GenomeNet

Database: PDB
Entry: 2V6A
LinkDB: 2V6A
Original site: 2V6A 
HEADER    OXIDOREDUCTASE                          14-JUL-07   2V6A              
TITLE     CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII RUBISCO WITH           
TITLE    2 LARGE-SUBUNIT MUTATIONS V331A, G344S                                 
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 CHAIN;          
COMPND   5 EC: 4.1.1.39;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1;           
COMPND  10 CHAIN: I, J, K, L, M, N, O, P;                                       
COMPND  11 SYNONYM: RUBISCO SMALL SUBUNIT 1,RIBULOSE-1,5-BISPHOSPHATE           
COMPND  12  CARBOXYLASE SMALL CHAIN;                                            
COMPND  13 EC: 4.1.1.39;                                                        
COMPND  14 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 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;                      
SOURCE   9 ORGANISM_TAXID: 3055;                                                
SOURCE  10 STRAIN: 2137;                                                        
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
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 2V6A    1       VERSN                                    
REVDAT   5   23-OCT-07 2V6A    1       REMARK                                   
REVDAT   4   02-OCT-07 2V6A    1       JRNL   REMARK                            
REVDAT   3   28-AUG-07 2V6A    1       AUTHOR                                   
REVDAT   2   07-AUG-07 2V6A    1       SOURCE REMARK                            
REVDAT   1   31-JUL-07 2V6A    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.    1.5  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) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 740735                         
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) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.192                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 39244                           
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) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 50643                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2550                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 2655                         
REMARK   3   BIN FREE R VALUE                    : 0.2690                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 38101                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 820                                     
REMARK   3   SOLVENT ATOMS            : 3492                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.34000                                              
REMARK   3    B22 (A**2) : 0.49000                                              
REMARK   3    B33 (A**2) : -0.84000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.074         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.071         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.045         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.204         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.965                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 39827 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 53897 ; 1.286 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4833 ; 5.963 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1878 ;31.136 ;23.248       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  6460 ;13.021 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   312 ;15.450 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  5701 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 30552 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A): 20657 ; 0.199 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 27474 ; 0.309 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  3474 ; 0.108 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    63 ; 0.214 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    16 ; 0.171 ; 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): 24714 ; 0.719 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 38792 ; 1.122 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 17315 ; 1.832 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 15105 ; 2.801 ; 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      89      2                      
REMARK   3           2     A     97       A    1477      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1825 ;  0.00 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1783 ;  0.00 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1825 ;  0.00 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1783 ;  0.00 ;  2.00           
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      89      2                      
REMARK   3           1     A     13       A      89      2                      
REMARK   3           2     B     97       B    1477      2                      
REMARK   3           2     A     97       A    1477      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    B    (A):   1825 ;  0.03 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  2    B    (A):   1782 ;  0.15 ;  0.50           
REMARK   3   TIGHT THERMAL      2    B (A**2):   1825 ;  0.14 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    B (A**2):   1782 ;  0.43 ;  2.00           
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      89      2                      
REMARK   3           1     A     13       A      89      2                      
REMARK   3           2     C     97       C    1477      2                      
REMARK   3           2     A     97       A    1477      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    C    (A):   1825 ;  0.02 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  3    C    (A):   1774 ;  0.18 ;  0.50           
REMARK   3   TIGHT THERMAL      3    C (A**2):   1825 ;  0.18 ;  0.50           
REMARK   3   MEDIUM THERMAL     3    C (A**2):   1774 ;  0.48 ;  2.00           
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      89      2                      
REMARK   3           1     A     13       A      89      2                      
REMARK   3           2     D     97       D    1477      2                      
REMARK   3           2     A     97       A    1477      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   4    D    (A):   1825 ;  0.03 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  4    D    (A):   1777 ;  0.20 ;  0.50           
REMARK   3   TIGHT THERMAL      4    D (A**2):   1825 ;  0.16 ;  0.50           
REMARK   3   MEDIUM THERMAL     4    D (A**2):   1777 ;  0.47 ;  2.00           
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      89      2                      
REMARK   3           1     A     13       A      89      2                      
REMARK   3           2     E     97       E    1477      2                      
REMARK   3           2     A     97       A    1477      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   5    E    (A):   1825 ;  0.02 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  5    E    (A):   1780 ;  0.18 ;  0.50           
