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Database: PDB
Entry: 2V63
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Original site: 2V63 
HEADER    OXIDOREDUCTASE                          13-JUL-07   2V63              
TITLE     CRYSTAL STRUCTURE OF RUBISCO FROM CHLAMYDOMONAS REINHARDTII           
TITLE    2 WITH A LARGE-SUBUNIT V331A MUTATION                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;             
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 SYNONYM: RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE LARGE                 
COMPND   5  CHAIN, RUBISCO LARGE SUBUNIT;                                       
COMPND   6 EC: 4.1.1.39;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1;           
COMPND  11 CHAIN: I, J, K, L, M, N, O, P;                                       
COMPND  12 SYNONYM: RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE SMALL                 
COMPND  13  CHAIN, RUBISCO SMALL SUBUNIT 1;                                     
COMPND  14 EC: 4.1.1.39;                                                        
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;                      
SOURCE   3 ORGANISM_TAXID: 3055;                                                
SOURCE   4 STRAIN: 2137;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PLS-V331A;                                
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;                      
SOURCE  10 ORGANISM_TAXID: 3055;                                                
SOURCE  11 STRAIN: 2137;                                                        
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: PLS-V331A                                 
KEYWDS    LARGE SUBUNIT LOOP 6 MUTATION, CO2/O2 SPECIFICITY, CARBON             
KEYWDS   2 DIOXIDE FIXATION, PHOTOSYNTHESIS, TRANSIT PEPTIDE,                   
KEYWDS   3 PHOTORESPIRATION, METAL-BINDING, HYDROXYLATION,                      
KEYWDS   4 OXIDOREDUCTASE, METHYLATION, CHLOROPLAST, CALVIN CYCLE,              
KEYWDS   5 MONOOXYGENASE, LYASE, RUBISCO, PLASTID, MAGNESIUM,                   
KEYWDS   6 ACETYLATION                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.KARKEHABADI,S.SATAGOPAN,T.C.TAYLOR,R.J.SPREITZER,                   
AUTHOR   2 I.ANDERSSON                                                          
REVDAT   6   24-FEB-09 2V63    1       VERSN                                    
REVDAT   5   23-OCT-07 2V63    1       REMARK                                   
REVDAT   4   02-OCT-07 2V63    1       JRNL   REMARK                            
REVDAT   3   28-AUG-07 2V63    1       AUTHOR                                   
REVDAT   2   07-AUG-07 2V63    1       SOURCE REMARK                            
REVDAT   1   31-JUL-07 2V63    0                                                
JRNL        AUTH   S.KARKEHABADI,S.SATAGOPAN,T.C.TAYLOR,R.J.SPREITZER,          
JRNL        AUTH 2 I.ANDERSSON                                                  
JRNL        TITL   STRUCTURAL ANALYSIS OF ALTERED LARGE-SUBUNIT LOOP-           
JRNL        TITL 2 6-CARBOXY-TERMINUS INTERACTIONS THAT INFLUENCE               
JRNL        TITL 3 CATALYTIC EFFICIENCY AND CO2 O2 SPECIFICITY OF               
JRNL        TITL 4 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE OXYGENASE              
JRNL        REF    BIOCHEMISTRY                  V.  46 11080 2007              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   17824672                                                     
JRNL        DOI    10.1021/BI701063F                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 369935                         
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) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 19621                           
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 17388                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 58.87                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2430                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 912                          
REMARK   3   BIN FREE R VALUE                    : 0.2700                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 37813                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 768                                     
REMARK   3   SOLVENT ATOMS            : 2892                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.05                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.44000                                              
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : -0.46000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.05000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.162         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.135         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.088         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.794         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 39483 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 53456 ; 1.108 ; 1.958       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4828 ; 5.631 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1859 ;30.604 ;23.168       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  6328 ;13.328 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   319 ;15.644 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  5656 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 30387 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A): 19533 ; 0.192 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 27022 ; 0.306 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  3203 ; 0.120 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    14 ; 0.024 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   127 ; 0.291 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.133 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 24678 ; 0.654 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 38601 ; 1.043 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 16985 ; 1.730 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 14855 ; 2.795 ; 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 : 16                                
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A                               
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     13       A     438      1                      
REMARK   3           2     A    440       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   3636 ;   .00 ;   .05           
REMARK   3   TIGHT THERMAL      1    A (A**2):   3636 ;   .00 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B     13       B     438      1                      
REMARK   3           1     A     13       A     438      1                      
REMARK   3           2     B    440       B     477      1                      
REMARK   3           2     A    440       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    B    (A):   3623 ;   .02 ;   .05           
REMARK   3   TIGHT THERMAL      2    B (A**2):   3623 ;   .09 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : C A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C     13       C     437      1                      
REMARK   3           1     A     13       A     437      1                      
REMARK   3           2     C    442       C     477      1                      
REMARK   3           2     A    442       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    C    (A):   3610 ;   .02 ;   .05           
REMARK   3   TIGHT THERMAL      3    C (A**2):   3610 ;   .09 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : D A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     D     13       D     438      1                      
REMARK   3           1     A     13       A     438      1                      
REMARK   3           2     D    440       D     477      1                      
REMARK   3           2     A    440       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   4    D    (A):   3620 ;   .02 ;   .05           
REMARK   3   TIGHT THERMAL      4    D (A**2):   3620 ;   .09 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 5                                  
REMARK   3     CHAIN NAMES                    : E A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     E     13       E     438      1                      
REMARK   3           1     A     13       A     438      1                      
REMARK   3           2     E    440       E     477      1                      
REMARK   3           2     A    440       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   5    E    (A):   3620 ;   .02 ;   .05           
REMARK   3   TIGHT THERMAL      5    E (A**2):   3620 ;   .12 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 6                                  
REMARK   3     CHAIN NAMES                    : F A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     F     13       F     438      1                      
REMARK   3           1     A     13       A     438      1                      
REMARK   3           2     F    440       F     477      1                      
REMARK   3           2     A    440       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   6    F    (A):   3610 ;   .02 ;   .05           
REMARK   3   TIGHT THERMAL      6    F (A**2):   3610 ;   .15 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 7                                  
REMARK   3     CHAIN NAMES                    : G A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     G     13       G     438      1                      
REMARK   3           1     A     13       A     438      1                      
REMARK   3           2     G    440       G     477      1                      
REMARK   3           2     A    440       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   7    G    (A):   3618 ;   .02 ;   .05           
REMARK   3   TIGHT THERMAL      7    G (A**2):   3618 ;   .11 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 8                                  
REMARK   3     CHAIN NAMES                    : H A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     H     13       H     438      1                      
REMARK   3           1     A     13       A     438      1                      
REMARK   3           2     H    440       H     477      1                      
REMARK   3           2     A    440       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   8    H    (A):   3620 ;   .02 ;   .05           
REMARK   3   TIGHT THERMAL      8    H (A**2):   3620 ;   .09 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 9                                  
REMARK   3     CHAIN NAMES                    : I                               
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     I      1       I      83      1                      
REMARK   3           2     I     85       I     129      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   9    I    (A):   1039 ;   .00 ;   .05           
REMARK   3   TIGHT THERMAL      9    I (A**2):   1039 ;   .00 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 10                                 
REMARK   3     CHAIN NAMES                    : J I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     J      1       J      83      1                      
REMARK   3           1     I      1       I      83      1                      
REMARK   3           2     J     85       J     129      1                      
REMARK   3           2     I     85       I     129      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  10    J    (A):   1037 ;   .03 ;   .05           
REMARK   3   TIGHT THERMAL     10    J (A**2):   1037 ;   .08 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 11                                 
REMARK   3     CHAIN NAMES                    : K I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     K      1       K      83      1                      
REMARK   3           1     I      1       I      83      1                      
REMARK   3           2     K     85       K     129      1                      
REMARK   3           2     I     85       I     129      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  11    K    (A):   1037 ;   .02 ;   .05           
REMARK   3   TIGHT THERMAL     11    K (A**2):   1037 ;   .09 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 12                                 
REMARK   3     CHAIN NAMES                    : L I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     L      1       L      83      1                      
REMARK   3           1     I      1       I      83      1                      
REMARK   3           2     L     85       L     129      1                      
REMARK   3           2     I     85       I     129      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  12    L    (A):   1039 ;   .03 ;   .05           
REMARK   3   TIGHT THERMAL     12    L (A**2):   1039 ;   .10 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 13                                 
REMARK   3     CHAIN NAMES                    : M I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     M      1       M      83      1                      
REMARK   3           1     I      1       I      83      1                      
REMARK   3           2     M     85       M     129      1                      
REMARK   3           2     I     85       I     129      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  13    M    (A):   1036 ;   .03 ;   .05           
REMARK   3   TIGHT THERMAL     13    M (A**2):   1036 ;   .13 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 14                                 
REMARK   3     CHAIN NAMES                    : N I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     N      1       N      83      1                      
REMARK   3           1     I      1       I      83      1                      
REMARK   3           2     N     85       N     129      1                      
REMARK   3           2     I     85       I     129      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  14    N    (A):   1038 ;   .02 ;   .05           
REMARK   3   TIGHT THERMAL     14    N (A**2):   1038 ;   .12 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 15                                 
REMARK   3     CHAIN NAMES                    : O I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     O      1       O      83      1                      
REMARK   3           1     I      1       I      83      1                      
REMARK   3           2     O     85       O     129      1                      
REMARK   3           2     I     85       I     129      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  15    O    (A):   1037 ;   .02 ;   .05           
REMARK   3   TIGHT THERMAL     15    O (A**2):   1037 ;   .08 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 16                                 
REMARK   3     CHAIN NAMES                    : P I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     P      1       P      83      1                      
REMARK   3           1     I      1       I      83      1                      
REMARK   3           2     P     85       P     129      1                      
REMARK   3           2     I     85       I     129      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  16    P    (A):   1039 ;   .02 ;   .05           
REMARK   3   TIGHT THERMAL     16    P (A**2):   1039 ;   .12 ;   .50           
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 2V63 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-JUL-07.                  
