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Database: PDB
Entry: 3ZXW
LinkDB: 3ZXW
Original site: 3ZXW 
HEADER    LYASE                                   16-AUG-11   3ZXW              
TITLE     STRUCTURE OF ACTIVATED RUBISCO FROM THERMOSYNECHOCOCCUS ELONGATUS     
TITLE    2 COMPLEXED WITH 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;             
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 SYNONYM: RUBISCO LARGE SUBUNIT;                                      
COMPND   5 EC: 4.1.1.39;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN;             
COMPND   9 CHAIN: B, D, F, H;                                                   
COMPND  10 EC: 4.1.1.39;                                                        
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE   3 ORGANISM_TAXID: 197221;                                              
SOURCE   4 STRAIN: BP-1;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 668369;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: DH5[ALPHA];                                
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PUC18RBCLXSTH.EL;                         
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  11 ORGANISM_TAXID: 197221;                                              
SOURCE  12 STRAIN: BP-1;                                                        
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 668369;                                     
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: DH5[ALPHA];                                
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PUC18RBCLXSTH.EL                          
KEYWDS    CO2/O2 SPECIFICITY, CARBON DIOXIDE FIXATION, PHOTOSYNTHESIS,          
KEYWDS   2 THERMOSTABILITY, PHOTORESPIRATION, MONOOXYGENASE, HYDROXYLATION,     
KEYWDS   3 LYASE, CHLOROPLAST, CALVIN CYCLE, THERMOPHILIC CYANOBACTERIA         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.TERLECKA,V.WILHELMI,W.BIALEK,B.GUBERNATOR,A.SZCZEPANIAK,E.HOFMANN   
REVDAT   1   29-AUG-12 3ZXW    0                                                
JRNL        AUTH   B.TERLECKA,V.WILHELMI,W.BIALEK,B.GUBERNATOR,A.SZCZEPANIAK,   
JRNL        AUTH 2 E.HOFMANN                                                    
JRNL        TITL   STRUCTURE OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE           
JRNL        TITL 2 OXYGENASE FROM THERMOSYNECHOCOCCUS ELONGATUS                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0088                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.00                         
REMARK   3   NUMBER OF REFLECTIONS             : 137341                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.18276                         
REMARK   3   R VALUE            (WORKING SET) : 0.18102                         
REMARK   3   FREE R VALUE                     : 0.21350                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 7450                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.100                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.154                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9706                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.238                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 0                            
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 17680                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 202                                     
REMARK   3   SOLVENT ATOMS            : 905                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.997                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.30                                                 
REMARK   3    B22 (A**2) : 0.30                                                 
REMARK   3    B33 (A**2) : -0.61                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.213         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.169         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.122         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.571         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 18323 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 24871 ; 1.013 ; 1.953       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2236 ; 5.339 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   888 ;31.802 ;23.829       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2972 ;13.182 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   124 ;11.721 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2652 ; 0.071 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 14128 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1183 ; 0.559 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1914 ; 1.163 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   750 ; 1.762 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   722 ; 2.867 ; 4.500       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 5                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A G C E                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     12       A      89      2                      
REMARK   3           1     G     12       G      89      2                      
REMARK   3           1     C     12       C      89      2                      
REMARK   3           1     E     12       E      89      2                      
REMARK   3           2     A     93       A     475      2                      
REMARK   3           2     G     93       G     475      2                      
REMARK   3           2     C     93       C     475      2                      
REMARK   3           2     E     93       E     475      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1849 ;  0.08 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    G    (A):   1849 ;  0.10 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    C    (A):   1849 ;  0.07 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    E    (A):   1849 ;  0.09 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1796 ;  0.20 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    G    (A):   1796 ;  0.17 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   1796 ;  0.17 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    E    (A):   1796 ;  0.21 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1849 ;  1.10 ;  0.50           
REMARK   3   TIGHT THERMAL      1    G (A**2):   1849 ;  0.71 ;  0.50           
REMARK   3   TIGHT THERMAL      1    C (A**2):   1849 ;  0.81 ;  0.50           
REMARK   3   TIGHT THERMAL      1    E (A**2):   1849 ;  0.70 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1796 ;  1.11 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    G (A**2):   1796 ;  0.65 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   1796 ;  0.69 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    E (A**2):   1796 ;  0.64 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B F D H                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B     14       B      25      2                      
REMARK   3           1     F     14       F      25      2                      
REMARK   3           1     D     14       D      25      2                      
REMARK   3           1     H     14       H      25      2                      
REMARK   3           2     B     27       B     106      2                      
REMARK   3           2     F     27       F     106      2                      
REMARK   3           2     D     27       D     106      2                      
REMARK   3           2     H     27       H     106      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    B    (A):    368 ;  0.01 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    F    (A):    368 ;  0.01 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    D    (A):    368 ;  0.01 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    H    (A):    368 ;  0.01 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  2    B    (A):    389 ;  0.01 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    F    (A):    389 ;  0.01 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    D    (A):    389 ;  0.01 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    H    (A):    389 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL      2    B (A**2):    368 ;  0.02 ;  0.50           
REMARK   3   TIGHT THERMAL      2    F (A**2):    368 ;  0.02 ;  0.50           
REMARK   3   TIGHT THERMAL      2    D (A**2):    368 ;  0.02 ;  0.50           
REMARK   3   TIGHT THERMAL      2    H (A**2):    368 ;  0.03 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    B (A**2):    389 ;  0.02 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    F (A**2):    389 ;  0.02 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    D (A**2):    389 ;  0.02 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    H (A**2):    389 ;  0.02 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A G                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     90       A      92      2                      
REMARK   3           1     G     90       G      92      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    A    (A):     12 ;  0.01 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  3    G    (A):      7 ;  0.02 ;  0.50           
REMARK   3   TIGHT THERMAL      3    A (A**2):     12 ;  0.05 ;  0.50           
REMARK   3   MEDIUM THERMAL     3    G (A**2):      7 ;  0.03 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : E C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     E     90       E      92      2                      
REMARK   3           1     C     90       C      92      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   4    E    (A):     12 ;  0.02 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  4    C    (A):      7 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL      4    E (A**2):     12 ;  0.03 ;  0.50           
REMARK   3   MEDIUM THERMAL     4    C (A**2):      7 ;  0.03 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 5                                  
REMARK   3     CHAIN NAMES                    : B F D                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B     26       B      26      2                      
REMARK   3           1     F     26       F      26      2                      
REMARK   3           1     D     26       D      26      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   5    B    (A):      4 ;  0.00 ;  0.05           
REMARK   3   TIGHT POSITIONAL   5    F    (A):      4 ;  0.01 ;  0.05           
REMARK   3   TIGHT POSITIONAL   5    D    (A):      4 ;  0.00 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  5    B    (A):      7 ;  0.01 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  5    F    (A):      7 ;  0.01 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  5    D    (A):      7 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL      5    B (A**2):      4 ;  0.01 ;  0.50           
REMARK   3   TIGHT THERMAL      5    F (A**2):      4 ;  0.02 ;  0.50           
REMARK   3   TIGHT THERMAL      5    D (A**2):      4 ;  0.02 ;  0.50           
REMARK   3   MEDIUM THERMAL     5    B (A**2):      7 ;  0.01 ;  2.00           
REMARK   3   MEDIUM THERMAL     5    F (A**2):      7 ;  0.01 ;  2.00           
REMARK   3   MEDIUM THERMAL     5    D (A**2):      7 ;  0.01 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 3ZXW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-AUG-11.                  
REMARK 100 THE PDBE ID CODE IS EBI-49352.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-DEC-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978946                           
REMARK 200  MONOCHROMATOR                  : SI                                 
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 144795                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.10                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 7.7                                
REMARK 200  R MERGE                    (I) : 0.11                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.90                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.5                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.43                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.20                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: RUBISCO FROM TH.ELONGATUS WITHOUT LIGANDS            
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.4                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 80 MM HEPES, 20 MM MGCL2, 8%             
REMARK 280  (W/V) PEG4000, 30% (V/V) GLYCEROL, PH=8                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      198.50000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       55.75000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       55.75000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      297.75000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       55.75000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       55.75000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       99.25000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       55.75000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       55.75000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      297.75000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       55.75000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       55.75000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       99.25000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      198.50000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXADECAMERIC                     
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC              
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 92440 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 121140 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -420.4 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G, H, E, F, C, D                
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH C2152   LIES ON A SPECIAL POSITION.                         