REMARK   3   TIGHT THERMAL      5    E (A**2):   1825 ;  0.14 ;  0.50           
REMARK   3   MEDIUM THERMAL     5    E (A**2):   1780 ;  0.42 ;  2.00           
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      89      2                      
REMARK   3           1     A     13       A      89      2                      
REMARK   3           2     F     97       F    1477      2                      
REMARK   3           2     A     97       A    1477      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   6    F    (A):   1825 ;  0.02 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  6    F    (A):   1780 ;  0.18 ;  0.50           
REMARK   3   TIGHT THERMAL      6    F (A**2):   1825 ;  0.13 ;  0.50           
REMARK   3   MEDIUM THERMAL     6    F (A**2):   1780 ;  0.40 ;  2.00           
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      89      2                      
REMARK   3           1     A     13       A      89      2                      
REMARK   3           2     G     97       G    1477      2                      
REMARK   3           2     A     97       A    1477      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   7    G    (A):   1825 ;  0.05 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  7    G    (A):   1780 ;  0.20 ;  0.50           
REMARK   3   TIGHT THERMAL      7    G (A**2):   1825 ;  0.20 ;  0.50           
REMARK   3   MEDIUM THERMAL     7    G (A**2):   1780 ;  0.46 ;  2.00           
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      89      2                      
REMARK   3           1     A     13       A      89      2                      
REMARK   3           2     H     97       H    1477      2                      
REMARK   3           2     A     97       A    1477      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   8    H    (A):   1825 ;  0.03 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  8    H    (A):   1773 ;  0.18 ;  0.50           
REMARK   3   TIGHT THERMAL      8    H (A**2):   1825 ;  0.15 ;  0.50           
REMARK   3   MEDIUM THERMAL     8    H (A**2):   1773 ;  0.43 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 9                                  
REMARK   3     CHAIN NAMES                    : I                               
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     I      1       I     140      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   9    I    (A):    560 ;  0.00 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  9    I    (A):    587 ;  0.00 ;  0.50           
REMARK   3   TIGHT THERMAL      9    I (A**2):    560 ;  0.00 ;  0.50           
REMARK   3   MEDIUM THERMAL     9    I (A**2):    587 ;  0.00 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 10                                 
REMARK   3     CHAIN NAMES                    : J I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     J      1       J     140      2                      
REMARK   3           1     I      1       I     140      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  10    J    (A):    560 ;  0.05 ;  0.05           
REMARK   3   MEDIUM POSITIONAL 10    J    (A):    579 ;  0.25 ;  0.50           
REMARK   3   TIGHT THERMAL     10    J (A**2):    560 ;  0.16 ;  0.50           
REMARK   3   MEDIUM THERMAL    10    J (A**2):    579 ;  0.43 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 11                                 
REMARK   3     CHAIN NAMES                    : K I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     K      1       K     140      2                      
REMARK   3           1     I      1       I     140      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  11    K    (A):    560 ;  0.02 ;  0.05           
REMARK   3   MEDIUM POSITIONAL 11    K    (A):    569 ;  0.23 ;  0.50           
REMARK   3   TIGHT THERMAL     11    K (A**2):    560 ;  0.14 ;  0.50           
REMARK   3   MEDIUM THERMAL    11    K (A**2):    569 ;  0.36 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 12                                 
REMARK   3     CHAIN NAMES                    : L I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     L      1       L     140      2                      
REMARK   3           1     I      1       I     140      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  12    L    (A):    560 ;  0.02 ;  0.05           
REMARK   3   MEDIUM POSITIONAL 12    L    (A):    566 ;  0.24 ;  0.50           
REMARK   3   TIGHT THERMAL     12    L (A**2):    560 ;  0.11 ;  0.50           
REMARK   3   MEDIUM THERMAL    12    L (A**2):    566 ;  0.37 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 13                                 
REMARK   3     CHAIN NAMES                    : M I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     M      1       M     140      2                      
REMARK   3           1     I      1       I     140      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  13    M    (A):    560 ;  0.03 ;  0.05           
REMARK   3   MEDIUM POSITIONAL 13    M    (A):    567 ;  0.46 ;  0.50           
REMARK   3   TIGHT THERMAL     13    M (A**2):    560 ;  0.24 ;  0.50           
REMARK   3   MEDIUM THERMAL    13    M (A**2):    567 ;  0.55 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 14                                 
REMARK   3     CHAIN NAMES                    : N I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     N      1       N     140      2                      
REMARK   3           1     I      1       I     140      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  14    N    (A):    560 ;  0.02 ;  0.05           
REMARK   3   MEDIUM POSITIONAL 14    N    (A):    565 ;  0.25 ;  0.50           
REMARK   3   TIGHT THERMAL     14    N (A**2):    560 ;  0.11 ;  0.50           
REMARK   3   MEDIUM THERMAL    14    N (A**2):    565 ;  0.36 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 15                                 
REMARK   3     CHAIN NAMES                    : O I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     O      1       O     140      2                      
REMARK   3           1     I      1       I     140      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  15    O    (A):    560 ;  0.02 ;  0.05           
REMARK   3   MEDIUM POSITIONAL 15    O    (A):    573 ;  0.23 ;  0.50           
REMARK   3   TIGHT THERMAL     15    O (A**2):    560 ;  0.13 ;  0.50           
REMARK   3   MEDIUM THERMAL    15    O (A**2):    573 ;  0.41 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 16                                 
REMARK   3     CHAIN NAMES                    : P I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     P      1       P     140      2                      
REMARK   3           1     I      1       I     140      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  16    P    (A):    560 ;  0.04 ;  0.05           
REMARK   3   MEDIUM POSITIONAL 16    P    (A):    569 ;  0.28 ;  0.50           
REMARK   3   TIGHT THERMAL     16    P (A**2):    560 ;  0.14 ;  0.50           
REMARK   3   MEDIUM THERMAL    16    P (A**2):    569 ;  0.41 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2V6A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JUL-07.                  