REMARK 100 THE PDBE ID CODE IS EBI-33172.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9392                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 389935                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.80                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NONE                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.4                               
REMARK 200  DATA REDUNDANCY                : 14.8                               
REMARK 200  R MERGE                    (I) : 0.23                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.50                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 60.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.40                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1GK8                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):2.01                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       88.72300            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 127910 ANGSTROM**2                        
REMARK 350 SURFACE AREA OF THE COMPLEX: 153680 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -728.8 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,            
REMARK 350                    AND CHAINS: J, K, L, M, N, O, P                   
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, VAL 331 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, VAL 331 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, VAL 331 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, VAL 331 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN E, VAL 331 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, VAL 331 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN G, VAL 331 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN H, VAL 331 TO ALA                        
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     LYS A     8                                                      
REMARK 465     LEU A   475                                                      
REMARK 465     MET B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     GLN B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     LEU B   475                                                      
REMARK 465     MET C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     PRO C     3                                                      
REMARK 465     GLN C     4                                                      
REMARK 465     THR C     5                                                      
REMARK 465     GLU C     6                                                      
REMARK 465     THR C     7                                                      
REMARK 465     LYS C     8                                                      
REMARK 465     LEU C   475                                                      
REMARK 465     MET D     1                                                      
REMARK 465     VAL D     2                                                      
REMARK 465     PRO D     3                                                      
REMARK 465     GLN D     4                                                      
REMARK 465     THR D     5                                                      
REMARK 465     GLU D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     LYS D     8                                                      
REMARK 465     ALA D     9                                                      
REMARK 465     GLY D    10                                                      
REMARK 465     LEU D   475                                                      
REMARK 465     MET E     1                                                      
REMARK 465     VAL E     2                                                      
REMARK 465     PRO E     3                                                      
REMARK 465     GLN E     4                                                      
REMARK 465     THR E     5                                                      
REMARK 465     GLU E     6                                                      
REMARK 465     THR E     7                                                      
REMARK 465     LYS E     8                                                      
REMARK 465     ALA E     9                                                      
REMARK 465     GLY E    10                                                      
REMARK 465     LEU E   475                                                      
REMARK 465     MET F     1                                                      
REMARK 465     VAL F     2                                                      
REMARK 465     PRO F     3                                                      
REMARK 465     GLN F     4                                                      
REMARK 465     THR F     5                                                      
REMARK 465     GLU F     6                                                      
REMARK 465     THR F     7                                                      
REMARK 465     LYS F     8                                                      
REMARK 465     LEU F   475                                                      
REMARK 465     MET G     1                                                      
REMARK 465     VAL G     2                                                      
REMARK 465     PRO G     3                                                      
REMARK 465     GLN G     4                                                      
REMARK 465     THR G     5                                                      
REMARK 465     GLU G     6                                                      
REMARK 465     THR G     7                                                      
REMARK 465     LYS G     8                                                      
REMARK 465     LEU G   475                                                      
REMARK 465     MET H     1                                                      
REMARK 465     VAL H     2                                                      
REMARK 465     PRO H     3                                                      
REMARK 465     GLN H     4                                                      
REMARK 465     THR H     5                                                      
REMARK 465     GLU H     6                                                      
REMARK 465     THR H     7                                                      
REMARK 465     LYS H     8                                                      
REMARK 465     LEU H   475                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLU G    93  -  O    HOH G  2058              2.15            
REMARK 500   O    PRO I    20  -  O    HOH I  2010              2.16            
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 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      -80.48   -138.75                                   
REMARK 500    ASN A 207      -91.39   -119.63                                   
REMARK 500    MET A 212      107.84   -165.91                                   
REMARK 500    MET A 297       -8.68     86.32                                   
REMARK 500    ALA A 331      -44.89     73.92                                   
REMARK 500    SER B  62      -80.29   -137.18                                   
REMARK 500    ASN B 207      -89.56   -121.03                                   
REMARK 500    MET B 212      107.30   -165.96                                   
REMARK 500    MET B 297       -8.13     86.46                                   
REMARK 500    ALA B 331      -45.72     75.38                                   
REMARK 500    ASP B 357       89.92   -158.31                                   
REMARK 500    SER C  62      -81.52   -138.78                                   
REMARK 500    ASN C 207      -89.20   -119.69                                   
REMARK 500    MET C 212      106.63   -166.10                                   
REMARK 500    ALA C 296      130.98    -39.50                                   
REMARK 500    MET C 297       -8.47     87.63                                   
REMARK 500    ALA C 331      -46.61     72.82                                   
REMARK 500    ASP C 357       89.87   -158.38                                   
REMARK 500    SER D  62      -81.70   -137.81                                   
REMARK 500    ASN D 207      -90.69   -119.57                                   
REMARK 500    MET D 212      109.94   -164.83                                   
REMARK 500    ALA D 296      131.84    -38.70                                   
REMARK 500    MET D 297      -11.06     86.71                                   
REMARK 500    ALA D 331      -44.59     76.12                                   
REMARK 500    SER E  62      -81.43   -141.96                                   
REMARK 500    ASN E 207      -92.18   -119.57                                   
REMARK 500    MET E 212      109.88   -162.16                                   
REMARK 500    ALA E 296      130.78    -39.93                                   
REMARK 500    MET E 297       -9.13     87.21                                   
REMARK 500    ALA E 331      -42.96     73.74                                   
REMARK 500    SER F  62      -78.46   -138.37                                   
REMARK 500    ASN F 207      -90.38   -123.61                                   
REMARK 500    MET F 212      105.83   -164.64                                   
REMARK 500    MET F 297       -7.31     84.61                                   
REMARK 500    ALA F 331      -45.54     72.13                                   
REMARK 500    ASP F 357       90.65   -160.32                                   
REMARK 500    SER G  62      -80.59   -139.74                                   
REMARK 500    ASN G 207      -92.41   -121.87                                   
REMARK 500    MET G 212      107.41   -167.13                                   
REMARK 500    ALA G 296      132.46    -36.85                                   
REMARK 500    MET G 297       -8.51     86.96                                   
REMARK 500    ALA G 331      -45.15     72.66                                   
REMARK 500    SER H  62      -81.90   -135.62                                   
REMARK 500    ASN H 207      -92.48   -117.23                                   
REMARK 500    MET H 212      108.26   -164.19                                   
REMARK 500    MET H 297       -6.63     87.03                                   
REMARK 500    ALA H 331      -43.84     75.42                                   
REMARK 500    ASP H 357       89.64   -160.46                                   
REMARK 500    GLU I  13     -142.01     57.95                                   
REMARK 500    PHE I  15       -1.08     82.86                                   
REMARK 500    LYS I  77     -123.79     56.53                                   
REMARK 500    GLU J  13     -140.57     55.34                                   
REMARK 500    PHE J  15       -0.78     81.67                                   
REMARK 500    LYS J  77     -123.45     54.96                                   
REMARK 500    GLU K  13     -140.82     58.57                                   
REMARK 500    PHE K  15       -1.78     82.37                                   
REMARK 500    LYS K  77     -121.87     53.05                                   
REMARK 500    GLU L  13     -140.43     56.41                                   
REMARK 500    PHE L  15       -0.05     84.31                                   
REMARK 500    LYS L  77     -123.54     56.81                                   
REMARK 500    GLU M  13     -141.86     59.27                                   
REMARK 500    PHE M  15       -0.99     82.43                                   
REMARK 500    LYS M  77     -124.49     56.74                                   
REMARK 500    PHE N  12       44.63   -141.13                                   
REMARK 500    GLU N  13     -141.27     59.79                                   
REMARK 500    PHE N  15       -0.66     82.95                                   
REMARK 500    LYS N  77     -124.32     56.38                                   
REMARK 500    PHE O  12       48.83   -140.19                                   
REMARK 500    GLU O  13     -142.02     56.14                                   
REMARK 500    PHE O  15        1.62     82.39                                   
REMARK 500    LYS O  77     -123.34     55.54                                   
REMARK 500    PHE P  12       47.95   -143.04                                   
REMARK 500    GLU P  13     -142.69     57.40                                   
REMARK 500    PHE P  15       -0.31     81.86                                   
REMARK 500    LYS P  77     -124.07     58.34                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE)                                            
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 477  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX A 201   OQ1                                                    
REMARK 620 2 ASP A 203   OD1  90.2                                              
REMARK 620 3 CAP A 476   O2   94.4 104.3                                        
REMARK 620 4 GLU A 204   OE1  88.5  92.2 163.2                                  
REMARK 620 5 CAP A 476   O3   86.4 176.5  75.1  88.6                            
REMARK 620 6 CAP A 476   O7  169.3  96.9  76.1  99.1  86.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX B 201   OQ1                                                    
REMARK 620 2 CAP B 477   O2   98.3                                              
REMARK 620 3 CAP B 477   O3   91.0  75.9                                        
REMARK 620 4 ASP B 203   OD1  90.4 101.4 177.1                                  
REMARK 620 5 GLU B 204   OE1  90.7 163.2  89.8  92.7                            
REMARK 620 6 CAP B 477   O7  171.1  73.3  84.2  94.1  96.8                      
REMARK 620 N                    1     2     3     4     5                       
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 CAP C 477   O3                                                     
REMARK 620 2 KCX C 201   OQ1  89.7                                              
REMARK 620 3 ASP C 203   OD1 177.7  90.9                                        
REMARK 620 4 CAP C 477   O2   74.9  94.7 102.8                                  
REMARK 620 5 GLU C 204   OE1  89.3  91.5  92.9 163.0                            
REMARK 620 6 CAP C 477   O7   82.3 166.5  96.7  72.9  99.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 203   OD1                                                    
REMARK 620 2 GLU D 204   OE1  94.1                                              
REMARK 620 3 CAP D 477   O2  103.3 161.1                                        
REMARK 620 4 CAP D 477   O7   95.1  97.4  74.0                                  
REMARK 620 5 KCX D 201   OQ1  91.5  91.1  95.8 168.8                            
REMARK 620 6 CAP D 477   O3  177.7  88.0  74.7  85.3  87.7                      
REMARK 620 N                    1     2     3     4     5                       
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 CAP E 477   O2                                                     
REMARK 620 2 CAP E 477   O3   74.0                                              
REMARK 620 3 CAP E 477   O7   76.4  88.0                                        
REMARK 620 4 ASP E 203   OD1 103.6 175.5  95.2                                  
