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Database: PDB
Entry: 3A12
LinkDB: 3A12
Original site: 3A12 
HEADER    LYASE                                   25-MAR-09   3A12              
TITLE     CRYSTAL STRUCTURE OF TYPE III RUBISCO 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                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PYROCOCCUS KODAKARAENSIS;                       
SOURCE   3 ORGANISM_COMMON: THERMOCOCCUS KODAKARAENSIS;                         
SOURCE   4 ORGANISM_TAXID: 69014;                                               
SOURCE   5 STRAIN: KOD1;                                                        
SOURCE   6 GENE: RBCL, TK2290;                                                  
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3)PLYSS;                        
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET-21A(+)                                
KEYWDS    RIBULOSE-1, 5-BISPHOSPHATE CARBOXYLASE/OXYGENASE, RUBISCO, LYASE,     
KEYWDS   2 CARBON DIOXIDE FIXATION, MAGNESIUM, METAL-BINDING, MONOOXYGENASE,    
KEYWDS   3 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.NISHITANI,M.FUJIHASHI,T.DOI,S.YOSHIDA,H.ATOMI,T.IMANAKA,K.MIKI      
REVDAT   2   02-FEB-11 3A12    1       JRNL                                     
REVDAT   1   07-APR-10 3A12    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.    2.30 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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.39                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 257731                         
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) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 13630                           
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 18587                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.22                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2490                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 975                          
REMARK   3   BIN FREE R VALUE                    : 0.2990                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 34125                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 220                                     
REMARK   3   SOLVENT ATOMS            : 2306                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.08                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.52000                                              
REMARK   3    B22 (A**2) : -2.27000                                             
REMARK   3    B33 (A**2) : -2.25000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.268         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.216         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.146         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.948         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.927                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 35219 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 47835 ; 0.995 ; 1.958       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4354 ; 5.230 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1607 ;29.821 ;23.491       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  5588 ;14.192 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   220 ;19.538 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  5065 ; 0.068 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 27118 ; 0.004 ; 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): 21648 ; 0.421 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 34454 ; 0.822 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 13571 ; 1.274 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 13381 ; 2.142 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3A12 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-MAR-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB028677.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JUN-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
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          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 271962                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
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     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.37900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.900                              
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   (%): 60.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M ACETATE, 0.1M 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 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       86.64350            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      123.18850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       86.64350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      123.18850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 62500 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 124640 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -382.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, E, B                         
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 350   BIOMT1   2 -1.000000  0.000000  0.000000      173.28700            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 62190 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 124360 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -384.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, H, I, J, G                         
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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH G 592  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH I 652  LIES ON A SPECIAL POSITION.                          
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     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     PHE C     5                                                      
REMARK 465     ASP C     6                                                      
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     ILE D     8                                                      
REMARK 465     MET E     1                                                      
REMARK 465     VAL E     2                                                      
REMARK 465     GLU E     3                                                      
REMARK 465     LYS E     4                                                      
REMARK 465     PHE E     5                                                      
REMARK 465     ASP E     6                                                      
REMARK 465     LYS E   426                                                      
REMARK 465     THR E   427                                                      
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     ILE F     8                                                      
REMARK 465     LEU F    58                                                      
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     ILE G     8                                                      
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     THR H     7                                                      
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     THR I     7                                                      
REMARK 465     ILE I     8                                                      
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 465     THR J     7                                                      
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     ILE A   8    CG1  CG2  CD1                                       
REMARK 470     ASP A  10    CG   OD1  OD2                                       
REMARK 470     GLU A  18    CG   CD   OE1  OE2                                  
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     GLU A  65    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 148    CG   CD   CE   NZ                                   
REMARK 470     LYS A 153    CG   CD   CE   NZ                                   
REMARK 470     LYS A 175    CG   CD   CE   NZ                                   