REMARK 375      HOH C2162   LIES ON A SPECIAL POSITION.                         
REMARK 375      HOH C2167   LIES ON A SPECIAL POSITION.                         
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     TYR A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     GLN A     9                                                      
REMARK 465     LYS A    10                                                      
REMARK 465     VAL A    11                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LYS B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     PRO B     5                                                      
REMARK 465     LYS B     6                                                      
REMARK 465     GLU B     7                                                      
REMARK 465     ARG B     8                                                      
REMARK 465     ARG B     9                                                      
REMARK 465     TYR B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     THR B    12                                                      
REMARK 465     PHE B    13                                                      
REMARK 465     ASN B   107                                                      
REMARK 465     GLN B   108                                                      
REMARK 465     ALA B   109                                                      
REMARK 465     ASN B   110                                                      
REMARK 465     SER B   111                                                      
REMARK 465     GLY B   112                                                      
REMARK 465     TYR B   113                                                      
REMARK 465     SER B   114                                                      
REMARK 465     GLY B   115                                                      
REMARK 465     TYR B   116                                                      
REMARK 465     ARG B   117                                                      
REMARK 465     TYR B   118                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     TYR C     3                                                      
REMARK 465     THR C     4                                                      
REMARK 465     GLN C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     LYS C     7                                                      
REMARK 465     SER C     8                                                      
REMARK 465     GLN C     9                                                      
REMARK 465     LYS C    10                                                      
REMARK 465     VAL C    11                                                      
REMARK 465     MET D     1                                                      
REMARK 465     LYS D     2                                                      
REMARK 465     THR D     3                                                      
REMARK 465     LEU D     4                                                      
REMARK 465     PRO D     5                                                      
REMARK 465     LYS D     6                                                      
REMARK 465     GLU D     7                                                      
REMARK 465     ARG D     8                                                      
REMARK 465     ARG D     9                                                      
REMARK 465     TYR D    10                                                      
REMARK 465     GLU D    11                                                      
REMARK 465     THR D    12                                                      
REMARK 465     PHE D    13                                                      
REMARK 465     ASN D   107                                                      
REMARK 465     GLN D   108                                                      
REMARK 465     ALA D   109                                                      
REMARK 465     ASN D   110                                                      
REMARK 465     SER D   111                                                      
REMARK 465     GLY D   112                                                      
REMARK 465     TYR D   113                                                      
REMARK 465     SER D   114                                                      
REMARK 465     GLY D   115                                                      
REMARK 465     TYR D   116                                                      
REMARK 465     ARG D   117                                                      
REMARK 465     TYR D   118                                                      
REMARK 465     MET E     1                                                      
REMARK 465     ALA E     2                                                      
REMARK 465     TYR E     3                                                      
REMARK 465     THR E     4                                                      
REMARK 465     GLN E     5                                                      
REMARK 465     SER E     6                                                      
REMARK 465     LYS E     7                                                      
REMARK 465     SER E     8                                                      
REMARK 465     GLN E     9                                                      
REMARK 465     LYS E    10                                                      
REMARK 465     VAL E    11                                                      
REMARK 465     MET F     1                                                      
REMARK 465     LYS F     2                                                      
REMARK 465     THR F     3                                                      
REMARK 465     LEU F     4                                                      
REMARK 465     PRO F     5                                                      
REMARK 465     LYS F     6                                                      
REMARK 465     GLU F     7                                                      
REMARK 465     ARG F     8                                                      
REMARK 465     ARG F     9                                                      
REMARK 465     TYR F    10                                                      
REMARK 465     GLU F    11                                                      
REMARK 465     THR F    12                                                      
REMARK 465     PHE F    13                                                      
REMARK 465     ASN F   107                                                      
REMARK 465     GLN F   108                                                      
REMARK 465     ALA F   109                                                      
REMARK 465     ASN F   110                                                      
REMARK 465     SER F   111                                                      
REMARK 465     GLY F   112                                                      
REMARK 465     TYR F   113                                                      
REMARK 465     SER F   114                                                      
REMARK 465     GLY F   115                                                      
REMARK 465     TYR F   116                                                      
REMARK 465     ARG F   117                                                      
REMARK 465     TYR F   118                                                      
REMARK 465     MET G     1                                                      
REMARK 465     ALA G     2                                                      
REMARK 465     TYR G     3                                                      
REMARK 465     THR G     4                                                      
REMARK 465     GLN G     5                                                      
REMARK 465     SER G     6                                                      
REMARK 465     LYS G     7                                                      
REMARK 465     SER G     8                                                      
REMARK 465     GLN G     9                                                      
REMARK 465     LYS G    10                                                      
REMARK 465     VAL G    11                                                      