REMARK 620 5 GLU E 204   OE1 162.8  89.8  97.6  92.9                            
REMARK 620 6 KCX E 201   OQ1  93.4  84.6 168.8  91.8  90.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 203   OD1                                                    
REMARK 620 2 CAP F 477   O2  105.4                                              
REMARK 620 3 CAP F 477   O7   94.9  72.8                                        
REMARK 620 4 KCX F 201   OQ1  91.9  95.8 168.0                                  
REMARK 620 5 GLU F 204   OE1  91.0 162.6 100.6  89.2                            
REMARK 620 6 CAP F 477   O3  179.5  75.0  85.5  87.8  88.6                      
REMARK 620 N                    1     2     3     4     5                       
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 ASP G 203   OD1                                                    
REMARK 620 2 CAP G 477   O2  101.2                                              
REMARK 620 3 CAP G 477   O7   95.6  73.2                                        
REMARK 620 4 KCX G 201   OQ1  91.0  93.6 166.1                                  
REMARK 620 5 GLU G 204   OE1  95.6 162.3  99.9  91.6                            
REMARK 620 6 CAP G 477   O3  174.8  73.6  83.7  88.5  89.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAP H 477   O3                                                     
REMARK 620 2 KCX H 201   OQ1  87.5                                              
REMARK 620 3 CAP H 477   O2   74.6  95.0                                        
REMARK 620 4 CAP H 477   O7   87.4 170.8  76.3                                  
REMARK 620 5 ASP H 203   OD1 176.2  89.4 103.5  95.4                            
REMARK 620 6 GLU H 204   OE1  89.4  90.0 162.9  97.5  92.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG C 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG D 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG E 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG F 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP F 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG G 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG H 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO P1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO N1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO N1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO L1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO L1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO I1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1476                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1UW9   RELATED DB: PDB                                   
REMARK 900  L290F-A222T CHLAMYDOMONAS RUBISCO MUTANT                            
REMARK 900 RELATED ID: 1IR2   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ACTIVATED RIBULOSE-1,5                         
REMARK 900  -BISPHOSPHATECARBOXYLASE/OXYGENASE (RUBISCO) FROM                   
REMARK 900   GREEN ALGA,CHLAMYDOMONAS REINHARDTII COMPLEXED                     
REMARK 900   WITH 2-CARBOXYARABINITOL-1,5-BISPHOSPHATE (                        
REMARK 900  2-CABP)                                                             
REMARK 900 RELATED ID: 1UZD   RELATED DB: PDB                                   
REMARK 900  CHLAMYDOMONAS,SPINACH CHIMERIC RUBISCO                              
REMARK 900 RELATED ID: 1UZH   RELATED DB: PDB                                   
REMARK 900  A CHIMERIC CHLAMYDOMONAS, SPINACH RUBISCO                           
REMARK 900  ENZYME                                                              
REMARK 900 RELATED ID: 1GK8   RELATED DB: PDB                                   
REMARK 900  RUBISCO FROM CHLAMYDOMONAS REINHARDTII                              
REMARK 900 RELATED ID: 2V67   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII                      
REMARK 900  RUBISCO WITH A LARGE-SUBUNIT SUPRESSOR                              
REMARK 900  MUTATION T342I                                                      
REMARK 900 RELATED ID: 2V68   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII                      
REMARK 900  RUBISCO WITH LARGE-SUBUNIT MUTATIONS V331A,                         
REMARK 900  T342I                                                               
REMARK 900 RELATED ID: 2V69   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII                      
REMARK 900  RUBISCO WITH A LARGE-SUBUNIT MUTATION D473E                         
REMARK 900 RELATED ID: 2V6A   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII                      
REMARK 900  RUBISCO WITH LARGE-SUBUNIT MUTATIONS V331A,                         
REMARK 900  G344S                                                               
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE UNIPROT DATABASE ENTRY FOR THIS SEQUENCE (P00877)                
REMARK 999 HAS A VARIANT (LEU46PRO) WHICH OCCURS IN STRAIN 21GR                 
REMARK 999 AND 2137.                                                            
DBREF  2V63 A    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V63 B    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V63 C    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V63 D    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V63 E    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V63 F    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V63 G    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V63 H    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V63 I    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V63 J    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V63 K    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V63 L    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V63 M    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V63 N    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V63 O    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V63 P    1   140  UNP    P00873   RBS1_CHLRE      46    185             
SEQADV 2V63 PRO A   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V63 ALA A  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V63 PRO B   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V63 ALA B  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V63 PRO C   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V63 ALA C  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V63 PRO D   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V63 ALA D  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V63 PRO E   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V63 ALA E  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V63 PRO F   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V63 ALA F  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V63 PRO G   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V63 ALA G  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V63 PRO H   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V63 ALA H  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQRES   1 A  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 A  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 A  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 A  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 A  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 A  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 A  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 A  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 A  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 A  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 A  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 A  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 A  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY 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 VAL ASN SER          
SEQRES  17 A  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 A  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 A  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 A  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 A  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 A  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 A  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 A  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 A  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 A  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 A  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 A  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 A  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 A  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 A  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS 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 ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 A  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 A  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 A  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 A  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 B  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 B  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 B  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 B  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 B  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 B  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 B  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 B  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 B  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 B  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 B  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 B  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 B  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 B  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 B  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 B  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 B  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 B  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 B  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 B  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 B  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 B  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 B  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 B  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 B  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 B  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 B  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 B  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 B  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 B  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 B  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 B  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 B  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 B  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 B  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 B  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 B  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 C  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 C  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 C  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 C  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 C  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 C  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 C  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 C  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 C  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 C  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 C  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 C  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 C  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY 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 VAL ASN SER          
SEQRES  17 C  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 C  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 C  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 C  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 C  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 C  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 C  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 C  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 C  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 C  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 C  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 C  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 C  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 C  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 C  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS 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 ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 C  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 C  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 C  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 C  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 D  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 D  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 D  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 D  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 D  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 D  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 D  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 D  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 D  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 D  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 D  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 D  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 D  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 D  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 D  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 D  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 D  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 D  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 D  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 D  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 D  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 D  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 D  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 D  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 D  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 D  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 D  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 D  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 D  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 D  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 D  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 D  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 D  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 D  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 D  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 D  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 D  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 E  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 E  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 E  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 E  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 E  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 E  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 E  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 E  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 E  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 E  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 E  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 E  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 E  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY 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 VAL ASN SER          