REMARK 470     GLU A 203    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 346    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 429    CG   CD   CE   NZ                                   
REMARK 470     THR B   7    OG1  CG2                                            
REMARK 470     ILE B   8    CG1  CG2  CD1                                       
REMARK 470     ASP B  10    CG   OD1  OD2                                       
REMARK 470     THR B  57    OG1  CG2                                            
REMARK 470     LEU B  58    CG   CD1  CD2                                       
REMARK 470     GLU B  65    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 144    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 203    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 346    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 380    CG   CD   OE1  OE2                                  
REMARK 470     THR C   7    OG1  CG2                                            
REMARK 470     ASP C  10    CG   OD1  OD2                                       
REMARK 470     GLU C  35    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  65    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 153    CG   CD   CE   NZ                                   
REMARK 470     LYS C 211    CG   CD   CE   NZ                                   
REMARK 470     GLU C 346    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 380    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 422    CG   OD1  OD2                                       
REMARK 470     GLU C 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 429    CG   CD   CE   NZ                                   
REMARK 470     ASP D  10    CG   OD1  OD2                                       
REMARK 470     LEU D  58    CG   CD1  CD2                                       
REMARK 470     GLU D  65    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 211    CG   CD   CE   NZ                                   
REMARK 470     LYS D 343    CG   CD   CE   NZ                                   
REMARK 470     GLU D 346    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 429    CG   CD   CE   NZ                                   
REMARK 470     THR E   7    OG1  CG2                                            
REMARK 470     ILE E   8    CG1  CG2  CD1                                       
REMARK 470     GLU E  65    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 153    CG   CD   CE   NZ                                   
REMARK 470     LYS E 211    CG   CD   CE   NZ                                   
REMARK 470     GLU E 346    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 380    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 429    CG   CD   CE   NZ                                   
REMARK 470     GLU E 436    CG   CD   OE1  OE2                                  
REMARK 470     VAL E 441    CG1  CG2                                            
REMARK 470     ASP F  10    CG   OD1  OD2                                       
REMARK 470     TYR F  17    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU F  18    CG   CD   OE1  OE2                                  
REMARK 470     LYS F  21    CG   CD   CE   NZ                                   
REMARK 470     GLU F  40    CG   CD   OE1  OE2                                  
REMARK 470     THR F  57    OG1  CG2                                            
REMARK 470     TYR F  59    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU F  65    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS F 148    CG   CD   CE   NZ                                   
REMARK 470     LYS F 153    CG   CD   CE   NZ                                   
REMARK 470     GLU F 203    CG   CD   OE1  OE2                                  
REMARK 470     LYS F 343    CG   CD   CE   NZ                                   
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 426    CG   CD   CE   NZ                                   
REMARK 470     LYS F 429    CG   CD   CE   NZ                                   
REMARK 470     ASP G  10    CG   OD1  OD2                                       
REMARK 470     LEU G  58    CG   CD1  CD2                                       
REMARK 470     GLU G  65    CG   CD   OE1  OE2                                  
REMARK 470     GLU G 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS G 175    CG   CD   CE   NZ                                   
REMARK 470     GLU G 203    CG   CD   OE1  OE2                                  
REMARK 470     LYS G 211    CG   CD   CE   NZ                                   
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     ILE H   8    CG1  CG2  CD1                                       
REMARK 470     ASP H  10    CG   OD1  OD2                                       
REMARK 470     GLU H  65    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 153    CG   CD   CE   NZ                                   
REMARK 470     LYS H 211    CG   CD   CE   NZ                                   
REMARK 470     GLU H 346    CG   CD   OE1  OE2                                  
REMARK 470     GLU H 380    CG   CD   OE1  OE2                                  
REMARK 470     ASP H 422    CG   OD1  OD2                                       
REMARK 470     GLU H 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 429    CG   CD   CE   NZ                                   
REMARK 470     ASP I  10    CG   OD1  OD2                                       
REMARK 470     TYR I  59    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU I  65    CG   CD   OE1  OE2                                  
REMARK 470     LYS I 148    CG   CD   CE   NZ                                   
REMARK 470     LYS I 211    CG   CD   CE   NZ                                   
REMARK 470     GLU I 423    CG   CD   OE1  OE2                                  
REMARK 470     ILE J   8    CG1  CG2  CD1                                       
REMARK 470     GLU J  65    CG   CD   OE1  OE2                                  
REMARK 470     GLU J 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS J 153    CG   CD   CE   NZ                                   
REMARK 470     SER J 358    OG                                                  
REMARK 470     GLN J 376    CG   CD   OE1  NE2                                  
REMARK 470     GLU J 380    CG   CD   OE1  OE2                                  
REMARK 470     GLN J 410    CG   CD   OE1  NE2                                  
REMARK 470     GLU J 423    CG   CD   OE1  OE2                                  
REMARK 470     LYS J 426    CG   CD   CE   NZ                                   
REMARK 470     THR J 427    OG1  CG2                                            
REMARK 470     LYS J 429    CG   CD   CE   NZ                                   
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    SER A  51      -97.16   -142.26                                   
REMARK 500    ALA A 109       40.54   -140.14                                   
REMARK 500    THR A 195     -106.12   -122.75                                   
REMARK 500    ASN A 200       79.40   -163.21                                   
REMARK 500    ALA A 232     -177.74   -176.08                                   
REMARK 500    MET A 284      -19.12     94.46                                   
REMARK 500    TYR A 357     -116.60     51.48                                   
REMARK 500    ASP B  14       87.07   -153.84                                   
REMARK 500    SER B  51      -96.64   -135.39                                   
REMARK 500    ALA B 109       37.24   -142.62                                   
REMARK 500    THR B 195     -110.66   -117.69                                   
REMARK 500    ASN B 200       83.68   -161.41                                   
REMARK 500    MET B 284      -20.50     94.80                                   
REMARK 500    TYR B 357     -113.90     48.66                                   
REMARK 500    SER C  51      -93.20   -137.59                                   
REMARK 500    ASP C 154      -44.49   -133.30                                   
REMARK 500    THR C 195     -110.68   -114.49                                   
REMARK 500    ASN C 200       84.01   -164.15                                   
