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Database: PDB
Entry: 3KDO
LinkDB: 3KDO
Original site: 3KDO 
HEADER    LYASE                                   23-OCT-09   3KDO              
TITLE     CRYSTAL STRUCTURE OF TYPE III RUBISCO SP6 MUTANT COMPLEXED WITH 2-CABP
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE;                         
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J;                                 
COMPND   4 SYNONYM: RUBISCO;                                                    
COMPND   5 EC: 4.1.1.39;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOCOCCUS KODAKARAENSIS;                     
SOURCE   3 ORGANISM_TAXID: 69014;                                               
SOURCE   4 STRAIN: KOD1;                                                        
SOURCE   5 GENE: RBCL, TK2290;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3)PLYSS;                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-21A(+)                                
KEYWDS    RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE, RUBISCO, CARBON      
KEYWDS   2 DIOXIDE FIXATION, LYASE, MAGNESIUM, METAL-BINDING, MONOOXYGENASE     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.NISHITANI,M.FUJIHASHI,T.DOI,S.YOSHIDA,H.ATOMI,T.IMANAKA,K.MIKI      
REVDAT   2   02-FEB-11 3KDO    1       JRNL                                     
REVDAT   1   06-OCT-10 3KDO    0                                                
JRNL        AUTH   Y.NISHITANI,S.YOSHIDA,M.FUJIHASHI,K.KITAGAWA,T.DOI,H.ATOMI,  
JRNL        AUTH 2 T.IMANAKA,K.MIKI                                             
JRNL        TITL   STRUCTURE-BASED CATALYTIC OPTIMIZATION OF A TYPE III RUBISCO 
JRNL        TITL 2 FROM A HYPERTHERMOPHILE                                      
JRNL        REF    J.BIOL.CHEM.                  V. 285 39339 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20926376                                                     
JRNL        DOI    10.1074/JBC.M110.147587                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.36 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0066                                      
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) : 2.36                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.46                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 236721                         
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) : 0.221                           
REMARK   3   R VALUE            (WORKING SET) : 0.219                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 12530                           
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) : 2.36                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.42                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 16970                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.49                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2890                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 864                          
REMARK   3   BIN FREE R VALUE                    : 0.3320                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 34034                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 220                                     
REMARK   3   SOLVENT ATOMS            : 1811                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.61                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.54000                                              
REMARK   3    B22 (A**2) : -2.10000                                             
REMARK   3    B33 (A**2) : 0.28000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -2.52000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.329         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.248         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.180         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.579         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.928                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.892                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 35120 ; 0.002 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 47730 ; 0.589 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4369 ; 3.968 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1587 ;26.139 ;23.459       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  5492 ;11.065 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   216 ;13.734 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  5092 ; 0.042 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 27064 ; 0.002 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 21715 ; 0.204 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 34532 ; 0.379 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 13405 ; 0.392 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 13198 ; 0.685 ; 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   : 1.20                                          
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 3KDO COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-OCT-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055861.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-JUL-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 249468                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.360                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.36                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.38900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1GEH                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M ACETATE, 90MM CACL2, 5% PEG6000,    
REMARK 280  10% MPD, PH6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K     
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      123.28650            
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: DECAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 62170 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 127180 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -398.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, B, G, C, F, D, J, E, I          
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     PHE A     5                                                      
REMARK 465     ASP A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     ILE A     8                                                      
REMARK 465     MET B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     LYS B     4                                                      
REMARK 465     PHE B     5                                                      
REMARK 465     ASP B     6                                                      
REMARK 465     MET C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     GLU C     3                                                      
REMARK 465     LYS C     4                                                      
REMARK 465     MET D     1                                                      
REMARK 465     VAL D     2                                                      
REMARK 465     GLU D     3                                                      
REMARK 465     LYS D     4                                                      
REMARK 465     PHE D     5                                                      
REMARK 465     ASP D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     MET E     1                                                      
REMARK 465     VAL E     2                                                      
REMARK 465     GLU E     3                                                      
REMARK 465     LYS E     4                                                      
REMARK 465     MET F     1                                                      
REMARK 465     VAL F     2                                                      
REMARK 465     GLU F     3                                                      
REMARK 465     LYS F     4                                                      
REMARK 465     PHE F     5                                                      
REMARK 465     ASP F     6                                                      
REMARK 465     THR F     7                                                      
REMARK 465     MET G     1                                                      
REMARK 465     VAL G     2                                                      
REMARK 465     GLU G     3                                                      
REMARK 465     LYS G     4                                                      
REMARK 465     PHE G     5                                                      
REMARK 465     ASP G     6                                                      
REMARK 465     THR G     7                                                      
REMARK 465     MET H     1                                                      
REMARK 465     VAL H     2                                                      
REMARK 465     GLU H     3                                                      
REMARK 465     LYS H     4                                                      
REMARK 465     PHE H     5                                                      
REMARK 465     ASP H     6                                                      
REMARK 465     MET I     1                                                      
REMARK 465     VAL I     2                                                      
REMARK 465     GLU I     3                                                      
REMARK 465     LYS I     4                                                      
REMARK 465     PHE I     5                                                      
REMARK 465     ASP I     6                                                      
REMARK 465     MET J     1                                                      
REMARK 465     VAL J     2                                                      
REMARK 465     GLU J     3                                                      
REMARK 465     LYS J     4                                                      
REMARK 465     PHE J     5                                                      
REMARK 465     ASP J     6                                                      
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     TYR A   9    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP A  10    CG   OD1  OD2                                       
REMARK 470     GLU A  18    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  35    CG   CD   OE1  OE2                                  
REMARK 470     THR A  38    OG1  CG2                                            
REMARK 470     ILE A  39    CG1  CG2  CD1                                       
REMARK 470     GLN A  41    CG   CD   OE1  NE2                                  
REMARK 470     THR A  57    OG1  CG2                                            
REMARK 470     LEU A  58    CG   CD1  CD2                                       
REMARK 470     TYR A  59    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A 117    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 119    CG   CD   CE   NZ                                   
REMARK 470     LYS A 148    CG   CD   CE   NZ                                   
REMARK 470     LYS A 153    CG   CD   CE   NZ                                   
REMARK 470     GLU A 203    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 326    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 328    CG   OD1  OD2                                       
REMARK 470     LYS A 343    CG   CD   CE   NZ                                   
REMARK 470     GLU A 346    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 347    CG   OD1                                            
REMARK 470     GLU A 380    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 395    CG   CD1  CD2                                       
REMARK 470     LEU A 421    CG   CD1  CD2                                       
REMARK 470     GLU A 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 426    CG   CD   CE   NZ                                   
REMARK 470     LYS A 429    CG   CD   CE   NZ                                   
REMARK 470     ARG A 433    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B   7    OG1  CG2                                            
REMARK 470     ILE B   8    CG1  CG2  CD1                                       
REMARK 470     LEU B  58    CG   CD1  CD2                                       
REMARK 470     LYS B 119    CG   CD   CE   NZ                                   
REMARK 470     GLU B 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 153    CG   CD   CE   NZ                                   
REMARK 470     GLU B 203    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 211    CG   CD   CE   NZ                                   
REMARK 470     ASP B 328    CG   OD1  OD2                                       
REMARK 470     GLU B 346    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 380    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 417    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 421    CG   CD1  CD2                                       
REMARK 470     GLU B 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 426    CG   CD   CE   NZ                                   
REMARK 470     LYS B 429    CG   CD   CE   NZ                                   
REMARK 470     ARG B 433    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 436    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 437    CG   CD   CE   NZ                                   
