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Database: PDB
Entry: 1RBL
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Original site: 1RBL 
HEADER    LYASE                                   12-MAY-93   1RBL              
TITLE     STRUCTURE DETERMINATION AND REFINEMENT OF RIBULOSE 1,5 BISPHOSPHATE   
TITLE    2 CARBOXYLASE(SLASH)OXYGENASE FROM SYNECHOCOCCUS PCC6301               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE/OXYGENASE (LARGE     
COMPND   3 CHAIN);                                                              
COMPND   4 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   5 EC: 4.1.1.39;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE/OXYGENASE (SMALL     
COMPND   9 CHAIN);                                                              
COMPND  10 CHAIN: M, I, N, J, O, K, P, L;                                       
COMPND  11 EC: 4.1.1.39;                                                        
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS;                        
SOURCE   3 ORGANISM_TAXID: 269084;                                              
SOURCE   4 STRAIN: PCC 6301;                                                    
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS;                        
SOURCE   7 ORGANISM_TAXID: 269084;                                              
SOURCE   8 STRAIN: PCC 6301                                                     
KEYWDS    LYASE(CARBON-CARBON), LYASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.NEWMAN,S.GUTTERIDGE,C.-I.BRANDEN,T.A.JONES                          
REVDAT   4   13-JUL-11 1RBL    1       VERSN                                    
REVDAT   3   24-FEB-09 1RBL    1       VERSN                                    
REVDAT   2   08-MAR-95 1RBL    1       AUTHOR JRNL                              
REVDAT   1   22-JUN-94 1RBL    0                                                
JRNL        AUTH   J.NEWMAN,C.I.BRANDEN,T.A.JONES                               
JRNL        TITL   STRUCTURE DETERMINATION AND REFINEMENT OF RIBULOSE           
JRNL        TITL 2 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE FROM SYNECHOCOCCUS    
JRNL        TITL 3 PCC6301.                                                     
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  49   548 1993              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   15299492                                                     
JRNL        DOI    10.1107/S090744499300530X                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.NEWMAN,S.GUTTERIDGE                                        
REMARK   1  TITL   THE X-RAY STRUCTURE OF SYNECHOCOCCUS RIBULOSE BISPHOSPHATE   
REMARK   1  TITL 2 CARBOXYLASE(SLASH)OXYGENASE ACTIVATED QUATERNARY COMPLEX AT  
REMARK   1  TITL 3 2.2 ANGSTROMS RESOLUTION                                     
REMARK   1  REF    TO BE PUBLISHED                                              
REMARK   1  REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 36496                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 200                                     
REMARK   3   SOLVENT ATOMS            : 292                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.26                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.26                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  THERE ARE SEVEN NON-CRYSTALLOGRAPHIC SYMMETRY OPERATORS,            
REMARK   3  AND THESE MUST BE USED TO GENERATE THE ENTIRE L8S8                  
REMARK   3  MOLECULE.  THE FORMAT OF THE FOLLOWING TRANSFORMATIONS IS           
REMARK   3  FROM X-PLOR, THUS THE SYMMETRY RELATED CHAINS ARE GENERATED         
REMARK   3  BY R'=R*R + T, R=ROTATION MATRIX, T=TRANSLATION.                    
REMARK   4                                                                      
REMARK   4 1RBL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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      111.95000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       99.85000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.95000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       99.85000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      111.95000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.95000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THESE ARE THE ROTATION/TRANSLATION COMPONENTS TO MAP AN      
REMARK 300 LS MONOMER (AM) ONTO THE REST OF THE MOLECULE.  THESE                
REMARK 300 MATRICES WERE OBTAINED FROM X-PLOR AFTER REFINEMENT OF THE           
REMARK 300 WHOLE L8S8 920710.                                                   
REMARK 300                                                                      
REMARK 300 MTRIX 1 TAKES AM TO BI.                                              
REMARK 300                                                                      
REMARK 300 MTRIX 2 TAKES AM TO CN.                                              
REMARK 300                                                                      
REMARK 300 MTRIX 3 TAKES AM TO DJ.                                              
REMARK 300                                                                      
REMARK 300 MTRIX 4 TAKES AM TO EO.                                              
REMARK 300                                                                      
REMARK 300 MTRIX 5 TAKES AM TO FK.                                              
REMARK 300                                                                      
REMARK 300 MTRIX 6 TAKES AM TO GP.                                              
REMARK 300                                                                      
REMARK 300 MTRIX 7 TAKES AM TO HL.                                              
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: HEXADECAMERIC                     
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, M, B, I, C, N, D, J, E,            
REMARK 350                    AND CHAINS: O, F, K, G, P, H, L                   
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 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     SER A    9                                                       
REMARK 475     ALA A   10                                                       
REMARK 475     ALA A   11                                                       
REMARK 475     ARG M  122                                                       
REMARK 475     SER B    9                                                       
REMARK 475     ALA B   10                                                       
REMARK 475     ALA B   11                                                       
REMARK 475     ARG I  122                                                       
REMARK 475     SER C    9                                                       
REMARK 475     ALA C   10                                                       
REMARK 475     ALA C   11                                                       
REMARK 475     ARG N  122                                                       
REMARK 475     SER D    9                                                       
REMARK 475     ALA D   10                                                       
REMARK 475     ALA D   11                                                       
REMARK 475     ARG J  122                                                       
REMARK 475     SER E    9                                                       
REMARK 475     ALA E   10                                                       
REMARK 475     ALA E   11                                                       
REMARK 475     ARG O  122                                                       
REMARK 475     SER F    9                                                       
REMARK 475     ALA F   10                                                       
REMARK 475     ALA F   11                                                       
REMARK 475     ARG K  122                                                       
REMARK 475     SER G    9                                                       
REMARK 475     ALA G   10                                                       
REMARK 475     ALA G   11                                                       
REMARK 475     ARG P  122                                                       
REMARK 475     SER H    9                                                       
REMARK 475     ALA H   10                                                       
REMARK 475     ALA H   11                                                       
REMARK 475     ARG L  122                                                       
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 477  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 FMT A 478   O1                                                     
REMARK 620 2 FMT A 478   O2   43.5                                              
REMARK 620 3 CAP A 476   O2   81.4 100.6                                        
REMARK 620 4 GLU A 204   OE1 106.7 101.5 154.6                                  
REMARK 620 5 CAP A 476   O3   49.3  92.5  70.9  95.7                            
REMARK 620 6 CAP A 476   O7  137.4 166.5  68.6  90.9  91.5                      
REMARK 620 7 ASP A 203   OD1 131.0  89.1 100.5  92.3 171.4  85.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 477  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAP B 476   O3                                                     
REMARK 620 2 CAP B 476   O7   91.5                                              
REMARK 620 3 FMT B 478   O1   49.3 137.4                                        
REMARK 620 4 FMT B 478   O2   92.5 166.5  43.5                                  
REMARK 620 5 CAP B 476   O2   70.9  68.6  81.4 100.6                            
REMARK 620 6 GLU B 204   OE1  95.7  90.9 106.7 101.6 154.6                      
REMARK 620 7 ASP B 203   OD1 171.4  85.1 131.0  89.1 100.5  92.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 477  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 203   OD1                                                    
REMARK 620 2 GLU C 204   OE1  92.2                                              
REMARK 620 3 CAP C 476   O7   85.1  90.9                                        
REMARK 620 4 FMT C 478   O2   89.1 101.6 166.5                                  
REMARK 620 5 CAP C 476   O3  171.4  95.7  91.5  92.5                            
REMARK 620 6 CAP C 476   O2  100.5 154.6  68.6 100.6  70.9                      
REMARK 620 7 FMT C 478   O1  131.0 106.7 137.4  43.5  49.3  81.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 477  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAP D 476   O3                                                     
REMARK 620 2 FMT D 478   O1   49.3                                              
REMARK 620 3 CAP D 476   O2   71.0  81.4                                        
REMARK 620 4 FMT D 478   O2   92.5  43.5 100.6                                  
REMARK 620 5 GLU D 204   OE1  95.7 106.7 154.6 101.5                            
REMARK 620 6 CAP D 476   O7   91.5 137.5  68.6 166.5  90.9                      
REMARK 620 7 ASP D 203   OD1 171.4 131.0 100.5  89.1  92.2  85.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 477  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 FMT E 478   O2                                                     
REMARK 620 2 GLU E 204   OE1 101.5                                              
REMARK 620 3 ASP E 203   OD1  89.1  92.2                                        
REMARK 620 4 FMT E 478   O1   43.5 106.7 131.0                                  
REMARK 620 5 CAP E 476   O2  100.6 154.6 100.5  81.4                            
REMARK 620 6 CAP E 476   O7  166.5  90.9  85.1 137.5  68.6                      
REMARK 620 7 CAP E 476   O3   92.5  95.7 171.4  49.3  71.0  91.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F 477  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 FMT F 478   O2                                                     
REMARK 620 2 FMT F 478   O1   43.5                                              
REMARK 620 3 CAP F 476   O3   92.5  49.3                                        
REMARK 620 4 ASP F 203   OD1  89.1 130.9 171.4                                  
REMARK 620 5 CAP F 476   O2  100.6  81.4  70.9 100.4                            
REMARK 620 6 CAP F 476   O7  166.5 137.5  91.5  85.1  68.6                      
REMARK 620 7 GLU F 204   OE1 101.5 106.7  95.7  92.3 154.6  90.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G 477  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 204   OE1                                                    
REMARK 620 2 FMT G 478   O2  101.5                                              
REMARK 620 3 FMT G 478   O1  106.7  43.5                                        
REMARK 620 4 CAP G 476   O3   95.7  92.5  49.3                                  
REMARK 620 5 CAP G 476   O2  154.6 100.6  81.4  70.9                            
REMARK 620 6 ASP G 203   OD1  92.3  89.1 131.0 171.4 100.5                      
REMARK 620 7 CAP G 476   O7   90.9 166.5 137.5  91.5  68.6  85.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H 477  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAP H 476   O7                                                     
REMARK 620 2 ASP H 203   OD1  85.1                                              
REMARK 620 3 CAP H 476   O2   68.6 100.5                                        
REMARK 620 4 FMT H 478   O2  166.5  89.1 100.6                                  
REMARK 620 5 FMT H 478   O1  137.5 130.9  81.4  43.5                            
REMARK 620 6 CAP H 476   O3   91.5 171.4  70.9  92.5  49.3                      
REMARK 620 7 GLU H 204   OE1  90.9  92.2 154.6 101.5 106.7  95.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 HELICES A, B, BB, C, AND D PRESENTED ON THE HELIX RECORD             
REMARK 650 BELOW ARE THE HELICES OF THE N-TERMINAL DOMAIN.                      