REMARK 100 THE PDBE ID CODE IS EBI-33194.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
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                       : ID14-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.931                              
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   : 781039                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.50                               
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     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : 31.2                               
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.00                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.90                               
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   (%): 42.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):2.17                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       64.95300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      100.97500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       98.31450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      100.97500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       64.95300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       98.31450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: 125620 ANGSTROM**2                        
REMARK 350 SURFACE AREA OF THE COMPLEX: 152130 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -755.1 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 A, GLY 344 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, VAL 331 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, GLY 344 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, VAL 331 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, GLY 344 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, VAL 331 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, GLY 344 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN E, VAL 331 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN E, GLY 344 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, VAL 331 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, GLY 344 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN G, VAL 331 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN G, GLY 344 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN H, VAL 331 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN H, GLY 344 TO SER                        
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     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     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     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     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     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     ALA F     9                                                      
REMARK 465     GLY F    10                                                      
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     ALA G     9                                                      
REMARK 465     GLY G    10                                                      
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A 449   CA  -  CB  -  SG  ANGL. DEV. =   7.8 DEGREES          
REMARK 500    PRO B  91   C   -  N   -  CA  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    CYS C 449   CA  -  CB  -  SG  ANGL. DEV. =   7.5 DEGREES          
REMARK 500    CYS D 449   CA  -  CB  -  SG  ANGL. DEV. =   8.9 DEGREES          
REMARK 500    CYS F 449   CA  -  CB  -  SG  ANGL. DEV. =   6.7 DEGREES          
REMARK 500    CYS G 449   CA  -  CB  -  SG  ANGL. DEV. =   6.9 DEGREES          
REMARK 500    CYS H 449   CA  -  CB  -  SG  ANGL. DEV. =   7.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 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      -79.79   -141.08                                   
REMARK 500    THR A  65     -166.60   -129.37                                   
REMARK 500    THR A  75     -166.64   -122.77                                   
REMARK 500    CYS A 172      124.21   -173.53                                   
REMARK 500    ASN A 207      -93.66   -122.58                                   
REMARK 500    MET A 212      108.55   -166.19                                   
REMARK 500    ALA A 296      131.56    -38.62                                   
REMARK 500    MET A 297      -11.05     89.51                                   
REMARK 500    ALA A 331      -51.78     72.72                                   
REMARK 500    SER B  62      -79.23   -139.72                                   
REMARK 500    THR B  65     -165.72   -128.11                                   
REMARK 500    THR B  75     -166.04   -122.68                                   
REMARK 500    CYS B 172      123.82   -172.24                                   
REMARK 500    ASN B 207      -95.31   -123.69                                   
REMARK 500    MET B 212      110.49   -164.64                                   
REMARK 500    ALA B 296      133.58    -39.43                                   
REMARK 500    MET B 297      -12.35     88.12                                   
REMARK 500    ALA B 331      -48.98     70.48                                   
REMARK 500    SER C  62      -79.74   -139.38                                   
REMARK 500    THR C  65     -167.90   -129.17                                   
REMARK 500    THR C  75     -167.33   -122.41                                   
REMARK 500    CYS C 172      123.51   -172.22                                   
REMARK 500    ASN C 207      -92.91   -123.04                                   
REMARK 500    MET C 212      109.08   -165.47                                   
REMARK 500    MET C 297       -9.11     86.72                                   
REMARK 500    ALA C 331      -49.28     72.00                                   
REMARK 500    SER D  62      -80.97   -138.16                                   
REMARK 500    THR D  65     -164.66   -128.64                                   
REMARK 500    THR D  75     -167.01   -120.65                                   
REMARK 500    CYS D 172      125.67   -173.09                                   
REMARK 500    ASN D 207      -93.35   -123.89                                   
REMARK 500    MET D 212      109.57   -167.60                                   
REMARK 500    MET D 297      -12.93     89.66                                   
REMARK 500    ALA D 331      -50.88     70.75                                   
REMARK 500    SER E  62      -78.82   -141.74                                   
REMARK 500    THR E  65     -166.00   -129.74                                   
REMARK 500    THR E  75     -169.66   -123.91                                   
REMARK 500    CYS E 172      125.90   -174.04                                   
REMARK 500    ASN E 207      -96.56   -125.31                                   
REMARK 500    MET E 212      109.31   -165.73                                   
REMARK 500    ALA E 296      131.61    -38.30                                   
REMARK 500    MET E 297      -10.35     88.03                                   
REMARK 500    ALA E 331      -51.80     73.61                                   
REMARK 500    SER F  62      -78.08   -137.97                                   
REMARK 500    THR F  75     -168.88   -123.30                                   
REMARK 500    CYS F 172      125.50   -174.17                                   
REMARK 500    ASN F 207      -94.83   -123.97                                   
REMARK 500    MET F 212      109.88   -164.14                                   
REMARK 500    MET F 297      -10.58     87.44                                   
REMARK 500    ALA F 331      -52.48     70.14                                   
REMARK 500    SER G  62      -78.63   -137.43                                   
REMARK 500    THR G  75     -166.98   -121.02                                   
REMARK 500    CYS G 172      126.20   -172.31                                   
REMARK 500    ASN G 207      -95.29   -125.13                                   