REMARK 500    ALA C 232     -175.10   -177.46                                   
REMARK 500    MET C 284      -16.54     92.64                                   
REMARK 500    ALA C 318       30.12     70.37                                   
REMARK 500    TYR C 357     -114.06     52.82                                   
REMARK 500    SER D  51     -111.15   -141.23                                   
REMARK 500    THR D  56     -154.48   -114.45                                   
REMARK 500    ALA D 109       35.19   -145.39                                   
REMARK 500    ASP D 154      -40.53   -130.71                                   
REMARK 500    THR D 195     -108.09   -118.67                                   
REMARK 500    ASN D 200       81.83   -160.87                                   
REMARK 500    ALA D 232     -178.73   -174.26                                   
REMARK 500    MET D 284      -15.94     93.08                                   
REMARK 500    TYR D 357     -114.45     62.27                                   
REMARK 500    SER E  51     -107.85   -142.28                                   
REMARK 500    ALA E 109       39.46   -140.61                                   
REMARK 500    THR E 195     -104.08   -112.97                                   
REMARK 500    SER E 196       58.09   -142.86                                   
REMARK 500    ASN E 200       80.78   -157.40                                   
REMARK 500    ALA E 232     -173.20   -179.35                                   
REMARK 500    ALA E 283      128.72    -39.88                                   
REMARK 500    MET E 284      -22.10     97.56                                   
REMARK 500    TYR E 357     -116.70     46.67                                   
REMARK 500    ASN E 374       26.63   -148.76                                   
REMARK 500    SER F  51      -96.38   -142.89                                   
REMARK 500    THR F  54      144.31   -172.10                                   
REMARK 500    PRO F  60      100.26    -27.59                                   
REMARK 500    HIS F  78      105.54   -177.57                                   
REMARK 500    ALA F 109       38.40   -145.89                                   
REMARK 500    THR F 195     -104.61   -121.32                                   
REMARK 500    ASN F 200       80.14   -160.52                                   
REMARK 500    ALA F 232     -178.88   -171.66                                   
REMARK 500    MET F 284      -20.99     97.22                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      88 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 445  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX A 189   OQ2                                                    
REMARK 620 2 ASP A 191   OD1  88.7                                              
REMARK 620 3 GLU A 192   OE1  85.3  95.0                                        
REMARK 620 4 CAP A 446   O3   84.7 173.4  83.9                                  
REMARK 620 5 CAP A 446   O2   86.0 104.6 158.3  75.4                            
REMARK 620 6 CAP A 446   O7  161.6  99.4 110.1  87.0  76.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 445  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX B 189   OQ2                                                    
REMARK 620 2 ASP B 191   OD1  83.0                                              
REMARK 620 3 GLU B 192   OE1  88.2  85.9                                        
REMARK 620 4 CAP B 446   O7  170.6  99.3 101.0                                  
REMARK 620 5 CAP B 446   O2   94.0 110.1 163.9  76.6                            
REMARK 620 6 CAP B 446   O3   89.1 169.0  86.1  89.7  78.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 445  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX C 189   OQ2                                                    
REMARK 620 2 ASP C 191   OD1  87.2                                              
REMARK 620 3 GLU C 192   OE1  84.9  85.5                                        
REMARK 620 4 CAP C 446   O2   96.4 106.8 167.6                                  
REMARK 620 5 CAP C 446   O7  174.3  98.1  97.6  80.0                            
REMARK 620 6 CAP C 446   O3   84.5 170.5  89.2  78.7  90.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 445  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX D 189   OQ2                                                    
REMARK 620 2 ASP D 191   OD1  91.2                                              
REMARK 620 3 GLU D 192   OE1  87.9  87.8                                        
REMARK 620 4 CAP D 446   O2   98.6 108.6 162.1                                  
REMARK 620 5 CAP D 446   O3   85.2 173.4  86.5  77.5                            
REMARK 620 6 CAP D 446   O7  171.7  96.7  94.8  76.6  87.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 445  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX E 189   OQ2                                                    
REMARK 620 2 ASP E 191   OD2  92.9                                              
REMARK 620 3 GLU E 192   OE1  78.7  76.5                                        
REMARK 620 4 CAP E 446   O3   85.1 159.4  83.0                                  
REMARK 620 5 CAP E 446   O2   94.4 117.6 164.9  83.0                            
REMARK 620 6 CAP E 446   O7  176.3  89.2  98.8  91.8  87.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F 445  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 191   OD1                                                    
REMARK 620 2 GLU F 192   OE1  82.4                                              
REMARK 620 3 CAP F 446   O3  168.4  88.9                                        
REMARK 620 4 CAP F 446   O7   91.4  97.6  82.1                                  
REMARK 620 5 CAP F 446   O2  111.5 162.3  75.7  72.0                            
REMARK 620 6 KCX F 189   OQ2 102.8  98.3  86.0 159.9  89.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G 445  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX G 189   OQ2                                                    
REMARK 620 2 ASP G 191   OD2 100.4                                              
REMARK 620 3 GLU G 192   OE1  92.0  73.9                                        
REMARK 620 4 CAP G 446   O7  169.3  89.5  94.5                                  
REMARK 620 5 CAP G 446   O2   94.8 125.2 157.9  76.1                            
REMARK 620 6 CAP G 446   O3   84.7 157.6  84.2  87.5  75.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H 445  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX H 189   OQ2                                                    
REMARK 620 2 GLU H 192   OE1  77.2                                              
REMARK 620 3 CAP H 446   O7  150.0 103.2                                        
REMARK 620 4 CAP H 446   O2   86.0 151.2  80.0                                  
REMARK 620 5 CAP H 446   O3   76.7  79.7  74.0  73.7                            
REMARK 620 6 ASP H 191   OD2  99.7 118.0 106.0  87.6 161.1                      
REMARK 620 7 ASP H 191   OD1 107.2  76.0 101.8 132.0 153.6  45.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG I 445  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX I 189   OQ2                                                    
REMARK 620 2 ASP I 191   OD1  94.9                                              
REMARK 620 3 GLU I 192   OE1  88.7  89.8                                        
REMARK 620 4 CAP I 446   O2   93.0 108.2 161.7                                  
REMARK 620 5 CAP I 446   O3   83.0 176.5  87.3  74.8                            
REMARK 620 6 CAP I 446   O7  166.9  94.8 100.1  75.6  87.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG J 445  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX J 189   OQ2                                                    
REMARK 620 2 ASP J 191   OD1  92.3                                              
REMARK 620 3 GLU J 192   OE1  82.4  84.1                                        
REMARK 620 4 CAP J 446   O3   86.7 163.7  79.7                                  
REMARK 620 5 CAP J 446   O2   85.2 115.8 157.0  80.3                            
REMARK 620 6 CAP J 446   O7  168.4  91.4 108.9  92.8  83.3                      