REMARK 470     PHE C   5    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP C   6    CG   OD1  OD2                                       
REMARK 470     ILE C   8    CG1  CG2  CD1                                       
REMARK 470     GLU C  65    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 148    CG   CD   CE   NZ                                   
REMARK 470     LYS C 153    CG   CD   CE   NZ                                   
REMARK 470     LYS C 175    CG   CD   CE   NZ                                   
REMARK 470     GLU C 203    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 211    CG   CD   CE   NZ                                   
REMARK 470     ASP C 328    CG   OD1  OD2                                       
REMARK 470     GLU C 380    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 417    CG   CD   OE1  NE2                                  
REMARK 470     LEU C 421    CG   CD1  CD2                                       
REMARK 470     GLU C 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 426    CG   CD   CE   NZ                                   
REMARK 470     LYS C 429    CG   CD   CE   NZ                                   
REMARK 470     ILE D   8    CG1  CG2  CD1                                       
REMARK 470     GLU D  18    CG   CD   OE1  OE2                                  
REMARK 470     THR D  54    OG1  CG2                                            
REMARK 470     THR D  57    OG1  CG2                                            
REMARK 470     LEU D  58    CG   CD1  CD2                                       
REMARK 470     TYR D  59    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS D 153    CG   CD   CE   NZ                                   
REMARK 470     GLU D 346    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 429    CG   CD   CE   NZ                                   
REMARK 470     PHE E   5    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP E   6    CG   OD1  OD2                                       
REMARK 470     GLU E  65    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 144    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 326    CG   CD   OE1  OE2                                  
REMARK 470     ASP E 328    CG   OD1  OD2                                       
REMARK 470     LYS E 343    CG   CD   CE   NZ                                   
REMARK 470     GLN E 376    CG   CD   OE1  NE2                                  
REMARK 470     GLU E 380    CG   CD   OE1  OE2                                  
REMARK 470     GLN E 417    CG   CD   OE1  NE2                                  
REMARK 470     LEU E 421    CG   CD1  CD2                                       
REMARK 470     GLU E 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 426    CG   CD   CE   NZ                                   
REMARK 470     LYS E 429    CG   CD   CE   NZ                                   
REMARK 470     LEU E 431    CG   CD1  CD2                                       
REMARK 470     GLU E 436    CG   CD   OE1  OE2                                  
REMARK 470     THR E 442    OG1  CG2                                            
REMARK 470     ILE F   8    CG1  CG2  CD1                                       
REMARK 470     ASP F  10    CG   OD1  OD2                                       
REMARK 470     GLU F  18    CG   CD   OE1  OE2                                  
REMARK 470     LEU F  58    CG   CD1  CD2                                       
REMARK 470     LYS F  73    CG   CD   CE   NZ                                   
REMARK 470     LYS F 153    CG   CD   CE   NZ                                   
REMARK 470     GLU F 203    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 346    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 380    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS F 429    CG   CD   CE   NZ                                   
REMARK 470     ILE G   8    CG1  CG2  CD1                                       
REMARK 470     LYS G  15    CG   CD   CE   NZ                                   
REMARK 470     LEU G  58    CG   CD1  CD2                                       
REMARK 470     GLU G 144    CG   CD   OE1  OE2                                  
REMARK 470     GLU G 203    CG   CD   OE1  OE2                                  
REMARK 470     ASP G 328    CG   OD1  OD2                                       
REMARK 470     GLU G 346    CG   CD   OE1  OE2                                  
REMARK 470     GLU G 380    CG   CD   OE1  OE2                                  
REMARK 470     LYS G 429    CG   CD   CE   NZ                                   
REMARK 470     GLU H  65    CG   CD   OE1  OE2                                  
REMARK 470     GLU H 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 148    CG   CD   CE   NZ                                   
REMARK 470     LYS H 153    CG   CD   CE   NZ                                   
REMARK 470     GLU H 203    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 322    CG   CD   CE   NZ                                   
REMARK 470     GLU H 324    CG   CD   OE1  OE2                                  
REMARK 470     GLU H 326    CG   CD   OE1  OE2                                  
REMARK 470     ASP H 328    CG   OD1  OD2                                       
REMARK 470     GLU H 346    CG   CD   OE1  OE2                                  
REMARK 470     ASN H 347    CG   OD1                                            
REMARK 470     GLN H 376    CG   CD   OE1  NE2                                  
REMARK 470     GLU H 380    CG   CD   OE1  OE2                                  
REMARK 470     GLN H 417    CG   CD   OE1  NE2                                  
REMARK 470     LEU H 421    CG   CD1  CD2                                       
REMARK 470     GLU H 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 426    CG   CD   CE   NZ                                   
REMARK 470     LYS H 429    CG   CD   CE   NZ                                   
REMARK 470     ARG H 433    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU H 436    CG   CD   OE1  OE2                                  
REMARK 470     VAL H 444    CG1  CG2                                            
REMARK 470     THR I   7    OG1  CG2                                            
REMARK 470     ILE I   8    CG1  CG2  CD1                                       
REMARK 470     GLU I  49    CG   CD   OE1  OE2                                  
REMARK 470     THR I  54    OG1  CG2                                            
REMARK 470     LEU I  58    CG   CD1  CD2                                       
REMARK 470     TYR I  59    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU I  65    CG   CD   OE1  OE2                                  
REMARK 470     GLU I 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS I 153    CG   CD   CE   NZ                                   
REMARK 470     GLU I 326    CG   CD   OE1  OE2                                  
REMARK 470     LYS I 343    CG   CD   CE   NZ                                   
REMARK 470     GLU I 346    CG   CD   OE1  OE2                                  
REMARK 470     GLU I 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS I 429    CG   CD   CE   NZ                                   
REMARK 470     ILE J   8    CG1  CG2  CD1                                       
REMARK 470     GLU J 144    CG   CD   OE1  OE2                                  
REMARK 470     GLU J 326    CG   CD   OE1  OE2                                  
REMARK 470     GLU J 346    CG   CD   OE1  OE2                                  
REMARK 470     GLN J 376    CG   CD   OE1  NE2                                  
REMARK 470     GLU J 380    CG   CD   OE1  OE2                                  
REMARK 470     GLN J 417    CG   CD   OE1  NE2                                  
REMARK 470     LEU J 421    CG   CD1  CD2                                       
REMARK 470     GLU J 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS J 426    CG   CD   CE   NZ                                   
REMARK 470     LYS J 429    CG   CD   CE   NZ                                   
REMARK 470     GLU J 436    CG   CD   OE1  OE2                                  
REMARK 470     VAL J 441    CG1  CG2                                            
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    ASP A  14       88.15   -150.69                                   
REMARK 500    ALA A  34     -163.04    -64.15                                   
REMARK 500    SER A  51      -98.96   -152.87                                   
REMARK 500    ASP A  82        9.05   -168.78                                   
REMARK 500    ALA A 109       37.73   -144.96                                   
REMARK 500    ARG A 117       -6.75    -49.54                                   
REMARK 500    ASP A 154      -63.42   -109.52                                   
REMARK 500    LEU A 180      -73.49    -58.87                                   
REMARK 500    THR A 195     -107.24   -110.57                                   
REMARK 500    ASN A 200       84.24   -166.87                                   
REMARK 500    THR A 231      121.90    -37.75                                   
REMARK 500    ALA A 232     -167.73    179.45                                   
REMARK 500    ALA A 283      123.29    -38.20                                   
REMARK 500    MET A 284       -9.50     97.82                                   
REMARK 500    ALA A 286       -8.58    -49.76                                   
REMARK 500    PHE A 288       -1.14   -142.90                                   
REMARK 500    PRO A 344     -171.86    -61.83                                   
REMARK 500    TYR A 357     -107.70     55.78                                   
REMARK 500    PRO A 372       -9.23    -56.32                                   
REMARK 500    GLN A 376      -59.97    -28.01                                   
REMARK 500    ASP B  14       89.94   -153.20                                   
REMARK 500    SER B  51      -90.24   -140.66                                   
REMARK 500    ALA B 109       34.59   -151.79                                   
REMARK 500    ASP B 154      -35.47   -135.35                                   
REMARK 500    THR B 195     -107.12   -100.18                                   
REMARK 500    ASN B 200       81.31   -164.28                                   
REMARK 500    THR B 231      122.20    -39.73                                   
REMARK 500    ALA B 232     -171.45    179.55                                   
REMARK 500    MET B 284      -16.33     95.10                                   
REMARK 500    PHE B 288       -3.58   -140.19                                   
REMARK 500    TYR B 357     -121.90     52.84                                   
REMARK 500    ASN B 374       18.51   -161.67                                   
REMARK 500    PRO B 420      158.55    -41.99                                   
REMARK 500    LEU B 421       22.04    -74.70                                   
REMARK 500    ASP B 422      -59.03   -122.47                                   
REMARK 500    LYS B 429      -82.18    -55.74                                   
REMARK 500    GLU B 430      -58.08    -25.57                                   
REMARK 500    HIS B 440       18.63   -143.52                                   
REMARK 500    SER C  51      -90.47   -136.81                                   
REMARK 500    THR C 195     -108.93   -113.17                                   
REMARK 500    ASN C 200       88.11   -157.86                                   
REMARK 500    ALA C 232     -171.93   -179.10                                   
REMARK 500    MET C 284      -16.32     92.83                                   
REMARK 500    ARG C 327      -74.15    -53.17                                   
REMARK 500    TYR C 357     -119.16     50.80                                   
REMARK 500    SER D  51      -98.09   -127.22                                   
REMARK 500    ALA D 109       37.47   -157.63                                   
REMARK 500    THR D 195     -106.71   -120.66                                   
REMARK 500    ASN D 200       84.62   -162.81                                   
REMARK 500    ALA D 232     -168.40   -178.98                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     124 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              MG A 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX A 189   OQ2                                                    
REMARK 620 2 ASP A 191   OD1  82.8                                              
REMARK 620 3 GLU A 192   OE1  88.0  83.6                                        
REMARK 620 4 CAP A 600   O2   87.9 111.3 163.9                                  
REMARK 620 5 CAP A 600   O3   86.1 165.7  87.0  77.1                            
REMARK 620 6 CAP A 600   O7  164.5 103.3 106.8  76.5  89.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX B 189   OQ2                                                    
REMARK 620 2 ASP B 191   OD1  88.6                                              
REMARK 620 3 GLU B 192   OE1  82.3  74.5                                        
REMARK 620 4 CAP B 600   O2   98.0 120.0 165.4                                  
REMARK 620 5 CAP B 600   O3   83.7 154.1  80.0  85.5                            
REMARK 620 6 CAP B 600   O7  175.5  90.7  93.2  86.3  95.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX C 189   OQ2                                                    
REMARK 620 2 ASP C 191   OD2 112.8                                              
REMARK 620 3 GLU C 192   OE1  84.1 127.0                                        
REMARK 620 4 CAP C 600   O2   84.7  88.0 144.9                                  