REMARK 500    MET G 212      109.69   -166.03                                   
REMARK 500    MET G 297      -10.85     88.04                                   
REMARK 500    ALA G 331      -51.50     70.58                                   
REMARK 500    SER H  62      -80.75   -140.21                                   
REMARK 500    THR H  75     -163.09   -123.29                                   
REMARK 500    CYS H 172      125.75   -174.01                                   
REMARK 500    ASN H 207      -90.60   -124.54                                   
REMARK 500    MET H 212      111.19   -165.94                                   
REMARK 500    MET H 297       -8.87     88.44                                   
REMARK 500    ALA H 331      -52.19     69.04                                   
REMARK 500    PHE I  12       42.72   -145.07                                   
REMARK 500    GLU I  13     -141.92     62.74                                   
REMARK 500    PHE I  15       -1.77     83.09                                   
REMARK 500    LYS I  77     -124.37     57.42                                   
REMARK 500    PHE J  12       41.25   -144.13                                   
REMARK 500    GLU J  13     -141.83     62.69                                   
REMARK 500    PHE J  15       -1.56     79.11                                   
REMARK 500    LYS J  77     -121.65     54.46                                   
REMARK 500    PHE K  12       42.34   -144.27                                   
REMARK 500    GLU K  13     -141.38     60.66                                   
REMARK 500    PHE K  15       -0.91     81.89                                   
REMARK 500    LYS K  77     -122.99     53.41                                   
REMARK 500    PHE L  12       44.05   -146.49                                   
REMARK 500    GLU L  13     -143.56     58.76                                   
REMARK 500    PHE L  15        0.08     83.98                                   
REMARK 500    LYS L  77     -123.68     55.94                                   
REMARK 500    PHE M  12       42.15   -145.30                                   
REMARK 500    GLU M  13     -142.71     60.06                                   
REMARK 500    PHE M  15       -3.95     85.21                                   
REMARK 500    LYS M  77     -123.23     55.74                                   
REMARK 500    PHE N  12       43.50   -143.89                                   
REMARK 500    GLU N  13     -141.35     57.83                                   
REMARK 500    PHE N  15       -0.62     80.14                                   
REMARK 500    TRP N  73     -169.84   -108.41                                   
REMARK 500    LYS N  77     -123.31     55.34                                   
REMARK 500    PHE O  12       43.75   -142.85                                   
REMARK 500    GLU O  13     -139.65     60.92                                   
REMARK 500    PHE O  15       -1.21     82.97                                   
REMARK 500    LYS O  77     -123.10     55.38                                   
REMARK 500    PHE P  12       44.95   -142.64                                   
REMARK 500    GLU P  13     -137.23     60.09                                   
REMARK 500    PHE P  15       -0.23     82.13                                   
REMARK 500    LYS P  77     -121.16     55.43                                   
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 A1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 203   OD1                                                    
REMARK 620 2 GLU A 204   OE1  91.9                                              
REMARK 620 3 CAP A1477   O3  173.0  89.0                                        
REMARK 620 4 CAP A1477   O7   99.4  99.6  87.3                                  
REMARK 620 5 KCX A 201   OQ1  86.0  88.3  87.0 170.1                            
REMARK 620 6 CAP A1477   O2  104.1 164.0  75.3  76.5  94.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAP B1477   O2                                                     
REMARK 620 2 CAP B1477   O3   74.2                                              
REMARK 620 3 KCX B 201   OQ1  94.2  85.6                                        
REMARK 620 4 ASP B 203   OD1 103.2 174.8  90.1                                  
REMARK 620 5 GLU B 204   OE1 163.7  90.6  90.7  92.3                            
REMARK 620 6 CAP B1477   O7   74.3  86.9 167.6  96.8  99.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX C 201   OQ1                                                    
REMARK 620 2 ASP C 203   OD1  87.7                                              
REMARK 620 3 CAP C1477   O2   93.8 104.3                                        
REMARK 620 4 CAP C1477   O7  167.8 100.4  75.4                                  
REMARK 620 5 GLU C 204   OE1  89.7  91.5 163.9  99.1                            
REMARK 620 6 CAP C1477   O3   85.1 172.6  75.0  86.6  89.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX D 201   OQ1                                                    
REMARK 620 2 GLU D 204   OE1  90.6                                              
REMARK 620 3 CAP D1477   O3   86.6  89.9                                        
REMARK 620 4 ASP D 203   OD1  86.9  91.5 173.4                                  
REMARK 620 5 CAP D1477   O2   93.7 164.6  75.7 103.4                            
REMARK 620 6 CAP D1477   O7  169.1  98.5  87.4  98.8  75.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAP E1477   O2                                                     
REMARK 620 2 KCX E 201   OQ1  93.7                                              
REMARK 620 3 ASP E 203   OD1 105.2  88.8                                        
REMARK 620 4 CAP E1477   O3   75.2  85.5 174.3                                  
REMARK 620 5 GLU E 204   OE1 163.7  90.4  90.6  89.4                            
REMARK 620 6 CAP E1477   O7   74.9 167.8  98.1  87.5  99.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 203   OD1                                                    
REMARK 620 2 GLU F 204   OE1  91.7                                              
REMARK 620 3 CAP F1477   O2  104.1 163.2                                        
REMARK 620 4 CAP F1477   O7   97.4  97.5  75.2                                  
REMARK 620 5 KCX F 201   OQ1  88.7  90.6  95.3 169.6                            
REMARK 620 6 CAP F1477   O3  175.8  88.4  76.2  86.7  87.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAP G1477   O3                                                     
REMARK 620 2 CAP G1477   O7   88.4                                              
REMARK 620 3 KCX G 201   OQ1  85.3 169.2                                        
REMARK 620 4 ASP G 203   OD1 173.1  97.7  88.2                                  
REMARK 620 5 GLU G 204   OE1  91.3  99.5  89.4  91.0                            
REMARK 620 6 CAP G1477   O2   74.1  75.6  94.2 104.1 164.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAP H1477   O7                                                     
REMARK 620 2 ASP H 203   OD1  97.8                                              
REMARK 620 3 GLU H 204   OE1  98.5  88.8                                        
REMARK 620 4 CAP H1477   O3   86.7 175.5  90.0                                  
REMARK 620 5 KCX H 201   OQ1 170.2  86.1  90.5  89.7                            
REMARK 620 6 CAP H1477   O2   75.7 106.6 164.0  75.0  94.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG C1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG D1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG E1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG F1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP F1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG G1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG H1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO I1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO P1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO P1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO N1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO N1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1484                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO I1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO L1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO L1142                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1GK8   RELATED DB: PDB                                   