REMARK 465     MET H     1                                                      
REMARK 465     LYS H     2                                                      
REMARK 465     THR H     3                                                      
REMARK 465     LEU H     4                                                      
REMARK 465     PRO H     5                                                      
REMARK 465     LYS H     6                                                      
REMARK 465     GLU H     7                                                      
REMARK 465     ARG H     8                                                      
REMARK 465     ARG H     9                                                      
REMARK 465     TYR H    10                                                      
REMARK 465     GLU H    11                                                      
REMARK 465     THR H    12                                                      
REMARK 465     PHE H    13                                                      
REMARK 465     ASN H   107                                                      
REMARK 465     GLN H   108                                                      
REMARK 465     ALA H   109                                                      
REMARK 465     ASN H   110                                                      
REMARK 465     SER H   111                                                      
REMARK 465     GLY H   112                                                      
REMARK 465     TYR H   113                                                      
REMARK 465     SER H   114                                                      
REMARK 465     GLY H   115                                                      
REMARK 465     TYR H   116                                                      
REMARK 465     ARG H   117                                                      
REMARK 465     TYR H   118                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   SG   CYS C   247     SG   CYS C   247     7555     2.03            
REMARK 500   SG   CYS G   247     SG   CYS G   247     7555     2.04            
REMARK 500   O    HOH C  2169     O    HOH C  2169     7555     2.10            
REMARK 500   O    HOH G  2134     O    HOH G  2134     7555     1.70            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS C 172   CA  -  CB  -  SG  ANGL. DEV. =   7.1 DEGREES          
REMARK 500    CYS E 172   CA  -  CB  -  SG  ANGL. DEV. =   6.8 DEGREES          
REMARK 500    CYS G 172   CA  -  CB  -  SG  ANGL. DEV. =   7.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  62      -80.50   -140.32                                   
REMARK 500    THR A  75     -169.97   -122.19                                   
REMARK 500    HIS A 153      -58.52   -133.83                                   
REMARK 500    ASN A 207      -91.02   -123.14                                   
REMARK 500    ARG A 295       30.44    -98.17                                   
REMARK 500    MET A 297       -9.55     85.95                                   
REMARK 500    VAL A 331      -49.43     74.72                                   
REMARK 500    LYS B  57     -116.42     55.59                                   
REMARK 500    SER C  62      -80.41   -143.71                                   
REMARK 500    HIS C 153      -59.50   -134.18                                   
REMARK 500    ASN C 207      -89.66   -120.84                                   
REMARK 500    GLN C 212      107.33   -166.45                                   
REMARK 500    ALA C 296      129.63    -37.75                                   
REMARK 500    MET C 297      -12.41     90.61                                   
REMARK 500    VAL C 331      -53.88     74.60                                   
REMARK 500    ASP C 357       97.07   -160.22                                   
REMARK 500    THR C 406      -50.59   -120.22                                   
REMARK 500    LYS D  57     -116.79     56.04                                   
REMARK 500    SER E  62      -82.97   -138.19                                   
REMARK 500    ASP E  76       78.78   -110.28                                   
REMARK 500    HIS E 153      -54.68   -136.89                                   
REMARK 500    ASN E 207      -87.02   -118.91                                   
REMARK 500    GLN E 212      109.91   -166.18                                   
REMARK 500    ALA E 296      134.12    -39.43                                   
REMARK 500    MET E 297       -9.88     85.24                                   
REMARK 500    VAL E 331      -55.46     73.07                                   
REMARK 500    ASP E 357       89.71   -158.68                                   
REMARK 500    LYS F  57     -116.51     54.96                                   
REMARK 500    SER G  62      -80.09   -139.70                                   
REMARK 500    THR G  75     -166.34   -120.87                                   
REMARK 500    ASP G  76       76.78   -113.87                                   
REMARK 500    HIS G 153      -56.95   -133.45                                   
REMARK 500    ASN G 207      -92.05   -119.09                                   
REMARK 500    GLN G 212      107.52   -168.40                                   
REMARK 500    MET G 297       -9.90     89.71                                   
REMARK 500    VAL G 331      -52.53     77.94                                   
REMARK 500    ASP G 357       90.24   -162.05                                   
REMARK 500    LYS H  57     -116.52     56.24                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAP A 477   O7                                                     
REMARK 620 2 KCX A 201   OQ1 158.2                                              
REMARK 620 3 KCX A 201   OQ2 119.8  45.1                                        
REMARK 620 4 ASP A 203   OD1  98.5  92.3 136.8                                  
REMARK 620 5 GLU A 204   OE1  92.9 104.6 100.2  96.9                            
REMARK 620 6 CAP A 477   O2   68.1  90.5  72.1 108.5 149.9                      
REMARK 620 7 CAP A 477   O3   77.1  91.1  46.2 174.9  86.0  67.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 203   OD1                                                    
REMARK 620 2 KCX C 201   OQ1  96.2                                              
REMARK 620 3 KCX C 201   OQ2 141.2  45.8                                        
REMARK 620 4 GLU C 204   OE1  94.0 103.3 101.4                                  
REMARK 620 5 CAP C 477   O3  173.6  89.3  43.8  87.9                            
REMARK 620 6 CAP C 477   O2  106.3  90.3  72.5 154.2  70.2                      
REMARK 620 7 CAP C 477   O6   94.5 159.2 119.5  93.7  79.3  69.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX E 201   OQ1                                                    
REMARK 620 2 KCX E 201   OQ2  45.3                                              
REMARK 620 3 GLU E 204   OE1 106.3 102.0                                        
REMARK 620 4 CAP E 477   O2   93.0  77.3 152.1                                  
REMARK 620 5 CAP E 477   O3   89.9  44.7  88.4  71.3                            
REMARK 620 6 CAP E 477   O7  163.5 123.5  87.1  71.2  80.7                      
REMARK 620 7 ASP E 203   OD1 100.4 145.7  88.8 107.6 169.6  89.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX G 201   OQ1                                                    
REMARK 620 2 KCX G 201   OQ2  46.2                                              
REMARK 620 3 ASP G 203   OD1 101.9 147.4                                        
REMARK 620 4 CAP G 477   O2   92.9  72.9 108.6                                  
REMARK 620 5 CAP G 477   O3   91.4  45.6 166.7  69.7                            
REMARK 620 6 CAP G 477   O7  160.6 120.0  88.8  68.2  78.3                      
REMARK 620 7 GLU G 204   OE1 108.5 105.2  89.9 148.5  86.4  87.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700                                                                      
REMARK 700 THE SHEETS PRESENTED AS "CB" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700                                                                      
REMARK 700 THE SHEETS PRESENTED AS "EB" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700                                                                      
