 TRP B 693  ARG B 694  PRO B 697  VAL B 698                    
SITE     3 JC5 12 CLA B1237  MET I  21  PHE I  25  TYR L 102                    
SITE     1 JC6 12 PHE B 652  LEU B 655  VAL B 656  PHE B 663                    
SITE     2 JC6 12 VAL B 708  VAL B 711  HIS B 712  PQN B5002                    
SITE     3 JC6 12 BCR B6017  CLA B9023  MET I  21  BCR I6018                    
SITE     1 JC7  3 CLA B1138  ILE F  93  ILE F  97                               
SITE     1 JC8  4 ILE B  57  PHE B  58  LEU B 182  CLA B1210                    
SITE     1 JC9  6 SER B 340  PHE B 387  MET B 411  CLA B1216                    
SITE     2 JC9  6 CLA B1220  CLA B1227                                          
SITE     1 KC1  4 PRO B 310  PRO B 311  GLY B 312  ARG B 314                    
SITE     1 KC2  9 GLY 1 190  ASP 1 191  PHE B 459  CLA B1235                    
SITE     2 KC2  9 GLY F  75  GLN F  77  TRP F  80  CLA F1303                    
SITE     3 KC2  9 BCR F6016                                                     
SITE     1 KC3  2 CLA F1302  BCR F6016                                          
SITE     1 KC4  3 ILE 4 103  TRP 4 106  CLA 44012                               
SITE     1 KC5  1 TRP F  80                                                     
SITE     1 KC6  1 CLA 44005                                                     
SITE     1 KC7  1 CLA F4015                                                     
SITE     1 KC8  1 SER J  21                                                     
SITE     1 KC9  2 ARG G  28  PRO G  63                                          
SITE     1 LC1  2 PHE F 134  CLA J1307                                          
SITE     1 LC2 13 ASN H  33  SER H  34  GLN H  36  CLA H1505                    
SITE     2 LC2 13 TRP L  35  TYR L  36  LEU L  40  GLU L  55                    
SITE     3 LC2 13 LEU L  58  ALA L  59  TRP L 153  CLA L1502                    
SITE     4 LC2 13 CLA L1504                                                     
SITE     1 LC3 13 LEU B 687  ALA B 688  CLA H1501  TYR L  36                    
SITE     2 LC3 13 LEU L  40  GLU L  55  VAL L  56  ALA L  59                    
SITE     3 LC3 13 HIS L  60  LEU L  63  LEU L  64  CLA L1504                    
SITE     4 LC3 13 BCR L6020                                                     
SITE     1 LC4  6 VAL L  65  GLY L  66  PRO L  67  LEU L 161                    
SITE     2 LC4  6 PRO L 164  TYR L 165                                          
SITE     1 LC5  6 CLA A1136  CLA H1501  LEU L  32  TYR L  36                    
SITE     2 LC5  6 CLA L1130  CLA L1502                                          
SITE     1 LC6  3 LEU H  35  GLN H  36  CLA H1501                               
SITE     1 LC7  3 CLA 22005  GLU J  28  ARG J  31                               
SITE     1 LC8  3 HIS 1  46  ARG 1 152  CLA 41009                               
SITE     1 LC9  3 SER 1  42  TRP 1  49  CLA 11012                               
SITE     1 MC1  6 ALA 1  53  GLY 1  56  ILE 1  57  VAL 1  59                    
SITE     2 MC1  6 PRO 1  60  CLA 11013                                          
SITE     1 MC2  1 CLA 11004                                                     
SITE     1 MC3  4 LYS 1  70  GLN 1  72  TRP 1  74  CLA 11006                    
SITE     1 MC4  1 GLU 1 109                                                     
SITE     1 MC5  4 ALA 1 106  HIS 1 110  CLA 11005  CLA B1218                    
SITE     1 MC6  1 ASN 1 150                                                     
SITE     1 MC7  6 GLY 1 160  PHE 1 161  HIS 1 180  LEU 1 181                    
SITE     2 MC7  6 ALA 1 182  CLA 11008                                          
SITE     1 MC8  2 HIS 1 180  CLA 11003                                          
SITE     1 MC9  1 CLA 22007                                                     
SITE     1 NC1  3 ASN 2 166  LEU 2 169  ALA 2 170                               
SITE     1 NC2  1 CLA J2107                                                     
SITE     1 NC3  2 GLY 2  61  ILE 2  62                                          
SITE     1 NC4  2 GLU 2  98  LEU 2  99                                          
SITE     1 NC5  2 ALA 2 105  ARG 2 109                                          
SITE     1 NC6  3 LEU 2  99  GLY 2 103  GLU 2 106                               
SITE     1 NC7  2 CLA 22002  CLA 32009                                          
SITE     1 NC8  2 ILE 2 164  CLA 22007                                          
SITE     1 NC9  5 ALA 2 177  TRP 2 178  HIS 2 181  TYR 2 183                    
SITE     2 NC9  5 CLA 22008                                                     