REMARK 900  RUBISCO FROM CHLAMYDOMONAS REINHARDTII                              
REMARK 900 RELATED ID: 1UWA   RELATED DB: PDB                                   
REMARK 900  L290F MUTANT RUBISCO FROM CHLAMYDOMONAS                             
REMARK 900 RELATED ID: 1UW9   RELATED DB: PDB                                   
REMARK 900  L290F-A222T CHLAMYDOMONAS RUBISCO MUTANT                            
REMARK 900 RELATED ID: 1UZH   RELATED DB: PDB                                   
REMARK 900  A CHIMERIC CHLAMYDOMONAS, SPINACH RUBISCO                           
REMARK 900  ENZYME                                                              
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: 2V63   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF RUBISCO FROM                                   
REMARK 900  CHLAMYDOMONAS REINHARDTII WITH A LARGE-SUBUNIT                      
REMARK 900   V331A MUTATION                                                     
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 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  2V6A A    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V6A B    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V6A C    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V6A D    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V6A E    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V6A F    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V6A G    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V6A H    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V6A I    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V6A J    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V6A K    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V6A L    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V6A M    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V6A N    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V6A O    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V6A P    1   140  UNP    P00873   RBS1_CHLRE      46    185             
SEQADV 2V6A PRO A   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V6A ALA A  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V6A SER A  344  UNP  P00877    GLY   344 ENGINEERED MUTATION            
SEQADV 2V6A PRO B   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V6A ALA B  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V6A SER B  344  UNP  P00877    GLY   344 ENGINEERED MUTATION            
SEQADV 2V6A PRO C   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V6A ALA C  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V6A SER C  344  UNP  P00877    GLY   344 ENGINEERED MUTATION            
SEQADV 2V6A PRO D   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V6A ALA D  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V6A SER D  344  UNP  P00877    GLY   344 ENGINEERED MUTATION            
SEQADV 2V6A PRO E   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V6A ALA E  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V6A SER E  344  UNP  P00877    GLY   344 ENGINEERED MUTATION            
SEQADV 2V6A PRO F   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V6A ALA F  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V6A SER F  344  UNP  P00877    GLY   344 ENGINEERED MUTATION            
SEQADV 2V6A PRO G   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V6A ALA G  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V6A SER G  344  UNP  P00877    GLY   344 ENGINEERED MUTATION            
SEQADV 2V6A PRO H   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V6A ALA H  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V6A SER H  344  UNP  P00877    GLY   344 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 SER 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 SER 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 SER 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 SER 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 SER 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 SER 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 SER 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 SER 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 2V6A HYP A  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V6A HYP A  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V6A KCX A  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V6A SMC A  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V6A SMC A  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V6A HYP B  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V6A HYP B  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V6A KCX B  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V6A SMC B  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V6A SMC B  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V6A HYP C  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V6A HYP C  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V6A KCX C  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V6A SMC C  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V6A SMC C  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V6A HYP D  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V6A HYP D  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V6A KCX D  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V6A SMC D  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V6A SMC D  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V6A HYP E  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V6A HYP E  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V6A KCX E  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V6A SMC E  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V6A SMC E  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V6A HYP F  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V6A HYP F  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V6A KCX F  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V6A SMC F  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V6A SMC F  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V6A HYP G  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V6A HYP G  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V6A KCX G  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V6A SMC G  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V6A SMC G  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V6A HYP H  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V6A HYP H  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V6A KCX H  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V6A SMC H  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V6A SMC H  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V6A MME I    1  MET  N-METHYL METHIONINE                                
MODRES 2V6A MME J    1  MET  N-METHYL METHIONINE                                
MODRES 2V6A MME K    1  MET  N-METHYL METHIONINE                                
MODRES 2V6A MME L    1  MET  N-METHYL METHIONINE                                
MODRES 2V6A MME M    1  MET  N-METHYL METHIONINE                                
MODRES 2V6A MME N    1  MET  N-METHYL METHIONINE                                
MODRES 2V6A MME O    1  MET  N-METHYL METHIONINE                                
MODRES 2V6A 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     MG  A1476       1                                                       
HET    CAP  A1477      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     MG  B1476       1                                                       
HET    CAP  B1477      21                                                       
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     MG  C1476       1                                                       
HET    CAP  C1477      21                                                       