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 MG A 445                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A 446                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 445                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B 446                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 445                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C 446                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 445                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D 446                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 445                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 446                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 445                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP F 446                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 445                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G 446                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 445                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H 446                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 445                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP I 446                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG J 445                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP J 446                 
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: 3A13   RELATED DB: PDB                                   
DBREF  3A12 A    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3A12 B    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3A12 C    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3A12 D    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3A12 E    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3A12 F    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3A12 G    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3A12 H    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3A12 I    1   444  UNP    O93627   RBL_PYRKO        1    444             
DBREF  3A12 J    1   444  UNP    O93627   RBL_PYRKO        1    444             
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  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE 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  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE 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  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE 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  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE 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  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE 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  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE 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  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE 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  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE 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  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE 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  GLY LYS TRP ASP VAL ILE GLN ASN ALA ARG ILE 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 3A12 KCX A  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3A12 KCX B  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3A12 KCX C  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3A12 KCX D  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3A12 KCX E  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3A12 KCX F  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3A12 KCX G  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3A12 KCX H  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3A12 KCX I  189  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3A12 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     MG  A 445       1                                                       
HET    CAP  A 446      21                                                       
HET     MG  B 445       1                                                       
HET    CAP  B 446      21                                                       
HET     MG  C 445       1                                                       
HET    CAP  C 446      21                                                       
HET     MG  D 445       1                                                       
HET    CAP  D 446      21                                                       
HET     MG  E 445       1                                                       
HET    CAP  E 446      21                                                       
HET     MG  F 445       1                                                       
HET    CAP  F 446      21                                                       
HET     MG  G 445       1                                                       
HET    CAP  G 446      21                                                       
HET     MG  H 445       1                                                       
HET    CAP  H 446      21                                                       
HET     MG  I 445       1                                                       
HET    CAP  I 446      21                                                       
HET     MG  J 445       1                                                       
HET    CAP  J 446      21                                                       
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE                              
FORMUL   1  KCX    10(C7 H14 N2 O4)                                             
FORMUL  11   MG    10(MG 2+)                                                    
FORMUL  12  CAP    10(C6 H14 O13 P2)                                            
FORMUL  31  HOH   *2306(H2 O)                                                   
HELIX    1   1 TYR A    9  VAL A   13  5                                   5    
HELIX    2   2 THR A   38  SER A   50  1                                  13    
HELIX    3   3 GLU A   63  LEU A   70  1                                   8    
HELIX    4   4 HIS A   94  PHE A   96  5                                   3    
HELIX    5   5 ASN A  100  ALA A  109  1                                  10    
HELIX    6   6 GLY A  110  MET A  115  5                                   6    
HELIX    7   7 PRO A  129  ARG A  134  1                                   6    
HELIX    8   8 PHE A  141  GLU A  151  1                                  11    
HELIX    9   9 SER A  169  ASN A  183  1                                  15    
HELIX   10  10 ARG A  201  GLY A  221  1                                  21    
HELIX   11  11 ASP A  233  LEU A  247  1                                  15    
HELIX   12  12 VAL A  256  GLY A  260  1                                   5    
HELIX   13  13 GLY A  260  GLY A  275  1                                  16    
HELIX   14  14 HIS A  285  ARG A  290  1                                   6    
HELIX   15  15 SER A  297  GLY A  309  1                                  13    
HELIX   16  16 GLY A  326  GLU A  339  1                                  14    
HELIX   17  17 HIS A  371  ASN A  374  5                                   4    
HELIX   18  18 ILE A  375  GLY A  383  1                                   9    
HELIX   19  19 GLY A  391  GLY A  396  1                                   6    
HELIX   20  20 GLY A  400  GLY A  418  1                                  19    
HELIX   21  21 PRO A  420  LYS A  426  1                                   7    
HELIX   22  22 HIS A  428  GLY A  439  1                                  12    
HELIX   23  23 THR B    7  VAL B   13  5                                   7    
HELIX   24  24 THR B   38  SER B   51  1                                  14    
HELIX   25  25 GLU B   63  SER B   71  1                                   9    
HELIX   26  26 HIS B   94  PHE B   96  5                                   3    
HELIX   27  27 ASN B  100  ALA B  109  1                                  10    
HELIX   28  28 GLY B  110  MET B  115  5                                   6    