SEQRES  17 E  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 E  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 E  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 E  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 E  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 E  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 E  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 E  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 E  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 E  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 E  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 E  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 E  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 E  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 E  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS 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 ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 E  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 E  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 E  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 E  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 F  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 F  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 F  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 F  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 F  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 F  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 F  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 F  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 F  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 F  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 F  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 F  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 F  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 F  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 F  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 F  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 F  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 F  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 F  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 F  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 F  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 F  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 F  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 F  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 F  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 F  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 F  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 F  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 F  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 F  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 F  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 F  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 F  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 F  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 F  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 F  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 F  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 G  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 G  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 G  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 G  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 G  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 G  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 G  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 G  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 G  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 G  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 G  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 G  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 G  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY 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 VAL ASN SER          
SEQRES  17 G  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 G  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 G  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 G  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 G  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 G  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 G  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 G  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 G  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 G  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 G  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 G  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 G  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 G  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 G  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS 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 ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 G  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 G  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 G  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 G  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 H  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 H  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 H  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 H  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 H  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 H  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 H  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 H  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 H  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 H  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 H  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 H  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 H  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 H  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 H  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 H  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 H  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 H  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 H  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 H  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 H  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 H  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 H  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 H  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 H  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 H  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 H  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 H  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 H  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 H  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 H  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 H  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 H  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 H  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 H  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 H  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 H  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 I  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 I  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 I  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 I  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 I  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 I  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 I  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 I  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 I  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 I  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 I  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 J  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 J  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 J  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 J  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 J  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 J  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 J  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 J  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 J  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 J  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 J  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 K  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 K  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 K  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 K  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 K  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 K  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 K  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 K  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 K  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 K  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 K  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 L  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 L  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 L  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 L  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 L  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 L  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 L  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 L  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 L  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 L  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 L  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 M  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 M  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 M  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 M  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 M  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 M  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 M  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 M  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 M  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 M  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 M  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 N  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 N  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 N  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 N  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 N  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 N  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 N  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 N  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 N  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 N  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 N  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 O  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 O  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 O  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 O  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 O  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 O  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 O  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 O  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 O  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 O  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 O  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 P  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 P  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 P  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 P  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 P  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 P  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 P  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 P  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 P  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 P  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 P  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
MODRES 2V63 HYP A  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V63 HYP A  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V63 KCX A  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V63 SMC A  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V63 SMC A  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V63 HYP B  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V63 HYP B  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V63 KCX B  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V63 SMC B  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V63 SMC B  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V63 HYP C  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V63 HYP C  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V63 KCX C  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V63 SMC C  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V63 SMC C  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V63 HYP D  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V63 HYP D  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V63 KCX D  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V63 SMC D  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V63 SMC D  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V63 HYP E  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V63 HYP E  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V63 KCX E  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V63 SMC E  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V63 SMC E  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V63 HYP F  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V63 HYP F  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V63 KCX F  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V63 SMC F  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V63 SMC F  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V63 HYP G  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V63 HYP G  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V63 KCX G  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V63 SMC G  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V63 SMC G  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V63 HYP H  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V63 HYP H  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V63 KCX H  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V63 SMC H  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V63 SMC H  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V63 MME I    1  MET  N-METHYL METHIONINE                                
MODRES 2V63 MME J    1  MET  N-METHYL METHIONINE                                
MODRES 2V63 MME K    1  MET  N-METHYL METHIONINE                                
MODRES 2V63 MME L    1  MET  N-METHYL METHIONINE                                
MODRES 2V63 MME M    1  MET  N-METHYL METHIONINE                                
MODRES 2V63 MME N    1  MET  N-METHYL METHIONINE                                