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 SHEET LN1 IS -2X, +1, +2X.                                           
REMARK 700 THE DSSP RUN DID NOT INDICATE THAT STRAND 2 WAS INDEED A             
REMARK 700 STRAND.  HOWEVER, THE A/B BARREL IS CLEARLY THAT, SO STRAND          
REMARK 700 2 IS INCLUDED AS A "REAL" STRAND.                                    
REMARK 700 SHEET SS1 IS +1,-2X,-1.                                              
REMARK 700 THE SHEET PRESENTED AS *LC1* ON SHEET RECORDS BELOW IS               
REMARK 700 ACTUALLY AN EIGHT-STRANDED BETA-BARREL.  THIS IS                     
REMARK 700 REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST              
REMARK 700 AND LAST STRANDS ARE IDENTICAL.                                      
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: MG                                                  
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: THE MAGNESIUM BINDING SITE                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: 1P                                                  
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: THE BINDING SITE OF THE FIRST PHOSPHATE GROUP OF   
REMARK 800  THE CAP                                                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: 2P                                                  
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: THE BINDING SITE OF THE 2ND PHOSPHATE OF CAP       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CAB                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: OTHER RESIDUES INVOLVED IN BINDING THE CAP         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MG2                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: 1P2                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: 2P2                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CA2                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MG3                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: 1P3                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: 2P3                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CA3                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MG4                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: 1P4                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: 2P4                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CA4                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MG5                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: 1P5                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: 2P5                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CA5                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MG6                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: 1P6                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: 2P6                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CA6                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MG7                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: 1P7                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: 2P7                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CA7                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MG8                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: 1P8                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: 2P8                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CA8                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP F 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT E 478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT F 478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT H 478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT G 478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 477                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 477                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 477                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 477                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 477                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 477                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 477                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 477                  
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SEQUENCE ADVISORY NOTICE                                             
REMARK 999      DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.                 
REMARK 999                                                                      
REMARK 999      SWISS-PROT ENTRY NAME: RBL_SYNP6                                
REMARK 999                                                                      
REMARK 999      SWISS-PROT RESIDUE      PDB SEQRES                              
REMARK 999                                                                      
REMARK 999        NAME   NUMBER         NAME   CHAIN  SEQ/INSERT CODE           
REMARK 999        PRO       38          ARG     A       41                      
REMARK 999        VAL       39          PHE     A       42                      
REMARK 999        GLN       88          ALA     A       91                      
REMARK 999        ARG      353          ALA     A      356                      
REMARK 999        ASP       64          ALA     M       76                      
REMARK 999        LYS       66          ALA     M       78                      
REMARK 999        SER       67          ALA     M       79                      
REMARK 999        GLN       97          GLU     M      109                      
REMARK 999        VAL      101          SER     M      113                      
DBREF  1RBL A    9   475  UNP    P00880   RBL_SYNP6        6    472             
DBREF  1RBL M    2   122  UNP    P04716   RBS_SYNP6        1    109             
DBREF  1RBL B    9   475  UNP    P00880   RBL_SYNP6        6    472             
DBREF  1RBL I    2   122  UNP    P04716   RBS_SYNP6        1    109             
DBREF  1RBL C    9   475  UNP    P00880   RBL_SYNP6        6    472             
DBREF  1RBL N    2   122  UNP    P04716   RBS_SYNP6        1    109             
DBREF  1RBL D    9   475  UNP    P00880   RBL_SYNP6        6    472             
DBREF  1RBL J    2   122  UNP    P04716   RBS_SYNP6        1    109             
DBREF  1RBL E    9   475  UNP    P00880   RBL_SYNP6        6    472             
DBREF  1RBL O    2   122  UNP    P04716   RBS_SYNP6        1    109             
DBREF  1RBL F    9   475  UNP    P00880   RBL_SYNP6        6    472             
DBREF  1RBL K    2   122  UNP    P04716   RBS_SYNP6        1    109             
DBREF  1RBL G    9   475  UNP    P00880   RBL_SYNP6        6    472             
DBREF  1RBL P    2   122  UNP    P04716   RBS_SYNP6        1    109             
DBREF  1RBL H    9   475  UNP    P00880   RBL_SYNP6        6    472             
DBREF  1RBL L    2   122  UNP    P04716   RBS_SYNP6        1    109             
SEQADV 1RBL ARG A   41  UNP  P00880    PRO    38 CONFLICT                       
SEQADV 1RBL PHE A   42  UNP  P00880    VAL    39 CONFLICT                       
SEQADV 1RBL ALA A   91  UNP  P00880    GLN    88 CONFLICT                       
SEQADV 1RBL ALA A  356  UNP  P00880    ARG   353 CONFLICT                       
SEQADV 1RBL ALA M   76  UNP  P04716    ASP    63 CONFLICT                       
SEQADV 1RBL ALA M   78  UNP  P04716    LYS    65 CONFLICT                       
SEQADV 1RBL ALA M   79  UNP  P04716    SER    66 CONFLICT                       
SEQADV 1RBL GLU M  109  UNP  P04716    GLN    96 CONFLICT                       
SEQADV 1RBL SER M  113  UNP  P04716    VAL   100 CONFLICT                       
SEQADV 1RBL ARG B   41  UNP  P00880    PRO    38 CONFLICT                       
SEQADV 1RBL PHE B   42  UNP  P00880    VAL    39 CONFLICT                       
SEQADV 1RBL ALA B   91  UNP  P00880    GLN    88 CONFLICT                       
SEQADV 1RBL ALA B  356  UNP  P00880    ARG   353 CONFLICT                       
SEQADV 1RBL ALA I   76  UNP  P04716    ASP    63 CONFLICT                       
SEQADV 1RBL ALA I   78  UNP  P04716    LYS    65 CONFLICT                       
SEQADV 1RBL ALA I   79  UNP  P04716    SER    66 CONFLICT                       
SEQADV 1RBL GLU I  109  UNP  P04716    GLN    96 CONFLICT                       
SEQADV 1RBL SER I  113  UNP  P04716    VAL   100 CONFLICT                       
SEQADV 1RBL ARG C   41  UNP  P00880    PRO    38 CONFLICT                       
SEQADV 1RBL PHE C   42  UNP  P00880    VAL    39 CONFLICT                       
SEQADV 1RBL ALA C   91  UNP  P00880    GLN    88 CONFLICT                       
SEQADV 1RBL ALA C  356  UNP  P00880    ARG   353 CONFLICT                       
SEQADV 1RBL ALA N   76  UNP  P04716    ASP    63 CONFLICT                       
SEQADV 1RBL ALA N   78  UNP  P04716    LYS    65 CONFLICT                       
SEQADV 1RBL ALA N   79  UNP  P04716    SER    66 CONFLICT                       
SEQADV 1RBL GLU N  109  UNP  P04716    GLN    96 CONFLICT                       
SEQADV 1RBL SER N  113  UNP  P04716    VAL   100 CONFLICT                       
SEQADV 1RBL ARG D   41  UNP  P00880    PRO    38 CONFLICT                       
SEQADV 1RBL PHE D   42  UNP  P00880    VAL    39 CONFLICT                       
SEQADV 1RBL ALA D   91  UNP  P00880    GLN    88 CONFLICT                       
SEQADV 1RBL ALA D  356  UNP  P00880    ARG   353 CONFLICT                       
SEQADV 1RBL ALA J   76  UNP  P04716    ASP    63 CONFLICT                       
SEQADV 1RBL ALA J   78  UNP  P04716    LYS    65 CONFLICT                       
SEQADV 1RBL ALA J   79  UNP  P04716    SER    66 CONFLICT                       
SEQADV 1RBL GLU J  109  UNP  P04716    GLN    96 CONFLICT                       
SEQADV 1RBL SER J  113  UNP  P04716    VAL   100 CONFLICT                       
SEQADV 1RBL ARG E   41  UNP  P00880    PRO    38 CONFLICT                       
SEQADV 1RBL PHE E   42  UNP  P00880    VAL    39 CONFLICT                       
SEQADV 1RBL ALA E   91  UNP  P00880    GLN    88 CONFLICT                       
SEQADV 1RBL ALA E  356  UNP  P00880    ARG   353 CONFLICT                       
SEQADV 1RBL ALA O   76  UNP  P04716    ASP    63 CONFLICT                       
SEQADV 1RBL ALA O   78  UNP  P04716    LYS    65 CONFLICT                       
SEQADV 1RBL ALA O   79  UNP  P04716    SER    66 CONFLICT                       
SEQADV 1RBL GLU O  109  UNP  P04716    GLN    96 CONFLICT                       
SEQADV 1RBL SER O  113  UNP  P04716    VAL   100 CONFLICT                       
SEQADV 1RBL ARG F   41  UNP  P00880    PRO    38 CONFLICT                       
SEQADV 1RBL PHE F   42  UNP  P00880    VAL    39 CONFLICT                       
SEQADV 1RBL ALA F   91  UNP  P00880    GLN    88 CONFLICT                       
SEQADV 1RBL ALA F  356  UNP  P00880    ARG   353 CONFLICT                       
SEQADV 1RBL ALA K   76  UNP  P04716    ASP    63 CONFLICT                       
SEQADV 1RBL ALA K   78  UNP  P04716    LYS    65 CONFLICT                       
SEQADV 1RBL ALA K   79  UNP  P04716    SER    66 CONFLICT                       
SEQADV 1RBL GLU K  109  UNP  P04716    GLN    96 CONFLICT                       
SEQADV 1RBL SER K  113  UNP  P04716    VAL   100 CONFLICT                       
SEQADV 1RBL ARG G   41  UNP  P00880    PRO    38 CONFLICT                       
SEQADV 1RBL PHE G   42  UNP  P00880    VAL    39 CONFLICT                       
SEQADV 1RBL ALA G   91  UNP  P00880    GLN    88 CONFLICT                       
SEQADV 1RBL ALA G  356  UNP  P00880    ARG   353 CONFLICT                       
SEQADV 1RBL ALA P   76  UNP  P04716    ASP    63 CONFLICT                       
SEQADV 1RBL ALA P   78  UNP  P04716    LYS    65 CONFLICT                       