HELIX   29  29 PRO B  129  ARG B  134  1                                   6    
HELIX   30  30 PHE B  141  GLU B  151  1                                  11    
HELIX   31  31 SER B  169  ASN B  183  1                                  15    
HELIX   32  32 ARG B  201  GLY B  221  1                                  21    
HELIX   33  33 ASP B  233  LEU B  247  1                                  15    
HELIX   34  34 VAL B  256  GLY B  260  1                                   5    
HELIX   35  35 GLY B  260  TYR B  274  1                                  15    
HELIX   36  36 HIS B  285  ARG B  290  1                                   6    
HELIX   37  37 SER B  297  GLY B  309  1                                  13    
HELIX   38  38 GLY B  326  GLU B  339  1                                  14    
HELIX   39  39 HIS B  371  ASN B  374  5                                   4    
HELIX   40  40 ILE B  375  GLY B  383  1                                   9    
HELIX   41  41 GLY B  391  GLY B  396  1                                   6    
HELIX   42  42 GLY B  400  GLY B  418  1                                  19    
HELIX   43  43 PRO B  420  ALA B  425  1                                   6    
HELIX   44  44 HIS B  428  GLY B  439  1                                  12    
HELIX   45  45 ILE C    8  VAL C   13  5                                   6    
HELIX   46  46 THR C   38  SER C   50  1                                  13    
HELIX   47  47 GLU C   63  SER C   71  1                                   9    
HELIX   48  48 HIS C   94  PHE C   96  5                                   3    
HELIX   49  49 ASN C  100  ALA C  109  1                                  10    
HELIX   50  50 GLY C  110  MET C  115  5                                   6    
HELIX   51  51 PRO C  129  ARG C  134  1                                   6    
HELIX   52  52 PHE C  141  GLU C  151  1                                  11    
HELIX   53  53 SER C  169  ASN C  183  1                                  15    
HELIX   54  54 ARG C  201  GLY C  221  1                                  21    
HELIX   55  55 ASP C  233  GLY C  248  1                                  16    
HELIX   56  56 VAL C  256  GLY C  260  1                                   5    
HELIX   57  57 GLY C  260  TYR C  274  1                                  15    
HELIX   58  58 HIS C  285  ARG C  290  1                                   6    
HELIX   59  59 SER C  297  GLY C  309  1                                  13    
HELIX   60  60 GLY C  326  GLU C  339  1                                  14    
HELIX   61  61 HIS C  371  ASN C  374  5                                   4    
HELIX   62  62 ILE C  375  GLY C  383  1                                   9    
HELIX   63  63 GLY C  391  GLY C  396  1                                   6    
HELIX   64  64 GLY C  400  GLN C  417  1                                  18    
HELIX   65  65 PRO C  420  ALA C  425  1                                   6    
HELIX   66  66 HIS C  428  GLY C  439  1                                  12    
HELIX   67  67 TYR D    9  VAL D   13  5                                   5    
HELIX   68  68 THR D   38  SER D   50  1                                  13    
HELIX   69  69 GLU D   63  SER D   71  1                                   9    
HELIX   70  70 HIS D   94  PHE D   96  5                                   3    
HELIX   71  71 ASN D  100  ALA D  109  1                                  10    
HELIX   72  72 GLY D  110  MET D  115  5                                   6    
HELIX   73  73 PRO D  129  ARG D  134  1                                   6    
HELIX   74  74 PHE D  141  GLU D  151  1                                  11    
HELIX   75  75 SER D  169  ASN D  183  1                                  15    
HELIX   76  76 ARG D  201  GLY D  221  1                                  21    
HELIX   77  77 ASP D  233  LEU D  247  1                                  15    
HELIX   78  78 VAL D  256  GLY D  260  1                                   5    
HELIX   79  79 GLY D  260  TYR D  274  1                                  15    
HELIX   80  80 HIS D  285  ARG D  290  1                                   6    
HELIX   81  81 SER D  297  GLY D  309  1                                  13    
HELIX   82  82 GLY D  326  GLU D  339  1                                  14    
HELIX   83  83 HIS D  371  ASN D  374  5                                   4    
HELIX   84  84 ILE D  375  GLY D  383  1                                   9    
HELIX   85  85 GLY D  391  GLY D  396  1                                   6    
HELIX   86  86 GLY D  400  GLY D  418  1                                  19    
HELIX   87  87 PRO D  420  LYS D  426  1                                   7    
HELIX   88  88 HIS D  428  GLY D  439  1                                  12    
HELIX   89  89 ILE E    8  VAL E   13  5                                   6    
HELIX   90  90 THR E   38  SER E   50  1                                  13    
HELIX   91  91 GLU E   63  SER E   71  1                                   9    
HELIX   92  92 HIS E   94  PHE E   96  5                                   3    
HELIX   93  93 ASN E  100  ALA E  109  1                                  10    
HELIX   94  94 GLY E  110  MET E  115  5                                   6    
HELIX   95  95 PRO E  129  ARG E  134  1                                   6    
HELIX   96  96 PHE E  141  GLU E  151  1                                  11    
HELIX   97  97 SER E  169  ASN E  183  1                                  15    
HELIX   98  98 ARG E  201  GLY E  221  1                                  21    
HELIX   99  99 ASP E  233  GLY E  248  1                                  16    
HELIX  100 100 VAL E  256  GLY E  260  1                                   5    
HELIX  101 101 GLY E  260  TYR E  274  1                                  15    
HELIX  102 102 HIS E  285  ARG E  290  1                                   6    
HELIX  103 103 SER E  297  GLY E  309  1                                  13    
HELIX  104 104 GLY E  326  GLU E  339  1                                  14    
HELIX  105 105 ILE E  375  GLY E  383  1                                   9    
HELIX  106 106 GLY E  391  GLY E  396  1                                   6    
HELIX  107 107 GLY E  400  GLN E  417  1                                  18    
HELIX  108 108 PRO E  420  ALA E  425  1                                   6    
HELIX  109 109 HIS E  428  GLY E  439  1                                  12    
HELIX  110 110 TYR F    9  VAL F   13  5                                   5    
HELIX  111 111 THR F   38  SER F   50  1                                  13    
HELIX  112 112 GLU F   63  SER F   71  1                                   9    
HELIX  113 113 HIS F   94  PHE F   96  5                                   3    
HELIX  114 114 ASN F  100  ALA F  109  1                                  10    
HELIX  115 115 GLY F  110  MET F  115  5                                   6    
HELIX  116 116 PRO F  129  ARG F  134  1                                   6    
HELIX  117 117 PHE F  141  GLU F  151  1                                  11    
HELIX  118 118 SER F  169  ASN F  183  1                                  15    
HELIX  119 119 ARG F  201  GLY F  221  1                                  21    
HELIX  120 120 ASP F  233  GLY F  248  1                                  16    
HELIX  121 121 VAL F  256  GLY F  260  1                                   5    
HELIX  122 122 GLY F  260  GLY F  275  1                                  16    
HELIX  123 123 HIS F  285  ARG F  290  1                                   6    
HELIX  124 124 SER F  297  GLY F  309  1                                  13    
HELIX  125 125 GLY F  326  GLU F  339  1                                  14    
HELIX  126 126 HIS F  371  GLY F  383  1                                  13    
HELIX  127 127 GLY F  391  GLY F  396  1                                   6    
HELIX  128 128 GLY F  400  GLN F  417  1                                  18    
HELIX  129 129 PRO F  420  ALA F  425  1                                   6    
HELIX  130 130 HIS F  428  GLY F  439  1                                  12    
HELIX  131 131 TYR G    9  VAL G   13  5                                   5    