REMARK 700 THE SHEETS PRESENTED AS "GB" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG C 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG E 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG G 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1479                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2YBV   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF RUBISCO FROM THERMOSYNECHOCOCCUS ELONGATUS             
DBREF  3ZXW A    1   475  UNP    Q8DIS5   RBL_THEEB        1    475             
DBREF  3ZXW B    1   118  UNP    Q8DIS7   Q8DIS7_THEEB     1    118             
DBREF  3ZXW C    1   475  UNP    Q8DIS5   RBL_THEEB        1    475             
DBREF  3ZXW D    1   118  UNP    Q8DIS7   Q8DIS7_THEEB     1    118             
DBREF  3ZXW E    1   475  UNP    Q8DIS5   RBL_THEEB        1    475             
DBREF  3ZXW F    1   118  UNP    Q8DIS7   Q8DIS7_THEEB     1    118             
DBREF  3ZXW G    1   475  UNP    Q8DIS5   RBL_THEEB        1    475             
DBREF  3ZXW H    1   118  UNP    Q8DIS7   Q8DIS7_THEEB     1    118             
SEQRES   1 A  475  MET ALA TYR THR GLN SER LYS SER GLN LYS VAL GLY TYR          
SEQRES   2 A  475  GLN ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 A  475  PRO ASP TYR THR PRO LYS ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 A  475  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PHE GLU GLU          
SEQRES   5 A  475  ALA ALA ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 A  475  TRP THR THR VAL TRP THR ASP LEU LEU THR ASP LEU ASP          
SEQRES   7 A  475  ARG TYR LYS GLY CYS CYS TYR ASP ILE GLU PRO LEU PRO          
SEQRES   8 A  475  GLY GLU ASP ASN GLN PHE ILE ALA TYR ILE ALA TYR PRO          
SEQRES   9 A  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET LEU          
SEQRES  10 A  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 A  475  LYS ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO VAL ALA          
SEQRES  12 A  475  TYR LEU LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN          
SEQRES  13 A  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU          
SEQRES  14 A  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 A  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 A  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN ILE ASN SER          
SEQRES  17 A  475  GLN PRO PHE GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 A  475  ALA ASP ALA ILE HIS LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 A  475  ILE LYS GLY HIS TYR LEU ASN VAL THR ALA PRO THR CYS          
SEQRES  20 A  475  GLU GLU MET LEU LYS ARG ALA GLU PHE ALA LYS GLU LEU          
SEQRES  21 A  475  GLU MET PRO ILE ILE MET HIS ASP PHE LEU THR ALA GLY          
SEQRES  22 A  475  PHE THR ALA ASN THR THR LEU SER LYS TRP CYS ARG ASP          
SEQRES  23 A  475  ASN GLY MET LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 A  475  VAL MET ASP ARG GLN LYS ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 A  475  VAL LEU ALA LYS CYS LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 A  475  ILE HIS THR GLY THR VAL VAL GLY LYS LEU GLU GLY ASP          
SEQRES  27 A  475  LYS ALA VAL THR LEU GLY PHE VAL ASP LEU LEU ARG GLU          
SEQRES  28 A  475  ASN TYR ILE GLU GLN ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 A  475  THR GLN ASP TRP ALA SER MET PRO GLY VAL MET ALA VAL          
SEQRES  30 A  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 A  475  VAL ASP ILE PHE GLY ASP ASP ALA VAL LEU GLN PHE GLY          
SEQRES  32 A  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 A  475  ALA THR ALA ASN ARG VAL ALA LEU GLU ALA CYS ILE GLN          
SEQRES  34 A  475  ALA ARG ASN GLU GLY ARG ASP LEU MET ARG GLU GLY GLY          
SEQRES  35 A  475  ASP ILE ILE ARG GLU ALA ALA ARG TRP SER PRO GLU LEU          
SEQRES  36 A  475  ALA ALA ALA CYS GLU LEU TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 A  475  PHE GLU ALA GLN ASP THR ILE                                  
SEQRES   1 B  118  MET LYS THR LEU PRO LYS GLU ARG ARG TYR GLU THR PHE          
SEQRES   2 B  118  SER TYR LEU PRO PRO LEU SER ASP ALA GLN ILE ALA ARG          
SEQRES   3 B  118  GLN ILE GLN TYR ALA ILE ASP GLN GLY TYR HIS PRO CYS          
SEQRES   4 B  118  VAL GLU PHE ASN GLU THR SER ASN ALA GLU ILE ARG TYR          
SEQRES   5 B  118  TRP THR MET TRP LYS LEU PRO LEU PHE ASN CYS THR ASN          
SEQRES   6 B  118  ALA GLN ASP VAL LEU ASN GLU VAL GLN GLN CYS ARG SER          
SEQRES   7 B  118  GLU TYR PRO ASN CYS PHE ILE ARG VAL VAL ALA PHE ASP          
SEQRES   8 B  118  ASN ILE LYS GLN CYS GLN VAL MET SER PHE ILE VAL TYR          
SEQRES   9 B  118  LYS PRO ASN GLN ALA ASN SER GLY TYR SER GLY TYR ARG          
SEQRES  10 B  118  TYR                                                          
SEQRES   1 C  475  MET ALA TYR THR GLN SER LYS SER GLN LYS VAL GLY TYR          
SEQRES   2 C  475  GLN ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 C  475  PRO ASP TYR THR PRO LYS ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 C  475  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PHE GLU GLU          
SEQRES   5 C  475  ALA ALA ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 C  475  TRP THR THR VAL TRP THR ASP LEU LEU THR ASP LEU ASP          
SEQRES   7 C  475  ARG TYR LYS GLY CYS CYS TYR ASP ILE GLU PRO LEU PRO          
SEQRES   8 C  475  GLY GLU ASP ASN GLN PHE ILE ALA TYR ILE ALA TYR PRO          
SEQRES   9 C  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET LEU          
SEQRES  10 C  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 C  475  LYS ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO VAL ALA          
SEQRES  12 C  475  TYR LEU LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN          
SEQRES  13 C  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU          
SEQRES  14 C  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 C  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 C  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN ILE ASN SER          
SEQRES  17 C  475  GLN PRO PHE GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 C  475  ALA ASP ALA ILE HIS LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 C  475  ILE LYS GLY HIS TYR LEU ASN VAL THR ALA PRO THR CYS          
SEQRES  20 C  475  GLU GLU MET LEU LYS ARG ALA GLU PHE ALA LYS GLU LEU          
SEQRES  21 C  475  GLU MET PRO ILE ILE MET HIS ASP PHE LEU THR ALA GLY          
SEQRES  22 C  475  PHE THR ALA ASN THR THR LEU SER LYS TRP CYS ARG ASP          
SEQRES  23 C  475  ASN GLY MET LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 C  475  VAL MET ASP ARG GLN LYS ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 C  475  VAL LEU ALA LYS CYS LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 C  475  ILE HIS THR GLY THR VAL VAL GLY LYS LEU GLU GLY ASP          
SEQRES  27 C  475  LYS ALA VAL THR LEU GLY PHE VAL ASP LEU LEU ARG GLU          
SEQRES  28 C  475  ASN TYR ILE GLU GLN ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 C  475  THR GLN ASP TRP ALA SER MET PRO GLY VAL MET ALA VAL          
SEQRES  30 C  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 C  475  VAL ASP ILE PHE GLY ASP ASP ALA VAL LEU GLN PHE GLY          
SEQRES  32 C  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 C  475  ALA THR ALA ASN ARG VAL ALA LEU GLU ALA CYS ILE GLN          
SEQRES  34 C  475  ALA ARG ASN GLU GLY ARG ASP LEU MET ARG GLU GLY GLY          
SEQRES  35 C  475  ASP ILE ILE ARG GLU ALA ALA ARG TRP SER PRO GLU LEU          
SEQRES  36 C  475  ALA ALA ALA CYS GLU LEU TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 C  475  PHE GLU ALA GLN ASP THR ILE                                  
SEQRES   1 D  118  MET LYS THR LEU PRO LYS GLU ARG ARG TYR GLU THR PHE          
SEQRES   2 D  118  SER TYR LEU PRO PRO LEU SER ASP ALA GLN ILE ALA ARG          
SEQRES   3 D  118  GLN ILE GLN TYR ALA ILE ASP GLN GLY TYR HIS PRO CYS          
SEQRES   4 D  118  VAL GLU PHE ASN GLU THR SER ASN ALA GLU ILE ARG TYR          
SEQRES   5 D  118  TRP THR MET TRP LYS LEU PRO LEU PHE ASN CYS THR ASN          
SEQRES   6 D  118  ALA GLN ASP VAL LEU ASN GLU VAL GLN GLN CYS ARG SER          
SEQRES   7 D  118  GLU TYR PRO ASN CYS PHE ILE ARG VAL VAL ALA PHE ASP          
SEQRES   8 D  118  ASN ILE LYS GLN CYS GLN VAL MET SER PHE ILE VAL TYR          
SEQRES   9 D  118  LYS PRO ASN GLN ALA ASN SER GLY TYR SER GLY TYR ARG          
SEQRES  10 D  118  TYR                                                          
SEQRES   1 E  475  MET ALA TYR THR GLN SER LYS SER GLN LYS VAL GLY TYR          
SEQRES   2 E  475  GLN ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 E  475  PRO ASP TYR THR PRO LYS ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 E  475  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PHE GLU GLU          