SEQADV 1RBL ALA P   79  UNP  P04716    SER    66 CONFLICT                       
SEQADV 1RBL GLU P  109  UNP  P04716    GLN    96 CONFLICT                       
SEQADV 1RBL SER P  113  UNP  P04716    VAL   100 CONFLICT                       
SEQADV 1RBL ARG H   41  UNP  P00880    PRO    38 CONFLICT                       
SEQADV 1RBL PHE H   42  UNP  P00880    VAL    39 CONFLICT                       
SEQADV 1RBL ALA H   91  UNP  P00880    GLN    88 CONFLICT                       
SEQADV 1RBL ALA H  356  UNP  P00880    ARG   353 CONFLICT                       
SEQADV 1RBL ALA L   76  UNP  P04716    ASP    63 CONFLICT                       
SEQADV 1RBL ALA L   78  UNP  P04716    LYS    65 CONFLICT                       
SEQADV 1RBL ALA L   79  UNP  P04716    SER    66 CONFLICT                       
SEQADV 1RBL GLU L  109  UNP  P04716    GLN    96 CONFLICT                       
SEQADV 1RBL SER L  113  UNP  P04716    VAL   100 CONFLICT                       
SEQRES   1 A  467  SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS          
SEQRES   2 A  467  LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR          
SEQRES   3 A  467  ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY          
SEQRES   4 A  467  VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU          
SEQRES   5 A  467  SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU          
SEQRES   6 A  467  LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS          
SEQRES   7 A  467  ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA          
SEQRES   8 A  467  PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER          
SEQRES   9 A  467  VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE          
SEQRES  10 A  467  GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE          
SEQRES  11 A  467  ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO          
SEQRES  12 A  467  PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS          
SEQRES  13 A  467  TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS          
SEQRES  14 A  467  LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR          
SEQRES  15 A  467  GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP          
SEQRES  16 A  467  GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP          
SEQRES  17 A  467  ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN          
SEQRES  18 A  467  ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL          
SEQRES  19 A  467  THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU          
SEQRES  20 A  467  PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP          
SEQRES  21 A  467  PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA          
SEQRES  22 A  467  LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS          
SEQRES  23 A  467  ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS          
SEQRES  24 A  467  GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU          
SEQRES  25 A  467  SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY          
SEQRES  26 A  467  LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL          
SEQRES  27 A  467  ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER          
SEQRES  28 A  467  ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO          
SEQRES  29 A  467  GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP          
SEQRES  30 A  467  HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER          
SEQRES  31 A  467  VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP          
SEQRES  32 A  467  GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU          
SEQRES  33 A  467  GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU          
SEQRES  34 A  467  TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS          
SEQRES  35 A  467  TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS          
SEQRES  36 A  467  GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU              
SEQRES   1 M  109  SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR          
SEQRES   2 M  109  PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA          
SEQRES   3 M  109  ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO          
SEQRES   4 M  109  LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE          
SEQRES   5 M  109  TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA          
SEQRES   6 M  109  ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG          
SEQRES   7 M  109  SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE          
SEQRES   8 M  109  ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL          
SEQRES   9 M  109  HIS ARG PRO GLY ARG                                          
SEQRES   1 B  467  SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS          
SEQRES   2 B  467  LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR          
SEQRES   3 B  467  ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY          
SEQRES   4 B  467  VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU          
SEQRES   5 B  467  SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU          
SEQRES   6 B  467  LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS          
SEQRES   7 B  467  ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA          
SEQRES   8 B  467  PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER          
SEQRES   9 B  467  VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE          
SEQRES  10 B  467  GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE          
SEQRES  11 B  467  ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO          
SEQRES  12 B  467  PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS          
SEQRES  13 B  467  TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS          
SEQRES  14 B  467  LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR          
SEQRES  15 B  467  GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP          
SEQRES  16 B  467  GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP          
SEQRES  17 B  467  ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN          
SEQRES  18 B  467  ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL          
SEQRES  19 B  467  THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU          
SEQRES  20 B  467  PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP          
SEQRES  21 B  467  PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA          
SEQRES  22 B  467  LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS          
SEQRES  23 B  467  ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS          
SEQRES  24 B  467  GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU          
SEQRES  25 B  467  SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY          
SEQRES  26 B  467  LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL          
SEQRES  27 B  467  ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER          
SEQRES  28 B  467  ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO          
SEQRES  29 B  467  GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP          
SEQRES  30 B  467  HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER          
SEQRES  31 B  467  VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP          
SEQRES  32 B  467  GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU          
SEQRES  33 B  467  GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU          
SEQRES  34 B  467  TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS          
SEQRES  35 B  467  TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS          
SEQRES  36 B  467  GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU              
SEQRES   1 I  109  SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR          
SEQRES   2 I  109  PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA          
SEQRES   3 I  109  ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO          
SEQRES   4 I  109  LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE          
SEQRES   5 I  109  TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA          
SEQRES   6 I  109  ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG          
SEQRES   7 I  109  SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE          
SEQRES   8 I  109  ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL          
SEQRES   9 I  109  HIS ARG PRO GLY ARG                                          
SEQRES   1 C  467  SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS          
SEQRES   2 C  467  LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR          
SEQRES   3 C  467  ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY          
SEQRES   4 C  467  VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU          
SEQRES   5 C  467  SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU          
SEQRES   6 C  467  LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS          
SEQRES   7 C  467  ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA          
SEQRES   8 C  467  PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER          
SEQRES   9 C  467  VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE          
SEQRES  10 C  467  GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE          
SEQRES  11 C  467  ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO          
SEQRES  12 C  467  PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS          
SEQRES  13 C  467  TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS          
SEQRES  14 C  467  LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR          
SEQRES  15 C  467  GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP          
SEQRES  16 C  467  GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP          
SEQRES  17 C  467  ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN          
SEQRES  18 C  467  ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL          
SEQRES  19 C  467  THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU          
SEQRES  20 C  467  PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP          
SEQRES  21 C  467  PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA          
SEQRES  22 C  467  LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS          
SEQRES  23 C  467  ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS          
SEQRES  24 C  467  GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU          
SEQRES  25 C  467  SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY          
SEQRES  26 C  467  LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL          
SEQRES  27 C  467  ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER          
SEQRES  28 C  467  ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO          
SEQRES  29 C  467  GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP          
SEQRES  30 C  467  HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER          
SEQRES  31 C  467  VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP          
SEQRES  32 C  467  GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU          
SEQRES  33 C  467  GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU          
SEQRES  34 C  467  TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS          
SEQRES  35 C  467  TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS          
SEQRES  36 C  467  GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU              
SEQRES   1 N  109  SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR          
SEQRES   2 N  109  PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA          
SEQRES   3 N  109  ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO          
SEQRES   4 N  109  LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE          
SEQRES   5 N  109  TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA          