HELIX  132 132 THR G   38  SER G   50  1                                  13    
HELIX  133 133 GLU G   63  SER G   71  1                                   9    
HELIX  134 134 HIS G   94  PHE G   96  5                                   3    
HELIX  135 135 ASN G  100  ALA G  109  1                                  10    
HELIX  136 136 GLY G  110  MET G  115  5                                   6    
HELIX  137 137 PRO G  129  ARG G  134  1                                   6    
HELIX  138 138 PHE G  141  GLU G  151  1                                  11    
HELIX  139 139 SER G  169  ASN G  183  1                                  15    
HELIX  140 140 ARG G  201  GLY G  221  1                                  21    
HELIX  141 141 ASP G  233  LEU G  247  1                                  15    
HELIX  142 142 VAL G  256  GLY G  260  1                                   5    
HELIX  143 143 GLY G  260  TYR G  274  1                                  15    
HELIX  144 144 HIS G  285  ARG G  290  1                                   6    
HELIX  145 145 SER G  297  GLY G  309  1                                  13    
HELIX  146 146 GLY G  326  GLU G  339  1                                  14    
HELIX  147 147 HIS G  371  ASN G  374  5                                   4    
HELIX  148 148 ILE G  375  GLY G  383  1                                   9    
HELIX  149 149 GLY G  391  GLY G  396  1                                   6    
HELIX  150 150 GLY G  400  GLY G  418  1                                  19    
HELIX  151 151 PRO G  420  ALA G  425  1                                   6    
HELIX  152 152 HIS G  428  GLY G  439  1                                  12    
HELIX  153 153 TYR H    9  VAL H   13  5                                   5    
HELIX  154 154 THR H   38  SER H   50  1                                  13    
HELIX  155 155 GLU H   63  SER H   71  1                                   9    
HELIX  156 156 HIS H   94  PHE H   96  5                                   3    
HELIX  157 157 ASN H  100  ALA H  109  1                                  10    
HELIX  158 158 GLY H  110  MET H  115  5                                   6    
HELIX  159 159 PRO H  129  ARG H  134  1                                   6    
HELIX  160 160 PHE H  141  GLU H  151  1                                  11    
HELIX  161 161 SER H  169  ASN H  183  1                                  15    
HELIX  162 162 ARG H  201  GLY H  221  1                                  21    
HELIX  163 163 ASP H  233  LEU H  247  1                                  15    
HELIX  164 164 VAL H  256  GLY H  260  1                                   5    
HELIX  165 165 GLY H  260  TYR H  274  1                                  15    
HELIX  166 166 HIS H  285  ARG H  290  1                                   6    
HELIX  167 167 SER H  297  GLY H  309  1                                  13    
HELIX  168 168 GLY H  326  GLU H  339  1                                  14    
HELIX  169 169 HIS H  371  ASN H  374  5                                   4    
HELIX  170 170 ILE H  375  GLY H  383  1                                   9    
HELIX  171 171 GLY H  391  GLY H  396  1                                   6    
HELIX  172 172 GLY H  400  GLN H  417  1                                  18    
HELIX  173 173 PRO H  420  THR H  427  1                                   8    
HELIX  174 174 HIS H  428  GLY H  439  1                                  12    
HELIX  175 175 TYR I    9  VAL I   13  5                                   5    
HELIX  176 176 THR I   38  SER I   50  1                                  13    
HELIX  177 177 GLU I   63  SER I   71  1                                   9    
HELIX  178 178 HIS I   94  PHE I   96  5                                   3    
HELIX  179 179 ASN I  100  ALA I  109  1                                  10    
HELIX  180 180 GLY I  110  MET I  115  5                                   6    
HELIX  181 181 PRO I  129  ARG I  134  1                                   6    
HELIX  182 182 PHE I  141  GLU I  151  1                                  11    
HELIX  183 183 SER I  169  ASN I  183  1                                  15    
HELIX  184 184 ARG I  201  GLY I  221  1                                  21    
HELIX  185 185 ASP I  233  GLY I  248  1                                  16    
HELIX  186 186 VAL I  256  GLY I  260  1                                   5    
HELIX  187 187 GLY I  260  TYR I  274  1                                  15    
HELIX  188 188 HIS I  285  ARG I  290  1                                   6    
HELIX  189 189 SER I  297  GLY I  309  1                                  13    
HELIX  190 190 GLY I  326  GLU I  339  1                                  14    
HELIX  191 191 HIS I  371  ASN I  374  5                                   4    
HELIX  192 192 ILE I  375  GLY I  383  1                                   9    
HELIX  193 193 GLY I  391  GLY I  396  1                                   6    
HELIX  194 194 GLY I  400  GLY I  418  1                                  19    
HELIX  195 195 PRO I  420  LYS I  426  1                                   7    
HELIX  196 196 HIS I  428  GLY I  439  1                                  12    
HELIX  197 197 ILE J    8  VAL J   13  5                                   6    
HELIX  198 198 THR J   38  SER J   50  1                                  13    
HELIX  199 199 GLU J   63  SER J   71  1                                   9    
HELIX  200 200 HIS J   94  PHE J   96  5                                   3    
HELIX  201 201 ASN J  100  ALA J  109  1                                  10    
HELIX  202 202 GLY J  110  MET J  115  5                                   6    
HELIX  203 203 PRO J  129  ARG J  134  1                                   6    
HELIX  204 204 PHE J  141  GLU J  151  1                                  11    
HELIX  205 205 SER J  169  ASN J  183  1                                  15    
HELIX  206 206 ARG J  201  GLY J  221  1                                  21    
HELIX  207 207 ASP J  233  LEU J  247  1                                  15    
HELIX  208 208 VAL J  256  GLY J  260  1                                   5    
HELIX  209 209 GLY J  260  TYR J  274  1                                  15    
HELIX  210 210 HIS J  285  ARG J  290  1                                   6    
HELIX  211 211 SER J  297  GLY J  309  1                                  13    
HELIX  212 212 GLY J  326  GLU J  339  1                                  14    
HELIX  213 213 ILE J  375  GLY J  383  1                                   9    
HELIX  214 214 GLY J  391  GLY J  396  1                                   6    
HELIX  215 215 GLY J  400  GLY J  418  1                                  19    
HELIX  216 216 PRO J  420  ALA J  425  1                                   6    
HELIX  217 217 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  LYS A 119   N  THR A  32           
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  SER A 366           
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 123           
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  ALA B 252           
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  SER B 366           
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  ALA C  90   N  LYS C  73           
SHEET    3   G 5 ASP C  24  PRO C  33 -1  N  VAL C  31   O  TRP C  85           
SHEET    4   G 5 VAL C 118  TYR C 127 -1  O  LYS C 119   N  THR C  32           
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 279   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  SER C 366           
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  ILE D  25   O  TYR D  91           
SHEET    4   J 5 VAL D 118  TYR D 127 -1  O  LYS D 119   N  THR D  32           
SHEET    5   J 5 GLY D 295  ILE D 296  1  O  GLY D 295   N  LEU D 123           
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  SER D 366           
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  ILE E  86   N  HIS E  78           
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  TYR E 127   N  ILE E  26           
SHEET    5   M 5 GLY E 295  ILE E 296  1  O  GLY E 295   N  LEU E 121           
SHEET    1   N 9 ILE E 157  VAL E 160  0                                        