MODRES 2V63 MME O    1  MET  N-METHYL METHIONINE                                
MODRES 2V63 MME P    1  MET  N-METHYL METHIONINE                                
HET    HYP  A 104       8                                                       
HET    HYP  A 151       8                                                       
HET    KCX  A 201      12                                                       
HET    SMC  A 256       7                                                       
HET    SMC  A 369       7                                                       
HET    CAP  A 476      21                                                       
HET     MG  A 477       1                                                       
HET     MG  B 476       1                                                       
HET    CAP  B 477      21                                                       
HET     MG  C 476       1                                                       
HET    CAP  C 477      21                                                       
HET     MG  D 476       1                                                       
HET    CAP  D 477      21                                                       
HET     MG  E 476       1                                                       
HET    CAP  E 477      21                                                       
HET     MG  F 476       1                                                       
HET    CAP  F 477      21                                                       
HET     MG  G 476       1                                                       
HET    CAP  G 477      21                                                       
HET     MG  H 476       1                                                       
HET    CAP  H 477      21                                                       
HET    HYP  B 104       8                                                       
HET    HYP  B 151       8                                                       
HET    KCX  B 201      12                                                       
HET    SMC  B 256       7                                                       
HET    SMC  B 369       7                                                       
HET    HYP  C 104       8                                                       
HET    HYP  C 151       8                                                       
HET    KCX  C 201      12                                                       
HET    SMC  C 256       7                                                       
HET    SMC  C 369       7                                                       
HET    HYP  D 104       8                                                       
HET    HYP  D 151       8                                                       
HET    KCX  D 201      12                                                       
HET    SMC  D 256       7                                                       
HET    SMC  D 369       7                                                       
HET    HYP  E 104       8                                                       
HET    HYP  E 151       8                                                       
HET    KCX  E 201      12                                                       
HET    SMC  E 256       7                                                       
HET    SMC  E 369       7                                                       
HET    HYP  F 104       8                                                       
HET    HYP  F 151       8                                                       
HET    KCX  F 201      12                                                       
HET    SMC  F 256       7                                                       
HET    SMC  F 369       7                                                       
HET    HYP  G 104       8                                                       
HET    HYP  G 151       8                                                       
HET    KCX  G 201      12                                                       
HET    SMC  G 256       7                                                       
HET    SMC  G 369       7                                                       
HET    HYP  H 104       8                                                       
HET    HYP  H 151       8                                                       
HET    KCX  H 201      12                                                       
HET    SMC  H 256       7                                                       
HET    SMC  H 369       7                                                       
HET    MME  I   1       9                                                       
HET    MME  J   1       9                                                       
HET    MME  K   1       9                                                       
HET    MME  L   1       9                                                       
HET    MME  M   1       9                                                       
HET    MME  N   1       9                                                       
HET    MME  O   1       9                                                       
HET    MME  P   1       9                                                       
HET    EDO  A1477       4                                                       
HET    EDO  A1478       4                                                       
HET    EDO  A1479       4                                                       
HET    EDO  H1477       4                                                       
HET    EDO  H1478       4                                                       
HET    EDO  O1141       4                                                       
HET    EDO  O1142       4                                                       
HET    EDO  C1475       4                                                       
HET    EDO  K1141       4                                                       
HET    EDO  B1475       4                                                       
HET    EDO  B1476       4                                                       
HET    EDO  B1477       4                                                       
HET    EDO  B1478       4                                                       
HET    EDO  J1141       4                                                       
HET    EDO  G1479       4                                                       
HET    EDO  D1475       4                                                       
HET    EDO  D1476       4                                                       
HET    EDO  E1475       4                                                       
HET    EDO  E1477       4                                                       
HET    EDO  J1142       4                                                       
HET    EDO  D1477       4                                                       
HET    EDO  D1478       4                                                       
HET    EDO  P1141       4                                                       
HET    EDO  N1141       4                                                       
HET    EDO  N1142       4                                                       
HET    EDO  L1141       4                                                       
HET    EDO  L1142       4                                                       
HET    EDO  A1480       4                                                       
HET    EDO  C1477       4                                                       
HET    EDO  C1478       4                                                       
HET    EDO  C1479       4                                                       
HET    EDO  G1480       4                                                       
HET    EDO  I1141       4                                                       
HET    EDO  K1142       4                                                       
HET    EDO  M1141       4                                                       
HET    EDO  M1142       4                                                       
HET    EDO  C1476       4                                                       
HET    EDO  H1475       4                                                       
HET    EDO  H1476       4                                                       
HET    EDO  G1475       4                                                       
HET    EDO  G1476       4                                                       
HET    EDO  G1477       4                                                       
HET    EDO  G1478       4                                                       
HET    EDO  E1476       4                                                       
HET    EDO  F1475       4                                                       
HET    EDO  F1476       4                                                       
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE                              
HETNAM     HYP 4-HYDROXYPROLINE                                                 
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETNAM     SMC S-METHYLCYSTEINE                                                 
HETNAM     MME N-METHYL METHIONINE                                              
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL  17  HYP    16(C5 H9 N O3)                                               
FORMUL  18  KCX    8(C7 H14 N2 O4)                                              
FORMUL  19  SMC    16(C4 H9 N O2 S)                                             
FORMUL  20  MME    8(C6 H13 N O2 S)                                             
FORMUL  21  EDO    46(C2 H6 O2)                                                 
FORMUL  22   MG    8(MG 2+)                                                     
FORMUL  23  CAP    8(C6 H14 O13 P2)                                             
FORMUL  24  HOH   *2892(H2 O1)                                                  
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 SER A   76  LYS A   81  1                                   6    
HELIX    5   5 HYP A  104  PHE A  108  5                                   5    
HELIX    6   6 SER A  112  GLY A  122  1                                  11    
HELIX    7   7 ASN A  123  GLY A  126  5                                   4    
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  VAL A  255  1                                  10    
HELIX   13  13 TYR 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 GLU A  338  ASP 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  GLU A  433  1                                  22    
HELIX   22  22 ASP A  436  LYS A  463  1                                  28    
HELIX   23  23 TYR B   20  TYR B   25  1                                   6    
HELIX   24  24 PRO B   49  SER B   61  1                                  13    
HELIX   25  25 VAL B   69  THR B   75  5                                   7    
HELIX   26  26 SER B   76  LYS B   81  1                                   6    
HELIX   27  27 HYP B  104  PHE B  108  5                                   5    
HELIX   28  28 SER B  112  GLY B  122  1                                  11    
HELIX   29  29 ASN B  123  GLY B  126  5                                   4    
HELIX   30  30 PRO B  141  LYS B  146  1                                   6    
HELIX   31  31 GLY B  154  ASN B  163  1                                  10    
HELIX   32  32 SER B  181  GLY B  195  1                                  15    
HELIX   33  33 ARG B  213  GLY B  233  1                                  21    
HELIX   34  34 THR B  246  VAL B  255  1                                  10    
HELIX   35  35 TYR B  269  GLY B  288  1                                  20    
HELIX   36  36 MET B  297  ARG B  303  1                                   7    
HELIX   37  37 HIS B  310  GLY B  322  1                                  13    
HELIX   38  38 GLU B  338  ASP B  351  1                                  14    
HELIX   39  39 ARG B  358  GLY B  361  5                                   4    
HELIX   40  40 HIS B  383  TRP B  385  5                                   3    
HELIX   41  41 HIS B  386  GLY B  395  1                                  10    
HELIX   42  42 GLY B  403  GLY B  408  1                                   6    
HELIX   43  43 GLY B  412  GLU B  433  1                                  22    
HELIX   44  44 ASP B  436  LYS B  463  1                                  28    
HELIX   45  45 TYR C   20  TYR C   25  1                                   6    
HELIX   46  46 PRO C   49  SER C   61  1                                  13    
HELIX   47  47 VAL C   69  THR C   75  5                                   7    
HELIX   48  48 SER C   76  LYS C   81  1                                   6    
HELIX   49  49 HYP C  104  PHE C  108  5                                   5    
HELIX   50  50 SER C  112  GLY C  122  1                                  11    
HELIX   51  51 ASN C  123  GLY C  126  5                                   4    
HELIX   52  52 PRO C  141  LYS C  146  1                                   6    
HELIX   53  53 GLY C  154  ASN C  163  1                                  10    
HELIX   54  54 SER C  181  GLY C  195  1                                  15    
HELIX   55  55 ARG C  213  GLY C  233  1                                  21    
HELIX   56  56 THR C  246  VAL C  255  1                                  10    
HELIX   57  57 TYR C  269  GLY C  288  1                                  20    
HELIX   58  58 MET C  297  ARG C  303  1                                   7    
HELIX   59  59 HIS C  310  GLY C  322  1                                  13    
HELIX   60  60 GLU C  338  ASP C  351  1                                  14    
HELIX   61  61 ARG C  358  GLY C  361  5                                   4    
HELIX   62  62 HIS C  383  TRP C  385  5                                   3    
HELIX   63  63 HIS C  386  GLY C  395  1                                  10    
HELIX   64  64 GLY C  403  GLY C  408  1                                   6    
HELIX   65  65 GLY C  412  GLU C  433  1                                  22    
HELIX   66  66 GLU C  440  SER C  452  1                                  13    
HELIX   67  67 SER C  452  LYS C  463  1                                  12    
HELIX   68  68 TYR D   20  TYR D   25  1                                   6    
HELIX   69  69 PRO D   49  SER D   61  1                                  13    
HELIX   70  70 VAL D   69  THR D   75  5                                   7    
HELIX   71  71 SER D   76  LYS D   81  1                                   6    
HELIX   72  72 HYP D  104  PHE D  108  5                                   5    
HELIX   73  73 SER D  112  GLY D  122  1                                  11    
HELIX   74  74 ASN D  123  GLY D  126  5                                   4    
HELIX   75  75 PRO D  141  LYS D  146  1                                   6    
HELIX   76  76 GLY D  154  ASN D  163  1                                  10    
HELIX   77  77 SER D  181  GLY D  195  1                                  15    
HELIX   78  78 ARG D  213  GLY D  233  1                                  21    
HELIX   79  79 THR D  246  VAL D  255  1                                  10    
HELIX   80  80 TYR D  269  GLY D  288  1                                  20    
HELIX   81  81 MET D  297  ARG D  303  1                                   7    
HELIX   82  82 HIS D  310  GLY D  322  1                                  13    
HELIX   83  83 GLU D  338  ASP D  351  1                                  14    