SEQRES   5 E  475  ALA ALA ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 E  475  TRP THR THR VAL TRP THR ASP LEU LEU THR ASP LEU ASP          
SEQRES   7 E  475  ARG TYR LYS GLY CYS CYS TYR ASP ILE GLU PRO LEU PRO          
SEQRES   8 E  475  GLY GLU ASP ASN GLN PHE ILE ALA TYR ILE ALA TYR PRO          
SEQRES   9 E  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET LEU          
SEQRES  10 E  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 E  475  LYS ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO VAL ALA          
SEQRES  12 E  475  TYR LEU LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN          
SEQRES  13 E  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU          
SEQRES  14 E  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 E  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 E  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN ILE ASN SER          
SEQRES  17 E  475  GLN PRO PHE GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 E  475  ALA ASP ALA ILE HIS LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 E  475  ILE LYS GLY HIS TYR LEU ASN VAL THR ALA PRO THR CYS          
SEQRES  20 E  475  GLU GLU MET LEU LYS ARG ALA GLU PHE ALA LYS GLU LEU          
SEQRES  21 E  475  GLU MET PRO ILE ILE MET HIS ASP PHE LEU THR ALA GLY          
SEQRES  22 E  475  PHE THR ALA ASN THR THR LEU SER LYS TRP CYS ARG ASP          
SEQRES  23 E  475  ASN GLY MET LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 E  475  VAL MET ASP ARG GLN LYS ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 E  475  VAL LEU ALA LYS CYS LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 E  475  ILE HIS THR GLY THR VAL VAL GLY LYS LEU GLU GLY ASP          
SEQRES  27 E  475  LYS ALA VAL THR LEU GLY PHE VAL ASP LEU LEU ARG GLU          
SEQRES  28 E  475  ASN TYR ILE GLU GLN ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 E  475  THR GLN ASP TRP ALA SER MET PRO GLY VAL MET ALA VAL          
SEQRES  30 E  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 E  475  VAL ASP ILE PHE GLY ASP ASP ALA VAL LEU GLN PHE GLY          
SEQRES  32 E  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 E  475  ALA THR ALA ASN ARG VAL ALA LEU GLU ALA CYS ILE GLN          
SEQRES  34 E  475  ALA ARG ASN GLU GLY ARG ASP LEU MET ARG GLU GLY GLY          
SEQRES  35 E  475  ASP ILE ILE ARG GLU ALA ALA ARG TRP SER PRO GLU LEU          
SEQRES  36 E  475  ALA ALA ALA CYS GLU LEU TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 E  475  PHE GLU ALA GLN ASP THR ILE                                  
SEQRES   1 F  118  MET LYS THR LEU PRO LYS GLU ARG ARG TYR GLU THR PHE          
SEQRES   2 F  118  SER TYR LEU PRO PRO LEU SER ASP ALA GLN ILE ALA ARG          
SEQRES   3 F  118  GLN ILE GLN TYR ALA ILE ASP GLN GLY TYR HIS PRO CYS          
SEQRES   4 F  118  VAL GLU PHE ASN GLU THR SER ASN ALA GLU ILE ARG TYR          
SEQRES   5 F  118  TRP THR MET TRP LYS LEU PRO LEU PHE ASN CYS THR ASN          
SEQRES   6 F  118  ALA GLN ASP VAL LEU ASN GLU VAL GLN GLN CYS ARG SER          
SEQRES   7 F  118  GLU TYR PRO ASN CYS PHE ILE ARG VAL VAL ALA PHE ASP          
SEQRES   8 F  118  ASN ILE LYS GLN CYS GLN VAL MET SER PHE ILE VAL TYR          
SEQRES   9 F  118  LYS PRO ASN GLN ALA ASN SER GLY TYR SER GLY TYR ARG          
SEQRES  10 F  118  TYR                                                          
SEQRES   1 G  475  MET ALA TYR THR GLN SER LYS SER GLN LYS VAL GLY TYR          
SEQRES   2 G  475  GLN ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 G  475  PRO ASP TYR THR PRO LYS ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 G  475  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PHE GLU GLU          
SEQRES   5 G  475  ALA ALA ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 G  475  TRP THR THR VAL TRP THR ASP LEU LEU THR ASP LEU ASP          
SEQRES   7 G  475  ARG TYR LYS GLY CYS CYS TYR ASP ILE GLU PRO LEU PRO          
SEQRES   8 G  475  GLY GLU ASP ASN GLN PHE ILE ALA TYR ILE ALA TYR PRO          
SEQRES   9 G  475  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET LEU          
SEQRES  10 G  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 G  475  LYS ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO VAL ALA          
SEQRES  12 G  475  TYR LEU LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN          
SEQRES  13 G  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU          
SEQRES  14 G  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 G  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 G  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN ILE ASN SER          
SEQRES  17 G  475  GLN PRO PHE GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 G  475  ALA ASP ALA ILE HIS LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 G  475  ILE LYS GLY HIS TYR LEU ASN VAL THR ALA PRO THR CYS          
SEQRES  20 G  475  GLU GLU MET LEU LYS ARG ALA GLU PHE ALA LYS GLU LEU          
SEQRES  21 G  475  GLU MET PRO ILE ILE MET HIS ASP PHE LEU THR ALA GLY          
SEQRES  22 G  475  PHE THR ALA ASN THR THR LEU SER LYS TRP CYS ARG ASP          
SEQRES  23 G  475  ASN GLY MET LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 G  475  VAL MET ASP ARG GLN LYS ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 G  475  VAL LEU ALA LYS CYS LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 G  475  ILE HIS THR GLY THR VAL VAL GLY LYS LEU GLU GLY ASP          
SEQRES  27 G  475  LYS ALA VAL THR LEU GLY PHE VAL ASP LEU LEU ARG GLU          
SEQRES  28 G  475  ASN TYR ILE GLU GLN ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 G  475  THR GLN ASP TRP ALA SER MET PRO GLY VAL MET ALA VAL          
SEQRES  30 G  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 G  475  VAL ASP ILE PHE GLY ASP ASP ALA VAL LEU GLN PHE GLY          
SEQRES  32 G  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 G  475  ALA THR ALA ASN ARG VAL ALA LEU GLU ALA CYS ILE GLN          
SEQRES  34 G  475  ALA ARG ASN GLU GLY ARG ASP LEU MET ARG GLU GLY GLY          
SEQRES  35 G  475  ASP ILE ILE ARG GLU ALA ALA ARG TRP SER PRO GLU LEU          
SEQRES  36 G  475  ALA ALA ALA CYS GLU LEU TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 G  475  PHE GLU ALA GLN ASP THR ILE                                  
SEQRES   1 H  118  MET LYS THR LEU PRO LYS GLU ARG ARG TYR GLU THR PHE          
SEQRES   2 H  118  SER TYR LEU PRO PRO LEU SER ASP ALA GLN ILE ALA ARG          
SEQRES   3 H  118  GLN ILE GLN TYR ALA ILE ASP GLN GLY TYR HIS PRO CYS          
SEQRES   4 H  118  VAL GLU PHE ASN GLU THR SER ASN ALA GLU ILE ARG TYR          
SEQRES   5 H  118  TRP THR MET TRP LYS LEU PRO LEU PHE ASN CYS THR ASN          
SEQRES   6 H  118  ALA GLN ASP VAL LEU ASN GLU VAL GLN GLN CYS ARG SER          
SEQRES   7 H  118  GLU TYR PRO ASN CYS PHE ILE ARG VAL VAL ALA PHE ASP          
SEQRES   8 H  118  ASN ILE LYS GLN CYS GLN VAL MET SER PHE ILE VAL TYR          
SEQRES   9 H  118  LYS PRO ASN GLN ALA ASN SER GLY TYR SER GLY TYR ARG          
SEQRES  10 H  118  TYR                                                          
MODRES 3ZXW KCX A  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3ZXW KCX C  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3ZXW KCX E  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3ZXW KCX G  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
HET    KCX  A 201      12                                                       
HET    KCX  C 201      12                                                       
HET    KCX  E 201      12                                                       
HET    KCX  G 201      12                                                       
HET     MG  A 476       1                                                       
HET    CAP  A 477      21                                                       
HET    GOL  A1476       6                                                       
HET    GOL  A1477       6                                                       
HET    GOL  A1478       6                                                       
HET    GOL  A1479       6                                                       
HET     MG  C 476       1                                                       
HET    CAP  C 477      21                                                       
HET    GOL  C1476       6                                                       
HET    GOL  C1477       6                                                       
HET    GOL  C1478       6                                                       