SHEET    2   N 9 TYR E 187  KCX E 189  1  O  KCX E 189   N  VAL E 160           
SHEET    3   N 9 THR E 225  ASN E 229  1  O  PHE E 227   N  MET E 188           
SHEET    4   N 9 HIS E 251  ASP E 255  1  O  MET E 253   N  ALA E 228           
SHEET    5   N 9 ALA E 277  HIS E 281  1  O  ALA E 277   N  ALA E 252           
SHEET    6   N 9 GLN E 312  HIS E 314  1  O  GLN E 312   N  GLY E 280           
SHEET    7   N 9 PHE E 363  SER E 367  1  O  PHE E 363   N  LEU E 313           
SHEET    8   N 9 VAL E 387  GLN E 389  1  O  VAL E 387   N  SER E 366           
SHEET    9   N 9 ILE E 157  VAL E 160  1  N  ILE E 157   O  LEU E 388           
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  76  0                                        
SHEET    2   P 5 TRP F  85  PRO F  92 -1  O  ALA F  90   N  LYS F  73           
SHEET    3   P 5 ASP F  24  PRO F  33 -1  N  ILE F  25   O  TYR F  91           
SHEET    4   P 5 VAL F 118  TYR F 127 -1  O  TYR F 127   N  ILE F  26           
SHEET    5   P 5 GLY F 295  ILE F 296  1  O  GLY F 295   N  LEU F 123           
SHEET    1   Q 8 THR F 225  PHE F 227  0                                        
SHEET    2   Q 8 TYR F 187  KCX F 189  1  N  MET F 188   O  PHE F 227           
SHEET    3   Q 8 ILE F 157  VAL F 160  1  N  VAL F 160   O  KCX F 189           
SHEET    4   Q 8 VAL F 387  GLN F 389  1  O  LEU F 388   N  ILE F 157           
SHEET    5   Q 8 PHE F 363  SER F 367  1  N  SER F 366   O  VAL F 387           
SHEET    6   Q 8 GLN F 312  HIS F 314  1  N  LEU F 313   O  THR F 365           
SHEET    7   Q 8 ALA F 277  HIS F 281  1  N  GLY F 280   O  GLN F 312           
SHEET    8   Q 8 HIS F 251  ASP F 255  1  N  VAL F 254   O  HIS F 281           
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  LYS G 119   N  THR G  32           
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  ALA G 252           
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  SER G 366           
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  PHE H  29   O  VAL H  87           
SHEET    4   V 5 VAL H 118  TYR H 127 -1  O  LYS H 119   N  THR H  32           
SHEET    5   V 5 GLY H 295  ILE H 296  1  O  GLY H 295   N  LEU H 123           
SHEET    1   W 8 THR H 225  PHE H 227  0                                        
SHEET    2   W 8 TYR H 187  KCX H 189  1  N  MET H 188   O  PHE H 227           
SHEET    3   W 8 ILE H 157  VAL H 160  1  N  VAL H 160   O  KCX H 189           
SHEET    4   W 8 VAL H 387  GLN H 389  1  O  LEU H 388   N  ILE H 157           
SHEET    5   W 8 PHE H 363  SER H 367  1  N  PRO H 364   O  VAL H 387           
SHEET    6   W 8 GLN H 312  HIS H 314  1  N  LEU H 313   O  PHE H 363           
SHEET    7   W 8 ALA H 277  HIS H 281  1  N  GLY H 280   O  GLN H 312           
SHEET    8   W 8 HIS H 251  ASP H 255  1  N  VAL H 254   O  HIS H 281           
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 123           
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  ALA I 277   N  ALA I 252           
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  SER I 366           
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  GLU J 124   N  VAL J  28           
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  PHE J 363           
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 281           
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  1.32  
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  1.32  
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 445     1555   1555  2.00  
LINK         OD1 ASP A 191                MG    MG A 445     1555   1555  2.01  
LINK         OE1 GLU A 192                MG    MG A 445     1555   1555  1.97  
LINK         OQ2 KCX B 189                MG    MG B 445     1555   1555  2.01  
LINK         OD1 ASP B 191                MG    MG B 445     1555   1555  1.97  
LINK         OE1 GLU B 192                MG    MG B 445     1555   1555  2.02  
LINK         OQ2 KCX C 189                MG    MG C 445     1555   1555  1.94  
LINK         OD1 ASP C 191                MG    MG C 445     1555   1555  1.94  
LINK         OE1 GLU C 192                MG    MG C 445     1555   1555  2.08  
LINK         OQ2 KCX D 189                MG    MG D 445     1555   1555  1.91  
LINK         OD1 ASP D 191                MG    MG D 445     1555   1555  1.90  
LINK         OE1 GLU D 192                MG    MG D 445     1555   1555  2.14  
LINK         OQ2 KCX E 189                MG    MG E 445     1555   1555  2.06  
LINK         OD2 ASP E 191                MG    MG E 445     1555   1555  2.25  
LINK         OE1 GLU E 192                MG    MG E 445     1555   1555  2.17  
LINK         OD1 ASP F 191                MG    MG F 445     1555   1555  2.01  
LINK         OE1 GLU F 192                MG    MG F 445     1555   1555  1.99  
LINK         OQ2 KCX G 189                MG    MG G 445     1555   1555  2.07  
LINK         OD2 ASP G 191                MG    MG G 445     1555   1555  2.43  
LINK         OE1 GLU G 192                MG    MG G 445     1555   1555  2.06  
LINK         OQ2 KCX H 189                MG    MG H 445     1555   1555  2.22  
LINK         OE1 GLU H 192                MG    MG H 445     1555   1555  2.07  
LINK         OQ2 KCX I 189                MG    MG I 445     1555   1555  1.94  
LINK         OD1 ASP I 191                MG    MG I 445     1555   1555  1.96  
LINK         OE1 GLU I 192                MG    MG I 445     1555   1555  2.00  
LINK         OQ2 KCX J 189                MG    MG J 445     1555   1555  2.08  
LINK         OD1 ASP J 191                MG    MG J 445     1555   1555  2.18  
LINK         OE1 GLU J 192                MG    MG J 445     1555   1555  2.00  
LINK        MG    MG A 445                 O3  CAP A 446     1555   1555  2.14  
LINK        MG    MG A 445                 O2  CAP A 446     1555   1555  2.38  
LINK        MG    MG A 445                 O7  CAP A 446     1555   1555  1.92  
LINK        MG    MG B 445                 O7  CAP B 446     1555   1555  2.02  
LINK        MG    MG B 445                 O2  CAP B 446     1555   1555  2.19  
LINK        MG    MG B 445                 O3  CAP B 446     1555   1555  2.11  
LINK        MG    MG C 445                 O2  CAP C 446     1555   1555  2.38  
LINK        MG    MG C 445                 O7  CAP C 446     1555   1555  1.84  
LINK        MG    MG C 445                 O3  CAP C 446     1555   1555  2.14  
LINK        MG    MG D 445                 O2  CAP D 446     1555   1555  2.29  
LINK        MG    MG D 445                 O3  CAP D 446     1555   1555  2.11  
LINK        MG    MG D 445                 O7  CAP D 446     1555   1555  2.18  
LINK        MG    MG E 445                 O3  CAP E 446     1555   1555  2.04  
LINK        MG    MG E 445                 O2  CAP E 446     1555   1555  2.20  
LINK        MG    MG E 445                 O7  CAP E 446     1555   1555  1.79  
LINK        MG    MG F 445                 O3  CAP F 446     1555   1555  2.21  
LINK        MG    MG F 445                 O7  CAP F 446     1555   1555  2.19  
LINK        MG    MG F 445                 O2  CAP F 446     1555   1555  2.36  
LINK        MG    MG G 445                 O7  CAP G 446     1555   1555  2.09  
LINK        MG    MG G 445                 O2  CAP G 446     1555   1555  2.32  
LINK        MG    MG G 445                 O3  CAP G 446     1555   1555  2.19  
LINK        MG    MG H 445                 O7  CAP H 446     1555   1555  1.98  
LINK        MG    MG H 445                 O2  CAP H 446     1555   1555  2.36  
LINK        MG    MG H 445                 O3  CAP H 446     1555   1555  2.30  
LINK        MG    MG I 445                 O2  CAP I 446     1555   1555  2.28  
LINK        MG    MG I 445                 O3  CAP I 446     1555   1555  2.13  
LINK        MG    MG I 445                 O7  CAP I 446     1555   1555  2.09  
LINK        MG    MG J 445                 O3  CAP J 446     1555   1555  2.08  
LINK        MG    MG J 445                 O2  CAP J 446     1555   1555  2.32  
LINK         OQ2 KCX F 189                MG    MG F 445     1555   1555  1.71  
LINK        MG    MG J 445                 O7  CAP J 446     1555   1555  1.72  
LINK         OD2 ASP H 191                MG    MG H 445     1555   1555  2.73  