SITE     1 OC1  2 ALA 2 197  CLA 22003                                          
SITE     1 OC2  1 ASN B 499                                                     
SITE     1 OC3  2 VAL 3 185  LYS 3 186                                          
SITE     1 OC4  3 MET 3  67  LEU 3 196  PHE 3 199                               
SITE     1 OC5  1 CLA 33011                                                     
SITE     1 OC6  4 ALA 3  73  GLU 3  77  GLY 3  80  LYS 3  81                    
SITE     1 OC7  2 ASP 3 110  GLU 3 118                                          
SITE     1 OC8  2 VAL 3 116  MET 3 119                                          
SITE     1 OC9  3 PHE 3  65  LEU 3  68  CLA 33002                               
SITE     1 PC1  1 CLA 33012                                                     
SITE     1 PC2  3 ARG 3  64  CLA 33001  CLA 33007                               
SITE     1 PC3  1 CLA 33002                                                     
SITE     1 PC4  2 TYR 3 198  GLN 3 201                                          
SITE     1 PC5  1 LEU 4 147                                                     
SITE     1 PC6  4 GLU 4  44  ILE 4 154  ALA 4 155  ARG 4 158                    
SITE     1 PC7  4 ASN 4  47  PHE 4 164  CLA 44012  CLA F1306                    
SITE     1 PC8  3 GLY 4  57  LEU 4  60  TYR 4  76                               
SITE     1 PC9  3 LEU 4  90  PHE 4  95  CLA 44010                               
SITE     1 QC1  1 CLA 44013                                                     
SITE     1 QC2  6 GLN 4  42  ARG 4  49  ARG 4 105  ASP 4 108                    
SITE     2 QC2  6 SER 4 114  PRO 4 119                                          
SITE     1 QC3  7 ALA 4  43  VAL 4  46  TRP 4  50  GLU 4 102                    
SITE     2 QC3  7 TRP 4 106  CLA 41304  CLA 44005                               
SITE     1 QC4  4 ARG 4  49  MET 4  52  LEU 4  53  ASP 4 118                    
SITE     1 QC5  1 GLU 4 151                                                     
SITE     1 QC6  2 ASN 4 156  LEU 4 159                                          
SITE     1 QC7  3 LEU 4 162  PHE 4 167  GLN 4 170                               
SITE     1 QC8  2 HIS 4 185  ILE 4 186                                          
SITE     1 QC9  9 CYS A 581  ASP A 582  CYS A 590  CYS B 559                    
SITE     2 QC9  9 ASP B 560  GLY B 561  PRO B 562  CYS B 568                    
SITE     3 QC9  9 TRP B 667                                                     
SITE     1 RC1  9 CYS C  21  VAL C  25  CYS C  48  VAL C  49                    
SITE     2 RC1  9 GLY C  50  CYS C  51  LYS C  52  ARG C  53                    
SITE     3 RC1  9 CYS C  54                                                     
SITE     1 RC2  6 CYS C  11  ILE C  12  CYS C  17  VAL C  18                    
SITE     2 RC2  6 CYS C  58  PRO C  59                                          
SITE     1 RC3 11 TRP A  55  MET A 691  PHE A 692  SER A 695                    
SITE     2 RC3 11 GLY A 696  TRP A 700  ALA A 724  LEU A 725                    
SITE     3 RC3 11 CLA A1140  CLA B1138  CLA F1139                               
SITE     1 RC4 11 MET B 662  PHE B 663  SER B 666  TRP B 667                    
SITE     2 RC4 11 ARG B 668  TRP B 671  ALA B 699  LEU B 700                    
SITE     3 RC4 11 ALA B 705  CLA B1239  BCR B6017                               
SITE     1 RC5  6 GLY A 681  PHE A 684  ALA A 744  TRP A 747                    
SITE     2 RC5  6 CLA A1126  CLA B9012                                          
SITE     1 RC6  6 CLA B1228  GLY F  95  TRP F  99  LEU F 144                    
SITE     2 RC6  6 CLA F1302  CLA F1303                                          
SITE     1 RC7  9 TRP B 648  MET B 649  PHE B 652  CLA B1205                    
SITE     2 RC7  9 CLA B1206  CLA B1237  CLA B1239  PQN B5002                    
SITE     3 RC7  9 CLA B9023                                                     
SITE     1 RC8  6 CLA B1207  CLA B1239  VAL I  12  PHE I  16                    
SITE     2 RC8  6 CLA I1204  BCR L6020                                          
SITE     1 RC9  6 CLA A1131  CLA B1207  CLA B1237  BCR I6018                    
SITE     2 RC9  6 LEU L  91  CLA L1502                                          
CRYST1  120.054  188.784  127.518  90.00  95.19  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      0.008330  0.000000  0.000757        0.00000                         
SCALE2      0.000000  0.005297  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007874        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system