REMARK 620 5 CAP C 600   O7  142.6 100.9  88.5  80.7                            
REMARK 620 6 CAP C 600   O3   64.9 158.6  74.4  70.7  77.8                      
REMARK 620 7 ASP C 191   OD1 125.8  47.8  80.9 131.6  88.7 152.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX D 189   OQ2                                                    
REMARK 620 2 ASP D 191   OD1  89.8                                              
REMARK 620 3 GLU D 192   OE1  89.4  93.5                                        
REMARK 620 4 CAP D 600   O2   86.6 108.7 157.4                                  
REMARK 620 5 CAP D 600   O3   77.6 167.1  83.5  73.9                            
REMARK 620 6 CAP D 600   O7  162.5 102.7 101.7  77.9  90.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX E 189   OQ2                                                    
REMARK 620 2 ASP E 191   OD1  81.4                                              
REMARK 620 3 GLU E 192   OE1  75.2  71.3                                        
REMARK 620 4 CAP E 600   O2   89.7 120.7 159.6                                  
REMARK 620 5 CAP E 600   O3   75.8 152.7  88.4  74.4                            
REMARK 620 6 CAP E 600   O6  168.8 101.2 115.9  79.6 104.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX F 189   OQ2                                                    
REMARK 620 2 ASP F 191   OD1  84.6                                              
REMARK 620 3 GLU F 192   OE1  86.5  78.8                                        
REMARK 620 4 CAP F 600   O2   94.6 110.5 170.7                                  
REMARK 620 5 CAP F 600   O3   88.2 168.5  91.7  79.1                            
REMARK 620 6 CAP F 600   O7  174.3  93.4  98.4  81.1  94.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX G 189   OQ2                                                    
REMARK 620 2 ASP G 191   OD1  86.1                                              
REMARK 620 3 GLU G 192   OE1  87.4  84.9                                        
REMARK 620 4 CAP G 600   O2   93.4 109.4 165.7                                  
REMARK 620 5 CAP G 600   O3   83.7 167.1  86.7  79.2                            
REMARK 620 6 CAP G 600   O7  175.0  93.5  97.5  82.0  97.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX H 189   OQ2                                                    
REMARK 620 2 GLU H 192   OE1  85.7                                              
REMARK 620 3 CAP H 600   O2   96.6 154.2                                        
REMARK 620 4 CAP H 600   O3   72.2  81.6  74.8                                  
REMARK 620 5 CAP H 600   O7  151.4  85.2  80.6  79.7                            
REMARK 620 6 ASP H 191   OD1 119.2 110.3  91.1 163.3  89.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG I 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX I 189   OQ2                                                    
REMARK 620 2 ASP I 191   OD1  86.8                                              
REMARK 620 3 GLU I 192   OE1  85.7  83.5                                        
REMARK 620 4 CAP I 600   O2   92.5 110.2 166.1                                  
REMARK 620 5 CAP I 600   O3   87.0 167.5  85.2  80.9                            
REMARK 620 6 CAP I 600   O7  170.4  92.9 103.8  78.6  95.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG J 500  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX J 189   OQ2                                                    
REMARK 620 2 ASP J 191   OD2  86.7                                              
REMARK 620 3 GLU J 192   OE1  82.1  68.1                                        
REMARK 620 4 CAP J 600   O2   89.3 126.0 163.2                                  
REMARK 620 5 CAP J 600   O3   76.9 152.0  87.1  76.9                            
REMARK 620 6 CAP J 600   O7  172.1 100.1 104.2  83.4  98.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP F 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP I 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP J 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG J 500                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1GEH   RELATED DB: PDB                                   
REMARK 900 THE APO-FORM ABOUT THE SAME ENZYME                                   
REMARK 900 RELATED ID: 3KBN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3A12   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3A13   RELATED DB: PDB                                   
DBREF  3KDO A    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3KDO B    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3KDO C    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3KDO D    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3KDO E    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3KDO F    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3KDO G    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3KDO H    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3KDO I    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3KDO J    1   444  UNP    O93627   RBL_PYRKO        1    444             
SEQADV 3KDO GLU A  326  UNP  O93627    GLY   326 ENGINEERED                     
SEQADV 3KDO ARG A  327  UNP  O93627    LYS   327 ENGINEERED                     
SEQADV 3KDO ASP A  328  UNP  O93627    TRP   328 ENGINEERED                     
SEQADV 3KDO ILE A  329  UNP  O93627    ASP   329 ENGINEERED                     
SEQADV 3KDO THR A  330  UNP  O93627    VAL   330 ENGINEERED                     
SEQADV 3KDO LEU A  331  UNP  O93627    ILE   331 ENGINEERED                     
SEQADV 3KDO GLY A  332  UNP  O93627    GLN   332 ENGINEERED                     
SEQADV 3KDO PHE A  333  UNP  O93627    ASN   333 ENGINEERED                     
SEQADV 3KDO VAL A  334  UNP  O93627    ALA   334 ENGINEERED                     
SEQADV 3KDO ASP A  335  UNP  O93627    ARG   335 ENGINEERED                     
SEQADV 3KDO LEU A  336  UNP  O93627    ILE   336 ENGINEERED                     
SEQADV 3KDO GLU B  326  UNP  O93627    GLY   326 ENGINEERED                     
SEQADV 3KDO ARG B  327  UNP  O93627    LYS   327 ENGINEERED                     
SEQADV 3KDO ASP B  328  UNP  O93627    TRP   328 ENGINEERED                     
SEQADV 3KDO ILE B  329  UNP  O93627    ASP   329 ENGINEERED                     
SEQADV 3KDO THR B  330  UNP  O93627    VAL   330 ENGINEERED                     
SEQADV 3KDO LEU B  331  UNP  O93627    ILE   331 ENGINEERED                     
SEQADV 3KDO GLY B  332  UNP  O93627    GLN   332 ENGINEERED                     
SEQADV 3KDO PHE B  333  UNP  O93627    ASN   333 ENGINEERED                     
SEQADV 3KDO VAL B  334  UNP  O93627    ALA   334 ENGINEERED                     
SEQADV 3KDO ASP B  335  UNP  O93627    ARG   335 ENGINEERED                     
SEQADV 3KDO LEU B  336  UNP  O93627    ILE   336 ENGINEERED                     
SEQADV 3KDO GLU C  326  UNP  O93627    GLY   326 ENGINEERED                     
SEQADV 3KDO ARG C  327  UNP  O93627    LYS   327 ENGINEERED                     
SEQADV 3KDO ASP C  328  UNP  O93627    TRP   328 ENGINEERED                     
SEQADV 3KDO ILE C  329  UNP  O93627    ASP   329 ENGINEERED                     
SEQADV 3KDO THR C  330  UNP  O93627    VAL   330 ENGINEERED                     
SEQADV 3KDO LEU C  331  UNP  O93627    ILE   331 ENGINEERED                     
SEQADV 3KDO GLY C  332  UNP  O93627    GLN   332 ENGINEERED                     
SEQADV 3KDO PHE C  333  UNP  O93627    ASN   333 ENGINEERED                     
SEQADV 3KDO VAL C  334  UNP  O93627    ALA   334 ENGINEERED                     
SEQADV 3KDO ASP C  335  UNP  O93627    ARG   335 ENGINEERED                     
SEQADV 3KDO LEU C  336  UNP  O93627    ILE   336 ENGINEERED                     
SEQADV 3KDO GLU D  326  UNP  O93627    GLY   326 ENGINEERED                     
SEQADV 3KDO ARG D  327  UNP  O93627    LYS   327 ENGINEERED                     
SEQADV 3KDO ASP D  328  UNP  O93627    TRP   328 ENGINEERED                     
SEQADV 3KDO ILE D  329  UNP  O93627    ASP   329 ENGINEERED                     
SEQADV 3KDO THR D  330  UNP  O93627    VAL   330 ENGINEERED                     
SEQADV 3KDO LEU D  331  UNP  O93627    ILE   331 ENGINEERED                     
SEQADV 3KDO GLY D  332  UNP  O93627    GLN   332 ENGINEERED                     
SEQADV 3KDO PHE D  333  UNP  O93627    ASN   333 ENGINEERED                     
SEQADV 3KDO VAL D  334  UNP  O93627    ALA   334 ENGINEERED                     
SEQADV 3KDO ASP D  335  UNP  O93627    ARG   335 ENGINEERED                     
SEQADV 3KDO LEU D  336  UNP  O93627    ILE   336 ENGINEERED                     
SEQADV 3KDO GLU E  326  UNP  O93627    GLY   326 ENGINEERED                     
SEQADV 3KDO ARG E  327  UNP  O93627    LYS   327 ENGINEERED                     
SEQADV 3KDO ASP E  328  UNP  O93627    TRP   328 ENGINEERED                     
SEQADV 3KDO ILE E  329  UNP  O93627    ASP   329 ENGINEERED                     
SEQADV 3KDO THR E  330  UNP  O93627    VAL   330 ENGINEERED                     
SEQADV 3KDO LEU E  331  UNP  O93627    ILE   331 ENGINEERED                     
SEQADV 3KDO GLY E  332  UNP  O93627    GLN   332 ENGINEERED                     
SEQADV 3KDO PHE E  333  UNP  O93627    ASN   333 ENGINEERED                     
SEQADV 3KDO VAL E  334  UNP  O93627    ALA   334 ENGINEERED                     
SEQADV 3KDO ASP E  335  UNP  O93627    ARG   335 ENGINEERED                     
SEQADV 3KDO LEU E  336  UNP  O93627    ILE   336 ENGINEERED                     
SEQADV 3KDO GLU F  326  UNP  O93627    GLY   326 ENGINEERED                     
SEQADV 3KDO ARG F  327  UNP  O93627    LYS   327 ENGINEERED                     
SEQADV 3KDO ASP F  328  UNP  O93627    TRP   328 ENGINEERED                     
SEQADV 3KDO ILE F  329  UNP  O93627    ASP   329 ENGINEERED                     
SEQADV 3KDO THR F  330  UNP  O93627    VAL   330 ENGINEERED                     
SEQADV 3KDO LEU F  331  UNP  O93627    ILE   331 ENGINEERED                     
SEQADV 3KDO GLY F  332  UNP  O93627    GLN   332 ENGINEERED                     
SEQADV 3KDO PHE F  333  UNP  O93627    ASN   333 ENGINEERED                     
SEQADV 3KDO VAL F  334  UNP  O93627    ALA   334 ENGINEERED                     
SEQADV 3KDO ASP F  335  UNP  O93627    ARG   335 ENGINEERED                     
SEQADV 3KDO LEU F  336  UNP  O93627    ILE   336 ENGINEERED                     
SEQADV 3KDO GLU G  326  UNP  O93627    GLY   326 ENGINEERED                     
SEQADV 3KDO ARG G  327  UNP  O93627    LYS   327 ENGINEERED                     
SEQADV 3KDO ASP G  328  UNP  O93627    TRP   328 ENGINEERED                     
SEQADV 3KDO ILE G  329  UNP  O93627    ASP   329 ENGINEERED                     
SEQADV 3KDO THR G  330  UNP  O93627    VAL   330 ENGINEERED                     
SEQADV 3KDO LEU G  331  UNP  O93627    ILE   331 ENGINEERED                     
SEQADV 3KDO GLY G  332  UNP  O93627    GLN   332 ENGINEERED                     
SEQADV 3KDO PHE G  333  UNP  O93627    ASN   333 ENGINEERED                     
SEQADV 3KDO VAL G  334  UNP  O93627    ALA   334 ENGINEERED                     
SEQADV 3KDO ASP G  335  UNP  O93627    ARG   335 ENGINEERED                     
SEQADV 3KDO LEU G  336  UNP  O93627    ILE   336 ENGINEERED                     
SEQADV 3KDO GLU H  326  UNP  O93627    GLY   326 ENGINEERED                     
SEQADV 3KDO ARG H  327  UNP  O93627    LYS   327 ENGINEERED                     
SEQADV 3KDO ASP H  328  UNP  O93627    TRP   328 ENGINEERED                     
SEQADV 3KDO ILE H  329  UNP  O93627    ASP   329 ENGINEERED                     
SEQADV 3KDO THR H  330  UNP  O93627    VAL   330 ENGINEERED                     
SEQADV 3KDO LEU H  331  UNP  O93627    ILE   331 ENGINEERED                     
SEQADV 3KDO GLY H  332  UNP  O93627    GLN   332 ENGINEERED                     
SEQADV 3KDO PHE H  333  UNP  O93627    ASN   333 ENGINEERED                     
SEQADV 3KDO VAL H  334  UNP  O93627    ALA   334 ENGINEERED                     
SEQADV 3KDO ASP H  335  UNP  O93627    ARG   335 ENGINEERED                     
SEQADV 3KDO LEU H  336  UNP  O93627    ILE   336 ENGINEERED                     
SEQADV 3KDO GLU I  326  UNP  O93627    GLY   326 ENGINEERED                     
SEQADV 3KDO ARG I  327  UNP  O93627    LYS   327 ENGINEERED                     
SEQADV 3KDO ASP I  328  UNP  O93627    TRP   328 ENGINEERED                     
SEQADV 3KDO ILE I  329  UNP  O93627    ASP   329 ENGINEERED                     
SEQADV 3KDO THR I  330  UNP  O93627    VAL   330 ENGINEERED                     
SEQADV 3KDO LEU I  331  UNP  O93627    ILE   331 ENGINEERED                     
SEQADV 3KDO GLY I  332  UNP  O93627    GLN   332 ENGINEERED                     
SEQADV 3KDO PHE I  333  UNP  O93627    ASN   333 ENGINEERED                     
SEQADV 3KDO VAL I  334  UNP  O93627    ALA   334 ENGINEERED                     
SEQADV 3KDO ASP I  335  UNP  O93627    ARG   335 ENGINEERED                     
SEQADV 3KDO LEU I  336  UNP  O93627    ILE   336 ENGINEERED                     
SEQADV 3KDO GLU J  326  UNP  O93627    GLY   326 ENGINEERED                     
SEQADV 3KDO ARG J  327  UNP  O93627    LYS   327 ENGINEERED                     
SEQADV 3KDO ASP J  328  UNP  O93627    TRP   328 ENGINEERED                     
SEQADV 3KDO ILE J  329  UNP  O93627    ASP   329 ENGINEERED                     
SEQADV 3KDO THR J  330  UNP  O93627    VAL   330 ENGINEERED                     
SEQADV 3KDO LEU J  331  UNP  O93627    ILE   331 ENGINEERED                     
SEQADV 3KDO GLY J  332  UNP  O93627    GLN   332 ENGINEERED                     
SEQADV 3KDO PHE J  333  UNP  O93627    ASN   333 ENGINEERED                     
SEQADV 3KDO VAL J  334  UNP  O93627    ALA   334 ENGINEERED                     
SEQADV 3KDO ASP J  335  UNP  O93627    ARG   335 ENGINEERED                     