SEQRES   6 N  109  ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG          
SEQRES   7 N  109  SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE          
SEQRES   8 N  109  ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL          
SEQRES   9 N  109  HIS ARG PRO GLY ARG                                          
SEQRES   1 D  467  SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS          
SEQRES   2 D  467  LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR          
SEQRES   3 D  467  ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY          
SEQRES   4 D  467  VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU          
SEQRES   5 D  467  SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU          
SEQRES   6 D  467  LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS          
SEQRES   7 D  467  ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA          
SEQRES   8 D  467  PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER          
SEQRES   9 D  467  VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE          
SEQRES  10 D  467  GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE          
SEQRES  11 D  467  ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO          
SEQRES  12 D  467  PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS          
SEQRES  13 D  467  TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS          
SEQRES  14 D  467  LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR          
SEQRES  15 D  467  GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP          
SEQRES  16 D  467  GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP          
SEQRES  17 D  467  ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN          
SEQRES  18 D  467  ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL          
SEQRES  19 D  467  THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU          
SEQRES  20 D  467  PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP          
SEQRES  21 D  467  PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA          
SEQRES  22 D  467  LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS          
SEQRES  23 D  467  ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS          
SEQRES  24 D  467  GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU          
SEQRES  25 D  467  SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY          
SEQRES  26 D  467  LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL          
SEQRES  27 D  467  ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER          
SEQRES  28 D  467  ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO          
SEQRES  29 D  467  GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP          
SEQRES  30 D  467  HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER          
SEQRES  31 D  467  VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP          
SEQRES  32 D  467  GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU          
SEQRES  33 D  467  GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU          
SEQRES  34 D  467  TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS          
SEQRES  35 D  467  TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS          
SEQRES  36 D  467  GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU              
SEQRES   1 J  109  SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR          
SEQRES   2 J  109  PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA          
SEQRES   3 J  109  ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO          
SEQRES   4 J  109  LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE          
SEQRES   5 J  109  TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA          
SEQRES   6 J  109  ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG          
SEQRES   7 J  109  SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE          
SEQRES   8 J  109  ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL          
SEQRES   9 J  109  HIS ARG PRO GLY ARG                                          
SEQRES   1 E  467  SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS          
SEQRES   2 E  467  LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR          
SEQRES   3 E  467  ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY          
SEQRES   4 E  467  VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU          
SEQRES   5 E  467  SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU          
SEQRES   6 E  467  LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS          
SEQRES   7 E  467  ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA          
SEQRES   8 E  467  PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER          
SEQRES   9 E  467  VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE          
SEQRES  10 E  467  GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE          
SEQRES  11 E  467  ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO          
SEQRES  12 E  467  PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS          
SEQRES  13 E  467  TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS          
SEQRES  14 E  467  LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR          
SEQRES  15 E  467  GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP          
SEQRES  16 E  467  GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP          
SEQRES  17 E  467  ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN          
SEQRES  18 E  467  ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL          
SEQRES  19 E  467  THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU          
SEQRES  20 E  467  PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP          
SEQRES  21 E  467  PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA          
SEQRES  22 E  467  LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS          
SEQRES  23 E  467  ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS          
SEQRES  24 E  467  GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU          
SEQRES  25 E  467  SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY          
SEQRES  26 E  467  LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL          
SEQRES  27 E  467  ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER          
SEQRES  28 E  467  ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO          
SEQRES  29 E  467  GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP          
SEQRES  30 E  467  HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER          
SEQRES  31 E  467  VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP          
SEQRES  32 E  467  GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU          
SEQRES  33 E  467  GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU          
SEQRES  34 E  467  TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS          
SEQRES  35 E  467  TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS          
SEQRES  36 E  467  GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU              
SEQRES   1 O  109  SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR          
SEQRES   2 O  109  PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA          
SEQRES   3 O  109  ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO          
SEQRES   4 O  109  LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE          
SEQRES   5 O  109  TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA          
SEQRES   6 O  109  ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG          
SEQRES   7 O  109  SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE          
SEQRES   8 O  109  ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL          
SEQRES   9 O  109  HIS ARG PRO GLY ARG                                          
SEQRES   1 F  467  SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS          
SEQRES   2 F  467  LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR          
SEQRES   3 F  467  ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY          
SEQRES   4 F  467  VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU          
SEQRES   5 F  467  SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU          
SEQRES   6 F  467  LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS          
SEQRES   7 F  467  ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA          
SEQRES   8 F  467  PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER          
SEQRES   9 F  467  VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE          
SEQRES  10 F  467  GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE          
SEQRES  11 F  467  ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO          
SEQRES  12 F  467  PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS          
SEQRES  13 F  467  TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS          
SEQRES  14 F  467  LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR          
SEQRES  15 F  467  GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP          
SEQRES  16 F  467  GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP          
SEQRES  17 F  467  ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN          
SEQRES  18 F  467  ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL          
SEQRES  19 F  467  THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU          
SEQRES  20 F  467  PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP          
SEQRES  21 F  467  PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA          
SEQRES  22 F  467  LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS          
SEQRES  23 F  467  ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS          
SEQRES  24 F  467  GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU          
SEQRES  25 F  467  SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY          
SEQRES  26 F  467  LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL          
SEQRES  27 F  467  ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER          
SEQRES  28 F  467  ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO          
SEQRES  29 F  467  GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP          
SEQRES  30 F  467  HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER          
SEQRES  31 F  467  VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP          
SEQRES  32 F  467  GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU          
SEQRES  33 F  467  GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU          
SEQRES  34 F  467  TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS          
SEQRES  35 F  467  TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS          
SEQRES  36 F  467  GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU              
SEQRES   1 K  109  SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR          
SEQRES   2 K  109  PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA          
SEQRES   3 K  109  ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO          
SEQRES   4 K  109  LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE          
SEQRES   5 K  109  TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA          
SEQRES   6 K  109  ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG          
SEQRES   7 K  109  SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE          
SEQRES   8 K  109  ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL          
SEQRES   9 K  109  HIS ARG PRO GLY ARG                                          
SEQRES   1 G  467  SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS          
SEQRES   2 G  467  LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR          
SEQRES   3 G  467  ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY          
SEQRES   4 G  467  VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU          
SEQRES   5 G  467  SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU          