HET    GOL  C1479       6                                                       
HET     MG  E 476       1                                                       
HET    CAP  E 477      21                                                       
HET    GOL  E1476       6                                                       
HET    GOL  E1477       6                                                       
HET     MG  G 476       1                                                       
HET    CAP  G 477      21                                                       
HET    GOL  G1476       6                                                       
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE                              
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   9  KCX    4(C7 H14 N2 O4)                                              
FORMUL  10   MG    4(MG 2+)                                                     
FORMUL  11  CAP    4(C6 H14 O13 P2)                                             
FORMUL  12  GOL    11(C3 H8 O3)                                                 
FORMUL  13  HOH   *905(H2 O)                                                    
HELIX    1   1 TYR A   20  TYR A   25  1                                   6    
HELIX    2   2 PRO A   49  SER A   61  1                                  13    
HELIX    3   3 VAL A   69  THR A   75  5                                   7    
HELIX    4   4 ASP A   76  LYS A   81  1                                   6    
HELIX    5   5 PRO A  104  PHE A  108  5                                   5    
HELIX    6   6 SER A  112  GLY A  122  1                                  11    
HELIX    7   7 ASN A  123  PHE A  127  5                                   5    
HELIX    8   8 PRO A  141  LYS A  146  1                                   6    
HELIX    9   9 GLY A  154  ASN A  163  1                                  10    
HELIX   10  10 SER A  181  GLY A  195  1                                  15    
HELIX   11  11 ARG A  213  GLY A  233  1                                  21    
HELIX   12  12 THR A  246  LEU A  260  1                                  15    
HELIX   13  13 PHE A  269  GLY A  288  1                                  20    
HELIX   14  14 MET A  297  ARG A  303  1                                   7    
HELIX   15  15 HIS A  310  GLY A  322  1                                  13    
HELIX   16  16 ASP A  338  GLU A  351  1                                  14    
HELIX   17  17 ARG A  358  GLY A  361  5                                   4    
HELIX   18  18 HIS A  383  TRP A  385  5                                   3    
HELIX   19  19 HIS A  386  GLY A  395  1                                  10    
HELIX   20  20 GLY A  403  GLY A  408  1                                   6    
HELIX   21  21 GLY A  412  ASN A  432  1                                  21    
HELIX   22  22 GLU A  440  SER A  452  1                                  13    
HELIX   23  23 SER A  452  LYS A  463  1                                  12    
HELIX   24  24 SER B   20  GLY B   35  1                                  16    
HELIX   25  25 ASN B   65  TYR B   80  1                                  16    
HELIX   26  26 TYR C   20  TYR C   25  1                                   6    
HELIX   27  27 PRO C   49  SER C   61  1                                  13    
HELIX   28  28 VAL C   69  THR C   75  5                                   7    
HELIX   29  29 ASP C   76  LYS C   81  1                                   6    
HELIX   30  30 PRO C  104  PHE C  108  5                                   5    
HELIX   31  31 SER C  112  GLY C  122  1                                  11    
HELIX   32  32 ASN C  123  PHE C  127  5                                   5    
HELIX   33  33 PRO C  141  LYS C  146  1                                   6    
HELIX   34  34 GLY C  154  ASN C  163  1                                  10    
HELIX   35  35 SER C  181  GLY C  195  1                                  15    
HELIX   36  36 ARG C  213  GLY C  233  1                                  21    
HELIX   37  37 THR C  246  LEU C  260  1                                  15    
HELIX   38  38 PHE C  269  GLY C  288  1                                  20    
HELIX   39  39 MET C  297  ARG C  303  1                                   7    
HELIX   40  40 HIS C  310  GLY C  322  1                                  13    
HELIX   41  41 ASP C  338  GLU C  351  1                                  14    
HELIX   42  42 ARG C  358  GLY C  361  5                                   4    
HELIX   43  43 HIS C  383  TRP C  385  5                                   3    
HELIX   44  44 HIS C  386  GLY C  395  1                                  10    
HELIX   45  45 GLY C  403  GLY C  408  1                                   6    
HELIX   46  46 GLY C  412  GLY C  434  1                                  23    
HELIX   47  47 GLU C  440  SER C  452  1                                  13    
HELIX   48  48 SER C  452  TRP C  462  1                                  11    
HELIX   49  49 SER D   20  GLY D   35  1                                  16    
HELIX   50  50 ASN D   65  TYR D   80  1                                  16    
HELIX   51  51 TYR E   20  TYR E   25  1                                   6    
HELIX   52  52 PRO E   49  SER E   61  1                                  13    
HELIX   53  53 VAL E   69  THR E   75  5                                   7    
HELIX   54  54 ASP E   76  LYS E   81  1                                   6    
HELIX   55  55 PRO E  104  PHE E  108  5                                   5    
HELIX   56  56 SER E  112  GLY E  122  1                                  11    
HELIX   57  57 ASN E  123  PHE E  127  5                                   5    
HELIX   58  58 PRO E  141  LYS E  146  1                                   6    
HELIX   59  59 GLY E  154  ASN E  163  1                                  10    
HELIX   60  60 SER E  181  GLY E  195  1                                  15    
HELIX   61  61 ARG E  213  GLY E  233  1                                  21    
HELIX   62  62 THR E  246  LEU E  260  1                                  15    
HELIX   63  63 PHE E  269  GLY E  288  1                                  20    
HELIX   64  64 MET E  297  ARG E  303  1                                   7    
HELIX   65  65 HIS E  310  GLY E  322  1                                  13    
HELIX   66  66 ASP E  338  GLU E  351  1                                  14    
HELIX   67  67 ARG E  358  GLY E  361  5                                   4    
HELIX   68  68 HIS E  383  TRP E  385  5                                   3    
HELIX   69  69 HIS E  386  GLY E  395  1                                  10    
HELIX   70  70 GLY E  403  GLY E  408  1                                   6    
HELIX   71  71 GLY E  412  ASN E  432  1                                  21    
HELIX   72  72 GLU E  440  ARG E  450  1                                  11    
HELIX   73  73 SER E  452  TRP E  462  1                                  11    
HELIX   74  74 SER F   20  GLY F   35  1                                  16    
HELIX   75  75 ASN F   65  TYR F   80  1                                  16    
HELIX   76  76 TYR G   20  TYR G   25  1                                   6    
HELIX   77  77 PRO G   49  SER G   61  1                                  13    
HELIX   78  78 VAL G   69  THR G   75  5                                   7    
HELIX   79  79 ASP G   76  LYS G   81  1                                   6    
HELIX   80  80 PRO G  104  PHE G  108  5                                   5    
HELIX   81  81 SER G  112  GLY G  122  1                                  11    
HELIX   82  82 ASN G  123  PHE G  127  5                                   5    
HELIX   83  83 PRO G  141  LYS G  146  1                                   6    
HELIX   84  84 GLY G  154  ASN G  163  1                                  10    
HELIX   85  85 SER G  181  GLY G  195  1                                  15    
HELIX   86  86 ARG G  213  GLY G  233  1                                  21    
HELIX   87  87 THR G  246  LEU G  260  1                                  15    
HELIX   88  88 PHE G  269  GLY G  288  1                                  20    
HELIX   89  89 MET G  297  ARG G  303  1                                   7    
HELIX   90  90 HIS G  310  GLY G  322  1                                  13    
HELIX   91  91 ASP G  338  GLU G  351  1                                  14    
HELIX   92  92 ARG G  358  GLY G  361  5                                   4    