SEQADV 3KDO LEU J  336  UNP  O93627    ILE   336 ENGINEERED                     
SEQRES   1 A  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 A  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 A  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 A  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 A  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 A  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 A  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 A  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 A  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 A  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 A  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 A  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 A  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 A  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 A  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR          
SEQRES  16 A  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 A  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 A  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 A  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 A  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 A  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 A  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 A  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 A  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 A  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 A  444  GLU ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG          
SEQRES  27 A  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 A  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 A  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 A  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 A  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 A  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 A  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 A  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 A  444  PRO VAL                                                      
SEQRES   1 B  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 B  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 B  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 B  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 B  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 B  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 B  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 B  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 B  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 B  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 B  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 B  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 B  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 B  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 B  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR          
SEQRES  16 B  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 B  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 B  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 B  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 B  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 B  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 B  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 B  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 B  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 B  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 B  444  GLU ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG          
SEQRES  27 B  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 B  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 B  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 B  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 B  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 B  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 B  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 B  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 B  444  PRO VAL                                                      
SEQRES   1 C  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 C  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 C  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 C  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 C  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 C  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 C  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 C  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 C  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 C  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 C  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 C  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 C  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 C  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 C  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR          
SEQRES  16 C  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 C  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 C  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 C  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 C  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 C  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 C  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 C  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 C  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 C  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 C  444  GLU ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG          
SEQRES  27 C  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 C  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 C  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 C  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 C  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 C  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 C  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 C  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 C  444  PRO VAL                                                      
SEQRES   1 D  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 D  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 D  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 D  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 D  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 D  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 D  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 D  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 D  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 D  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 D  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 D  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 D  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 D  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 D  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR          
SEQRES  16 D  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 D  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 D  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 D  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 D  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 D  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 D  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 D  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 D  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 D  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 D  444  GLU ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG          
SEQRES  27 D  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 D  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 D  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 D  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 D  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 D  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 D  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 D  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 D  444  PRO VAL                                                      
SEQRES   1 E  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 E  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 E  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 E  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 E  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 E  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 E  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 E  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 E  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 E  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 E  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 E  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 E  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 E  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 E  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR          
SEQRES  16 E  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 E  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 E  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 E  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 E  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 E  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 E  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 E  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 E  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 E  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 E  444  GLU ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG          
SEQRES  27 E  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 E  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 E  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 E  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 E  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 E  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 E  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 E  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 E  444  PRO VAL                                                      
SEQRES   1 F  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 F  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 F  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 F  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 F  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 F  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 F  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 F  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 F  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 F  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 F  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 F  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 F  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 F  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 F  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR          
SEQRES  16 F  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 F  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 F  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 F  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 F  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 F  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 F  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 F  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 F  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 F  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 F  444  GLU ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG          
SEQRES  27 F  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 F  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 F  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 F  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 F  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 F  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 F  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 F  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 F  444  PRO VAL                                                      
SEQRES   1 G  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 G  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 G  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 G  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 G  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 G  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 G  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 G  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 G  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 G  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 G  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 G  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 G  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 G  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 G  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR          
SEQRES  16 G  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 G  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 G  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 G  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 G  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 G  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 G  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 G  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 G  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 G  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 G  444  GLU ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG          