SEQRES   6 G  467  LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS          
SEQRES   7 G  467  ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA          
SEQRES   8 G  467  PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER          
SEQRES   9 G  467  VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE          
SEQRES  10 G  467  GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE          
SEQRES  11 G  467  ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO          
SEQRES  12 G  467  PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS          
SEQRES  13 G  467  TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS          
SEQRES  14 G  467  LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR          
SEQRES  15 G  467  GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP          
SEQRES  16 G  467  GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP          
SEQRES  17 G  467  ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN          
SEQRES  18 G  467  ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL          
SEQRES  19 G  467  THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU          
SEQRES  20 G  467  PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP          
SEQRES  21 G  467  PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA          
SEQRES  22 G  467  LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS          
SEQRES  23 G  467  ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS          
SEQRES  24 G  467  GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU          
SEQRES  25 G  467  SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY          
SEQRES  26 G  467  LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL          
SEQRES  27 G  467  ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER          
SEQRES  28 G  467  ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO          
SEQRES  29 G  467  GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP          
SEQRES  30 G  467  HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER          
SEQRES  31 G  467  VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP          
SEQRES  32 G  467  GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU          
SEQRES  33 G  467  GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU          
SEQRES  34 G  467  TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS          
SEQRES  35 G  467  TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS          
SEQRES  36 G  467  GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU              
SEQRES   1 P  109  SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR          
SEQRES   2 P  109  PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA          
SEQRES   3 P  109  ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO          
SEQRES   4 P  109  LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE          
SEQRES   5 P  109  TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA          
SEQRES   6 P  109  ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG          
SEQRES   7 P  109  SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE          
SEQRES   8 P  109  ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL          
SEQRES   9 P  109  HIS ARG PRO GLY ARG                                          
SEQRES   1 H  467  SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS          
SEQRES   2 H  467  LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR          
SEQRES   3 H  467  ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY          
SEQRES   4 H  467  VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU          
SEQRES   5 H  467  SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU          
SEQRES   6 H  467  LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS          
SEQRES   7 H  467  ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA          
SEQRES   8 H  467  PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER          
SEQRES   9 H  467  VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE          
SEQRES  10 H  467  GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE          
SEQRES  11 H  467  ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO          
SEQRES  12 H  467  PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS          
SEQRES  13 H  467  TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS          
SEQRES  14 H  467  LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR          
SEQRES  15 H  467  GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP          
SEQRES  16 H  467  GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP          
SEQRES  17 H  467  ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN          
SEQRES  18 H  467  ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL          
SEQRES  19 H  467  THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU          
SEQRES  20 H  467  PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP          
SEQRES  21 H  467  PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA          
SEQRES  22 H  467  LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS          
SEQRES  23 H  467  ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS          
SEQRES  24 H  467  GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU          
SEQRES  25 H  467  SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY          
SEQRES  26 H  467  LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL          
SEQRES  27 H  467  ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER          
SEQRES  28 H  467  ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO          
SEQRES  29 H  467  GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP          
SEQRES  30 H  467  HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER          
SEQRES  31 H  467  VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP          
SEQRES  32 H  467  GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU          
SEQRES  33 H  467  GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU          
SEQRES  34 H  467  TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS          
SEQRES  35 H  467  TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS          
SEQRES  36 H  467  GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU              
SEQRES   1 L  109  SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR          
SEQRES   2 L  109  PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA          
SEQRES   3 L  109  ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO          
SEQRES   4 L  109  LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE          
SEQRES   5 L  109  TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA          
SEQRES   6 L  109  ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG          
SEQRES   7 L  109  SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE          
SEQRES   8 L  109  ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL          
SEQRES   9 L  109  HIS ARG PRO GLY ARG                                          
HET     MG  A 477       1                                                       
HET     MG  B 477       1                                                       
HET     MG  C 477       1                                                       
HET     MG  D 477       1                                                       
HET     MG  E 477       1                                                       
HET     MG  F 477       1                                                       
HET     MG  G 477       1                                                       
HET     MG  H 477       1                                                       
HET    CAP  A 476      21                                                       
HET    CAP  B 476      21                                                       
HET    CAP  C 476      21                                                       
HET    CAP  D 476      21                                                       
HET    CAP  E 476      21                                                       
HET    CAP  F 476      21                                                       
HET    CAP  G 476      21                                                       
HET    CAP  H 476      21                                                       
HET    FMT  A 478       3                                                       
HET    FMT  B 478       3                                                       
HET    FMT  C 478       3                                                       
HET    FMT  D 478       3                                                       
HET    FMT  E 478       3                                                       
HET    FMT  F 478       3                                                       
HET    FMT  G 478       3                                                       
HET    FMT  H 478       3                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE                              
HETNAM     FMT FORMIC ACID                                                      
FORMUL  17   MG    8(MG 2+)                                                     
FORMUL  25  CAP    8(C6 H14 O13 P2)                                             
FORMUL  33  FMT    8(C H2 O2)                                                   
FORMUL  41  HOH   *292(H2 O)                                                    
HELIX    1   A LYS A   21  TYR A   24  1SEE REMARK 8.                      4    
HELIX    2   B ALA A   50  GLU A   60  1SEE REMARK 8.                     11    
HELIX    3  BB MET A   77  TYR A   80  1SEE REMARK 8.                      4    
HELIX    4   C VAL A  113  VAL A  121  1SEE REMARK 8.                      9    
HELIX    5   D VAL A  142  VAL A  145  1SEE REMARK 8.                      4    
HELIX    6   E ILE A  155  LEU A  162  1LINKS N-TERM & C-TERM DOMAINS      8    
HELIX    7   1 ALA A  182  ARG A  194  1FIRST HELIX OF A/B BARREL         13    
HELIX    8   2 TRP A  214  THR A  232  12ND HELIX OF A/B BARREL           19    
HELIX    9   3 CYS A  247  GLU A  259  13RD HELIX OF A/B BARREL           13    
HELIX   10   4 PHE A  269  ASN A  287  14TH HELIX OF A/B BARREL           19    
HELIX   11   F HIS A  298  ASP A  302  1                                   5    
HELIX   12   5 PHE A  311  SER A  321  15TH HELIX OF A/B BARREL           11    
HELIX   13   6 LYS A  339  ARG A  350  16TH HELIX OF A/B BARREL           12    
HELIX   14   7 MET A  387  PHE A  394  17TH HELIX OF A/B BARREL            8    
HELIX   15   P GLY A  404  LEU A  407  1P FOR PHOSPHATE BINDING HELIX      4    
HELIX   16   8 ASN A  413  GLU A  433  18TH HELIX OF A/B BARREL           21    
HELIX   17   G LEU A  437  TRP A  451  1                                  15    
HELIX   18   H PRO A  453  TRP A  462  1                                  10    
HELIX   19  B' TYR A   80  GLU A   93  12ND HELIX - SMALL SUBUNIT         14    
HELIX   20   A LYS B   21  TYR B   24  1SEE REMARK 8.                      4    
HELIX   21   B ALA B   50  GLU B   60  1SEE REMARK 8.                     11    
HELIX   22  BB MET B   77  TYR B   80  1SEE REMARK 8.                      4    
HELIX   23   C VAL B  113  VAL B  121  1SEE REMARK 8.                      9    
HELIX   24   D VAL B  142  VAL B  145  1SEE REMARK 8.                      4    
HELIX   25   E ILE B  155  LEU B  162  1LINKS N-TERM & C-TERM DOMAINS      8    
HELIX   26   1 ALA B  182  ARG B  194  1FIRST HELIX OF A/B BARREL         13    
HELIX   27   2 TRP B  214  THR B  232  12ND HELIX OF A/B BARREL           19    
HELIX   28   3 CYS B  247  GLU B  259  13RD HELIX OF A/B BARREL           13    
HELIX   29   4 PHE B  269  ASN B  287  14TH HELIX OF A/B BARREL           19    
HELIX   30   F HIS B  298  ASP B  302  1                                   5    
HELIX   31   5 PHE B  311  SER B  321  15TH HELIX OF A/B BARREL           11    