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     MG  D1476       1                                                       
HET    CAP  D1477      21                                                       
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     MG  E1476       1                                                       
HET    CAP  E1477      21                                                       
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     MG  F1476       1                                                       
HET    CAP  F1477      21                                                       
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     MG  G1476       1                                                       
HET    CAP  G1477      21                                                       
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     MG  H1476       1                                                       
HET    CAP  H1477      21                                                       
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  A1478       4                                                       
HET    EDO  A1479       4                                                       
HET    EDO  A1480       4                                                       
HET    EDO  A1481       4                                                       
HET    EDO  A1482       4                                                       
HET    EDO  C1478       4                                                       
HET    EDO  C1479       4                                                       
HET    EDO  C1480       4                                                       
HET    EDO  C1481       4                                                       
HET    EDO  C1482       4                                                       
HET    EDO  E1478       4                                                       
HET    EDO  E1479       4                                                       
HET    EDO  E1480       4                                                       
HET    EDO  E1481       4                                                       
HET    EDO  G1478       4                                                       
HET    EDO  G1479       4                                                       
HET    EDO  G1480       4                                                       
HET    EDO  G1481       4                                                       
HET    EDO  G1482       4                                                       
HET    EDO  I1141       4                                                       
HET    EDO  K1141       4                                                       
HET    EDO  K1142       4                                                       
HET    EDO  M1141       4                                                       
HET    EDO  M1142       4                                                       
HET    EDO  O1141       4                                                       
HET    EDO  O1142       4                                                       
HET    EDO  F1478       4                                                       
HET    EDO  A1483       4                                                       
HET    EDO  H1478       4                                                       
HET    EDO  B1478       4                                                       
HET    EDO  B1479       4                                                       
HET    EDO  B1480       4                                                       
HET    EDO  B1481       4                                                       
HET    EDO  B1482       4                                                       
HET    EDO  H1479       4                                                       
HET    EDO  H1480       4                                                       
HET    EDO  H1481       4                                                       
HET    EDO  H1482       4                                                       
HET    EDO  F1479       4                                                       
HET    EDO  F1480       4                                                       
HET    EDO  F1481       4                                                       
HET    EDO  F1482       4                                                       
HET    EDO  F1483       4                                                       
HET    EDO  D1478       4                                                       
HET    EDO  D1479       4                                                       
HET    EDO  D1480       4                                                       
HET    EDO  D1481       4                                                       
HET    EDO  J1141       4                                                       
HET    EDO  J1142       4                                                       
HET    EDO  P1141       4                                                       
HET    EDO  P1142       4                                                       
HET    EDO  N1141       4                                                       
HET    EDO  N1142       4                                                       
HET    EDO  C1483       4                                                       
HET    EDO  A1484       4                                                       
HET    EDO  I1142       4                                                       
HET    EDO  D1482       4                                                       
HET    EDO  L1141       4                                                       
HET    EDO  L1142       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE                              
HETNAM     MME N-METHYL METHIONINE                                              
HETNAM     SMC S-METHYLCYSTEINE                                                 
HETNAM     HYP 4-HYDROXYPROLINE                                                 
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL  17  EDO    59(C2 H6 O2)                                                 
FORMUL  18  CAP    8(C6 H14 O13 P2)                                             
FORMUL  19  MME    8(C6 H13 N O2 S)                                             
FORMUL  20  SMC    16(C4 H9 N O2 S)                                             
FORMUL  21  HYP    16(C5 H9 N O3)                                               
FORMUL  22   MG    8(MG 2+)                                                     
FORMUL  23  KCX    8(C7 H14 N2 O4)                                              
FORMUL  24  HOH   *3492(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 ASP C  436  LYS C  463  1                                  28    
HELIX   67  67 TYR D   20  TYR D   25  1                                   6    
HELIX   68  68 PRO D   49  SER D   61  1                                  13    
HELIX   69  69 VAL D   69  THR D   75  5                                   7    
HELIX   70  70 SER D   76  LYS D   81  1                                   6    
HELIX   71  71 HYP D  104  PHE D  108  5                                   5    
HELIX   72  72 SER D  112  GLY D  122  1                                  11    
HELIX   73  73 ASN D  123  GLY D  126  5                                   4    
HELIX   74  74 PRO D  141  LYS D  146  1                                   6    
HELIX   75  75 GLY D  154  ASN D  163  1                                  10    
HELIX   76  76 SER D  181  GLY D  195  1                                  15    
HELIX   77  77 ARG D  213  GLY D  233  1                                  21    
HELIX   78  78 THR D  246  VAL D  255  1                                  10    
HELIX   79  79 TYR D  269  GLY D  288  1                                  20    
HELIX   80  80 MET D  297  ARG D  303  1                                   7    
HELIX   81  81 HIS D  310  GLY D  322  1                                  13    
HELIX   82  82 GLU D  338  ASP D  351  1                                  14    
HELIX   83  83 ARG D  358  GLY D  361  5                                   4    