SEQRES  27 G  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 G  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 G  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 G  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 G  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 G  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 G  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 G  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 G  444  PRO VAL                                                      
SEQRES   1 H  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 H  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 H  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 H  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 H  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 H  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 H  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 H  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 H  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 H  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 H  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 H  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 H  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 H  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 H  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR          
SEQRES  16 H  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 H  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 H  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 H  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 H  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 H  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 H  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 H  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 H  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 H  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 H  444  GLU ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG          
SEQRES  27 H  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 H  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 H  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 H  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 H  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 H  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 H  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 H  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 H  444  PRO VAL                                                      
SEQRES   1 I  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 I  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 I  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 I  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 I  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 I  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 I  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 I  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 I  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 I  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 I  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 I  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 I  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 I  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 I  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR          
SEQRES  16 I  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 I  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 I  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 I  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 I  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 I  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 I  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 I  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 I  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 I  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 I  444  GLU ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG          
SEQRES  27 I  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 I  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 I  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 I  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 I  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 I  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 I  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 I  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 I  444  PRO VAL                                                      
SEQRES   1 J  444  MET VAL GLU LYS PHE ASP THR ILE TYR ASP TYR TYR VAL          
SEQRES   2 J  444  ASP LYS GLY TYR GLU PRO SER LYS LYS ARG ASP ILE ILE          
SEQRES   3 J  444  ALA VAL PHE ARG VAL THR PRO ALA GLU GLY TYR THR ILE          
SEQRES   4 J  444  GLU GLN ALA ALA GLY ALA VAL ALA ALA GLU SER SER THR          
SEQRES   5 J  444  GLY THR TRP THR THR LEU TYR PRO TRP TYR GLU GLN GLU          
SEQRES   6 J  444  ARG TRP ALA ASP LEU SER ALA LYS ALA TYR ASP PHE HIS          
SEQRES   7 J  444  ASP MET GLY ASP GLY SER TRP ILE VAL ARG ILE ALA TYR          
SEQRES   8 J  444  PRO PHE HIS ALA PHE GLU GLU ALA ASN LEU PRO GLY LEU          
SEQRES   9 J  444  LEU ALA SER ILE ALA GLY ASN ILE PHE GLY MET LYS ARG          
SEQRES  10 J  444  VAL LYS GLY LEU ARG LEU GLU ASP LEU TYR PHE PRO GLU          
SEQRES  11 J  444  LYS LEU ILE ARG GLU PHE ASP GLY PRO ALA PHE GLY ILE          
SEQRES  12 J  444  GLU GLY VAL ARG LYS MET LEU GLU ILE LYS ASP ARG PRO          
SEQRES  13 J  444  ILE TYR GLY VAL VAL PRO LYS PRO LYS VAL GLY TYR SER          
SEQRES  14 J  444  PRO GLU GLU PHE GLU LYS LEU ALA TYR ASP LEU LEU SER          
SEQRES  15 J  444  ASN GLY ALA ASP TYR MET KCX ASP ASP GLU ASN LEU THR          
SEQRES  16 J  444  SER PRO TRP TYR ASN ARG PHE GLU GLU ARG ALA GLU ILE          
SEQRES  17 J  444  MET ALA LYS ILE ILE ASP LYS VAL GLU ASN GLU THR GLY          
SEQRES  18 J  444  GLU LYS LYS THR TRP PHE ALA ASN ILE THR ALA ASP LEU          
SEQRES  19 J  444  LEU GLU MET GLU GLN ARG LEU GLU VAL LEU ALA ASP LEU          
SEQRES  20 J  444  GLY LEU LYS HIS ALA MET VAL ASP VAL VAL ILE THR GLY          
SEQRES  21 J  444  TRP GLY ALA LEU ARG TYR ILE ARG ASP LEU ALA ALA ASP          
SEQRES  22 J  444  TYR GLY LEU ALA ILE HIS GLY HIS ARG ALA MET HIS ALA          
SEQRES  23 J  444  ALA PHE THR ARG ASN PRO TYR HIS GLY ILE SER MET PHE          
SEQRES  24 J  444  VAL LEU ALA LYS LEU TYR ARG LEU ILE GLY ILE ASP GLN          
SEQRES  25 J  444  LEU HIS VAL GLY THR ALA GLY ALA GLY LYS LEU GLU GLY          
SEQRES  26 J  444  GLU ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG          
SEQRES  27 J  444  GLU SER HIS TYR LYS PRO ASP GLU ASN ASP VAL PHE HIS          
SEQRES  28 J  444  LEU GLU GLN LYS PHE TYR SER ILE LYS ALA ALA PHE PRO          
SEQRES  29 J  444  THR SER SER GLY GLY LEU HIS PRO GLY ASN ILE GLN PRO          
SEQRES  30 J  444  VAL ILE GLU ALA LEU GLY THR ASP ILE VAL LEU GLN LEU          
SEQRES  31 J  444  GLY GLY GLY THR LEU GLY HIS PRO ASP GLY PRO ALA ALA          
SEQRES  32 J  444  GLY ALA ARG ALA VAL ARG GLN ALA ILE ASP ALA ILE MET          
SEQRES  33 J  444  GLN GLY ILE PRO LEU ASP GLU TYR ALA LYS THR HIS LYS          
SEQRES  34 J  444  GLU LEU ALA ARG ALA LEU GLU LYS TRP GLY HIS VAL THR          
SEQRES  35 J  444  PRO VAL                                                      
MODRES 3KDO KCX A  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3KDO KCX B  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3KDO KCX C  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3KDO KCX D  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3KDO KCX E  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3KDO KCX F  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3KDO KCX G  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3KDO KCX H  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3KDO KCX I  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3KDO KCX J  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
HET    KCX  A 189      12                                                       
HET    KCX  B 189      12                                                       
HET    KCX  C 189      12                                                       
HET    KCX  D 189      12                                                       
HET    KCX  E 189      12                                                       
HET    KCX  F 189      12                                                       
HET    KCX  G 189      12                                                       
HET    KCX  H 189      12                                                       
HET    KCX  I 189      12                                                       
HET    KCX  J 189      12                                                       
HET    CAP  A 600      21                                                       
HET     MG  A 500       1                                                       
HET    CAP  B 600      21                                                       
HET     MG  B 500       1                                                       
HET    CAP  C 600      21                                                       
HET     MG  C 500       1                                                       
HET    CAP  D 600      21                                                       
HET     MG  D 500       1                                                       
HET    CAP  E 600      21                                                       
HET     MG  E 500       1                                                       
HET    CAP  F 600      21                                                       
HET     MG  F 500       1                                                       
HET    CAP  G 600      21                                                       
HET     MG  G 500       1                                                       
HET    CAP  H 600      21                                                       
HET     MG  H 500       1                                                       
HET    CAP  I 600      21                                                       
HET     MG  I 500       1                                                       
HET    CAP  J 600      21                                                       
HET     MG  J 500       1                                                       
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE                              
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   1  KCX    10(C7 H14 N2 O4)                                             
FORMUL  11  CAP    10(C6 H14 O13 P2)                                            
FORMUL  12   MG    10(MG 2+)                                                    
FORMUL  31  HOH   *1811(H2 O)                                                   
HELIX    1   1 THR A   38  SER A   50  1                                  13    
HELIX    2   2 GLU A   63  SER A   71  1                                   9    
HELIX    3   3 HIS A   94  PHE A   96  5                                   3    
HELIX    4   4 ASN A  100  ALA A  109  1                                  10    
HELIX    5   5 GLY A  110  MET A  115  5                                   6    
HELIX    6   6 PRO A  129  ARG A  134  1                                   6    
HELIX    7   7 PHE A  141  GLU A  151  1                                  11    
HELIX    8   8 SER A  169  ASN A  183  1                                  15    
HELIX    9   9 ARG A  201  THR A  220  1                                  20    
HELIX   10  10 ASP A  233  GLY A  248  1                                  16    
HELIX   11  11 VAL A  256  GLY A  260  1                                   5    
HELIX   12  12 GLY A  260  GLY A  275  1                                  16    
HELIX   13  13 HIS A  285  ARG A  290  1                                   6    
HELIX   14  14 SER A  297  GLY A  309  1                                  13    
HELIX   15  15 GLU A  326  GLU A  339  1                                  14    
HELIX   16  16 ILE A  375  GLY A  383  1                                   9    
HELIX   17  17 GLY A  391  GLY A  396  1                                   6    
HELIX   18  18 GLY A  400  GLY A  418  1                                  19    
HELIX   19  19 PRO A  420  LYS A  426  1                                   7    
HELIX   20  20 HIS A  428  GLY A  439  1                                  12    
HELIX   21  21 THR B    7  VAL B   13  5                                   7    
HELIX   22  22 THR B   38  SER B   50  1                                  13    
HELIX   23  23 GLU B   63  SER B   71  1                                   9    
HELIX   24  24 HIS B   94  PHE B   96  5                                   3    
HELIX   25  25 ASN B  100  ALA B  109  1                                  10    
HELIX   26  26 GLY B  110  MET B  115  5                                   6    
HELIX   27  27 PRO B  129  ARG B  134  1                                   6    
HELIX   28  28 PHE B  141  GLU B  151  1                                  11    
HELIX   29  29 SER B  169  ASN B  183  1                                  15    
HELIX   30  30 ARG B  201  GLY B  221  1                                  21    
HELIX   31  31 ASP B  233  GLY B  248  1                                  16    
HELIX   32  32 VAL B  256  GLY B  260  1                                   5    
HELIX   33  33 GLY B  260  TYR B  274  1                                  15    