HELIX   84  84 ARG D  358  GLY D  361  5                                   4    
HELIX   85  85 HIS D  383  TRP D  385  5                                   3    
HELIX   86  86 HIS D  386  GLY D  395  1                                  10    
HELIX   87  87 GLY D  403  GLY D  408  1                                   6    
HELIX   88  88 GLY D  412  GLU D  433  1                                  22    
HELIX   89  89 ASP D  436  LYS D  463  1                                  28    
HELIX   90  90 TYR E   20  TYR E   25  1                                   6    
HELIX   91  91 PRO E   49  SER E   61  1                                  13    
HELIX   92  92 VAL E   69  THR E   75  5                                   7    
HELIX   93  93 SER E   76  LYS E   81  1                                   6    
HELIX   94  94 HYP E  104  PHE E  108  5                                   5    
HELIX   95  95 SER E  112  GLY E  122  1                                  11    
HELIX   96  96 ASN E  123  GLY E  126  5                                   4    
HELIX   97  97 PRO E  141  LYS E  146  1                                   6    
HELIX   98  98 GLY E  154  ASN E  163  1                                  10    
HELIX   99  99 SER E  181  GLY E  195  1                                  15    
HELIX  100 100 ARG E  213  GLY E  233  1                                  21    
HELIX  101 101 THR E  246  VAL E  255  1                                  10    
HELIX  102 102 TYR E  269  GLY E  288  1                                  20    
HELIX  103 103 MET E  297  ARG E  303  1                                   7    
HELIX  104 104 HIS E  310  GLY E  322  1                                  13    
HELIX  105 105 GLU E  338  ASP E  351  1                                  14    
HELIX  106 106 ARG E  358  GLY E  361  5                                   4    
HELIX  107 107 HIS E  383  TRP E  385  5                                   3    
HELIX  108 108 HIS E  386  GLY E  395  1                                  10    
HELIX  109 109 GLY E  403  GLY E  408  1                                   6    
HELIX  110 110 GLY E  412  GLU E  433  1                                  22    
HELIX  111 111 ASP E  436  LYS E  463  1                                  28    
HELIX  112 112 TYR F   20  TYR F   25  1                                   6    
HELIX  113 113 PRO F   49  SER F   61  1                                  13    
HELIX  114 114 VAL F   69  THR F   75  5                                   7    
HELIX  115 115 SER F   76  LYS F   81  1                                   6    
HELIX  116 116 HYP F  104  PHE F  108  5                                   5    
HELIX  117 117 SER F  112  GLY F  122  1                                  11    
HELIX  118 118 ASN F  123  GLY F  126  5                                   4    
HELIX  119 119 PRO F  141  LYS F  146  1                                   6    
HELIX  120 120 GLY F  154  ASN F  163  1                                  10    
HELIX  121 121 SER F  181  GLY F  195  1                                  15    
HELIX  122 122 ARG F  213  GLY F  233  1                                  21    
HELIX  123 123 THR F  246  VAL F  255  1                                  10    
HELIX  124 124 TYR F  269  GLY F  288  1                                  20    
HELIX  125 125 MET F  297  ARG F  303  1                                   7    
HELIX  126 126 HIS F  310  GLY F  322  1                                  13    
HELIX  127 127 GLU F  338  ASP F  351  1                                  14    
HELIX  128 128 ARG F  358  GLY F  361  5                                   4    
HELIX  129 129 HIS F  383  TRP F  385  5                                   3    
HELIX  130 130 HIS F  386  GLY F  395  1                                  10    
HELIX  131 131 GLY F  403  GLY F  408  1                                   6    
HELIX  132 132 GLY F  412  GLU F  433  1                                  22    
HELIX  133 133 ASP F  436  LYS F  463  1                                  28    
HELIX  134 134 TYR G   20  TYR G   25  1                                   6    
HELIX  135 135 PRO G   49  SER G   61  1                                  13    
HELIX  136 136 VAL G   69  THR G   75  5                                   7    
HELIX  137 137 SER G   76  LYS G   81  1                                   6    
HELIX  138 138 HYP G  104  PHE G  108  5                                   5    
HELIX  139 139 SER G  112  GLY G  122  1                                  11    
HELIX  140 140 ASN G  123  GLY G  126  5                                   4    
HELIX  141 141 PRO G  141  LYS G  146  1                                   6    
HELIX  142 142 GLY G  154  ASN G  163  1                                  10    
HELIX  143 143 SER G  181  GLY G  195  1                                  15    
HELIX  144 144 ARG G  213  GLY G  233  1                                  21    
HELIX  145 145 THR G  246  VAL G  255  1                                  10    
HELIX  146 146 TYR G  269  GLY G  288  1                                  20    
HELIX  147 147 MET G  297  ARG G  303  1                                   7    
HELIX  148 148 HIS G  310  GLY G  322  1                                  13    
HELIX  149 149 GLU G  338  ASP G  351  1                                  14    
HELIX  150 150 ARG G  358  GLY G  361  5                                   4    
HELIX  151 151 HIS G  383  TRP G  385  5                                   3    
HELIX  152 152 HIS G  386  GLY G  395  1                                  10    
HELIX  153 153 GLY G  403  GLY G  408  1                                   6    
HELIX  154 154 GLY G  412  GLU G  433  1                                  22    
HELIX  155 155 ASP G  436  LYS G  463  1                                  28    
HELIX  156 156 TYR H   20  TYR H   25  1                                   6    
HELIX  157 157 PRO H   49  SER H   61  1                                  13    
HELIX  158 158 VAL H   69  THR H   75  5                                   7    
HELIX  159 159 SER H   76  LYS H   81  1                                   6    
HELIX  160 160 HYP H  104  PHE H  108  5                                   5    
HELIX  161 161 SER H  112  GLY H  122  1                                  11    
HELIX  162 162 ASN H  123  GLY H  126  5                                   4    
HELIX  163 163 PRO H  141  LYS H  146  1                                   6    
HELIX  164 164 GLY H  154  ASN H  163  1                                  10    
HELIX  165 165 SER H  181  GLY H  195  1                                  15    
HELIX  166 166 ARG H  213  GLY H  233  1                                  21    
HELIX  167 167 THR H  246  VAL H  255  1                                  10    
HELIX  168 168 TYR H  269  GLY H  288  1                                  20    
HELIX  169 169 MET H  297  ARG H  303  1                                   7    
HELIX  170 170 HIS H  310  GLY H  322  1                                  13    
HELIX  171 171 GLU H  338  ASP H  351  1                                  14    
HELIX  172 172 ARG H  358  GLY H  361  5                                   4    
HELIX  173 173 HIS H  383  TRP H  385  5                                   3    
HELIX  174 174 HIS H  386  GLY H  395  1                                  10    
HELIX  175 175 GLY H  403  GLY H  408  1                                   6    
HELIX  176 176 GLY H  412  GLU H  433  1                                  22    
HELIX  177 177 ASP H  436  LYS H  463  1                                  28    
HELIX  178 178 THR I   22  GLY I   37  1                                  16    
HELIX  179 179 GLU I   46  ALA I   50  5                                   5    
HELIX  180 180 ASN I   54  PHE I   60  5                                   7    
HELIX  181 181 ASP I   85  PHE I  100  1                                  16    
HELIX  182 182 PRO I  134  ARG I  138  5                                   5    
HELIX  183 183 THR J   22  GLY J   37  1                                  16    
HELIX  184 184 GLU J   46  ALA J   50  5                                   5    
HELIX  185 185 ASN J   54  PHE J   60  5                                   7    
HELIX  186 186 ASP J   85  PHE J  100  1                                  16    
HELIX  187 187 PRO J  134  ARG J  138  5                                   5    
HELIX  188 188 THR K   22  GLY K   37  1                                  16    
HELIX  189 189 GLU K   46  ALA K   50  5                                   5    
HELIX  190 190 ASN K   54  PHE K   60  5                                   7    
HELIX  191 191 ASP K   85  PHE K  100  1                                  16    
HELIX  192 192 PRO K  134  ARG K  138  5                                   5    
HELIX  193 193 THR L   22  ASN L   36  1                                  15    
HELIX  194 194 GLU L   46  ALA L   50  5                                   5    
HELIX  195 195 ASN L   54  PHE L   60  5                                   7    
HELIX  196 196 ASP L   85  PHE L  100  1                                  16    
HELIX  197 197 PRO L  134  ARG L  138  5                                   5    
HELIX  198 198 THR M   22  GLY M   37  1                                  16    
HELIX  199 199 GLU M   46  ALA M   50  5                                   5    
HELIX  200 200 ASN M   54  PHE M   60  5                                   7    
HELIX  201 201 ASP M   85  PHE M  100  1                                  16    
HELIX  202 202 PRO M  134  ARG M  138  5                                   5    
HELIX  203 203 THR N   22  GLY N   37  1                                  16    
HELIX  204 204 GLU N   46  ALA N   50  5                                   5    
HELIX  205 205 ASN N   54  PHE N   60  5                                   7    
HELIX  206 206 ASP N   85  PHE N  100  1                                  16    
HELIX  207 207 PRO N  134  ARG N  138  5                                   5    
HELIX  208 208 THR O   22  GLY O   37  1                                  16    
HELIX  209 209 GLU O   46  ALA O   50  5                                   5    
HELIX  210 210 ASN O   54  PHE O   60  5                                   7    
HELIX  211 211 ASP O   85  PHE O  100  1                                  16    
HELIX  212 212 PRO O  134  ARG O  138  5                                   5    
HELIX  213 213 THR P   22  ASN P   36  1                                  15    
HELIX  214 214 GLU P   46  ALA P   50  5                                   5    
HELIX  215 215 ASN P   54  PHE P   60  5                                   7    
HELIX  216 216 ASP P   85  PHE P  100  1                                  16    
HELIX  217 217 PRO P  134  ARG P  138  5                                   5    
SHEET    1  AA 5 ARG A  83  PRO A  89  0                                        
SHEET    2  AA 5 TYR 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  ARG 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 8 LEU A 169  GLY A 171  0                                        
SHEET    2  AB 8 CYS A 399  GLN A 401  1  O  LEU A 400   N  GLY A 171           
SHEET    3  AB 8 MET A 375  SER A 379  1  O  PRO A 376   N  CYS A 399           
SHEET    4  AB 8 HIS A 325  HIS A 327  1  O  LEU A 326   N  VAL A 377           
SHEET    5  AB 8 LEU A 290  HIS A 294  1  O  ILE A 293   N  HIS A 327           
SHEET    6  AB 8 ILE A 264  ASP A 268  1  O  ILE A 265   N  HIS A 292           
SHEET    7  AB 8 GLY A 237  ASN A 241  1  O  LEU A 240   N  MET A 266           
SHEET    8  AB 8 PHE A 199  KCX A 201  1  O  THR A 200   N  TYR A 239           
SHEET    1  AC 2 TYR A 353  VAL A 354  0                                        
SHEET    2  AC 2 GLN A 366  ASP A 367 -1  O  GLN A 366   N  VAL A 354           
SHEET    1  BA 5 ARG B  83  PRO B  89  0                                        
SHEET    2  BA 5 TYR B  97  TYR B 103 -1  O  ILE B  98   N  GLU B  88           
SHEET    3  BA 5 ILE B  36  PRO B  44 -1  O  ILE B  36   N  TYR B 103           
SHEET    4  BA 5 LEU B 130  ARG B 139 -1  N  ARG B 131   O  THR B  43           
SHEET    5  BA 5 GLY B 308  ILE B 309  1  O  GLY B 308   N  LEU B 135           
SHEET    1  BB 8 LEU B 169  GLY B 171  0                                        
SHEET    2  BB 8 CYS B 399  GLN B 401  1  O  LEU B 400   N  GLY B 171           
SHEET    3  BB 8 MET B 375  SER B 379  1  O  PRO B 376   N  CYS B 399           
SHEET    4  BB 8 HIS B 325  HIS B 327  1  O  LEU B 326   N  VAL B 377           
SHEET    5  BB 8 LEU B 290  HIS B 294  1  O  ILE B 293   N  HIS B 327           
SHEET    6  BB 8 ILE B 264  ASP B 268  1  O  ILE B 265   N  HIS B 292           
SHEET    7  BB 8 GLY B 237  ASN B 241  1  O  LEU B 240   N  MET B 266           
SHEET    8  BB 8 PHE B 199  KCX B 201  1  O  THR B 200   N  TYR B 239           
SHEET    1  BC 2 TYR B 353  VAL B 354  0                                        
SHEET    2  BC 2 GLN B 366  ASP B 367 -1  O  GLN B 366   N  VAL B 354           
SHEET    1  CA 5 ARG C  83  PRO C  89  0                                        
SHEET    2  CA 5 TYR 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  ARG 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 8 LEU C 169  GLY C 171  0                                        
SHEET    2  CB 8 CYS C 399  GLN C 401  1  O  LEU C 400   N  GLY C 171           
SHEET    3  CB 8 MET C 375  SER C 379  1  O  PRO C 376   N  CYS C 399           
SHEET    4  CB 8 HIS C 325  HIS C 327  1  O  LEU C 326   N  VAL C 377           
SHEET    5  CB 8 LEU C 290  HIS C 294  1  O  ILE C 293   N  HIS C 327           
SHEET    6  CB 8 ILE C 264  ASP C 268  1  O  ILE C 265   N  HIS C 292           
SHEET    7  CB 8 GLY C 237  ASN C 241  1  O  LEU C 240   N  MET C 266           
SHEET    8  CB 8 PHE C 199  KCX C 201  1  O  THR C 200   N  TYR C 239           
SHEET    1  CC 2 TYR C 353  VAL C 354  0                                        
SHEET    2  CC 2 GLN C 366  ASP C 367 -1  O  GLN C 366   N  VAL C 354           
SHEET    1  DA 5 ARG D  83  PRO D  89  0                                        
SHEET    2  DA 5 TYR D  97  TYR D 103 -1  O  ILE D  98   N  GLU D  88           
SHEET    3  DA 5 ILE D  36  PRO D  44 -1  O  ILE D  36   N  TYR D 103           
SHEET    4  DA 5 LEU D 130  ARG D 139 -1  N  ARG D 131   O  THR D  43           
SHEET    5  DA 5 GLY D 308  ILE D 309  1  O  GLY D 308   N  LEU D 135           
SHEET    1  DB 8 LEU D 169  GLY D 171  0                                        
SHEET    2  DB 8 CYS D 399  GLN D 401  1  O  LEU D 400   N  GLY D 171           
SHEET    3  DB 8 MET D 375  SER D 379  1  O  PRO D 376   N  CYS D 399           
SHEET    4  DB 8 HIS D 325  HIS D 327  1  O  LEU D 326   N  VAL D 377           
SHEET    5  DB 8 LEU D 290  HIS D 294  1  O  ILE D 293   N  HIS D 327           
SHEET    6  DB 8 ILE D 264  ASP D 268  1  O  ILE D 265   N  HIS D 292           
SHEET    7  DB 8 GLY D 237  ASN D 241  1  O  LEU D 240   N  MET D 266           
SHEET    8  DB 8 PHE D 199  KCX D 201  1  O  THR D 200   N  TYR D 239           
SHEET    1  DC 2 TYR D 353  VAL D 354  0                                        
SHEET    2  DC 2 GLN D 366  ASP D 367 -1  O  GLN D 366   N  VAL D 354           
SHEET    1  EA 5 ARG E  83  PRO E  89  0                                        
SHEET    2  EA 5 TYR 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  ARG 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 8 LEU E 169  GLY E 171  0                                        
SHEET    2  EB 8 CYS E 399  GLN E 401  1  O  LEU E 400   N  GLY E 171           
SHEET    3  EB 8 MET E 375  SER E 379  1  O  PRO E 376   N  CYS E 399           
SHEET    4  EB 8 HIS E 325  HIS E 327  1  O  LEU E 326   N  VAL E 377           