LINK         OD1 ASP H 191                MG    MG H 445     1555   1555  2.94  
CISPEP   1 LYS A  163    PRO A  164          0         6.12                     
CISPEP   2 LYS B  163    PRO B  164          0         5.42                     
CISPEP   3 LYS C  163    PRO C  164          0         5.75                     
CISPEP   4 LYS D  163    PRO D  164          0         8.10                     
CISPEP   5 LYS E  163    PRO E  164          0         3.07                     
CISPEP   6 LYS F  163    PRO F  164          0         8.05                     
CISPEP   7 LYS G  163    PRO G  164          0         4.80                     
CISPEP   8 LYS H  163    PRO H  164          0         4.80                     
CISPEP   9 LYS I  163    PRO I  164          0         5.67                     
CISPEP  10 LYS J  163    PRO J  164          0         5.36                     
SITE     1 AC1  5 KCX A 189  ASP A 191  GLU A 192  CAP A 446                    
SITE     2 AC1  5 ASN C 111                                                     
SITE     1 AC2 30 VAL A 161  LYS A 163  LYS A 165  KCX A 189                    
SITE     2 AC2 30 ASP A 191  GLU A 192  HIS A 281  ARG A 282                    
SITE     3 AC2 30 HIS A 314  LYS A 322  LEU A 323  SER A 367                    
SITE     4 AC2 30 GLY A 368  GLY A 369  GLN A 389  GLY A 391                    
SITE     5 AC2 30 GLY A 392   MG A 445  HOH A 521  HOH A 523                    
SITE     6 AC2 30 HOH A 528  HOH A 574  HOH A 579  HOH A 615                    
SITE     7 AC2 30 HOH A 626  HOH A 684  GLU C  49  THR C  54                    
SITE     8 AC2 30 TRP C  55  ASN C 111                                          
SITE     1 AC3  5 ASN B 111  KCX B 189  ASP B 191  GLU B 192                    
SITE     2 AC3  5 CAP B 446                                                     
SITE     1 AC4 29 GLU B  49  TRP B  55  ASN B 111  LYS B 163                    
SITE     2 AC4 29 LYS B 165  KCX B 189  ASP B 191  GLU B 192                    
SITE     3 AC4 29 HIS B 281  ARG B 282  HIS B 314  LYS B 322                    
SITE     4 AC4 29 LEU B 323  SER B 367  GLY B 368  GLY B 369                    
SITE     5 AC4 29 GLN B 389  GLY B 391  GLY B 392   MG B 445                    
SITE     6 AC4 29 HOH B 519  HOH B 521  HOH B 542  HOH B 551                    
SITE     7 AC4 29 HOH B 556  HOH B 559  HOH B 692  HOH B 712                    
SITE     8 AC4 29 HOH B 713                                                     
SITE     1 AC5  4 KCX C 189  ASP C 191  GLU C 192  CAP C 446                    
SITE     1 AC6 28 GLU A  49  TRP A  55  ASN A 111  HOH A 611                    
SITE     2 AC6 28 LYS C 163  LYS C 165  KCX C 189  ASP C 191                    
SITE     3 AC6 28 GLU C 192  HIS C 281  ARG C 282  HIS C 314                    
SITE     4 AC6 28 LYS C 322  LEU C 323  SER C 367  GLY C 368                    
SITE     5 AC6 28 GLY C 369  GLN C 389  GLY C 391  GLY C 392                    
SITE     6 AC6 28  MG C 445  HOH C 524  HOH C 528  HOH C 557                    
SITE     7 AC6 28 HOH C 562  HOH C 591  HOH C 658  HOH C 740                    
SITE     1 AC7  4 KCX D 189  ASP D 191  GLU D 192  CAP D 446                    
SITE     1 AC8 28 LYS D 163  LYS D 165  KCX D 189  ASP D 191                    
SITE     2 AC8 28 GLU D 192  HIS D 281  ARG D 282  HIS D 314                    
SITE     3 AC8 28 LYS D 322  LEU D 323  SER D 367  GLY D 368                    
SITE     4 AC8 28 GLY D 369  GLN D 389  GLY D 391  GLY D 392                    
SITE     5 AC8 28  MG D 445  HOH D 515  HOH D 519  HOH D 524                    
SITE     6 AC8 28 HOH D 537  HOH D 538  HOH D 539  HOH D 665                    
SITE     7 AC8 28 HOH D 716  GLU E  49  TRP E  55  ASN E 111                    
SITE     1 AC9  4 KCX E 189  ASP E 191  GLU E 192  CAP E 446                    
SITE     1 BC1 28 GLU D  49  TRP D  55  ASN D 111  HOH D 682                    
SITE     2 BC1 28 LYS E 163  LYS E 165  KCX E 189  ASP E 191                    
SITE     3 BC1 28 GLU E 192  HIS E 281  ARG E 282  HIS E 314                    
SITE     4 BC1 28 LYS E 322  LEU E 323  SER E 367  GLY E 368                    
SITE     5 BC1 28 GLY E 369  GLN E 389  GLY E 391  GLY E 392                    
SITE     6 BC1 28  MG E 445  HOH E 525  HOH E 532  HOH E 543                    
SITE     7 BC1 28 HOH E 570  HOH E 574  HOH E 580  HOH E 608                    
SITE     1 BC2  4 KCX F 189  ASP F 191  GLU F 192  CAP F 446                    
SITE     1 BC3 27 LYS F 163  LYS F 165  KCX F 189  ASP F 191                    
SITE     2 BC3 27 GLU F 192  HIS F 281  ARG F 282  HIS F 314                    
SITE     3 BC3 27 LYS F 322  LEU F 323  SER F 367  GLY F 368                    
SITE     4 BC3 27 GLY F 369  GLN F 389  GLY F 391  GLY F 392                    
SITE     5 BC3 27  MG F 445  HOH F 519  HOH F 525  HOH F 536                    
SITE     6 BC3 27 HOH F 537  HOH F 556  GLU H  49  THR H  54                    
SITE     7 BC3 27 TRP H  55  ASN H 111  HOH H 513                               
SITE     1 BC4  4 KCX G 189  ASP G 191  GLU G 192  CAP G 446                    
SITE     1 BC5 29 GLU G  49  TRP G  55  ASN G 111  LYS G 163                    
SITE     2 BC5 29 LYS G 165  KCX G 189  ASP G 191  GLU G 192                    
SITE     3 BC5 29 HIS G 281  ARG G 282  HIS G 314  LYS G 322                    
SITE     4 BC5 29 LEU G 323  SER G 367  GLY G 368  GLY G 369                    
SITE     5 BC5 29 GLN G 389  GLY G 391  GLY G 392   MG G 445                    
SITE     6 BC5 29 HOH G 507  HOH G 524  HOH G 529  HOH G 536                    
SITE     7 BC5 29 HOH G 540  HOH G 561  HOH G 574  HOH G 602                    
SITE     8 BC5 29 HOH G 607                                                     
SITE     1 BC6  7 ASN F 111  LYS H 163  LYS H 165  KCX H 189                    
SITE     2 BC6  7 ASP H 191  GLU H 192  CAP H 446                               
SITE     1 BC7 28 GLU F  49  TRP F  55  ASN F 111  LYS H 163                    
SITE     2 BC7 28 LYS H 165  KCX H 189  ASP H 191  GLU H 192                    
SITE     3 BC7 28 HIS H 281  ARG H 282  HIS H 314  LYS H 322                    
SITE     4 BC7 28 LEU H 323  SER H 367  GLY H 368  GLY H 369                    
SITE     5 BC7 28 GLN H 389  GLY H 391  GLY H 392   MG H 445                    
SITE     6 BC7 28 HOH H 520  HOH H 547  HOH H 571  HOH H 584                    
SITE     7 BC7 28 HOH H 595  HOH H 601  HOH H 604  HOH H 613                    
SITE     1 BC8  4 KCX I 189  ASP I 191  GLU I 192  CAP I 446                    
SITE     1 BC9 28 LYS I 163  LYS I 165  KCX I 189  ASP I 191                    
SITE     2 BC9 28 GLU I 192  HIS I 281  ARG I 282  HIS I 314                    
SITE     3 BC9 28 LYS I 322  LEU I 323  SER I 367  GLY I 368                    
SITE     4 BC9 28 GLY I 369  GLN I 389  GLY I 391  GLY I 392                    
SITE     5 BC9 28  MG I 445  HOH I 515  HOH I 518  HOH I 521                    
SITE     6 BC9 28 HOH I 525  HOH I 531  HOH I 616  HOH I 662                    
SITE     7 BC9 28 HOH I 744  GLU J  49  TRP J  55  ASN J 111                    
SITE     1 CC1  6 ASN I 111  LYS J 163  KCX J 189  ASP J 191                    
SITE     2 CC1  6 GLU J 192  CAP J 446                                          
SITE     1 CC2 28 GLU I  49  TRP I  55  ASN I 111  HOH I 603                    
SITE     2 CC2 28 LYS J 163  LYS J 165  KCX J 189  ASP J 191                    
SITE     3 CC2 28 GLU J 192  HIS J 281  ARG J 282  HIS J 314                    
SITE     4 CC2 28 LYS J 322  LEU J 323  SER J 367  GLY J 368                    
SITE     5 CC2 28 GLY J 369  GLN J 389  GLY J 391  GLY J 392                    
SITE     6 CC2 28  MG J 445  HOH J 502  HOH J 546  HOH J 566                    
SITE     7 CC2 28 HOH J 580  HOH J 586  HOH J 587  HOH J 633                    
CRYST1  173.287  246.377  144.589  90.00  90.00  90.00 P 21 21 2    40          
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      0.005771  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004059  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006916        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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