HELIX   34  34 HIS B  285  ARG B  290  1                                   6    
HELIX   35  35 SER B  297  GLY B  309  1                                  13    
HELIX   36  36 GLU B  326  GLU B  339  1                                  14    
HELIX   37  37 HIS B  371  ASN B  374  5                                   4    
HELIX   38  38 ILE B  375  GLY B  383  1                                   9    
HELIX   39  39 GLY B  391  GLY B  396  1                                   6    
HELIX   40  40 GLY B  400  GLY B  418  1                                  19    
HELIX   41  41 HIS B  428  TRP B  438  1                                  11    
HELIX   42  42 ILE C    8  VAL C   13  5                                   6    
HELIX   43  43 THR C   38  SER C   50  1                                  13    
HELIX   44  44 GLU C   63  SER C   71  1                                   9    
HELIX   45  45 HIS C   94  PHE C   96  5                                   3    
HELIX   46  46 ASN C  100  ALA C  109  1                                  10    
HELIX   47  47 GLY C  110  MET C  115  5                                   6    
HELIX   48  48 PRO C  129  ARG C  134  1                                   6    
HELIX   49  49 PHE C  141  GLU C  151  1                                  11    
HELIX   50  50 SER C  169  SER C  182  1                                  14    
HELIX   51  51 ARG C  201  GLY C  221  1                                  21    
HELIX   52  52 ASP C  233  GLY C  248  1                                  16    
HELIX   53  53 VAL C  256  GLY C  260  1                                   5    
HELIX   54  54 GLY C  260  GLY C  275  1                                  16    
HELIX   55  55 HIS C  285  ARG C  290  1                                   6    
HELIX   56  56 SER C  297  GLY C  309  1                                  13    
HELIX   57  57 GLU C  326  GLU C  339  1                                  14    
HELIX   58  58 ILE C  375  GLY C  383  1                                   9    
HELIX   59  59 GLY C  391  GLY C  396  1                                   6    
HELIX   60  60 GLY C  400  GLY C  418  1                                  19    
HELIX   61  61 PRO C  420  LYS C  426  1                                   7    
HELIX   62  62 HIS C  428  GLY C  439  1                                  12    
HELIX   63  63 TYR D    9  VAL D   13  5                                   5    
HELIX   64  64 THR D   38  SER D   50  1                                  13    
HELIX   65  65 GLU D   63  SER D   71  1                                   9    
HELIX   66  66 HIS D   94  PHE D   96  5                                   3    
HELIX   67  67 ASN D  100  ALA D  109  1                                  10    
HELIX   68  68 GLY D  110  MET D  115  5                                   6    
HELIX   69  69 PRO D  129  ARG D  134  1                                   6    
HELIX   70  70 PHE D  141  LEU D  150  1                                  10    
HELIX   71  71 SER D  169  ASN D  183  1                                  15    
HELIX   72  72 ARG D  201  GLY D  221  1                                  21    
HELIX   73  73 ASP D  233  LEU D  247  1                                  15    
HELIX   74  74 VAL D  256  GLY D  260  1                                   5    
HELIX   75  75 GLY D  260  GLY D  275  1                                  16    
HELIX   76  76 HIS D  285  ARG D  290  1                                   6    
HELIX   77  77 SER D  297  GLY D  309  1                                  13    
HELIX   78  78 GLU D  326  GLU D  339  1                                  14    
HELIX   79  79 HIS D  371  ASN D  374  5                                   4    
HELIX   80  80 ILE D  375  GLY D  383  1                                   9    
HELIX   81  81 GLY D  391  GLY D  396  1                                   6    
HELIX   82  82 GLY D  400  GLN D  417  1                                  18    
HELIX   83  83 PRO D  420  ALA D  425  1                                   6    
HELIX   84  84 HIS D  428  GLY D  439  1                                  12    
HELIX   85  85 ASP E    6  TYR E   11  1                                   6    
HELIX   86  86 THR E   38  SER E   50  1                                  13    
HELIX   87  87 GLU E   63  SER E   71  1                                   9    
HELIX   88  88 HIS E   94  PHE E   96  5                                   3    
HELIX   89  89 ASN E  100  ALA E  109  1                                  10    
HELIX   90  90 GLY E  110  MET E  115  5                                   6    
HELIX   91  91 PRO E  129  ARG E  134  1                                   6    
HELIX   92  92 PHE E  141  GLU E  151  1                                  11    
HELIX   93  93 SER E  169  ASN E  183  1                                  15    
HELIX   94  94 ARG E  201  GLY E  221  1                                  21    
HELIX   95  95 ASP E  233  LEU E  247  1                                  15    
HELIX   96  96 VAL E  256  GLY E  260  1                                   5    
HELIX   97  97 ALA E  263  GLY E  275  1                                  13    
HELIX   98  98 HIS E  285  ARG E  290  1                                   6    
HELIX   99  99 SER E  297  GLY E  309  1                                  13    
HELIX  100 100 GLU E  326  GLU E  339  1                                  14    
HELIX  101 101 HIS E  371  ASN E  374  5                                   4    
HELIX  102 102 ILE E  375  GLY E  383  1                                   9    
HELIX  103 103 GLY E  391  GLY E  396  1                                   6    
HELIX  104 104 GLY E  400  GLY E  418  1                                  19    
HELIX  105 105 TYR E  424  THR E  427  5                                   4    
HELIX  106 106 HIS E  428  GLY E  439  1                                  12    
HELIX  107 107 ILE F    8  VAL F   13  5                                   6    
HELIX  108 108 THR F   38  SER F   50  1                                  13    
HELIX  109 109 GLU F   63  SER F   71  1                                   9    
HELIX  110 110 HIS F   94  PHE F   96  5                                   3    
HELIX  111 111 ASN F  100  ALA F  109  1                                  10    
HELIX  112 112 GLY F  110  MET F  115  5                                   6    
HELIX  113 113 PRO F  129  ARG F  134  1                                   6    
HELIX  114 114 PHE F  141  GLU F  151  1                                  11    
HELIX  115 115 SER F  169  SER F  182  1                                  14    
HELIX  116 116 ARG F  201  GLY F  221  1                                  21    
HELIX  117 117 ASP F  233  LEU F  247  1                                  15    
HELIX  118 118 VAL F  256  GLY F  260  1                                   5    
HELIX  119 119 GLY F  260  TYR F  274  1                                  15    
HELIX  120 120 HIS F  285  ARG F  290  1                                   6    
HELIX  121 121 SER F  297  GLY F  309  1                                  13    
HELIX  122 122 GLU F  326  GLU F  339  1                                  14    
HELIX  123 123 HIS F  371  ASN F  374  5                                   4    
HELIX  124 124 ILE F  375  GLY F  383  1                                   9    
HELIX  125 125 GLY F  391  GLY F  396  1                                   6    
HELIX  126 126 GLY F  400  GLY F  418  1                                  19    
HELIX  127 127 PRO F  420  LYS F  426  1                                   7    
HELIX  128 128 HIS F  428  GLY F  439  1                                  12    
HELIX  129 129 ILE G    8  VAL G   13  5                                   6    
HELIX  130 130 THR G   38  SER G   50  1                                  13    
HELIX  131 131 GLU G   63  LEU G   70  1                                   8    
HELIX  132 132 HIS G   94  PHE G   96  5                                   3    
HELIX  133 133 ASN G  100  ALA G  109  1                                  10    
HELIX  134 134 GLY G  110  MET G  115  5                                   6    
HELIX  135 135 PRO G  129  ARG G  134  1                                   6    
HELIX  136 136 PHE G  141  GLU G  151  1                                  11    
HELIX  137 137 SER G  169  ASN G  183  1                                  15    
HELIX  138 138 ARG G  201  GLY G  221  1                                  21    
HELIX  139 139 ASP G  233  LEU G  247  1                                  15    
HELIX  140 140 VAL G  256  GLY G  260  1                                   5    
HELIX  141 141 GLY G  260  TYR G  274  1                                  15    
HELIX  142 142 HIS G  285  ARG G  290  1                                   6    
HELIX  143 143 SER G  297  GLY G  309  1                                  13    
HELIX  144 144 GLU G  326  GLU G  339  1                                  14    
HELIX  145 145 ILE G  375  GLY G  383  1                                   9    
HELIX  146 146 GLY G  391  GLY G  396  1                                   6    
HELIX  147 147 GLY G  400  GLY G  418  1                                  19    
HELIX  148 148 PRO G  420  ALA G  425  1                                   6    
HELIX  149 149 HIS G  428  GLY G  439  1                                  12    
HELIX  150 150 TYR H    9  VAL H   13  5                                   5    
HELIX  151 151 THR H   38  SER H   50  1                                  13    
HELIX  152 152 GLU H   63  SER H   71  1                                   9    
HELIX  153 153 HIS H   94  PHE H   96  5                                   3    
HELIX  154 154 ASN H  100  ALA H  109  1                                  10    
HELIX  155 155 GLY H  110  MET H  115  5                                   6    
HELIX  156 156 PRO H  129  ARG H  134  1                                   6    
HELIX  157 157 PHE H  141  GLU H  151  1                                  11    
HELIX  158 158 SER H  169  ASN H  183  1                                  15    
HELIX  159 159 ARG H  201  GLY H  221  1                                  21    
HELIX  160 160 ASP H  233  GLY H  248  1                                  16    
HELIX  161 161 VAL H  256  GLY H  260  1                                   5    
HELIX  162 162 ALA H  263  GLY H  275  1                                  13    
HELIX  163 163 HIS H  285  ARG H  290  1                                   6    
HELIX  164 164 SER H  297  GLY H  309  1                                  13    
HELIX  165 165 GLU H  326  GLU H  339  1                                  14    
HELIX  166 166 ILE H  375  GLY H  383  1                                   9    
HELIX  167 167 GLY H  391  GLY H  396  1                                   6    
HELIX  168 168 GLY H  400  GLY H  418  1                                  19    
HELIX  169 169 PRO H  420  LYS H  426  1                                   7    
HELIX  170 170 HIS H  428  GLY H  439  1                                  12    
HELIX  171 171 ILE I    8  TYR I   12  5                                   5    
HELIX  172 172 THR I   38  SER I   50  1                                  13    
HELIX  173 173 GLU I   63  SER I   71  1                                   9    
HELIX  174 174 HIS I   94  PHE I   96  5                                   3    
HELIX  175 175 ASN I  100  ALA I  109  1                                  10    
HELIX  176 176 GLY I  110  MET I  115  5                                   6    
HELIX  177 177 PRO I  129  ARG I  134  1                                   6    
HELIX  178 178 PHE I  141  GLU I  151  1                                  11    
HELIX  179 179 SER I  169  SER I  182  1                                  14    
HELIX  180 180 ARG I  201  GLY I  221  1                                  21    
HELIX  181 181 ASP I  233  GLY I  248  1                                  16    
HELIX  182 182 VAL I  256  GLY I  260  1                                   5    
HELIX  183 183 GLY I  260  TYR I  274  1                                  15    
HELIX  184 184 HIS I  285  ARG I  290  1                                   6    
HELIX  185 185 SER I  297  GLY I  309  1                                  13    
HELIX  186 186 GLU I  326  GLU I  339  1                                  14    
HELIX  187 187 ILE I  375  GLY I  383  1                                   9    
HELIX  188 188 GLY I  391  GLY I  396  1                                   6    
HELIX  189 189 GLY I  400  GLY I  418  1                                  19    
HELIX  190 190 PRO I  420  ALA I  425  1                                   6    
HELIX  191 191 HIS I  428  GLY I  439  1                                  12    
HELIX  192 192 ILE J    8  VAL J   13  5                                   6    
HELIX  193 193 THR J   38  SER J   50  1                                  13    
HELIX  194 194 GLU J   63  SER J   71  1                                   9    
HELIX  195 195 HIS J   94  PHE J   96  5                                   3    
HELIX  196 196 ASN J  100  ALA J  109  1                                  10    
HELIX  197 197 GLY J  110  MET J  115  5                                   6    
HELIX  198 198 PRO J  129  ARG J  134  1                                   6    
HELIX  199 199 PHE J  141  GLU J  151  1                                  11    
HELIX  200 200 SER J  169  ASN J  183  1                                  15    
HELIX  201 201 ARG J  201  GLY J  221  1                                  21    
HELIX  202 202 ASP J  233  LEU J  247  1                                  15    
HELIX  203 203 VAL J  256  GLY J  260  1                                   5    
HELIX  204 204 ALA J  263  GLY J  275  1                                  13    
HELIX  205 205 HIS J  285  ARG J  290  1                                   6    