SHEET    5  EB 8 LEU E 290  HIS E 294  1  O  ILE E 293   N  HIS E 327           
SHEET    6  EB 8 ILE E 264  ASP E 268  1  O  ILE E 265   N  HIS E 292           
SHEET    7  EB 8 GLY E 237  ASN E 241  1  O  LEU E 240   N  MET E 266           
SHEET    8  EB 8 PHE E 199  KCX E 201  1  O  THR E 200   N  TYR E 239           
SHEET    1  EC 2 TYR E 353  VAL E 354  0                                        
SHEET    2  EC 2 GLN E 366  ASP E 367 -1  O  GLN E 366   N  VAL E 354           
SHEET    1  FA 5 ARG F  83  PRO F  89  0                                        
SHEET    2  FA 5 TYR F  97  TYR F 103 -1  O  ILE F  98   N  GLU F  88           
SHEET    3  FA 5 ILE F  36  PRO F  44 -1  O  ILE F  36   N  TYR F 103           
SHEET    4  FA 5 LEU F 130  ARG F 139 -1  N  ARG F 131   O  THR F  43           
SHEET    5  FA 5 GLY F 308  ILE F 309  1  O  GLY F 308   N  LEU F 135           
SHEET    1  FB 8 LEU F 169  GLY F 171  0                                        
SHEET    2  FB 8 CYS F 399  GLN F 401  1  O  LEU F 400   N  GLY F 171           
SHEET    3  FB 8 MET F 375  SER F 379  1  O  PRO F 376   N  CYS F 399           
SHEET    4  FB 8 HIS F 325  HIS F 327  1  O  LEU F 326   N  VAL F 377           
SHEET    5  FB 8 LEU F 290  HIS F 294  1  O  ILE F 293   N  HIS F 327           
SHEET    6  FB 8 ILE F 264  ASP F 268  1  O  ILE F 265   N  HIS F 292           
SHEET    7  FB 8 GLY F 237  ASN F 241  1  O  LEU F 240   N  MET F 266           
SHEET    8  FB 8 PHE F 199  KCX F 201  1  O  THR F 200   N  TYR F 239           
SHEET    1  FC 2 TYR F 353  VAL F 354  0                                        
SHEET    2  FC 2 GLN F 366  ASP F 367 -1  O  GLN F 366   N  VAL F 354           
SHEET    1  GA 5 ARG G  83  PRO G  89  0                                        
SHEET    2  GA 5 TYR 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  ARG 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 8 LEU G 169  GLY G 171  0                                        
SHEET    2  GB 8 CYS G 399  GLN G 401  1  O  LEU G 400   N  GLY G 171           
SHEET    3  GB 8 MET G 375  SER G 379  1  O  PRO G 376   N  CYS G 399           
SHEET    4  GB 8 HIS G 325  HIS G 327  1  O  LEU G 326   N  VAL G 377           
SHEET    5  GB 8 LEU G 290  HIS G 294  1  O  ILE G 293   N  HIS G 327           
SHEET    6  GB 8 ILE G 264  ASP G 268  1  O  ILE G 265   N  HIS G 292           
SHEET    7  GB 8 GLY G 237  ASN G 241  1  O  LEU G 240   N  MET G 266           
SHEET    8  GB 8 PHE G 199  KCX G 201  1  O  THR G 200   N  TYR G 239           
SHEET    1  GC 2 TYR G 353  VAL G 354  0                                        
SHEET    2  GC 2 GLN G 366  ASP G 367 -1  O  GLN G 366   N  VAL G 354           
SHEET    1  HA 5 ARG H  83  PRO H  89  0                                        
SHEET    2  HA 5 TYR H  97  TYR H 103 -1  O  ILE H  98   N  GLU H  88           
SHEET    3  HA 5 ILE H  36  PRO H  44 -1  O  ILE H  36   N  TYR H 103           
SHEET    4  HA 5 LEU H 130  ARG H 139 -1  N  ARG H 131   O  THR H  43           
SHEET    5  HA 5 GLY H 308  ILE H 309  1  O  GLY H 308   N  LEU H 135           
SHEET    1  HB 8 LEU H 169  GLY H 171  0                                        
SHEET    2  HB 8 CYS H 399  GLN H 401  1  O  LEU H 400   N  GLY H 171           
SHEET    3  HB 8 MET H 375  SER H 379  1  O  PRO H 376   N  CYS H 399           
SHEET    4  HB 8 HIS H 325  HIS H 327  1  O  LEU H 326   N  VAL H 377           
SHEET    5  HB 8 LEU H 290  HIS H 294  1  O  ILE H 293   N  HIS H 327           
SHEET    6  HB 8 ILE H 264  ASP H 268  1  O  ILE H 265   N  HIS H 292           
SHEET    7  HB 8 GLY H 237  ASN H 241  1  O  LEU H 240   N  MET H 266           
SHEET    8  HB 8 PHE H 199  KCX H 201  1  O  THR H 200   N  TYR H 239           
SHEET    1  HC 2 TYR H 353  VAL H 354  0                                        
SHEET    2  HC 2 GLN H 366  ASP H 367 -1  O  GLN H 366   N  VAL H 354           
SHEET    1  IA 4 THR I  74  TRP I  76  0                                        
SHEET    2  IA 4 ILE I  39  ALA I  45 -1  O  LEU I  42   N  TRP I  76           
SHEET    3  IA 4 TYR I 104  ASP I 111 -1  O  TYR I 104   N  ALA I  45           
SHEET    4  IA 4 VAL I 116  GLN I 124 -1  O  VAL I 116   N  ASP I 111           
SHEET    1  JA 4 THR J  74  TRP J  76  0                                        
SHEET    2  JA 4 ILE J  39  ALA J  45 -1  O  LEU J  42   N  TRP J  76           
SHEET    3  JA 4 TYR J 104  ASP J 111 -1  O  TYR J 104   N  ALA J  45           
SHEET    4  JA 4 VAL J 116  GLN J 124 -1  O  VAL J 116   N  ASP J 111           
SHEET    1  KA 4 THR K  74  TRP K  76  0                                        
SHEET    2  KA 4 ILE K  39  ALA K  45 -1  O  LEU K  42   N  TRP K  76           
SHEET    3  KA 4 TYR K 104  ASP K 111 -1  O  TYR K 104   N  ALA K  45           
SHEET    4  KA 4 VAL K 116  GLN K 124 -1  O  VAL K 116   N  ASP K 111           
SHEET    1  LA 4 THR L  74  TRP L  76  0                                        
SHEET    2  LA 4 ILE L  39  ALA L  45 -1  O  LEU L  42   N  TRP L  76           
SHEET    3  LA 4 TYR L 104  ASP L 111 -1  O  TYR L 104   N  ALA L  45           
SHEET    4  LA 4 VAL L 116  GLN L 124 -1  O  VAL L 116   N  ASP L 111           
SHEET    1  MA 4 THR M  74  TRP M  76  0                                        
SHEET    2  MA 4 ILE M  39  ALA M  45 -1  O  LEU M  42   N  TRP M  76           
SHEET    3  MA 4 TYR M 104  ASP M 111 -1  O  TYR M 104   N  ALA M  45           
SHEET    4  MA 4 VAL M 116  GLN M 124 -1  O  VAL M 116   N  ASP M 111           
SHEET    1  NA 4 THR N  74  TRP N  76  0                                        
SHEET    2  NA 4 ILE N  39  ALA N  45 -1  O  LEU N  42   N  TRP N  76           
SHEET    3  NA 4 TYR N 104  ASP N 111 -1  O  TYR N 104   N  ALA N  45           
SHEET    4  NA 4 VAL N 116  GLN N 124 -1  O  VAL N 116   N  ASP N 111           
SHEET    1  OA 4 THR O  74  TRP O  76  0                                        
SHEET    2  OA 4 ILE O  39  ALA O  45 -1  O  LEU O  42   N  TRP O  76           
SHEET    3  OA 4 TYR O 104  ASP O 111 -1  O  TYR O 104   N  ALA O  45           
SHEET    4  OA 4 VAL O 116  GLN O 124 -1  O  VAL O 116   N  ASP O 111           
SHEET    1  PA 4 THR P  74  TRP P  76  0                                        
SHEET    2  PA 4 ILE P  39  ALA P  45 -1  O  LEU P  42   N  TRP P  76           
SHEET    3  PA 4 TYR P 104  ASP P 111 -1  O  TYR P 104   N  ALA P  45           
SHEET    4  PA 4 VAL P 116  GLN P 124 -1  O  VAL P 116   N  ASP P 111           
SSBOND   1 CYS A  247    CYS B  247                          1555   1555  2.08  
SSBOND   2 CYS C  247    CYS D  247                          1555   1555  2.08  
SSBOND   3 CYS E  247    CYS F  247                          1555   1555  2.07  
SSBOND   4 CYS G  247    CYS H  247                          1555   1555  2.09  
LINK         C   TYR A 103                 N   HYP A 104     1555   1555  1.35  
LINK         C   HYP A 104                 N   ILE A 105     1555   1555  1.33  
LINK         C   GLY A 150                 N   HYP A 151     1555   1555  1.34  
LINK         C   HYP A 151                 N   PRO A 152     1555   1555  1.35  
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         C   VAL A 255                 N   SMC A 256     1555   1555  1.33  
LINK         C   SMC A 256                 N   ALA A 257     1555   1555  1.33  
LINK         C   TRP A 368                 N   SMC A 369     1555   1555  1.33  
LINK         C   SMC A 369                 N   SER A 370     1555   1555  1.33  
LINK        MG    MG A 477                 OQ1 KCX A 201     1555   1555  2.02  
LINK        MG    MG A 477                 OD1 ASP A 203     1555   1555  1.98  
LINK        MG    MG A 477                 O2  CAP A 476     1555   1555  2.25  
LINK        MG    MG A 477                 OE1 GLU A 204     1555   1555  2.03  
LINK        MG    MG A 477                 O3  CAP A 476     1555   1555  2.14  
LINK        MG    MG A 477                 O7  CAP A 476     1555   1555  2.11  
LINK         C   TYR B 103                 N   HYP B 104     1555   1555  1.35  
LINK         C   HYP B 104                 N   ILE B 105     1555   1555  1.33  
LINK         C   GLY B 150                 N   HYP B 151     1555   1555  1.34  
LINK         C   HYP B 151                 N   PRO B 152     1555   1555  1.34  
LINK         C   THR B 200                 N   KCX B 201     1555   1555  1.33  
LINK         C   KCX B 201                 N   ASP B 202     1555   1555  1.34  
LINK         C   VAL B 255                 N   SMC B 256     1555   1555  1.34  
LINK         C   SMC B 256                 N   ALA B 257     1555   1555  1.33  
LINK         C   TRP B 368                 N   SMC B 369     1555   1555  1.33  
LINK         C   SMC B 369                 N   SER B 370     1555   1555  1.34  
LINK        MG    MG B 476                 OQ1 KCX B 201     1555   1555  1.99  
LINK        MG    MG B 476                 O2  CAP B 477     1555   1555  2.27  
LINK        MG    MG B 476                 O3  CAP B 477     1555   1555  2.07  
LINK        MG    MG B 476                 OD1 ASP B 203     1555   1555  2.03  
LINK        MG    MG B 476                 OE1 GLU B 204     1555   1555  2.01  
LINK        MG    MG B 476                 O7  CAP B 477     1555   1555  2.24  
LINK         C   TYR C 103                 N   HYP C 104     1555   1555  1.34  
LINK         C   HYP C 104                 N   ILE C 105     1555   1555  1.33  
LINK         C   GLY C 150                 N   HYP C 151     1555   1555  1.34  
LINK         C   HYP C 151                 N   PRO C 152     1555   1555  1.34  
LINK         C   THR C 200                 N   KCX C 201     1555   1555  1.33  
LINK         C   KCX C 201                 N   ASP C 202     1555   1555  1.34  
LINK         C   VAL C 255                 N   SMC C 256     1555   1555  1.33  
LINK         C   SMC C 256                 N   ALA C 257     1555   1555  1.33  
LINK         C   TRP C 368                 N   SMC C 369     1555   1555  1.33  
LINK         C   SMC C 369                 N   SER C 370     1555   1555  1.33  
LINK        MG    MG C 476                 O3  CAP C 477     1555   1555  2.11  
LINK        MG    MG C 476                 OQ1 KCX C 201     1555   1555  1.95  
LINK        MG    MG C 476                 OD1 ASP C 203     1555   1555  1.97  
LINK        MG    MG C 476                 O2  CAP C 477     1555   1555  2.33  
LINK        MG    MG C 476                 OE1 GLU C 204     1555   1555  1.98  
LINK        MG    MG C 476                 O7  CAP C 477     1555   1555  2.17  
LINK         C   TYR D 103                 N   HYP D 104     1555   1555  1.34  
LINK         C   HYP D 104                 N   ILE D 105     1555   1555  1.33  
LINK         C   GLY D 150                 N   HYP D 151     1555   1555  1.35  
LINK         C   HYP D 151                 N   PRO D 152     1555   1555  1.34  
LINK         C   THR D 200                 N   KCX D 201     1555   1555  1.32  
LINK         C   KCX D 201                 N   ASP D 202     1555   1555  1.33  
LINK         C   VAL D 255                 N   SMC D 256     1555   1555  1.33  
LINK         C   SMC D 256                 N   ALA D 257     1555   1555  1.33  
LINK         C   TRP D 368                 N   SMC D 369     1555   1555  1.33  
LINK         C   SMC D 369                 N   SER D 370     1555   1555  1.33  
LINK        MG    MG D 476                 O7  CAP D 477     1555   1555  2.14  
LINK        MG    MG D 476                 O2  CAP D 477     1555   1555  2.24  
LINK        MG    MG D 476                 O3  CAP D 477     1555   1555  2.13  
LINK        MG    MG D 476                 OQ1 KCX D 201     1555   1555  1.97  
LINK        MG    MG D 476                 OE1 GLU D 204     1555   1555  2.08  
LINK        MG    MG D 476                 OD1 ASP D 203     1555   1555  1.96  
LINK         C   TYR E 103                 N   HYP E 104     1555   1555  1.35  
LINK         C   HYP E 104                 N   ILE E 105     1555   1555  1.33  
LINK         C   GLY E 150                 N   HYP E 151     1555   1555  1.35  
LINK         C   HYP E 151                 N   PRO E 152     1555   1555  1.34  
LINK         C   THR E 200                 N   KCX E 201     1555   1555  1.33  
LINK         C   KCX E 201                 N   ASP E 202     1555   1555  1.33  
LINK         C   VAL E 255                 N   SMC E 256     1555   1555  1.33  
LINK         C   SMC E 256                 N   ALA E 257     1555   1555  1.33  
LINK         C   TRP E 368                 N   SMC E 369     1555   1555  1.33  
LINK         C   SMC E 369                 N   SER E 370     1555   1555  1.33  
LINK        MG    MG E 476                 OQ1 KCX E 201     1555   1555  1.99  
LINK        MG    MG E 476                 OD1 ASP E 203     1555   1555  1.97  
LINK        MG    MG E 476                 O7  CAP E 477     1555   1555  2.14  
LINK        MG    MG E 476                 OE1 GLU E 204     1555   1555  2.05  
LINK        MG    MG E 476                 O3  CAP E 477     1555   1555  2.13  
LINK        MG    MG E 476                 O2  CAP E 477     1555   1555  2.24  
LINK         C   TYR F 103                 N   HYP F 104     1555   1555  1.35  
LINK         C   HYP F 104                 N   ILE F 105     1555   1555  1.33  
LINK         C   GLY F 150                 N   HYP F 151     1555   1555  1.34  
LINK         C   HYP F 151                 N   PRO F 152     1555   1555  1.35  
LINK         C   THR F 200                 N   KCX F 201     1555   1555  1.32  
LINK         C   KCX F 201                 N   ASP F 202     1555   1555  1.33  
LINK         C   VAL F 255                 N   SMC F 256     1555   1555  1.34  
LINK         C   SMC F 256                 N   ALA F 257     1555   1555  1.33  
LINK         C   TRP F 368                 N   SMC F 369     1555   1555  1.33  
LINK         C   SMC F 369                 N   SER F 370     1555   1555  1.34  
LINK        MG    MG F 476                 OE1 GLU F 204     1555   1555  2.01  
LINK        MG    MG F 476                 O3  CAP F 477     1555   1555  2.16  
LINK        MG    MG F 476                 OQ1 KCX F 201     1555   1555  1.98  
LINK        MG    MG F 476                 O7  CAP F 477     1555   1555  2.13  
LINK        MG    MG F 476                 O2  CAP F 477     1555   1555  2.28  
LINK        MG    MG F 476                 OD1 ASP F 203     1555   1555  1.96  
LINK         C   TYR G 103                 N   HYP G 104     1555   1555  1.35  
LINK         C   HYP G 104                 N   ILE G 105     1555   1555  1.33  
LINK         C   GLY G 150                 N   HYP G 151     1555   1555  1.34  
LINK         C   HYP G 151                 N   PRO G 152     1555   1555  1.34  
LINK         C   THR G 200                 N   KCX G 201     1555   1555  1.33  
LINK         C   KCX G 201                 N   ASP G 202     1555   1555  1.33  
LINK         C   VAL G 255                 N   SMC G 256     1555   1555  1.33  
LINK         C   SMC G 256                 N   ALA G 257     1555   1555  1.33  
LINK         C   TRP G 368                 N   SMC G 369     1555   1555  1.33  
LINK         C   SMC G 369                 N   SER G 370     1555   1555  1.33  
LINK        MG    MG G 476                 OD1 ASP G 203     1555   1555  1.95  
LINK        MG    MG G 476                 O2  CAP G 477     1555   1555  2.25  
LINK        MG    MG G 476                 O7  CAP G 477     1555   1555  2.21  
LINK        MG    MG G 476                 OQ1 KCX G 201     1555   1555  1.96  
LINK        MG    MG G 476                 O3  CAP G 477     1555   1555  2.15  
LINK        MG    MG G 476                 OE1 GLU G 204     1555   1555  1.96  