HELIX   84  84 HIS D  383  TRP D  385  5                                   3    
HELIX   85  85 HIS D  386  GLY D  395  1                                  10    
HELIX   86  86 GLY D  403  GLY D  408  1                                   6    
HELIX   87  87 GLY D  412  GLU D  433  1                                  22    
HELIX   88  88 ASP D  436  LYS D  463  1                                  28    
HELIX   89  89 TYR E   20  TYR E   25  1                                   6    
HELIX   90  90 PRO E   49  SER E   61  1                                  13    
HELIX   91  91 VAL E   69  THR E   75  5                                   7    
HELIX   92  92 SER E   76  LYS E   81  1                                   6    
HELIX   93  93 HYP E  104  PHE E  108  5                                   5    
HELIX   94  94 SER E  112  GLY E  122  1                                  11    
HELIX   95  95 ASN E  123  GLY E  126  5                                   4    
HELIX   96  96 PRO E  141  LYS E  146  1                                   6    
HELIX   97  97 GLY E  154  ASN E  163  1                                  10    
HELIX   98  98 SER E  181  GLY E  195  1                                  15    
HELIX   99  99 ARG E  213  GLY E  233  1                                  21    
HELIX  100 100 THR E  246  VAL E  255  1                                  10    
HELIX  101 101 TYR E  269  GLY E  288  1                                  20    
HELIX  102 102 MET E  297  ARG E  303  1                                   7    
HELIX  103 103 HIS E  310  GLY E  322  1                                  13    
HELIX  104 104 GLU E  338  ASP E  351  1                                  14    
HELIX  105 105 ARG E  358  GLY E  361  5                                   4    
HELIX  106 106 HIS E  383  TRP E  385  5                                   3    
HELIX  107 107 HIS E  386  GLY E  395  1                                  10    
HELIX  108 108 GLY E  403  GLY E  408  1                                   6    
HELIX  109 109 GLY E  412  GLU E  433  1                                  22    
HELIX  110 110 ASP E  436  LYS E  463  1                                  28    
HELIX  111 111 TYR F   20  TYR F   25  1                                   6    
HELIX  112 112 PRO F   49  SER F   61  1                                  13    
HELIX  113 113 VAL F   69  THR F   75  5                                   7    
HELIX  114 114 SER F   76  LYS F   81  1                                   6    
HELIX  115 115 HYP F  104  PHE F  108  5                                   5    
HELIX  116 116 SER F  112  GLY F  122  1                                  11    
HELIX  117 117 ASN F  123  GLY F  126  5                                   4    
HELIX  118 118 PRO F  141  LYS F  146  1                                   6    
HELIX  119 119 GLY F  154  ASN F  163  1                                  10    
HELIX  120 120 SER F  181  GLY F  195  1                                  15    
HELIX  121 121 ARG F  213  GLY F  233  1                                  21    
HELIX  122 122 THR F  246  VAL F  255  1                                  10    
HELIX  123 123 TYR F  269  GLY F  288  1                                  20    
HELIX  124 124 MET F  297  ARG F  303  1                                   7    
HELIX  125 125 HIS F  310  GLY F  322  1                                  13    
HELIX  126 126 GLU F  338  ASP F  351  1                                  14    
HELIX  127 127 ARG F  358  GLY F  361  5                                   4    
HELIX  128 128 HIS F  383  TRP F  385  5                                   3    
HELIX  129 129 HIS F  386  GLY F  395  1                                  10    
HELIX  130 130 GLY F  403  GLY F  408  1                                   6    
HELIX  131 131 GLY F  412  GLU F  433  1                                  22    
HELIX  132 132 ASP F  436  LYS F  463  1                                  28    
HELIX  133 133 TYR G   20  TYR G   25  1                                   6    
HELIX  134 134 PRO G   49  SER G   61  1                                  13    
HELIX  135 135 VAL G   69  THR G   75  5                                   7    
HELIX  136 136 SER G   76  LYS G   81  1                                   6    
HELIX  137 137 HYP G  104  PHE G  108  5                                   5    
HELIX  138 138 SER G  112  GLY G  122  1                                  11    
HELIX  139 139 ASN G  123  GLY G  126  5                                   4    
HELIX  140 140 PRO G  141  LYS G  146  1                                   6    
HELIX  141 141 GLY G  154  ASN G  163  1                                  10    
HELIX  142 142 SER G  181  GLY G  195  1                                  15    
HELIX  143 143 ARG G  213  GLY G  233  1                                  21    
HELIX  144 144 THR G  246  VAL G  255  1                                  10    
HELIX  145 145 TYR G  269  GLY G  288  1                                  20    
HELIX  146 146 MET G  297  ARG G  303  1                                   7    
HELIX  147 147 HIS G  310  GLY G  322  1                                  13    
HELIX  148 148 GLU G  338  ASP G  351  1                                  14    
HELIX  149 149 ARG G  358  GLY G  361  5                                   4    
HELIX  150 150 HIS G  383  TRP G  385  5                                   3    
HELIX  151 151 HIS G  386  GLY G  395  1                                  10    
HELIX  152 152 GLY G  403  GLY G  408  1                                   6    
HELIX  153 153 GLY G  412  GLU G  433  1                                  22    
HELIX  154 154 ASP G  436  LYS G  463  1                                  28    
HELIX  155 155 TYR H   20  TYR H   25  1                                   6    
HELIX  156 156 PRO H   49  SER H   61  1                                  13    
HELIX  157 157 VAL H   69  THR H   75  5                                   7    
HELIX  158 158 SER H   76  LYS H   81  1                                   6    
HELIX  159 159 HYP H  104  PHE H  108  5                                   5    
HELIX  160 160 SER H  112  GLY H  122  1                                  11    
HELIX  161 161 ASN H  123  GLY H  126  5                                   4    
HELIX  162 162 PRO H  141  LYS H  146  1                                   6    
HELIX  163 163 GLY H  154  ASN H  163  1                                  10    
HELIX  164 164 SER H  181  GLY H  195  1                                  15    
HELIX  165 165 ARG H  213  GLY H  233  1                                  21    
HELIX  166 166 THR H  246  VAL H  255  1                                  10    
HELIX  167 167 TYR H  269  GLY H  288  1                                  20    
HELIX  168 168 MET H  297  ARG H  303  1                                   7    
HELIX  169 169 HIS H  310  GLY H  322  1                                  13    
HELIX  170 170 GLU H  338  ASP H  351  1                                  14    
HELIX  171 171 ARG H  358  GLY H  361  5                                   4    
HELIX  172 172 HIS H  383  TRP H  385  5                                   3    
HELIX  173 173 HIS H  386  GLY H  395  1                                  10    
HELIX  174 174 GLY H  403  GLY H  408  1                                   6    
HELIX  175 175 GLY H  412  GLU H  433  1                                  22    
HELIX  176 176 ASP H  436  LYS H  463  1                                  28    
HELIX  177 177 THR I   22  ASN I   36  1                                  15    
HELIX  178 178 GLU I   46  ALA I   50  5                                   5    
HELIX  179 179 ASN I   54  PHE I   60  5                                   7    
HELIX  180 180 ASP I   85  PHE I  100  1                                  16    
HELIX  181 181 PRO I  134  ARG I  138  5                                   5    
HELIX  182 182 THR J   22  GLY J   37  1                                  16    
HELIX  183 183 GLU J   46  ALA J   50  5                                   5    
HELIX  184 184 ASN J   54  PHE J   60  5                                   7    
HELIX  185 185 ASP J   85  PHE J  100  1                                  16    