HELIX   93  93 HIS G  383  TRP G  385  5                                   3    
HELIX   94  94 HIS G  386  GLY G  395  1                                  10    
HELIX   95  95 GLY G  403  GLY G  408  1                                   6    
HELIX   96  96 GLY G  412  GLU G  433  1                                  22    
HELIX   97  97 GLU G  440  ARG G  450  1                                  11    
HELIX   98  98 SER G  452  LYS G  463  1                                  12    
HELIX   99  99 SER H   20  GLY H   35  1                                  16    
HELIX  100 100 ASN H   65  TYR H   80  1                                  16    
SHEET    1  AA 5 CYS A  83  PRO A  89  0                                        
SHEET    2  AA 5 PHE A  97  TYR A 103 -1  O  ILE A  98   N  GLU A  88           
SHEET    3  AA 5 ILE A  36  PRO A  44 -1  O  ILE A  36   N  TYR A 103           
SHEET    4  AA 5 LEU A 130  ARG A 139 -1  N  LYS A 131   O  THR A  43           
SHEET    5  AA 5 GLY A 308  ILE A 309  1  O  GLY A 308   N  LEU A 135           
SHEET    1  AB 9 LEU A 169  THR A 173  0                                        
SHEET    2  AB 9 ALA A 398  GLN A 401  1  O  ALA A 398   N  LEU A 169           
SHEET    3  AB 9 MET A 375  SER A 379  1  O  ALA A 376   N  VAL A 399           
SHEET    4  AB 9 HIS A 325  HIS A 327  1  O  ILE A 326   N  VAL A 377           
SHEET    5  AB 9 LEU A 290  HIS A 294  1  O  ILE A 293   N  HIS A 327           
SHEET    6  AB 9 ILE A 264  ASP A 268  1  O  ILE A 265   N  HIS A 292           
SHEET    7  AB 9 GLY A 237  ASN A 241  1  O  LEU A 240   N  MET A 266           
SHEET    8  AB 9 PHE A 199  KCX A 201  1  O  THR A 200   N  TYR A 239           
SHEET    9  AB 9 LEU A 169  THR A 173  1  O  LEU A 170   N  PHE A 199           
SHEET    1  AC 2 TYR A 353  ILE A 354  0                                        
SHEET    2  AC 2 GLN A 366  ASP A 367 -1  O  GLN A 366   N  ILE A 354           
SHEET    1  BA 4 THR B  54  TRP B  56  0                                        
SHEET    2  BA 4 HIS B  37  ASN B  43 -1  O  VAL B  40   N  TRP B  56           
SHEET    3  BA 4 PHE B  84  ASP B  91 -1  O  PHE B  84   N  ASN B  43           
SHEET    4  BA 4 CYS B  96  TYR B 104 -1  O  CYS B  96   N  ASP B  91           
SHEET    1  CA 5 CYS C  83  PRO C  89  0                                        
SHEET    2  CA 5 PHE C  97  TYR C 103 -1  O  ILE C  98   N  GLU C  88           
SHEET    3  CA 5 ILE C  36  PRO C  44 -1  O  ILE C  36   N  TYR C 103           
SHEET    4  CA 5 LEU C 130  ARG C 139 -1  N  LYS C 131   O  THR C  43           
SHEET    5  CA 5 GLY C 308  ILE C 309  1  O  GLY C 308   N  LEU C 135           
SHEET    1  CB 9 LEU C 169  THR C 173  0                                        
SHEET    2  CB 9 ALA C 398  GLN C 401  1  O  ALA C 398   N  LEU C 169           
SHEET    3  CB 9 MET C 375  SER C 379  1  O  ALA C 376   N  VAL C 399           
SHEET    4  CB 9 HIS C 325  HIS C 327  1  O  ILE C 326   N  VAL C 377           
SHEET    5  CB 9 LEU C 290  HIS C 294  1  O  ILE C 293   N  HIS C 327           
SHEET    6  CB 9 ILE C 264  ASP C 268  1  O  ILE C 265   N  HIS C 292           
SHEET    7  CB 9 GLY C 237  ASN C 241  1  O  LEU C 240   N  MET C 266           
SHEET    8  CB 9 PHE C 199  KCX C 201  1  O  THR C 200   N  TYR C 239           
SHEET    9  CB 9 LEU C 169  THR C 173  1  O  LEU C 170   N  PHE C 199           
SHEET    1  CC 2 TYR C 353  ILE C 354  0                                        
SHEET    2  CC 2 GLN C 366  ASP C 367 -1  O  GLN C 366   N  ILE C 354           
SHEET    1  DA 4 THR D  54  TRP D  56  0                                        
SHEET    2  DA 4 HIS D  37  ASN D  43 -1  O  VAL D  40   N  TRP D  56           
SHEET    3  DA 4 PHE D  84  ASP D  91 -1  O  PHE D  84   N  ASN D  43           
SHEET    4  DA 4 CYS D  96  TYR D 104 -1  O  CYS D  96   N  ASP D  91           
SHEET    1  EA 5 CYS E  83  PRO E  89  0                                        
SHEET    2  EA 5 PHE E  97  TYR E 103 -1  O  ILE E  98   N  GLU E  88           
SHEET    3  EA 5 ILE E  36  PRO E  44 -1  O  ILE E  36   N  TYR E 103           
SHEET    4  EA 5 LEU E 130  ARG E 139 -1  N  LYS E 131   O  THR E  43           
SHEET    5  EA 5 GLY E 308  ILE E 309  1  O  GLY E 308   N  LEU E 135           
SHEET    1  EB 9 LEU E 169  THR E 173  0                                        
SHEET    2  EB 9 ALA E 398  GLN E 401  1  O  ALA E 398   N  LEU E 169           
SHEET    3  EB 9 MET E 375  SER E 379  1  O  ALA E 376   N  VAL E 399           
SHEET    4  EB 9 HIS E 325  HIS E 327  1  O  ILE E 326   N  VAL E 377           
SHEET    5  EB 9 LEU E 290  HIS E 294  1  O  ILE E 293   N  HIS E 327           
SHEET    6  EB 9 ILE E 264  ASP E 268  1  O  ILE E 265   N  HIS E 292           
SHEET    7  EB 9 GLY E 237  ASN E 241  1  O  LEU E 240   N  MET E 266           
SHEET    8  EB 9 PHE E 199  KCX E 201  1  O  THR E 200   N  TYR E 239           
SHEET    9  EB 9 LEU E 169  THR E 173  1  O  LEU E 170   N  PHE E 199           
SHEET    1  EC 2 TYR E 353  ILE E 354  0                                        
SHEET    2  EC 2 GLN E 366  ASP E 367 -1  O  GLN E 366   N  ILE E 354           
SHEET    1  FA 4 THR F  54  TRP F  56  0                                        
SHEET    2  FA 4 HIS F  37  ASN F  43 -1  O  VAL F  40   N  TRP F  56           
SHEET    3  FA 4 PHE F  84  ASP F  91 -1  O  PHE F  84   N  ASN F  43           
SHEET    4  FA 4 CYS F  96  TYR F 104 -1  O  CYS F  96   N  ASP F  91           
SHEET    1  GA 5 CYS G  83  PRO G  89  0                                        
SHEET    2  GA 5 PHE G  97  TYR G 103 -1  O  ILE G  98   N  GLU G  88           
SHEET    3  GA 5 ILE G  36  PRO G  44 -1  O  ILE G  36   N  TYR G 103           
SHEET    4  GA 5 LEU G 130  ARG G 139 -1  N  LYS G 131   O  THR G  43           
SHEET    5  GA 5 GLY G 308  ILE G 309  1  O  GLY G 308   N  LEU G 135           
SHEET    1  GB 9 LEU G 169  THR G 173  0                                        
SHEET    2  GB 9 ALA G 398  GLN G 401  1  O  ALA G 398   N  LEU G 169           
SHEET    3  GB 9 MET G 375  SER G 379  1  O  ALA G 376   N  VAL G 399           
SHEET    4  GB 9 HIS G 325  HIS G 327  1  O  ILE G 326   N  VAL G 377           
SHEET    5  GB 9 LEU G 290  HIS G 294  1  O  ILE G 293   N  HIS G 327           
SHEET    6  GB 9 ILE G 264  ASP G 268  1  O  ILE G 265   N  HIS G 292           
SHEET    7  GB 9 GLY G 237  ASN G 241  1  O  LEU G 240   N  MET G 266           
SHEET    8  GB 9 PHE G 199  KCX G 201  1  O  THR G 200   N  TYR G 239           
SHEET    9  GB 9 LEU G 169  THR G 173  1  O  LEU G 170   N  PHE G 199           
SHEET    1  GC 2 TYR G 353  ILE G 354  0                                        
SHEET    2  GC 2 GLN G 366  ASP G 367 -1  O  GLN G 366   N  ILE G 354           
SHEET    1  HA 4 THR H  54  TRP H  56  0                                        
SHEET    2  HA 4 HIS H  37  ASN H  43 -1  O  VAL H  40   N  TRP H  56           
SHEET    3  HA 4 PHE H  84  ASP H  91 -1  O  PHE H  84   N  ASN H  43           
SHEET    4  HA 4 CYS H  96  TYR H 104 -1  O  CYS H  96   N  ASP H  91           
SSBOND   1 CYS A  172    CYS A  192                          1555   1555  2.08  
SSBOND   2 CYS A  247    CYS E  247                          1555   7555  2.04  
SSBOND   3 CYS C  172    CYS C  192                          1555   1555  2.08  
SSBOND   4 CYS E  172    CYS E  192                          1555   1555  2.08  
SSBOND   5 CYS G  172    CYS G  192                          1555   1555  2.08  
SSBOND   6 CYS C  247    CYS C  247                          1555   1555  2.03  
SSBOND   7 CYS G  247    CYS G  247                          1555   1555  2.04  
LINK         C   THR A 200                 N   KCX A 201     1555   1555  1.33  
LINK         C   KCX A 201                 N   ASP A 202     1555   1555  1.33  
LINK         OQ1 KCX A 201                MG    MG A 476     1555   1555  2.60  
LINK         OQ2 KCX A 201                MG    MG A 476     1555   1555  2.92  
LINK        MG    MG A 476                 O7  CAP A 477     1555   1555  2.29  
LINK        MG    MG A 476                 OD1 ASP A 203     1555   1555  1.86  
LINK        MG    MG A 476                 OE1 GLU A 204     1555   1555  2.07  
LINK        MG    MG A 476                 O2  CAP A 477     1555   1555  2.42  
LINK        MG    MG A 476                 O3  CAP A 477     1555   1555  2.46  
LINK         C   THR C 200                 N   KCX C 201     1555   1555  1.33  
LINK         C   KCX C 201                 N   ASP C 202     1555   1555  1.33  
LINK         OQ1 KCX C 201                MG    MG C 476     1555   1555  2.42  