LINK         C   TYR H 103                 N   HYP H 104     1555   1555  1.35  
LINK         C   HYP H 104                 N   ILE H 105     1555   1555  1.33  
LINK         C   GLY H 150                 N   HYP H 151     1555   1555  1.34  
LINK         C   HYP H 151                 N   PRO H 152     1555   1555  1.35  
LINK         C   THR H 200                 N   KCX H 201     1555   1555  1.33  
LINK         C   KCX H 201                 N   ASP H 202     1555   1555  1.33  
LINK         C   VAL H 255                 N   SMC H 256     1555   1555  1.33  
LINK         C   SMC H 256                 N   ALA H 257     1555   1555  1.33  
LINK         C   TRP H 368                 N   SMC H 369     1555   1555  1.33  
LINK         C   SMC H 369                 N   SER H 370     1555   1555  1.33  
LINK        MG    MG H 476                 OE1 GLU H 204     1555   1555  2.03  
LINK        MG    MG H 476                 OD1 ASP H 203     1555   1555  2.02  
LINK        MG    MG H 476                 O7  CAP H 477     1555   1555  2.13  
LINK        MG    MG H 476                 O2  CAP H 477     1555   1555  2.28  
LINK        MG    MG H 476                 OQ1 KCX H 201     1555   1555  1.97  
LINK        MG    MG H 476                 O3  CAP H 477     1555   1555  2.17  
LINK         C   MME I   1                 N   MET I   2     1555   1555  1.33  
LINK         C   MME J   1                 N   MET J   2     1555   1555  1.33  
LINK         C   MME K   1                 N   MET K   2     1555   1555  1.33  
LINK         C   MME L   1                 N   MET L   2     1555   1555  1.33  
LINK         C   MME M   1                 N   MET M   2     1555   1555  1.33  
LINK         C   MME N   1                 N   MET N   2     1555   1555  1.33  
LINK         C   MME O   1                 N   MET O   2     1555   1555  1.33  
LINK         C   MME P   1                 N   MET P   2     1555   1555  1.33  
CISPEP   1 LYS A  175    PRO A  176          0        -0.81                     
CISPEP   2 LYS B  175    PRO B  176          0         0.38                     
CISPEP   3 LYS C  175    PRO C  176          0        -1.96                     
CISPEP   4 LYS D  175    PRO D  176          0        -0.56                     
CISPEP   5 LYS E  175    PRO E  176          0        -1.12                     
CISPEP   6 LYS F  175    PRO F  176          0        -3.57                     
CISPEP   7 LYS G  175    PRO G  176          0        -0.77                     
CISPEP   8 LYS H  175    PRO H  176          0        -1.19                     
SITE     1 AC1 28 THR A 173  LYS A 175  LYS A 177  KCX A 201                    
SITE     2 AC1 28 ASP A 203  GLU A 204  HIS A 294  ARG A 295                    
SITE     3 AC1 28 HIS A 327  LYS A 334  LEU A 335  SER A 379                    
SITE     4 AC1 28 GLY A 380  GLY A 381  GLY A 403  GLY A 404                    
SITE     5 AC1 28  MG A 477  HOH A2125  HOH A2244  HOH A2289                    
SITE     6 AC1 28 HOH A2290  HOH A2291  HOH A2292  GLU B  60                    
SITE     7 AC1 28 THR B  65  TRP B  66  ASN B 123  HOH B2034                    
SITE     1 AC2  5 LYS A 177  KCX A 201  ASP A 203  GLU A 204                    
SITE     2 AC2  5 CAP A 476                                                     
SITE     1 AC3  4 KCX B 201  ASP B 203  GLU B 204  CAP B 477                    
SITE     1 AC4 30 GLU A  60  THR A  65  TRP A  66  ASN A 123                    
SITE     2 AC4 30 HOH A2091  HOH A2092  THR B 173  LYS B 175                    
SITE     3 AC4 30 LYS B 177  KCX B 201  ASP B 203  GLU B 204                    
SITE     4 AC4 30 HIS B 294  ARG B 295  HIS B 327  LYS B 334                    
SITE     5 AC4 30 LEU B 335  SER B 379  GLY B 380  GLY B 381                    
SITE     6 AC4 30 GLY B 403  GLY B 404   MG B 476  HOH B2115                    
SITE     7 AC4 30 HOH B2116  HOH B2233  HOH B2279  HOH B2280                    
SITE     8 AC4 30 HOH B2281  HOH B2282                                          
SITE     1 AC5  4 KCX C 201  ASP C 203  GLU C 204  CAP C 477                    
SITE     1 AC6 30 THR C 173  LYS C 175  LYS C 177  KCX C 201                    
SITE     2 AC6 30 ASP C 203  GLU C 204  HIS C 294  ARG C 295                    
SITE     3 AC6 30 HIS C 327  LYS C 334  LEU C 335  SER C 379                    
SITE     4 AC6 30 GLY C 380  GLY C 381  GLY C 403  GLY C 404                    
SITE     5 AC6 30  MG C 476  HOH C2120  HOH C2121  HOH C2226                    
SITE     6 AC6 30 HOH C2239  HOH C2273  HOH C2274  HOH C2275                    
SITE     7 AC6 30 GLU D  60  THR D  65  TRP D  66  ASN D 123                    
SITE     8 AC6 30 HOH D2034  HOH D2085                                          
SITE     1 AC7  5 LYS D 177  KCX D 201  ASP D 203  GLU D 204                    
SITE     2 AC7  5 CAP D 477                                                     
SITE     1 AC8 30 GLU C  60  THR C  65  TRP C  66  ASN C 123                    
SITE     2 AC8 30 HOH C2038  HOH C2088  THR D 173  LYS D 175                    
SITE     3 AC8 30 LYS D 177  KCX D 201  ASP D 203  GLU D 204                    
SITE     4 AC8 30 HIS D 294  ARG D 295  HIS D 327  LYS D 334                    
SITE     5 AC8 30 LEU D 335  SER D 379  GLY D 380  GLY D 381                    
SITE     6 AC8 30 GLY D 403  GLY D 404   MG D 476  HOH D2119                    
SITE     7 AC8 30 HOH D2120  HOH D2256  HOH D2257  HOH D2258                    
SITE     8 AC8 30 HOH D2259  HOH D2260                                          
SITE     1 AC9  5 LYS E 177  KCX E 201  ASP E 203  GLU E 204                    
SITE     2 AC9  5 CAP E 477                                                     
SITE     1 BC1 28 THR E 173  LYS E 175  LYS E 177  KCX E 201                    
SITE     2 BC1 28 ASP E 203  GLU E 204  HIS E 294  ARG E 295                    
SITE     3 BC1 28 HIS E 327  LYS E 334  LEU E 335  SER E 379                    
SITE     4 BC1 28 GLY E 380  GLY E 381  GLY E 403  GLY E 404                    
SITE     5 BC1 28  MG E 476  HOH E2096  HOH E2205  HOH E2220                    
SITE     6 BC1 28 HOH E2259  HOH E2260  HOH E2261  GLU F  60                    
SITE     7 BC1 28 THR F  65  TRP F  66  ASN F 123  HOH F2078                    
SITE     1 BC2  5 LYS F 177  KCX F 201  ASP F 203  GLU F 204                    
SITE     2 BC2  5 CAP F 477                                                     
SITE     1 BC3 29 GLU E  60  THR E  65  TRP E  66  ASN E 123                    
SITE     2 BC3 29 HOH E2023  HOH E2061  THR F 173  LYS F 175                    
SITE     3 BC3 29 LYS F 177  KCX F 201  ASP F 203  GLU F 204                    
SITE     4 BC3 29 HIS F 294  ARG F 295  HIS F 327  LYS F 334                    
SITE     5 BC3 29 LEU F 335  SER F 379  GLY F 380  GLY F 381                    
SITE     6 BC3 29 GLY F 403  GLY F 404   MG F 476  HOH F2245                    
SITE     7 BC3 29 HOH F2246  HOH F2247  HOH F2248  HOH F2249                    
SITE     8 BC3 29 HOH F2250                                                     
SITE     1 BC4  5 LYS G 177  KCX G 201  ASP G 203  GLU G 204                    
SITE     2 BC4  5 CAP G 477                                                     
SITE     1 BC5 29 THR G 173  LYS G 175  LYS G 177  KCX G 201                    
SITE     2 BC5 29 ASP G 203  GLU G 204  HIS G 294  ARG G 295                    
SITE     3 BC5 29 HIS G 327  LYS G 334  LEU G 335  SER G 379                    
SITE     4 BC5 29 GLY G 380  GLY G 381  GLY G 403  GLY G 404                    
SITE     5 BC5 29  MG G 476  HOH G2121  HOH G2227  HOH G2279                    
SITE     6 BC5 29 HOH G2280  HOH G2281  HOH G2282  GLU H  60                    
SITE     7 BC5 29 THR H  65  TRP H  66  ASN H 123  HOH H2038                    
SITE     8 BC5 29 HOH H2088                                                     
SITE     1 BC6  5 LYS H 177  KCX H 201  ASP H 203  GLU H 204                    
SITE     2 BC6  5 CAP H 477                                                     
SITE     1 BC7 30 GLU G  60  THR G  65  TRP G  66  ASN G 123                    
SITE     2 BC7 30 HOH G2038  HOH G2082  THR H 173  LYS H 175                    
SITE     3 BC7 30 LYS H 177  KCX H 201  ASP H 203  GLU H 204                    
SITE     4 BC7 30 HIS H 294  ARG H 295  HIS H 327  LYS H 334                    
SITE     5 BC7 30 LEU H 335  SER H 379  GLY H 380  GLY H 381                    
SITE     6 BC7 30 GLY H 403  GLY H 404   MG H 476  HOH H2119                    
SITE     7 BC7 30 HOH H2120  HOH H2234  HOH H2245  HOH H2277                    
SITE     8 BC7 30 HOH H2278  HOH H2279                                          
SITE     1 BC8  8 VAL A  17  LYS A  18  THR A  65  TRP A  66                    
SITE     2 BC8  8 THR A  67  THR A  68  HOH A2014  HOH A2293                    
SITE     1 BC9  2 GLU A  52  HOH A2294                                          
SITE     1 CC1  7 ARG A 295  SER A 328  GLY A 329  GLU A 336                    
SITE     2 CC1  7 PHE A 345  HOH A2193  HOH A2295                               
SITE     1 CC2  4 LYS H 466  GLU H 468  PHE H 469  HOH H2281                    
SITE     1 CC3  8 ARG H 295  HIS H 298  ASP H 302  PHE H 311                    
SITE     2 CC3  8 SER H 328  GLU H 336  PHE H 345  HOH H2199                    
SITE     1 CC4  4 TYR A 226  LYS O  49  GLU O  55  HOH O2079                    
SITE     1 CC5  6 GLY O  37  TRP O  38  PHE O  81  GLY O  82                    
SITE     2 CC5  6 CYS O  83  HOH O2081                                          
SITE     1 CC6  8 VAL C  17  LYS C  18  THR C  65  TRP C  66                    
SITE     2 CC6  8 THR C  67  THR C  68  HOH C2021  HOH C2040                    
SITE     1 CC7  5 GLY K  37  TRP K  38  ILE K  39  GLY K  82                    
SITE     2 CC7  5 CYS K  83                                                     
SITE     1 CC8  9 TYR B  24  GLY B  64  THR B  68  VAL B  69                    
SITE     2 CC8  9 ASP B  72  EDO B1476  HOH B2283  HOH B2284                    
SITE     3 CC8  9 HOH B2285                                                     
SITE     1 CC9  9 VAL B  17  LYS B  18  THR B  65  TRP B  66                    
SITE     2 CC9  9 THR B  67  THR B  68  EDO B1475  HOH B2283                    
SITE     3 CC9  9 HOH B2286                                                     
SITE     1 DC1  3 PHE A 469  HOH A2296  TYR B  20                               
SITE     1 DC2  5 HOH A2294  LYS B 466  PHE B 467  GLU B 468                    
SITE     2 DC2  5 PHE B 469                                                     
SITE     1 DC3  6 TYR H 226  ALA H 230  LYS J  49  GLU J  55                    
SITE     2 DC3  6 ASP J  69  HOH J2083                                          
SITE     1 DC4  6 LEU G 270  GLY G 273  PHE G 274  HOH G2287                    
SITE     2 DC4  6 LEU H 270  THR H 271                                          
SITE     1 DC5  8 LYS D  18  THR D  65  TRP D  66  THR D  67                    
SITE     2 DC5  8 THR D  68  EDO D1477  HOH D2037  HOH D2261                    
SITE     1 DC6  5 LYS D 466  PHE D 467  GLU D 468  PHE D 469                    
SITE     2 DC6  5 HOH D2262                                                     
SITE     1 DC7  6 TYR E  24  THR E  68  VAL E  69  ASP E  72                    
SITE     2 DC7  6 HOH E2026  HOH E2262                                          
SITE     1 DC8  4 LYS E 466  PHE E 467  GLU E 468  PHE E 469                    
SITE     1 DC9  6 GLY J  37  TRP J  38  PHE J  81  GLY J  82                    
SITE     2 DC9  6 CYS J  83  HOH J2084                                          
SITE     1 EC1  8 TYR D  24  THR D  68  VAL D  69  ASP D  72                    
SITE     2 EC1  8 EDO D1475  HOH D2036  HOH D2037  HOH D2045                    
SITE     1 EC2  5 ARG D 295  PHE D 311  GLY D 329  GLU D 336                    
SITE     2 EC2  5 HOH D2191                                                     
SITE     1 EC3  5 TYR F 226  LYS P  49  GLU P  55  HOH P2045                    
SITE     2 EC3  5 HOH P2077                                                     
SITE     1 EC4  6 TYR D 226  HOH D2146  LYS N  49  GLU N  55                    
SITE     2 EC4  6 ASP N  69  HOH N2033                                          
SITE     1 EC5  6 GLY N  37  ILE N  39  PHE N  81  GLY N  82                    
SITE     2 EC5  6 CYS N  83  HOH N2072                                          
SITE     1 EC6  7 TYR B 226  LYS B 227  HOH B2142  LYS L  49                    
SITE     2 EC6  7 GLU L  55  SER L  56  ASP L  69                               
SITE     1 EC7  5 GLY A  10  HOH A2051  GLY L  37  ILE L  39                    
SITE     2 EC7  5 GLY L  82                                                     
SITE     1 EC8  4 LYS A 466  GLU A 468  PHE A 469  HOH A2296                    
SITE     1 EC9  4 TYR C  20  GLU C  52  HOH C2277  HOH C2278                    
SITE     1 FC1  6 LYS C 466  PHE C 467  GLU C 468  PHE C 469                    
SITE     2 FC1  6 HOH C2279  HOH C2280                                          
SITE     1 FC2  5 ARG C 295  PHE C 345  ASP C 473  HOH C2281                    
SITE     2 FC2  5 HOH C2282                                                     
SITE     1 FC3  3 TYR G  20  GLU G  52  HOH H2281                               
SITE     1 FC4  5 TYR C 226  LYS I  49  GLU I  55  HOH I2039                    
SITE     2 FC4  5 HOH I2075                                                     
SITE     1 FC5  5 TYR E 226  HOH E2126  LYS K  49  GLU K  55                    
SITE     2 FC5  5 HOH K2051                                                     
SITE     1 FC6  5 TYR G 226  LYS M  49  GLU M  55  HOH M2056                    
SITE     2 FC6  5 HOH M2103                                                     
SITE     1 FC7  8 GLY H  10  GLY M  37  ILE M  39  PHE M  81                    
SITE     2 FC7  8 GLY M  82  HOH M2104  HOH M2105  HOH M2106                    
SITE     1 FC8  4 LEU C 270  HOH C2276  LEU D 270  HOH D2167                    
SITE     1 FC9  7 LYS H  18  THR H  65  TRP H  66  THR H  67                    
SITE     2 FC9  7 THR H  68  HOH H2019  HOH H2280                               
SITE     1 GC1  1 GLU H  52                                                     
SITE     1 GC2  9 TYR G  24  GLY G  64  THR G  68  VAL G  69                    
SITE     2 GC2  9 ASP G  72  EDO G1476  HOH G2283  HOH G2284                    
SITE     3 GC2  9 HOH G2285                                                     
SITE     1 GC3  8 LYS G  18  THR G  65  TRP G  66  THR G  67                    
SITE     2 GC3  8 THR G  68  EDO G1475  HOH G2013  HOH G2284                    
SITE     1 GC4  5 LYS G 466  PHE G 467  GLU G 468  PHE G 469                    
SITE     2 GC4  5 HOH G2286                                                     
SITE     1 GC5  3 ARG G 295  PHE G 345  ASP G 473                               
SITE     1 GC6  7 LYS E  18  THR E  65  TRP E  66  THR E  67                    
SITE     2 GC6  7 THR E  68  HOH E2006  HOH E2026                               
SITE     1 GC7  7 LYS F  18  THR F  65  TRP F  66  THR F  67                    
SITE     2 GC7  7 THR F  68  HOH F2251  HOH F2252                               
SITE     1 GC8  2 GLU F  52  HOH F2253                                          
CRYST1  121.377  177.446  122.568  90.00 117.65  90.00 P 1 21 1     16          
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      0.008239  0.000000  0.004316        0.00000                         
SCALE2      0.000000  0.005636  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009211        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system