HELIX  206 206 SER J  297  GLY J  309  1                                  13    
HELIX  207 207 GLU J  326  GLU J  339  1                                  14    
HELIX  208 208 ASN J  374  GLY J  383  1                                  10    
HELIX  209 209 GLY J  391  GLY J  396  1                                   6    
HELIX  210 210 GLY J  400  GLY J  418  1                                  19    
HELIX  211 211 PRO J  420  ALA J  425  1                                   6    
HELIX  212 212 HIS J  428  GLY J  439  1                                  12    
SHEET    1   A 5 LYS A  73  ASP A  79  0                                        
SHEET    2   A 5 TRP A  85  PRO A  92 -1  O  ALA A  90   N  LYS A  73           
SHEET    3   A 5 ASP A  24  PRO A  33 -1  N  PHE A  29   O  VAL A  87           
SHEET    4   A 5 VAL A 118  TYR A 127 -1  O  TYR A 127   N  ILE A  26           
SHEET    5   A 5 GLY A 295  ILE A 296  1  O  GLY A 295   N  LEU A 121           
SHEET    1   B 9 ILE A 157  VAL A 160  0                                        
SHEET    2   B 9 TYR A 187  KCX A 189  1  O  KCX A 189   N  VAL A 160           
SHEET    3   B 9 THR A 225  ASN A 229  1  O  PHE A 227   N  MET A 188           
SHEET    4   B 9 HIS A 251  ASP A 255  1  O  MET A 253   N  ALA A 228           
SHEET    5   B 9 ALA A 277  HIS A 281  1  O  HIS A 281   N  VAL A 254           
SHEET    6   B 9 GLN A 312  HIS A 314  1  O  GLN A 312   N  GLY A 280           
SHEET    7   B 9 PHE A 363  SER A 367  1  O  THR A 365   N  LEU A 313           
SHEET    8   B 9 VAL A 387  GLN A 389  1  O  VAL A 387   N  PRO A 364           
SHEET    9   B 9 ILE A 157  VAL A 160  1  N  ILE A 157   O  LEU A 388           
SHEET    1   C 2 HIS A 341  TYR A 342  0                                        
SHEET    2   C 2 GLN A 354  LYS A 355 -1  O  GLN A 354   N  TYR A 342           
SHEET    1   D 5 LYS B  73  ASP B  79  0                                        
SHEET    2   D 5 TRP B  85  PRO B  92 -1  O  ILE B  86   N  HIS B  78           
SHEET    3   D 5 ASP B  24  PRO B  33 -1  N  ILE B  25   O  TYR B  91           
SHEET    4   D 5 VAL B 118  TYR B 127 -1  O  LYS B 119   N  THR B  32           
SHEET    5   D 5 GLY B 295  ILE B 296  1  O  GLY B 295   N  LEU B 121           
SHEET    1   E 9 ILE B 157  VAL B 160  0                                        
SHEET    2   E 9 TYR B 187  KCX B 189  1  O  KCX B 189   N  VAL B 160           
SHEET    3   E 9 THR B 225  ASN B 229  1  O  PHE B 227   N  MET B 188           
SHEET    4   E 9 HIS B 251  ASP B 255  1  O  MET B 253   N  ALA B 228           
SHEET    5   E 9 ALA B 277  HIS B 281  1  O  HIS B 279   N  VAL B 254           
SHEET    6   E 9 GLN B 312  HIS B 314  1  O  GLN B 312   N  GLY B 280           
SHEET    7   E 9 PHE B 363  SER B 367  1  O  THR B 365   N  LEU B 313           
SHEET    8   E 9 VAL B 387  GLN B 389  1  O  VAL B 387   N  PRO B 364           
SHEET    9   E 9 ILE B 157  VAL B 160  1  N  ILE B 157   O  LEU B 388           
SHEET    1   F 2 HIS B 341  TYR B 342  0                                        
SHEET    2   F 2 GLN B 354  LYS B 355 -1  O  GLN B 354   N  TYR B 342           
SHEET    1   G 5 LYS C  73  ASP C  79  0                                        
SHEET    2   G 5 TRP C  85  PRO C  92 -1  O  ILE C  86   N  HIS C  78           
SHEET    3   G 5 ASP C  24  PRO C  33 -1  N  ILE C  25   O  TYR C  91           
SHEET    4   G 5 VAL C 118  TYR C 127 -1  O  GLU C 124   N  VAL C  28           
SHEET    5   G 5 GLY C 295  ILE C 296  1  O  GLY C 295   N  LEU C 121           
SHEET    1   H 9 ILE C 157  VAL C 160  0                                        
SHEET    2   H 9 TYR C 187  KCX C 189  1  O  KCX C 189   N  VAL C 160           
SHEET    3   H 9 THR C 225  ASN C 229  1  O  PHE C 227   N  MET C 188           
SHEET    4   H 9 HIS C 251  ASP C 255  1  O  MET C 253   N  ALA C 228           
SHEET    5   H 9 ALA C 277  HIS C 281  1  O  HIS C 281   N  VAL C 254           
SHEET    6   H 9 GLN C 312  HIS C 314  1  O  GLN C 312   N  GLY C 280           
SHEET    7   H 9 PHE C 363  SER C 367  1  O  THR C 365   N  LEU C 313           
SHEET    8   H 9 VAL C 387  GLN C 389  1  O  VAL C 387   N  PRO C 364           
SHEET    9   H 9 ILE C 157  VAL C 160  1  N  ILE C 157   O  LEU C 388           
SHEET    1   I 2 HIS C 341  TYR C 342  0                                        
SHEET    2   I 2 GLN C 354  LYS C 355 -1  O  GLN C 354   N  TYR C 342           
SHEET    1   J 5 LYS D  73  ASP D  79  0                                        
SHEET    2   J 5 TRP D  85  PRO D  92 -1  O  ILE D  86   N  HIS D  78           
SHEET    3   J 5 ASP D  24  PRO D  33 -1  N  VAL D  31   O  TRP D  85           
SHEET    4   J 5 VAL D 118  TYR D 127 -1  O  TYR D 127   N  ILE D  26           
SHEET    5   J 5 GLY D 295  ILE D 296  1  O  GLY D 295   N  LEU D 121           
SHEET    1   K 9 ILE D 157  VAL D 160  0                                        
SHEET    2   K 9 TYR D 187  KCX D 189  1  O  KCX D 189   N  VAL D 160           
SHEET    3   K 9 THR D 225  ASN D 229  1  O  PHE D 227   N  MET D 188           
SHEET    4   K 9 HIS D 251  ASP D 255  1  O  MET D 253   N  ALA D 228           
SHEET    5   K 9 ALA D 277  HIS D 281  1  O  ALA D 277   N  ALA D 252           
SHEET    6   K 9 GLN D 312  HIS D 314  1  O  GLN D 312   N  GLY D 280           
SHEET    7   K 9 PHE D 363  SER D 367  1  O  THR D 365   N  LEU D 313           
SHEET    8   K 9 VAL D 387  GLN D 389  1  O  VAL D 387   N  PRO D 364           
SHEET    9   K 9 ILE D 157  VAL D 160  1  N  ILE D 157   O  LEU D 388           
SHEET    1   L 2 HIS D 341  TYR D 342  0                                        
SHEET    2   L 2 GLN D 354  LYS D 355 -1  O  GLN D 354   N  TYR D 342           
SHEET    1   M 5 LYS E  73  ASP E  79  0                                        
SHEET    2   M 5 TRP E  85  PRO E  92 -1  O  ALA E  90   N  LYS E  73           
SHEET    3   M 5 ASP E  24  PRO E  33 -1  N  ILE E  25   O  TYR E  91           
SHEET    4   M 5 VAL E 118  TYR E 127 -1  O  LYS E 119   N  THR E  32           
SHEET    5   M 5 GLY E 295  ILE E 296  1  O  GLY E 295   N  LEU E 121           
SHEET    1   N 8 THR E 225  PHE E 227  0                                        
SHEET    2   N 8 TYR E 187  KCX E 189  1  N  MET E 188   O  PHE E 227           
SHEET    3   N 8 ILE E 157  VAL E 160  1  N  VAL E 160   O  KCX E 189           
SHEET    4   N 8 VAL E 387  GLN E 389  1  O  LEU E 388   N  ILE E 157           
SHEET    5   N 8 PHE E 363  SER E 367  1  N  PRO E 364   O  VAL E 387           
SHEET    6   N 8 GLN E 312  HIS E 314  1  N  LEU E 313   O  THR E 365           
SHEET    7   N 8 ALA E 277  HIS E 281  1  N  GLY E 280   O  GLN E 312           
SHEET    8   N 8 HIS E 251  ASP E 255  1  N  VAL E 254   O  HIS E 279           
SHEET    1   O 2 HIS E 341  TYR E 342  0                                        
SHEET    2   O 2 GLN E 354  LYS E 355 -1  O  GLN E 354   N  TYR E 342           
SHEET    1   P 5 LYS F  73  ASP F  79  0                                        
SHEET    2   P 5 TRP F  85  PRO F  92 -1  O  ILE F  86   N  HIS F  78           
SHEET    3   P 5 ASP F  24  PRO F  33 -1  N  VAL F  31   O  TRP F  85           
SHEET    4   P 5 VAL F 118  TYR F 127 -1  O  GLU F 124   N  VAL F  28           
SHEET    5   P 5 GLY F 295  ILE F 296  1  O  GLY F 295   N  LEU F 121           
SHEET    1   Q 9 ILE F 157  VAL F 160  0                                        
SHEET    2   Q 9 TYR F 187  KCX F 189  1  O  KCX F 189   N  VAL F 160           
SHEET    3   Q 9 THR F 225  ASN F 229  1  O  PHE F 227   N  MET F 188           
SHEET    4   Q 9 HIS F 251  ASP F 255  1  O  MET F 253   N  ALA F 228           
SHEET    5   Q 9 ALA F 277  HIS F 281  1  O  HIS F 279   N  VAL F 254           
SHEET    6   Q 9 GLN F 312  HIS F 314  1  O  GLN F 312   N  GLY F 280           
SHEET    7   Q 9 PHE F 363  SER F 367  1  O  THR F 365   N  LEU F 313           
SHEET    8   Q 9 VAL F 387  GLN F 389  1  O  VAL F 387   N  PRO F 364           
SHEET    9   Q 9 ILE F 157  VAL F 160  1  N  ILE F 157   O  LEU F 388           
SHEET    1   R 2 HIS F 341  TYR F 342  0                                        
SHEET    2   R 2 GLN F 354  LYS F 355 -1  O  GLN F 354   N  TYR F 342           
SHEET    1   S 5 LYS G  73  ASP G  79  0                                        
SHEET    2   S 5 TRP G  85  PRO G  92 -1  O  ILE G  86   N  HIS G  78           
SHEET    3   S 5 ASP G  24  PRO G  33 -1  N  ILE G  25   O  TYR G  91           
SHEET    4   S 5 VAL G 118  TYR G 127 -1  O  GLU G 124   N  VAL G  28           
SHEET    5   S 5 GLY G 295  ILE G 296  1  O  GLY G 295   N  LEU G 121           
SHEET    1   T 9 ILE G 157  VAL G 160  0                                        
SHEET    2   T 9 TYR G 187  KCX G 189  1  O  KCX G 189   N  VAL G 160           
SHEET    3   T 9 THR G 225  ASN G 229  1  O  PHE G 227   N  MET G 188           
SHEET    4   T 9 HIS G 251  ASP G 255  1  O  MET G 253   N  ALA G 228           
SHEET    5   T 9 ALA G 277  HIS G 281  1  O  HIS G 279   N  VAL G 254           
SHEET    6   T 9 GLN G 312  HIS G 314  1  O  GLN G 312   N  GLY G 280           
SHEET    7   T 9 PHE G 363  SER G 367  1  O  THR G 365   N  LEU G 313           
SHEET    8   T 9 VAL G 387  GLN G 389  1  O  VAL G 387   N  PRO G 364           
SHEET    9   T 9 ILE G 157  VAL G 160  1  N  ILE G 157   O  LEU G 388           
SHEET    1   U 2 HIS G 341  TYR G 342  0                                        
SHEET    2   U 2 GLN G 354  LYS G 355 -1  O  GLN G 354   N  TYR G 342           
SHEET    1   V 5 LYS H  73  ASP H  79  0                                        
SHEET    2   V 5 TRP H  85  PRO H  92 -1  O  ILE H  86   N  HIS H  78           
SHEET    3   V 5 ASP H  24  PRO H  33 -1  N  ILE H  25   O  TYR H  91           
SHEET    4   V 5 VAL H 118  TYR H 127 -1  O  GLU H 124   N  VAL H  28           
SHEET    5   V 5 GLY H 295  ILE H 296  1  O  GLY H 295   N  LEU H 123           
SHEET    1   W 9 ILE H 157  VAL H 160  0                                        
SHEET    2   W 9 TYR H 187  KCX H 189  1  O  TYR H 187   N  VAL H 160           
SHEET    3   W 9 THR H 225  ASN H 229  1  O  PHE H 227   N  MET H 188           
SHEET    4   W 9 HIS H 251  ASP H 255  1  O  MET H 253   N  ALA H 228           
SHEET    5   W 9 ALA H 277  HIS H 281  1  O  HIS H 281   N  VAL H 254           
SHEET    6   W 9 GLN H 312  HIS H 314  1  O  GLN H 312   N  GLY H 280           
SHEET    7   W 9 PHE H 363  SER H 367  1  O  THR H 365   N  LEU H 313           
SHEET    8   W 9 VAL H 387  GLN H 389  1  O  VAL H 387   N  PRO H 364           
SHEET    9   W 9 ILE H 157  VAL H 160  1  N  ILE H 157   O  LEU H 388           
SHEET    1   X 2 HIS H 341  TYR H 342  0                                        
SHEET    2   X 2 GLN H 354  LYS H 355 -1  O  GLN H 354   N  TYR H 342           
SHEET    1   Y 5 LYS I  73  ASP I  79  0                                        
SHEET    2   Y 5 TRP I  85  PRO I  92 -1  O  ILE I  86   N  HIS I  78           
SHEET    3   Y 5 ASP I  24  PRO I  33 -1  N  VAL I  31   O  TRP I  85           
SHEET    4   Y 5 VAL I 118  TYR I 127 -1  O  LYS I 119   N  THR I  32           
SHEET    5   Y 5 GLY I 295  ILE I 296  1  O  GLY I 295   N  LEU I 121           
SHEET    1   Z 9 ILE I 157  VAL I 160  0                                        
SHEET    2   Z 9 TYR I 187  KCX I 189  1  O  KCX I 189   N  VAL I 160           
SHEET    3   Z 9 THR I 225  ASN I 229  1  O  PHE I 227   N  MET I 188           
SHEET    4   Z 9 HIS I 251  ASP I 255  1  O  MET I 253   N  ALA I 228           
SHEET    5   Z 9 ALA I 277  HIS I 281  1  O  HIS I 281   N  VAL I 254           
SHEET    6   Z 9 GLN I 312  HIS I 314  1  O  GLN I 312   N  GLY I 280           
SHEET    7   Z 9 PHE I 363  SER I 367  1  O  THR I 365   N  LEU I 313           
SHEET    8   Z 9 VAL I 387  GLN I 389  1  O  VAL I 387   N  PRO I 364           
SHEET    9   Z 9 ILE I 157  VAL I 160  1  N  ILE I 157   O  LEU I 388           
SHEET    1  AA 2 HIS I 341  TYR I 342  0                                        
SHEET    2  AA 2 GLN I 354  LYS I 355 -1  O  GLN I 354   N  TYR I 342           
SHEET    1  AB 5 LYS J  73  ASP J  79  0                                        
SHEET    2  AB 5 TRP J  85  PRO J  92 -1  O  ILE J  86   N  HIS J  78           
SHEET    3  AB 5 ASP J  24  PRO J  33 -1  N  ILE J  25   O  TYR J  91           
SHEET    4  AB 5 VAL J 118  TYR J 127 -1  O  LYS J 119   N  THR J  32           
SHEET    5  AB 5 GLY J 295  ILE J 296  1  O  GLY J 295   N  LEU J 121           
SHEET    1  AC 8 THR J 225  PHE J 227  0                                        
SHEET    2  AC 8 TYR J 187  KCX J 189  1  N  MET J 188   O  PHE J 227           
SHEET    3  AC 8 ILE J 157  VAL J 160  1  N  VAL J 160   O  KCX J 189           
SHEET    4  AC 8 VAL J 387  GLN J 389  1  O  LEU J 388   N  ILE J 157           
SHEET    5  AC 8 PHE J 363  SER J 367  1  N  PRO J 364   O  VAL J 387           
SHEET    6  AC 8 GLN J 312  HIS J 314  1  N  LEU J 313   O  THR J 365           
SHEET    7  AC 8 ALA J 277  HIS J 281  1  N  GLY J 280   O  GLN J 312           
SHEET    8  AC 8 HIS J 251  ASP J 255  1  N  VAL J 254   O  HIS J 279           
SHEET    1  AD 2 HIS J 341  TYR J 342  0                                        
SHEET    2  AD 2 GLN J 354  LYS J 355 -1  O  GLN J 354   N  TYR J 342           
LINK         C   MET A 188                 N   KCX A 189     1555   1555  1.33  
LINK         C   KCX A 189                 N   ASP A 190     1555   1555  1.33  
LINK         C   MET B 188                 N   KCX B 189     1555   1555  1.33  
LINK         C   KCX B 189                 N   ASP B 190     1555   1555  1.33  
LINK         C   MET C 188                 N   KCX C 189     1555   1555  1.33  
LINK         C   KCX C 189                 N   ASP C 190     1555   1555  1.33  