HELIX   32   6 LYS B  339  ARG B  350  16TH HELIX OF A/B BARREL           12    
HELIX   33   7 MET B  387  PHE B  394  17TH HELIX OF A/B BARREL            8    
HELIX   34   P GLY B  404  LEU B  407  1P FOR PHOSPHATE BINDING HELIX      4    
HELIX   35   8 ASN B  413  GLU B  433  18TH HELIX OF A/B BARREL           21    
HELIX   36   G LEU B  437  TRP B  451  1                                  15    
HELIX   37   H PRO B  453  TRP B  462  1                                  10    
HELIX   38  B' TYR B   80  GLU B   93  12ND HELIX - SMALL SUBUNIT         14    
HELIX   39   A LYS C   21  TYR C   24  1SEE REMARK 8.                      4    
HELIX   40   B ALA C   50  GLU C   60  1SEE REMARK 8.                     11    
HELIX   41  BB MET C   77  TYR C   80  1SEE REMARK 8.                      4    
HELIX   42   C VAL C  113  VAL C  121  1SEE REMARK 8.                      9    
HELIX   43   D VAL C  142  VAL C  145  1SEE REMARK 8.                      4    
HELIX   44   E ILE C  155  LEU C  162  1LINKS N-TERM & C-TERM DOMAINS      8    
HELIX   45   1 ALA C  182  ARG C  194  1FIRST HELIX OF A/B BARREL         13    
HELIX   46   2 TRP C  214  THR C  232  12ND HELIX OF A/B BARREL           19    
HELIX   47   3 CYS C  247  GLU C  259  13RD HELIX OF A/B BARREL           13    
HELIX   48   4 PHE C  269  ASN C  287  14TH HELIX OF A/B BARREL           19    
HELIX   49   F HIS C  298  ASP C  302  1                                   5    
HELIX   50   5 PHE C  311  SER C  321  15TH HELIX OF A/B BARREL           11    
HELIX   51   6 LYS C  339  ARG C  350  16TH HELIX OF A/B BARREL           12    
HELIX   52   7 MET C  387  PHE C  394  17TH HELIX OF A/B BARREL            8    
HELIX   53   P GLY C  404  LEU C  407  1P FOR PHOSPHATE BINDING HELIX      4    
HELIX   54   8 ASN C  413  GLU C  433  18TH HELIX OF A/B BARREL           21    
HELIX   55   G LEU C  437  TRP C  451  1                                  15    
HELIX   56   H PRO C  453  TRP C  462  1                                  10    
HELIX   57  B' TYR C   80  GLU C   93  12ND HELIX - SMALL SUBUNIT         14    
HELIX   58   A LYS D   21  TYR D   24  1SEE REMARK 8.                      4    
HELIX   59   B ALA D   50  GLU D   60  1SEE REMARK 8.                     11    
HELIX   60  BB MET D   77  TYR D   80  1SEE REMARK 8.                      4    
HELIX   61   C VAL D  113  VAL D  121  1SEE REMARK 8.                      9    
HELIX   62   D VAL D  142  VAL D  145  1SEE REMARK 8.                      4    
HELIX   63   E ILE D  155  LEU D  162  1LINKS N-TERM & C-TERM DOMAINS      8    
HELIX   64   1 ALA D  182  ARG D  194  1FIRST HELIX OF A/B BARREL         13    
HELIX   65   2 TRP D  214  THR D  232  12ND HELIX OF A/B BARREL           19    
HELIX   66   3 CYS D  247  GLU D  259  13RD HELIX OF A/B BARREL           13    
HELIX   67   4 PHE D  269  ASN D  287  14TH HELIX OF A/B BARREL           19    
HELIX   68   F HIS D  298  ASP D  302  1                                   5    
HELIX   69   5 PHE D  311  SER D  321  15TH HELIX OF A/B BARREL           11    
HELIX   70   6 LYS D  339  ARG D  350  16TH HELIX OF A/B BARREL           12    
HELIX   71   7 MET D  387  PHE D  394  17TH HELIX OF A/B BARREL            8    
HELIX   72   P GLY D  404  LEU D  407  1P FOR PHOSPHATE BINDING HELIX      4    
HELIX   73   8 ASN D  413  GLU D  433  18TH HELIX OF A/B BARREL           21    
HELIX   74   G LEU D  437  TRP D  451  1                                  15    
HELIX   75   H PRO D  453  TRP D  462  1                                  10    
HELIX   76  B' TYR D   80  GLU D   93  12ND HELIX - SMALL SUBUNIT         14    
HELIX   77   A LYS E   21  TYR E   24  1SEE REMARK 8.                      4    
HELIX   78   B ALA E   50  GLU E   60  1SEE REMARK 8.                     11    
HELIX   79  BB MET E   77  TYR E   80  1SEE REMARK 8.                      4    
HELIX   80   C VAL E  113  VAL E  121  1SEE REMARK 8.                      9    
HELIX   81   D VAL E  142  VAL E  145  1SEE REMARK 8.                      4    
HELIX   82   E ILE E  155  LEU E  162  1LINKS N-TERM & C-TERM DOMAINS      8    
HELIX   83   1 ALA E  182  ARG E  194  1FIRST HELIX OF A/B BARREL         13    
HELIX   84   2 TRP E  214  THR E  232  12ND HELIX OF A/B BARREL           19    
HELIX   85   3 CYS E  247  GLU E  259  13RD HELIX OF A/B BARREL           13    
HELIX   86   4 PHE E  269  ASN E  287  14TH HELIX OF A/B BARREL           19    
HELIX   87   F HIS E  298  ASP E  302  1                                   5    
HELIX   88   5 PHE E  311  SER E  321  15TH HELIX OF A/B BARREL           11    
HELIX   89   6 LYS E  339  ARG E  350  16TH HELIX OF A/B BARREL           12    
HELIX   90   7 MET E  387  PHE E  394  17TH HELIX OF A/B BARREL            8    
HELIX   91   P GLY E  404  LEU E  407  1P FOR PHOSPHATE BINDING HELIX      4    
HELIX   92   8 ASN E  413  GLU E  433  18TH HELIX OF A/B BARREL           21    
HELIX   93   G LEU E  437  TRP E  451  1                                  15    
HELIX   94   H PRO E  453  TRP E  462  1                                  10    
HELIX   95  B' TYR E   80  GLU E   93  12ND HELIX - SMALL SUBUNIT         14    
HELIX   96   A LYS F   21  TYR F   24  1SEE REMARK 8.                      4    
HELIX   97   B ALA F   50  GLU F   60  1SEE REMARK 8.                     11    
HELIX   98  BB MET F   77  TYR F   80  1SEE REMARK 8.                      4    
HELIX   99   C VAL F  113  VAL F  121  1SEE REMARK 8.                      9    
HELIX  100   D VAL F  142  VAL F  145  1SEE REMARK 8.                      4    
HELIX  101   E ILE F  155  LEU F  162  1LINKS N-TERM & C-TERM DOMAINS      8    
HELIX  102   1 ALA F  182  ARG F  194  1FIRST HELIX OF A/B BARREL         13    
HELIX  103   2 TRP F  214  THR F  232  12ND HELIX OF A/B BARREL           19    
HELIX  104   3 CYS F  247  GLU F  259  13RD HELIX OF A/B BARREL           13    
HELIX  105   4 PHE F  269  ASN F  287  14TH HELIX OF A/B BARREL           19    
HELIX  106   F HIS F  298  ASP F  302  1                                   5    
HELIX  107   5 PHE F  311  SER F  321  15TH HELIX OF A/B BARREL           11    
HELIX  108   6 LYS F  339  ARG F  350  16TH HELIX OF A/B BARREL           12    
HELIX  109   7 MET F  387  PHE F  394  17TH HELIX OF A/B BARREL            8    
HELIX  110   P GLY F  404  LEU F  407  1P FOR PHOSPHATE BINDING HELIX      4    
HELIX  111   8 ASN F  413  GLU F  433  18TH HELIX OF A/B BARREL           21    
HELIX  112   G LEU F  437  TRP F  451  1                                  15    
HELIX  113   H PRO F  453  TRP F  462  1                                  10    
HELIX  114  B' TYR F   80  GLU F   93  12ND HELIX - SMALL SUBUNIT         14    
HELIX  115   A LYS G   21  TYR G   24  1SEE REMARK 8.                      4    
HELIX  116   B ALA G   50  GLU G   60  1SEE REMARK 8.                     11    
HELIX  117  BB MET G   77  TYR G   80  1SEE REMARK 8.                      4    
HELIX  118   C VAL G  113  VAL G  121  1SEE REMARK 8.                      9    
HELIX  119   D VAL G  142  VAL G  145  1SEE REMARK 8.                      4    
HELIX  120   E ILE G  155  LEU G  162  1LINKS N-TERM & C-TERM DOMAINS      8    
HELIX  121   1 ALA G  182  ARG G  194  1FIRST HELIX OF A/B BARREL         13    
HELIX  122   2 TRP G  214  THR G  232  12ND HELIX OF A/B BARREL           19    
HELIX  123   3 CYS G  247  GLU G  259  13RD HELIX OF A/B BARREL           13    
HELIX  124   4 PHE G  269  ASN G  287  14TH HELIX OF A/B BARREL           19    
HELIX  125   F HIS G  298  ASP G  302  1                                   5    
HELIX  126   5 PHE G  311  SER G  321  15TH HELIX OF A/B BARREL           11    
HELIX  127   6 LYS G  339  ARG G  350  16TH HELIX OF A/B BARREL           12    
HELIX  128   7 MET G  387  PHE G  394  17TH HELIX OF A/B BARREL            8    
HELIX  129   P GLY G  404  LEU G  407  1P FOR PHOSPHATE BINDING HELIX      4    
HELIX  130   8 ASN G  413  GLU G  433  18TH HELIX OF A/B BARREL           21    
HELIX  131   G LEU G  437  TRP G  451  1                                  15    
HELIX  132   H PRO G  453  TRP G  462  1                                  10    
HELIX  133  B' TYR G   80  GLU G   93  12ND HELIX - SMALL SUBUNIT         14    
HELIX  134   A LYS H   21  TYR H   24  1SEE REMARK 8.                      4    
HELIX  135   B ALA H   50  GLU H   60  1SEE REMARK 8.                     11    
HELIX  136  BB MET H   77  TYR H   80  1SEE REMARK 8.                      4    
HELIX  137   C VAL H  113  VAL H  121  1SEE REMARK 8.                      9    
HELIX  138   D VAL H  142  VAL H  145  1SEE REMARK 8.                      4    
HELIX  139   E ILE H  155  LEU H  162  1LINKS N-TERM & C-TERM DOMAINS      8    
HELIX  140   1 ALA H  182  ARG H  194  1FIRST HELIX OF A/B BARREL         13    
HELIX  141   2 TRP H  214  THR H  232  12ND HELIX OF A/B BARREL           19    
HELIX  142   3 CYS H  247  GLU H  259  13RD HELIX OF A/B BARREL           13    
HELIX  143   4 PHE H  269  ASN H  287  14TH HELIX OF A/B BARREL           19    
HELIX  144   F HIS H  298  ASP H  302  1                                   5    
HELIX  145   5 PHE H  311  SER H  321  15TH HELIX OF A/B BARREL           11    
HELIX  146   6 LYS H  339  ARG H  350  16TH HELIX OF A/B BARREL           12    
HELIX  147   7 MET H  387  PHE H  394  17TH HELIX OF A/B BARREL            8    
HELIX  148   P GLY H  404  LEU H  407  1P FOR PHOSPHATE BINDING HELIX      4    
HELIX  149   8 ASN H  413  GLU H  433  18TH HELIX OF A/B BARREL           21    
HELIX  150   G LEU H  437  TRP H  451  1                                  15    
HELIX  151   H PRO H  453  TRP H  462  1                                  10    
HELIX  152  B' TYR H   80  GLU H   93  12ND HELIX - SMALL SUBUNIT         14    
SHEET    1 LN1 4 LYS A  83  PRO A  89  0                                        
SHEET    2 LN1 4 SER A  96  TYR A 103 -1                                        
SHEET    3 LN1 4 LEU A  36  PRO A  44 -1                                        
SHEET    4 LN1 4 ILE A 130  ARG A 139 -1                                        
SHEET    1 LC1 9 MET A 169  GLY A 171  0                                        
SHEET    2 LC1 9 THR A 200  ASP A 202  1                                        
SHEET    3 LC1 9 LEU A 240  ASN A 241  1                                        
SHEET    4 LC1 9 ILE A 264  ASP A 268  1                                        
SHEET    5 LC1 9 LEU A 290  HIS A 294  1                                        
SHEET    6 LC1 9 HIS A 325  HIS A 327  1                                        
SHEET    7 LC1 9 LEU A 375  SER A 379  1                                        
SHEET    8 LC1 9 VAL A 399  GLN A 401  1                                        
SHEET    9 LC1 9 MET A 169  GLY A 171  1                                        
SHEET    1 SS1 4 THR M  68  MET M  69  0                                        
SHEET    2 SS1 4 HIS M  39  ASN M  45 -1                                        
SHEET    3 SS1 4 TYR M  98  ASP M 105 -1                                        
SHEET    4 SS1 4 CYS M 110  HIS M 118 -1                                        
SHEET    1 LN2 4 LYS B  83  PRO B  89  0                                        
SHEET    2 LN2 4 SER B  96  TYR B 103 -1                                        
SHEET    3 LN2 4 LEU B  36  PRO B  44 -1                                        
SHEET    4 LN2 4 ILE B 130  ARG B 139 -1                                        
SHEET    1 LC2 9 MET B 169  GLY B 171  0                                        
SHEET    2 LC2 9 THR B 200  ASP B 202  1                                        
SHEET    3 LC2 9 LEU B 240  ASN B 241  1                                        
SHEET    4 LC2 9 ILE B 264  ASP B 268  1                                        
SHEET    5 LC2 9 LEU B 290  HIS B 294  1                                        
SHEET    6 LC2 9 HIS B 325  HIS B 327  1                                        
SHEET    7 LC2 9 LEU B 375  SER B 379  1                                        
SHEET    8 LC2 9 VAL B 399  GLN B 401  1                                        