LINK         OQ2 KCX C 201                MG    MG C 476     1555   1555  2.93  
LINK        MG    MG C 476                 O2  CAP C 477     1555   1555  2.32  
LINK        MG    MG C 476                 O3  CAP C 477     1555   1555  2.38  
LINK        MG    MG C 476                 OE1 GLU C 204     1555   1555  2.06  
LINK        MG    MG C 476                 OD1 ASP C 203     1555   1555  1.95  
LINK        MG    MG C 476                 O6  CAP C 477     1555   1555  2.28  
LINK         C   THR E 200                 N   KCX E 201     1555   1555  1.33  
LINK         OQ2 KCX E 201                MG    MG E 476     1555   1555  2.96  
LINK         OQ1 KCX E 201                MG    MG E 476     1555   1555  2.46  
LINK         C   KCX E 201                 N   ASP E 202     1555   1555  1.33  
LINK        MG    MG E 476                 O3  CAP E 477     1555   1555  2.26  
LINK        MG    MG E 476                 O7  CAP E 477     1555   1555  2.30  
LINK        MG    MG E 476                 OD1 ASP E 203     1555   1555  2.06  
LINK        MG    MG E 476                 OE1 GLU E 204     1555   1555  2.09  
LINK        MG    MG E 476                 O2  CAP E 477     1555   1555  2.32  
LINK         C   THR G 200                 N   KCX G 201     1555   1555  1.33  
LINK         OQ2 KCX G 201                MG    MG G 476     1555   1555  2.90  
LINK         OQ1 KCX G 201                MG    MG G 476     1555   1555  2.42  
LINK         C   KCX G 201                 N   ASP G 202     1555   1555  1.33  
LINK        MG    MG G 476                 O2  CAP G 477     1555   1555  2.30  
LINK        MG    MG G 476                 O3  CAP G 477     1555   1555  2.36  
LINK        MG    MG G 476                 O7  CAP G 477     1555   1555  2.37  
LINK        MG    MG G 476                 OE1 GLU G 204     1555   1555  2.11  
LINK        MG    MG G 476                 OD1 ASP G 203     1555   1555  1.99  
CISPEP   1 LYS A  175    PRO A  176          0        -1.29                     
CISPEP   2 LYS C  175    PRO C  176          0        -1.70                     
CISPEP   3 LYS E  175    PRO E  176          0        -3.70                     
CISPEP   4 LYS G  175    PRO G  176          0        -4.35                     
SITE     1 AC1  5 LYS A 177  KCX A 201  ASP A 203  GLU A 204                    
SITE     2 AC1  5 CAP A 477                                                     
SITE     1 AC2 29 THR A 173  LYS A 175  LYS A 177  KCX A 201                    
SITE     2 AC2 29 ASP A 203  GLU A 204  HIS A 294  ARG A 295                    
SITE     3 AC2 29 HIS A 327  LYS A 334  LEU A 335  SER A 379                    
SITE     4 AC2 29 GLY A 380  GLY A 381  GLY A 403  GLY A 404                    
SITE     5 AC2 29  MG A 476  HOH A2105  HOH A2170  HOH A2171                    
SITE     6 AC2 29 HOH A2182  HOH A2216  HOH A2217  HOH A2231                    
SITE     7 AC2 29 GLU E  60  THR E  65  TRP E  66  ASN E 123                    
SITE     8 AC2 29 HOH E2028                                                     
SITE     1 AC3  4 KCX C 201  ASP C 203  GLU C 204  CAP C 477                    
SITE     1 AC4 29 GLU C  60  THR C  65  TRP C  66  ASN C 123                    
SITE     2 AC4 29 THR C 173  LYS C 175  LYS C 177  KCX C 201                    
SITE     3 AC4 29 ASP C 203  GLU C 204  HIS C 294  ARG C 295                    
SITE     4 AC4 29 HIS C 327  LYS C 334  LEU C 335  SER C 379                    
SITE     5 AC4 29 GLY C 380  GLY C 381  GLY C 403  GLY C 404                    
SITE     6 AC4 29  MG C 476  HOH C2038  HOH C2077  HOH C2116                    
SITE     7 AC4 29 HOH C2160  HOH C2161  HOH C2173  HOH C2206                    
SITE     8 AC4 29 HOH C2207                                                     
SITE     1 AC5  4 KCX E 201  ASP E 203  GLU E 204  CAP E 477                    
SITE     1 AC6 27 GLU A  60  THR A  65  TRP A  66  ASN A 123                    
SITE     2 AC6 27 HOH A2068  THR E 173  LYS E 175  LYS E 177                    
SITE     3 AC6 27 KCX E 201  ASP E 203  GLU E 204  HIS E 294                    
SITE     4 AC6 27 ARG E 295  HIS E 327  LYS E 334  LEU E 335                    
SITE     5 AC6 27 SER E 379  GLY E 380  GLY E 381  GLY E 403                    
SITE     6 AC6 27 GLY E 404   MG E 476  HOH E2142  HOH E2143                    
SITE     7 AC6 27 HOH E2154  HOH E2188  HOH E2189                               
SITE     1 AC7  4 KCX G 201  ASP G 203  GLU G 204  CAP G 477                    
SITE     1 AC8 28 GLU G  60  THR G  65  TRP G  66  ASN G 123                    
SITE     2 AC8 28 THR G 173  LYS G 175  LYS G 177  KCX G 201                    
SITE     3 AC8 28 ASP G 203  GLU G 204  HIS G 294  ARG G 295                    
SITE     4 AC8 28 HIS G 327  LYS G 334  LEU G 335  SER G 379                    
SITE     5 AC8 28 GLY G 380  GLY G 381  GLY G 403  GLY G 404                    
SITE     6 AC8 28  MG G 476  HOH G2041  HOH G2141  HOH G2142                    
SITE     7 AC8 28 HOH G2143  HOH G2154  HOH G2156  HOH G2186                    
SITE     1 AC9  5 LYS C  18  THR C  65  TRP C  66  THR C  67                    
SITE     2 AC9  5 THR C  68                                                     
SITE     1 BC1  6 LYS A  18  TYR A  24  TRP A  66  THR A  67                    
SITE     2 BC1  6 THR A  68  HOH A2007                                          
SITE     1 BC2  9 VAL E  17  LYS E  18  TYR E  20  TYR E  24                    
SITE     2 BC2  9 THR E  65  TRP E  66  THR E  67  THR E  68                    
SITE     3 BC2  9 HOH E2010                                                     
SITE     1 BC3  8 LYS G  18  TYR G  24  THR G  65  TRP G  66                    
SITE     2 BC3  8 THR G  67  THR G  68  HOH G2006  HOH G2040                    
SITE     1 BC4  5 ARG E 295  HIS E 298  ASP E 302  ASP E 473                    
SITE     2 BC4  5 HOH E2159                                                     
SITE     1 BC5  6 ARG A 295  HIS A 298  ASP A 302  GLU A 336                    
SITE     2 BC5  6 ASP A 473  HOH A2183                                          
SITE     1 BC6  2 GLU A  88  HOH A2232                                          
SITE     1 BC7  5 ASP C  86  ILE C  87  GLU C  88  ASP E  86                    
SITE     2 BC7  5 ILE E  87                                                     
SITE     1 BC8  7 ARG A 215  PHE A 256  GLU A 259  HOH A2146                    
SITE     2 BC8  7 HOH A2235  ASP G 286  ASN G 287                               
SITE     1 BC9  4 LYS C 258  GLU C 261  MET C 262  PRO C 263                    
SITE     1 CC1  5 ARG C 295  HIS C 298  ASP C 302  GLU C 336                    
SITE     2 CC1  5 ASP C 473                                                     
CRYST1  111.500  111.500  397.000  90.00  90.00  90.00 P 43 21 2    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      0.008969  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008969  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002519        0.00000                         
MTRIX1   1  0.004639 -1.000000 -0.002172       -6.72900    1                    
MTRIX2   1  0.994900  0.004835 -0.101100        0.00591    1                    
MTRIX3   1  0.101100 -0.001692  0.994900        0.33050    1                    
MTRIX1   2 -0.994800 -0.006256  0.101300       -6.69900    1                    
MTRIX2   2 -0.003863 -0.995000 -0.099390       -6.66000    1                    
MTRIX3   2  0.101400 -0.099270  0.989900       -0.05890    1                    
MTRIX1   3  0.001265  0.995700  0.092930       -0.07644    1                    
MTRIX2   3 -1.000000 -0.000943 -0.003507       -6.79500    1                    
MTRIX3   3 -0.003404 -0.092940  0.995700       -0.30890    1                    
MTRIX1   4 -0.000793 -1.000000 -0.004161       -6.71300    1                    
MTRIX2   4  0.994500 -0.000353 -0.104700        0.06493    1                    
MTRIX3   4  0.104700 -0.004222  0.994500        0.26590    1                    
MTRIX1   5 -0.995100 -0.004020  0.099140       -6.64900    1                    
MTRIX2   5 -0.006712 -0.994200 -0.107700       -6.90500    1                    
MTRIX3   5  0.098990 -0.107800  0.989200       -0.37200    1                    
MTRIX1   6 -0.003737  0.996200  0.086690       -0.45890    1                    
MTRIX2   6 -0.999900 -0.002806 -0.010850       -6.81900    1                    
MTRIX3   6 -0.010570 -0.086730  0.996200       -0.53710    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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