LINK         C   MET D 188                 N   KCX D 189     1555   1555  1.33  
LINK         C   KCX D 189                 N   ASP D 190     1555   1555  1.33  
LINK         C   MET E 188                 N   KCX E 189     1555   1555  1.33  
LINK         C   KCX E 189                 N   ASP E 190     1555   1555  1.33  
LINK         C   MET F 188                 N   KCX F 189     1555   1555  1.33  
LINK         C   KCX F 189                 N   ASP F 190     1555   1555  1.33  
LINK         C   MET G 188                 N   KCX G 189     1555   1555  1.33  
LINK         C   KCX G 189                 N   ASP G 190     1555   1555  1.33  
LINK         C   MET H 188                 N   KCX H 189     1555   1555  1.33  
LINK         C   KCX H 189                 N   ASP H 190     1555   1555  1.33  
LINK         C   MET I 188                 N   KCX I 189     1555   1555  1.33  
LINK         C   KCX I 189                 N   ASP I 190     1555   1555  1.33  
LINK         C   MET J 188                 N   KCX J 189     1555   1555  1.33  
LINK         C   KCX J 189                 N   ASP J 190     1555   1555  1.33  
LINK         OQ2 KCX A 189                MG    MG A 500     1555   1555  2.08  
LINK         OD1 ASP A 191                MG    MG A 500     1555   1555  1.94  
LINK         OE1 GLU A 192                MG    MG A 500     1555   1555  1.91  
LINK         OQ2 KCX B 189                MG    MG B 500     1555   1555  2.08  
LINK         OD1 ASP B 191                MG    MG B 500     1555   1555  2.13  
LINK         OE1 GLU B 192                MG    MG B 500     1555   1555  2.16  
LINK         OQ2 KCX C 189                MG    MG C 500     1555   1555  1.93  
LINK         OD2 ASP C 191                MG    MG C 500     1555   1555  2.41  
LINK         OE1 GLU C 192                MG    MG C 500     1555   1555  2.15  
LINK         OQ2 KCX D 189                MG    MG D 500     1555   1555  2.10  
LINK         OD1 ASP D 191                MG    MG D 500     1555   1555  1.83  
LINK         OE1 GLU D 192                MG    MG D 500     1555   1555  1.97  
LINK         OQ2 KCX E 189                MG    MG E 500     1555   1555  2.36  
LINK         OD1 ASP E 191                MG    MG E 500     1555   1555  2.12  
LINK         OE1 GLU E 192                MG    MG E 500     1555   1555  2.25  
LINK         OQ2 KCX F 189                MG    MG F 500     1555   1555  2.05  
LINK         OD1 ASP F 191                MG    MG F 500     1555   1555  2.12  
LINK         OE1 GLU F 192                MG    MG F 500     1555   1555  1.98  
LINK         OQ2 KCX G 189                MG    MG G 500     1555   1555  2.04  
LINK         OD1 ASP G 191                MG    MG G 500     1555   1555  2.08  
LINK         OE1 GLU G 192                MG    MG G 500     1555   1555  2.07  
LINK         OQ2 KCX H 189                MG    MG H 500     1555   1555  1.93  
LINK         OE1 GLU H 192                MG    MG H 500     1555   1555  2.36  
LINK         OQ2 KCX I 189                MG    MG I 500     1555   1555  2.01  
LINK         OD1 ASP I 191                MG    MG I 500     1555   1555  2.01  
LINK         OE1 GLU I 192                MG    MG I 500     1555   1555  2.01  
LINK         OQ2 KCX J 189                MG    MG J 500     1555   1555  2.10  
LINK         OD2 ASP J 191                MG    MG J 500     1555   1555  2.25  
LINK         OE1 GLU J 192                MG    MG J 500     1555   1555  2.19  
LINK         O2  CAP A 600                MG    MG A 500     1555   1555  2.37  
LINK         O3  CAP A 600                MG    MG A 500     1555   1555  2.12  
LINK         O7  CAP A 600                MG    MG A 500     1555   1555  2.00  
LINK         O2  CAP B 600                MG    MG B 500     1555   1555  2.19  
LINK         O3  CAP B 600                MG    MG B 500     1555   1555  2.03  
LINK         O7  CAP B 600                MG    MG B 500     1555   1555  1.80  
LINK         O2  CAP C 600                MG    MG C 500     1555   1555  2.43  
LINK         O7  CAP C 600                MG    MG C 500     1555   1555  1.78  
LINK         O2  CAP D 600                MG    MG D 500     1555   1555  2.40  
LINK         O3  CAP D 600                MG    MG D 500     1555   1555  2.21  
LINK         O7  CAP D 600                MG    MG D 500     1555   1555  1.92  
LINK         O2  CAP E 600                MG    MG E 500     1555   1555  2.34  
LINK         O3  CAP E 600                MG    MG E 500     1555   1555  2.27  
LINK         O6  CAP E 600                MG    MG E 500     1555   1555  1.77  
LINK         O2  CAP F 600                MG    MG F 500     1555   1555  2.38  
LINK         O3  CAP F 600                MG    MG F 500     1555   1555  2.08  
LINK         O7  CAP F 600                MG    MG F 500     1555   1555  1.78  
LINK         O2  CAP G 600                MG    MG G 500     1555   1555  2.35  
LINK         O3  CAP G 600                MG    MG G 500     1555   1555  2.06  
LINK         O7  CAP G 600                MG    MG G 500     1555   1555  1.79  
LINK         O2  CAP H 600                MG    MG H 500     1555   1555  2.22  
LINK         O3  CAP H 600                MG    MG H 500     1555   1555  2.42  
LINK         O7  CAP H 600                MG    MG H 500     1555   1555  2.04  
LINK         O2  CAP I 600                MG    MG I 500     1555   1555  2.31  
LINK         O3  CAP I 600                MG    MG I 500     1555   1555  2.04  
LINK         O7  CAP I 600                MG    MG I 500     1555   1555  1.91  
LINK         O2  CAP J 600                MG    MG J 500     1555   1555  2.28  
LINK         O3  CAP J 600                MG    MG J 500     1555   1555  2.25  
LINK         O7  CAP J 600                MG    MG J 500     1555   1555  1.73  
LINK         O3  CAP C 600                MG    MG C 500     1555   1555  2.52  
LINK         OD1 ASP H 191                MG    MG H 500     1555   1555  2.65  
LINK         OD1 ASP C 191                MG    MG C 500     1555   1555  2.89  
CISPEP   1 LYS A  163    PRO A  164          0         4.33                     
CISPEP   2 LYS B  163    PRO B  164          0         3.39                     
CISPEP   3 LYS C  163    PRO C  164          0         4.93                     
CISPEP   4 LYS D  163    PRO D  164          0         8.19                     
CISPEP   5 LYS E  163    PRO E  164          0         5.59                     
CISPEP   6 LYS F  163    PRO F  164          0         5.16                     
CISPEP   7 LYS G  163    PRO G  164          0         5.03                     
CISPEP   8 LYS H  163    PRO H  164          0         6.21                     
CISPEP   9 LYS I  163    PRO I  164          0         5.78                     
CISPEP  10 LYS J  163    PRO J  164          0         6.68                     
SITE     1 AC1 23 LYS A 163  LYS A 165  KCX A 189  ASP A 191                    
SITE     2 AC1 23 GLU A 192  HIS A 281  ARG A 282  HIS A 314                    
SITE     3 AC1 23 LYS A 322  LEU A 323  SER A 367  GLY A 368                    
SITE     4 AC1 23 GLY A 369  GLN A 389  GLY A 391  GLY A 392                    
SITE     5 AC1 23  MG A 500  HOH A 753  HOH A1643  THR H  54                    
SITE     6 AC1 23 TRP H  55  ASN H 111  HOH H1724                               
SITE     1 AC2  6 LYS A 165  KCX A 189  ASP A 191  GLU A 192                    
SITE     2 AC2  6 CAP A 600  ASN H 111                                          
SITE     1 AC3 27 LYS B 163  LYS B 165  KCX B 189  ASP B 191                    
SITE     2 AC3 27 GLU B 192  HIS B 281  ARG B 282  HIS B 314                    
SITE     3 AC3 27 LYS B 322  LEU B 323  SER B 367  GLY B 368                    
SITE     4 AC3 27 GLY B 369  GLN B 389  GLY B 391  GLY B 392                    
SITE     5 AC3 27 HOH B 445  HOH B 482   MG B 500  HOH B 619                    
SITE     6 AC3 27 HOH B1206  HOH B1246  HOH B1922  TRP G  55                    
SITE     7 AC3 27 ASN G 111  HOH G 474  HOH G1621                               
SITE     1 AC4  5 LYS B 163  KCX B 189  ASP B 191  GLU B 192                    
SITE     2 AC4  5 CAP B 600                                                     
SITE     1 AC5 27 LYS C 163  LYS C 165  KCX C 189  ASP C 191                    
SITE     2 AC5 27 GLU C 192  HIS C 281  ARG C 282  HIS C 314                    
SITE     3 AC5 27 LYS C 322  LEU C 323  SER C 367  GLY C 368                    
SITE     4 AC5 27 GLY C 369  GLN C 389  GLY C 391  GLY C 392                    
SITE     5 AC5 27 HOH C 481  HOH C 489  HOH C 497   MG C 500                    
SITE     6 AC5 27 HOH C1211  HOH C1336  HOH C1660  GLU F  49                    
SITE     7 AC5 27 TRP F  55  ASN F 111  HOH F 452                               
SITE     1 AC6  4 KCX C 189  ASP C 191  GLU C 192  CAP C 600                    
SITE     1 AC7 28 LYS D 163  LYS D 165  KCX D 189  ASP D 191                    
SITE     2 AC7 28 GLU D 192  HIS D 281  ARG D 282  HIS D 314                    
SITE     3 AC7 28 LYS D 322  LEU D 323  SER D 367  GLY D 368                    
SITE     4 AC7 28 GLY D 369  GLN D 389  GLY D 391  GLY D 392                    
SITE     5 AC7 28 HOH D 445  HOH D 465  HOH D 475  HOH D 498                    
SITE     6 AC7 28  MG D 500  HOH D 509  HOH D 992  HOH D1580                    
SITE     7 AC7 28 GLU J  49  THR J  54  TRP J  55  ASN J 111                    
SITE     1 AC8  5 LYS D 165  KCX D 189  ASP D 191  GLU D 192                    
SITE     2 AC8  5 CAP D 600                                                     
SITE     1 AC9 24 LYS E 163  LYS E 165  KCX E 189  ASP E 191                    
SITE     2 AC9 24 GLU E 192  HIS E 281  ARG E 282  HIS E 314                    
SITE     3 AC9 24 LYS E 322  LEU E 323  SER E 367  GLY E 368                    
SITE     4 AC9 24 GLY E 369  GLN E 389  GLY E 391  GLY E 392                    
SITE     5 AC9 24 HOH E 452   MG E 500  HOH E 532  HOH E 956                    
SITE     6 AC9 24 HOH E1175  HOH E1679  TRP I  55  ASN I 111                    
SITE     1 BC1  4 KCX E 189  ASP E 191  GLU E 192  CAP E 600                    
SITE     1 BC2 28 GLU C  49  THR C  54  TRP C  55  ASN C 111                    
SITE     2 BC2 28 HOH C 488  HOH C1632  LYS F 163  LYS F 165                    
SITE     3 BC2 28 KCX F 189  ASP F 191  GLU F 192  HIS F 281                    
SITE     4 BC2 28 ARG F 282  HIS F 314  LYS F 322  LEU F 323                    
SITE     5 BC2 28 SER F 367  GLY F 368  GLY F 369  GLN F 389                    
SITE     6 BC2 28 GLY F 391  GLY F 392  HOH F 447  HOH F 460                    
SITE     7 BC2 28 HOH F 485   MG F 500  HOH F1635  HOH F1780                    
SITE     1 BC3  5 LYS F 165  KCX F 189  ASP F 191  GLU F 192                    
SITE     2 BC3  5 CAP F 600                                                     
SITE     1 BC4 28 GLU B  49  TRP B  55  ASN B 111  HOH B 452                    
SITE     2 BC4 28 HOH B 453  LYS G 163  LYS G 165  KCX G 189                    
SITE     3 BC4 28 ASP G 191  GLU G 192  HIS G 281  ARG G 282                    
SITE     4 BC4 28 HIS G 314  LYS G 322  LEU G 323  SER G 367                    
SITE     5 BC4 28 GLY G 368  GLY G 369  GLN G 389  GLY G 391                    
SITE     6 BC4 28 GLY G 392  HOH G 445  HOH G 447  HOH G 454                    
SITE     7 BC4 28 HOH G 463  HOH G 478   MG G 500  HOH G1075                    
SITE     1 BC5  4 KCX G 189  ASP G 191  GLU G 192  CAP G 600                    
SITE     1 BC6 21 TRP A  55  ASN A 111  HOH A1819  LYS H 163                    
SITE     2 BC6 21 LYS H 165  KCX H 189  ASP H 191  GLU H 192                    
SITE     3 BC6 21 HIS H 281  ARG H 282  HIS H 314  LEU H 323                    
SITE     4 BC6 21 SER H 367  GLY H 368  GLY H 369  GLN H 389                    
SITE     5 BC6 21 GLY H 391  GLY H 392   MG H 500  HOH H1277                    
SITE     6 BC6 21 HOH H1918                                                     
SITE     1 BC7  4 KCX H 189  ASP H 191  GLU H 192  CAP H 600                    
SITE     1 BC8 28 GLU E  49  THR E  54  TRP E  55  ASN E 111                    
SITE     2 BC8 28 HOH E 994  LYS I 163  LYS I 165  KCX I 189                    
SITE     3 BC8 28 ASP I 191  GLU I 192  HIS I 281  ARG I 282                    
SITE     4 BC8 28 HIS I 314  LYS I 322  LEU I 323  SER I 367                    
SITE     5 BC8 28 GLY I 368  GLY I 369  GLN I 389  GLY I 391                    
SITE     6 BC8 28 GLY I 392  HOH I 445  HOH I 450  HOH I 455                    
SITE     7 BC8 28  MG I 500  HOH I 540  HOH I 995  HOH I1432                    
SITE     1 BC9  5 ASN E 111  KCX I 189  ASP I 191  GLU I 192                    
SITE     2 BC9  5 CAP I 600                                                     
SITE     1 CC1 26 GLU D  49  TRP D  55  ASN D 111  HOH D1771                    
SITE     2 CC1 26 LYS J 163  LYS J 165  KCX J 189  ASP J 191                    
SITE     3 CC1 26 GLU J 192  HIS J 281  ARG J 282  HIS J 314                    
SITE     4 CC1 26 LYS J 322  LEU J 323  SER J 367  GLY J 368                    
SITE     5 CC1 26 GLY J 369  GLN J 389  GLY J 391  GLY J 392                    
SITE     6 CC1 26 HOH J 475  HOH J 499   MG J 500  HOH J1614                    
SITE     7 CC1 26 HOH J1792  HOH J1936                                          
SITE     1 CC2  4 KCX J 189  ASP J 191  GLU J 192  CAP J 600                    
CRYST1   97.481  246.573  134.830  90.00 104.73  90.00 P 1 21 1     20          
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      0.010258  0.000000  0.002697        0.00000                         
SCALE2      0.000000  0.004056  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007669        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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