SHEET    9 LC2 9 MET B 169  GLY B 171  1                                        
SHEET    1 SS2 4 THR I  68  MET I  69  0                                        
SHEET    2 SS2 4 HIS I  39  ASN I  45 -1                                        
SHEET    3 SS2 4 TYR I  98  ASP I 105 -1                                        
SHEET    4 SS2 4 CYS I 110  HIS I 118 -1                                        
SHEET    1 LN3 4 LYS C  83  PRO C  89  0                                        
SHEET    2 LN3 4 SER C  96  TYR C 103 -1                                        
SHEET    3 LN3 4 LEU C  36  PRO C  44 -1                                        
SHEET    4 LN3 4 ILE C 130  ARG C 139 -1                                        
SHEET    1 LC3 9 MET C 169  GLY C 171  0                                        
SHEET    2 LC3 9 THR C 200  ASP C 202  1                                        
SHEET    3 LC3 9 LEU C 240  ASN C 241  1                                        
SHEET    4 LC3 9 ILE C 264  ASP C 268  1                                        
SHEET    5 LC3 9 LEU C 290  HIS C 294  1                                        
SHEET    6 LC3 9 HIS C 325  HIS C 327  1                                        
SHEET    7 LC3 9 LEU C 375  SER C 379  1                                        
SHEET    8 LC3 9 VAL C 399  GLN C 401  1                                        
SHEET    9 LC3 9 MET C 169  GLY C 171  1                                        
SHEET    1 SS3 4 THR N  68  MET N  69  0                                        
SHEET    2 SS3 4 HIS N  39  ASN N  45 -1                                        
SHEET    3 SS3 4 TYR N  98  ASP N 105 -1                                        
SHEET    4 SS3 4 CYS N 110  HIS N 118 -1                                        
SHEET    1 LN4 4 LYS D  83  PRO D  89  0                                        
SHEET    2 LN4 4 SER D  96  TYR D 103 -1                                        
SHEET    3 LN4 4 LEU D  36  PRO D  44 -1                                        
SHEET    4 LN4 4 ILE D 130  ARG D 139 -1                                        
SHEET    1 LC4 9 MET D 169  GLY D 171  0                                        
SHEET    2 LC4 9 THR D 200  ASP D 202  1                                        
SHEET    3 LC4 9 LEU D 240  ASN D 241  1                                        
SHEET    4 LC4 9 ILE D 264  ASP D 268  1                                        
SHEET    5 LC4 9 LEU D 290  HIS D 294  1                                        
SHEET    6 LC4 9 HIS D 325  HIS D 327  1                                        
SHEET    7 LC4 9 LEU D 375  SER D 379  1                                        
SHEET    8 LC4 9 VAL D 399  GLN D 401  1                                        
SHEET    9 LC4 9 MET D 169  GLY D 171  1                                        
SHEET    1 SS4 4 THR J  68  MET J  69  0                                        
SHEET    2 SS4 4 HIS J  39  ASN J  45 -1                                        
SHEET    3 SS4 4 TYR J  98  ASP J 105 -1                                        
SHEET    4 SS4 4 CYS J 110  HIS J 118 -1                                        
SHEET    1 LN5 4 LYS E  83  PRO E  89  0                                        
SHEET    2 LN5 4 SER E  96  TYR E 103 -1                                        
SHEET    3 LN5 4 LEU E  36  PRO E  44 -1                                        
SHEET    4 LN5 4 ILE E 130  ARG E 139 -1                                        
SHEET    1 LC5 9 MET E 169  GLY E 171  0                                        
SHEET    2 LC5 9 THR E 200  ASP E 202  1                                        
SHEET    3 LC5 9 LEU E 240  ASN E 241  1                                        
SHEET    4 LC5 9 ILE E 264  ASP E 268  1                                        
SHEET    5 LC5 9 LEU E 290  HIS E 294  1                                        
SHEET    6 LC5 9 HIS E 325  HIS E 327  1                                        
SHEET    7 LC5 9 LEU E 375  SER E 379  1                                        
SHEET    8 LC5 9 VAL E 399  GLN E 401  1                                        
SHEET    9 LC5 9 MET E 169  GLY E 171  1                                        
SHEET    1 SS5 4 THR O  68  MET O  69  0                                        
SHEET    2 SS5 4 HIS O  39  ASN O  45 -1                                        
SHEET    3 SS5 4 TYR O  98  ASP O 105 -1                                        
SHEET    4 SS5 4 CYS O 110  HIS O 118 -1                                        
SHEET    1 LN6 4 LYS F  83  PRO F  89  0                                        
SHEET    2 LN6 4 SER F  96  TYR F 103 -1                                        
SHEET    3 LN6 4 LEU F  36  PRO F  44 -1                                        
SHEET    4 LN6 4 ILE F 130  ARG F 139 -1                                        
SHEET    1 LC6 9 MET F 169  GLY F 171  0                                        
SHEET    2 LC6 9 THR F 200  ASP F 202  1                                        
SHEET    3 LC6 9 LEU F 240  ASN F 241  1                                        
SHEET    4 LC6 9 ILE F 264  ASP F 268  1                                        
SHEET    5 LC6 9 LEU F 290  HIS F 294  1                                        
SHEET    6 LC6 9 HIS F 325  HIS F 327  1                                        
SHEET    7 LC6 9 LEU F 375  SER F 379  1                                        
SHEET    8 LC6 9 VAL F 399  GLN F 401  1                                        
SHEET    9 LC6 9 MET F 169  GLY F 171  1                                        
SHEET    1 SS6 4 THR K  68  MET K  69  0                                        
SHEET    2 SS6 4 HIS K  39  ASN K  45 -1                                        
SHEET    3 SS6 4 TYR K  98  ASP K 105 -1                                        
SHEET    4 SS6 4 CYS K 110  HIS K 118 -1                                        
SHEET    1 LN7 4 LYS G  83  PRO G  89  0                                        
SHEET    2 LN7 4 SER G  96  TYR G 103 -1                                        
SHEET    3 LN7 4 LEU G  36  PRO G  44 -1                                        
SHEET    4 LN7 4 ILE G 130  ARG G 139 -1                                        
SHEET    1 LC7 9 MET G 169  GLY G 171  0                                        
SHEET    2 LC7 9 THR G 200  ASP G 202  1                                        
SHEET    3 LC7 9 LEU G 240  ASN G 241  1                                        
SHEET    4 LC7 9 ILE G 264  ASP G 268  1                                        
SHEET    5 LC7 9 LEU G 290  HIS G 294  1                                        
SHEET    6 LC7 9 HIS G 325  HIS G 327  1                                        
SHEET    7 LC7 9 LEU G 375  SER G 379  1                                        
SHEET    8 LC7 9 VAL G 399  GLN G 401  1                                        
SHEET    9 LC7 9 MET G 169  GLY G 171  1                                        
SHEET    1 SS7 4 THR P  68  MET P  69  0                                        
SHEET    2 SS7 4 HIS P  39  ASN P  45 -1                                        
SHEET    3 SS7 4 TYR P  98  ASP P 105 -1                                        
SHEET    4 SS7 4 CYS P 110  HIS P 118 -1                                        
SHEET    1 LN8 4 LYS H  83  PRO H  89  0                                        
SHEET    2 LN8 4 SER H  96  TYR H 103 -1                                        
SHEET    3 LN8 4 LEU H  36  PRO H  44 -1                                        
SHEET    4 LN8 4 ILE H 130  ARG H 139 -1                                        
SHEET    1 LC8 9 MET H 169  GLY H 171  0                                        
SHEET    2 LC8 9 THR H 200  ASP H 202  1                                        
SHEET    3 LC8 9 LEU H 240  ASN H 241  1                                        
SHEET    4 LC8 9 ILE H 264  ASP H 268  1                                        
SHEET    5 LC8 9 LEU H 290  HIS H 294  1                                        
SHEET    6 LC8 9 HIS H 325  HIS H 327  1                                        
SHEET    7 LC8 9 LEU H 375  SER H 379  1                                        
SHEET    8 LC8 9 VAL H 399  GLN H 401  1                                        
SHEET    9 LC8 9 MET H 169  GLY H 171  1                                        
SHEET    1 SS8 4 THR L  68  MET L  69  0                                        
SHEET    2 SS8 4 HIS L  39  ASN L  45 -1                                        
SHEET    3 SS8 4 TYR L  98  ASP L 105 -1                                        
SHEET    4 SS8 4 CYS L 110  HIS L 118 -1                                        
SSBOND   1 CYS A  247    CYS B  247                          1555   1555  2.19  
SSBOND   2 CYS C  247    CYS D  247                          1555   1555  2.18  
SSBOND   3 CYS E  247    CYS F  247                          1555   1555  2.18  
SSBOND   4 CYS G  247    CYS H  247                          1555   1555  2.23  
LINK         NZ  LYS A 201                 C   FMT A 478     1555   1555  1.45  
LINK         NZ  LYS B 201                 C   FMT B 478     1555   1555  1.45  
LINK         NZ  LYS C 201                 C   FMT C 478     1555   1555  1.45  
LINK         NZ  LYS D 201                 C   FMT D 478     1555   1555  1.45  
LINK         NZ  LYS E 201                 C   FMT E 478     1555   1555  1.45  
LINK         NZ  LYS F 201                 C   FMT F 478     1555   1555  1.45  
LINK         NZ  LYS G 201                 C   FMT G 478     1555   1555  1.45  
LINK         NZ  LYS H 201                 C   FMT H 478     1555   1555  1.45  
LINK        MG    MG A 477                 O1  FMT A 478     1555   1555  3.13  
LINK        MG    MG A 477                 O2  FMT A 478     1555   1555  2.37  
LINK        MG    MG A 477                 O2  CAP A 476     1555   1555  2.39  
LINK        MG    MG A 477                 OE1 GLU A 204     1555   1555  2.34  
LINK        MG    MG A 477                 O3  CAP A 476     1555   1555  2.36  
LINK        MG    MG A 477                 O7  CAP A 476     1555   1555  2.41  
LINK        MG    MG A 477                 OD1 ASP A 203     1555   1555  2.33  
LINK        MG    MG B 477                 O3  CAP B 476     1555   1555  2.36  
LINK        MG    MG B 477                 O7  CAP B 476     1555   1555  2.42  
LINK        MG    MG B 477                 O1  FMT B 478     1555   1555  3.13  
LINK        MG    MG B 477                 O2  FMT B 478     1555   1555  2.37  
LINK        MG    MG B 477                 O2  CAP B 476     1555   1555  2.39  
LINK        MG    MG B 477                 OE1 GLU B 204     1555   1555  2.34  
LINK        MG    MG B 477                 OD1 ASP B 203     1555   1555  2.33  
LINK        MG    MG C 477                 OD1 ASP C 203     1555   1555  2.33  
LINK        MG    MG C 477                 OE1 GLU C 204     1555   1555  2.34  
LINK        MG    MG C 477                 O7  CAP C 476     1555   1555  2.42  
LINK        MG    MG C 477                 O2  FMT C 478     1555   1555  2.37  
LINK        MG    MG C 477                 O3  CAP C 476     1555   1555  2.36  
LINK        MG    MG C 477                 O2  CAP C 476     1555   1555  2.39  
LINK        MG    MG C 477                 O1  FMT C 478     1555   1555  3.13  
LINK        MG    MG D 477                 O3  CAP D 476     1555   1555  2.36  
LINK        MG    MG D 477                 O1  FMT D 478     1555   1555  3.13  
LINK        MG    MG D 477                 O2  CAP D 476     1555   1555  2.39  
LINK        MG    MG D 477                 O2  FMT D 478     1555   1555  2.37  
LINK        MG    MG D 477                 OE1 GLU D 204     1555   1555  2.34  
LINK        MG    MG D 477                 O7  CAP D 476     1555   1555  2.42  
LINK        MG    MG D 477                 OD1 ASP D 203     1555   1555  2.33  
LINK        MG    MG E 477                 O2  FMT E 478     1555   1555  2.37  
LINK        MG    MG E 477                 OE1 GLU E 204     1555   1555  2.34  
LINK        MG    MG E 477                 OD1 ASP E 203     1555   1555  2.33  
LINK        MG    MG E 477                 O1  FMT E 478     1555   1555  3.13  
LINK        MG    MG E 477                 O2  CAP E 476     1555   1555  2.39  
LINK        MG    MG E 477                 O7  CAP E 476     1555   1555  2.41  
LINK        MG    MG E 477                 O3  CAP E 476     1555   1555  2.36  
LINK        MG    MG F 477                 O2  FMT F 478     1555   1555  2.37  
LINK        MG    MG F 477                 O1  FMT F 478     1555   1555  3.13  
LINK        MG    MG F 477                 O3  CAP F 476     1555   1555  2.36  
LINK        MG    MG F 477                 OD1 ASP F 203     1555   1555  2.33  
LINK        MG    MG F 477                 O2  CAP F 476     1555   1555  2.39  
LINK        MG    MG F 477                 O7  CAP F 476     1555   1555  2.41  
LINK        MG    MG F 477                 OE1 GLU F 204     1555   1555  2.34  
LINK        MG    MG G 477                 OE1 GLU G 204     1555   1555  2.34  
LINK        MG    MG G 477                 O2  FMT G 478     1555   1555  2.37  
LINK        MG    MG G 477                 O1  FMT G 478     1555   1555  3.13  
LINK        MG    MG G 477                 O3  CAP G 476     1555   1555  2.36  
LINK        MG    MG G 477                 O2  CAP G 476     1555   1555  2.39  
LINK        MG    MG G 477                 OD1 ASP G 203     1555   1555  2.33  
LINK        MG    MG G 477                 O7  CAP G 476     1555   1555  2.41  
LINK        MG    MG H 477                 O7  CAP H 476     1555   1555  2.41  
LINK        MG    MG H 477                 OD1 ASP H 203     1555   1555  2.33  
LINK        MG    MG H 477                 O2  CAP H 476     1555   1555  2.39  
LINK        MG    MG H 477                 O2  FMT H 478     1555   1555  2.37  
LINK        MG    MG H 477                 O1  FMT H 478     1555   1555  3.13  
LINK        MG    MG H 477                 O3  CAP H 476     1555   1555  2.36  
LINK        MG    MG H 477                 OE1 GLU H 204     1555   1555  2.34  
CISPEP   1 LYS A  175    PRO A  176          0        -4.06                     
CISPEP   2 LYS B  175    PRO B  176          0        -4.03                     
CISPEP   3 LYS C  175    PRO C  176          0        -4.16                     
CISPEP   4 LYS D  175    PRO D  176          0        -4.07                     
CISPEP   5 LYS E  175    PRO E  176          0        -4.05                     
CISPEP   6 LYS F  175    PRO F  176          0        -4.00                     
CISPEP   7 LYS G  175    PRO G  176          0        -4.05                     
CISPEP   8 LYS H  175    PRO H  176          0        -4.05                     
SITE     1  MG  3 LYS A 201  ASP A 203  GLU A 204                               
SITE     1  1P  4 PHE M  65  GLY A 404  GLY A 381  GLY A 403                    
SITE     1  2P  2 ARG A 295  HIS A 327                                          
SITE     1 CAB  4  MG A 477  LYS A 201  HIS A 294  SER A 379                    
SITE     1 MG2  3 LYS B 201  ASP B 203  GLU B 204                               
SITE     1 1P2  4 PHE I  65  GLY B 404  GLY B 381  GLY B 403                    
SITE     1 2P2  2 ARG B 295  HIS B 327                                          
SITE     1 CA2  4  MG B 477  LYS B 201  HIS B 294  SER B 379                    
SITE     1 MG3  3 LYS C 201  ASP C 203  GLU C 204                               
SITE     1 1P3  4 PHE N  65  GLY C 404  GLY C 381  GLY C 403                    
SITE     1 2P3  2 ARG C 295  HIS C 327                                          
SITE     1 CA3  4  MG C 477  LYS C 201  HIS C 294  SER C 379                    
SITE     1 MG4  3 LYS D 201  ASP D 203  GLU D 204                               
SITE     1 1P4  4 PHE J  65  GLY D 404  GLY D 381  GLY D 403                    
SITE     1 2P4  2 ARG D 295  HIS D 327                                          
SITE     1 CA4  4  MG D 477  LYS D 201  HIS D 294  SER D 379                    
SITE     1 MG5  3 LYS E 201  ASP E 203  GLU E 204                               
SITE     1 1P5  4 PHE O  65  GLY E 404  GLY E 381  GLY E 403                    
SITE     1 2P5  2 ARG E 295  HIS E 327                                          
SITE     1 CA5  4  MG E 477  LYS E 201  HIS E 294  SER E 379                    
SITE     1 MG6  3 LYS F 201  ASP F 203  GLU F 204                               
SITE     1 1P6  4 PHE K  65  GLY F 404  GLY F 381  GLY F 403                    
SITE     1 2P6  2 ARG F 295  HIS F 327                                          
SITE     1 CA6  4  MG F 477  LYS F 201  HIS F 294  SER F 379                    
SITE     1 MG7  3 LYS G 201  ASP G 203  GLU G 204                               
SITE     1 1P7  4 PHE P  65  GLY G 404  GLY G 381  GLY G 403                    
SITE     1 2P7  2 ARG G 295  HIS G 327                                          
SITE     1 CA7  4  MG G 477  LYS G 201  HIS G 294  SER G 379                    
SITE     1 MG8  3 LYS H 201  ASP H 203  GLU H 204                               
SITE     1 1P8  4 PHE L  65  GLY H 404  GLY H 381  GLY H 403                    
SITE     1 2P8  2 ARG H 295  HIS H 327                                          
SITE     1 CA8  4  MG H 477  LYS H 201  HIS H 294  SER H 379                    
SITE     1 AC1 23 THR A 173  LYS A 175  LYS A 177  HIS A 294                    
SITE     2 AC1 23 ARG A 295  HIS A 327  LYS A 334  LEU A 335                    
SITE     3 AC1 23 SER A 379  GLY A 380  GLY A 381  GLY A 403                    
SITE     4 AC1 23 GLY A 404  THR B  65  TRP B  66  ASN B 123                    
SITE     5 AC1 23 HOH A 514  HOH A 515  HOH A 520  HOH A 521                    
SITE     6 AC1 23 HOH A 569  HOH A 570  HOH A 571                               
SITE     1 AC2 18 THR A  65  TRP A  66  ASN A 123  THR B 173                    
SITE     2 AC2 18 LYS B 175  LYS B 177  HIS B 294  ARG B 295                    
SITE     3 AC2 18 HIS B 327  LYS B 334  LEU B 335  SER B 379                    
SITE     4 AC2 18 GLY B 380  GLY B 381  GLY B 403  GLY B 404                    
SITE     5 AC2 18 HOH A 502  HOH A 503                                          
SITE     1 AC3 16 THR C 173  LYS C 175  LYS C 177  HIS C 294                    
SITE     2 AC3 16 ARG C 295  HIS C 327  LYS C 334  LEU C 335                    
SITE     3 AC3 16 SER C 379  GLY C 380  GLY C 381  GLY C 403                    
SITE     4 AC3 16 GLY C 404  THR D  65  TRP D  66  ASN D 123                    
SITE     1 AC4 16 THR C  65  TRP C  66  ASN C 123  THR D 173                    
SITE     2 AC4 16 LYS D 175  LYS D 177  HIS D 294  ARG D 295                    
SITE     3 AC4 16 HIS D 327  LYS D 334  LEU D 335  SER D 379                    
SITE     4 AC4 16 GLY D 380  GLY D 381  GLY D 403  GLY D 404                    
SITE     1 AC5 16 THR G  65  TRP G  66  ASN G 123  THR H 173                    
SITE     2 AC5 16 LYS H 175  LYS H 177  HIS H 294  ARG H 295                    
SITE     3 AC5 16 HIS H 327  LYS H 334  LEU H 335  SER H 379                    
SITE     4 AC5 16 GLY H 380  GLY H 381  GLY H 403  GLY H 404                    
SITE     1 AC6 16 THR G 173  LYS G 175  LYS G 177  HIS G 294                    
SITE     2 AC6 16 ARG G 295  HIS G 327  LYS G 334  LEU G 335                    
SITE     3 AC6 16 SER G 379  GLY G 380  GLY G 381  GLY G 403                    
SITE     4 AC6 16 GLY G 404  THR H  65  TRP H  66  ASN H 123                    
SITE     1 AC7 16 THR E  65  TRP E  66  ASN E 123  THR F 173                    
SITE     2 AC7 16 LYS F 175  LYS F 177  HIS F 294  ARG F 295                    
SITE     3 AC7 16 HIS F 327  LYS F 334  LEU F 335  SER F 379                    
SITE     4 AC7 16 GLY F 380  GLY F 381  GLY F 403  GLY F 404                    
SITE     1 AC8 16 THR E 173  LYS E 175  LYS E 177  HIS E 294                    
SITE     2 AC8 16 ARG E 295  HIS E 327  LYS E 334  LEU E 335                    
SITE     3 AC8 16 SER E 379  GLY E 380  GLY E 381  GLY E 403                    
SITE     4 AC8 16 GLY E 404  THR F  65  TRP F  66  ASN F 123                    
SITE     1 AC9  6 LYS A 201  ASP A 202  ASP A 203  GLU A 204                    
SITE     2 AC9  6 HIS A 294  HIS A 327                                          
SITE     1 AD1  6 LYS D 201  ASP D 202  ASP D 203  GLU D 204                    
SITE     2 AD1  6 HIS D 294  HIS D 327                                          
SITE     1 AD2  6 LYS E 201  ASP E 202  ASP E 203  GLU E 204                    
SITE     2 AD2  6 HIS E 294  HIS E 327                                          
SITE     1 AD3  6 LYS F 201  ASP F 202  ASP F 203  GLU F 204                    
SITE     2 AD3  6 HIS F 294  HIS F 327                                          
SITE     1 AD4  6 LYS H 201  ASP H 202  ASP H 203  GLU H 204                    
SITE     2 AD4  6 HIS H 294  HIS H 327                                          
SITE     1 AD5  6 LYS G 201  ASP G 202  ASP G 203  GLU G 204                    
SITE     2 AD5  6 HIS G 294  HIS G 327                                          
SITE     1 AD6  6 LYS C 201  ASP C 202  ASP C 203  GLU C 204                    
SITE     2 AD6  6 HIS C 294  HIS C 327                                          
SITE     1 AD7  6 LYS B 201  ASP B 202  ASP B 203  GLU B 204                    
SITE     2 AD7  6 HIS B 294  HIS B 327                                          
SITE     1 AD8  2 ASP A 203  GLU A 204                                          
SITE     1 AD9  2 ASP B 203  GLU B 204                                          
SITE     1 AE1  2 ASP C 203  GLU C 204                                          
SITE     1 AE2  2 ASP D 203  GLU D 204                                          
SITE     1 AE3  2 ASP E 203  GLU E 204                                          
SITE     1 AE4  2 ASP F 203  GLU F 204                                          
SITE     1 AE5  2 ASP G 203  GLU G 204                                          
SITE     1 AE6  2 ASP H 203  GLU H 204                                          
CRYST1  223.900  111.900  199.700  90.00  90.00  90.00 P 21 21 21   32          
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      0.004466  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008937  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005008        0.00000                         
MTRIX1   1  0.055254  0.991591  0.117024       58.51700    1                    
MTRIX2   1  0.991747 -0.068084  0.108639      -60.77910    1                    
MTRIX3   1  0.115693  0.110056 -0.987169      -12.31830    1                    
MTRIX1   2 -0.001556  0.994481  0.104910       63.24410    1                    
MTRIX2   2 -0.993326  0.010562 -0.114852      104.72470    1                    
MTRIX3   2 -0.115326 -0.104388  0.987827       11.96200    1                    
MTRIX1   3  0.998390 -0.056422  0.005795        1.35870    1                    
MTRIX2   3 -0.056413 -0.998406 -0.001652       47.27970    1                    
MTRIX3   3  0.005879  0.001323 -0.999982       -0.77360    1                    
MTRIX1   4 -0.999944  0.000591 -0.010574      168.35741    1                    
MTRIX2   4  0.001717 -0.976187 -0.216926       41.89850    1                    
MTRIX3   4 -0.010451 -0.216932  0.976131        5.47850    1                    
MTRIX1   5 -0.055113 -0.992904 -0.105381      109.87600    1                    
MTRIX2   5 -0.993265  0.043745  0.107292      104.02560    1                    
MTRIX3   5 -0.101920  0.110584 -0.988627        5.96800    1                    
MTRIX1   6 -0.000233 -0.993280 -0.115738      105.29090    1                    
MTRIX2   6  0.994670  0.011703 -0.102440      -62.72860    1                    
MTRIX3   6  0.103106 -0.115145  0.987983       -6.23160    1                    
MTRIX1   7 -0.998513  0.054364  0.004006      167.12070    1                    
MTRIX2   7  0.053928  0.974438  0.218086       -3.88990    1                    
MTRIX3   7  0.007953  0.217978 -0.975921       -5.57330    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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