HELIX  186 186 PRO J  134  ARG J  138  5                                   5    
HELIX  187 187 THR K   22  ASN K   36  1                                  15    
HELIX  188 188 GLU K   46  ALA K   50  5                                   5    
HELIX  189 189 ASN K   54  PHE K   60  5                                   7    
HELIX  190 190 ASP K   85  PHE K  100  1                                  16    
HELIX  191 191 PRO K  134  ARG K  138  5                                   5    
HELIX  192 192 THR L   22  ASN L   36  1                                  15    
HELIX  193 193 GLU L   46  ALA L   50  5                                   5    
HELIX  194 194 ASN L   54  PHE L   60  5                                   7    
HELIX  195 195 ASP L   85  PHE L  100  1                                  16    
HELIX  196 196 PRO L  134  ARG L  138  5                                   5    
HELIX  197 197 THR M   22  ASN M   36  1                                  15    
HELIX  198 198 GLU M   46  ALA M   50  5                                   5    
HELIX  199 199 ASN M   54  PHE M   60  5                                   7    
HELIX  200 200 ASP M   85  PHE M  100  1                                  16    
HELIX  201 201 PRO M  134  ARG M  138  5                                   5    
HELIX  202 202 THR N   22  ASN N   36  1                                  15    
HELIX  203 203 GLU N   46  ALA N   50  5                                   5    
HELIX  204 204 ASN N   54  PHE N   60  5                                   7    
HELIX  205 205 ASP N   85  PHE N  100  1                                  16    
HELIX  206 206 PRO N  134  ARG N  138  5                                   5    
HELIX  207 207 THR O   22  ASN O   36  1                                  15    
HELIX  208 208 GLU O   46  ALA O   50  5                                   5    
HELIX  209 209 ASN O   54  PHE O   60  5                                   7    
HELIX  210 210 ASP O   85  PHE O  100  1                                  16    
HELIX  211 211 PRO O  134  ARG O  138  5                                   5    
HELIX  212 212 THR P   22  ASN P   36  1                                  15    
HELIX  213 213 GLU P   46  ALA P   50  5                                   5    
HELIX  214 214 ASN P   54  PHE P   60  5                                   7    
HELIX  215 215 ASP P   85  PHE P  100  1                                  16    
HELIX  216 216 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  449    CYS A  459                          1555   1555  2.07  
SSBOND   2 CYS B  449    CYS B  459                          1555   1555  2.07  
SSBOND   3 CYS C  247    CYS D  247                          1555   1555  2.08  
SSBOND   4 CYS C  449    CYS C  459                          1555   1555  2.06  
SSBOND   5 CYS D  449    CYS D  459                          1555   1555  2.08  
SSBOND   6 CYS E  247    CYS F  247                          1555   1555  2.07  
SSBOND   7 CYS F  449    CYS F  459                          1555   1555  2.06  
SSBOND   8 CYS G  247    CYS H  247                          1555   1555  2.09  
SSBOND   9 CYS G  449    CYS G  459                          1555   1555  2.05  
SSBOND  10 CYS H  449    CYS H  459                          1555   1555  2.05  
LINK         C   TYR A 103                 N   HYP A 104     1555   1555  1.34  
LINK         C   HYP A 104                 N   ILE A 105     1555   1555  1.32  
LINK         C   GLY A 150                 N   HYP A 151     1555   1555  1.33  
LINK         C   HYP A 151                 N   PRO A 152     1555   1555  1.34  
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  1.34  
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 A1476                 OD1 ASP A 203     1555   1555  1.96  
LINK        MG    MG A1476                 OE1 GLU A 204     1555   1555  2.06  
LINK        MG    MG A1476                 O3  CAP A1477     1555   1555  2.19  
LINK        MG    MG A1476                 O7  CAP A1477     1555   1555  2.10  
LINK        MG    MG A1476                 OQ1 KCX A 201     1555   1555  2.05  
LINK        MG    MG A1476                 O2  CAP A1477     1555   1555  2.25  
LINK         C   TYR B 103                 N   HYP B 104     1555   1555  1.34  
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  1.35  
LINK         C   THR B 200                 N   KCX B 201     1555   1555  1.33  
LINK         C   KCX B 201                 N   ASP B 202     1555   1555  1.33  
LINK         C   VAL B 255                 N   SMC B 256     1555   1555  1.33  
LINK         C   SMC B 256                 N   ALA B 257     1555   1555  1.33  
LINK         C   TRP B 368                 N   SMC B 369     1555   1555  1.34  
LINK         C   SMC B 369                 N   SER B 370     1555   1555  1.34  
LINK        MG    MG B1476                 O2  CAP B1477     1555   1555  2.29  
LINK        MG    MG B1476                 O3  CAP B1477     1555   1555  2.16  
LINK        MG    MG B1476                 OQ1 KCX B 201     1555   1555  2.02  
LINK        MG    MG B1476                 OD1 ASP B 203     1555   1555  1.97  
LINK        MG    MG B1476                 OE1 GLU B 204     1555   1555  2.02  
LINK        MG    MG B1476                 O7  CAP B1477     1555   1555  2.06  
LINK         C   TYR C 103                 N   HYP C 104     1555   1555  1.35  
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  1.32  
LINK         C   KCX C 201                 N   ASP C 202     1555   1555  1.33  
LINK         C   VAL C 255                 N   SMC C 256     1555   1555  1.33  
LINK         C   SMC C 256                 N   ALA C 257     1555   1555  1.34  
LINK         C   TRP C 368                 N   SMC C 369     1555   1555  1.34  
LINK         C   SMC C 369                 N   SER C 370     1555   1555  1.34  
LINK        MG    MG C1476                 OQ1 KCX C 201     1555   1555  2.08  
LINK        MG    MG C1476                 OD1 ASP C 203     1555   1555  1.97  
LINK        MG    MG C1476                 O2  CAP C1477     1555   1555  2.21  
LINK        MG    MG C1476                 O7  CAP C1477     1555   1555  2.09  
LINK        MG    MG C1476                 OE1 GLU C 204     1555   1555  2.03  
LINK        MG    MG C1476                 O3  CAP C1477     1555   1555  2.19  
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  1.34  
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  1.34  
LINK         C   TRP D 368                 N   SMC D 369     1555   1555  1.34  
LINK         C   SMC D 369                 N   SER D 370     1555   1555  1.33  
LINK        MG    MG D1476                 OE1 GLU D 204     1555   1555  2.00  
LINK        MG    MG D1476                 OQ1 KCX D 201     1555   1555  2.04  
LINK        MG    MG D1476                 O2  CAP D1477     1555   1555  2.21  
LINK        MG    MG D1476                 O7  CAP D1477     1555   1555  2.12  
LINK        MG    MG D1476                 OD1 ASP D 203     1555   1555  1.97  
LINK        MG    MG D1476                 O3  CAP D1477     1555   1555  2.16  
LINK         C   TYR E 103                 N   HYP E 104     1555   1555  1.34  
LINK         C   HYP E 104                 N   ILE E 105     1555   1555  1.33  
LINK         C   GLY E 150                 N   HYP E 151     1555   1555  1.34  
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  1.34  
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 E1476                 O3  CAP E1477     1555   1555  2.21  
LINK        MG    MG E1476                 OD1 ASP E 203     1555   1555  1.95  
LINK        MG    MG E1476                 OQ1 KCX E 201     1555   1555  2.07  
LINK        MG    MG E1476                 O2  CAP E1477     1555   1555  2.20  
LINK        MG    MG E1476                 O7  CAP E1477     1555   1555  2.11  
LINK        MG    MG E1476                 OE1 GLU E 204     1555   1555  2.01  
LINK         C   TYR F 103                 N   HYP F 104     1555   1555  1.34  
LINK         C   HYP F 104                 N   ILE F 105     1555   1555  1.33  
LINK         C   GLY F 150                 N   HYP F 151     1555   1555  1.35  
LINK         C   HYP F 151                 N   PRO F 152     1555   1555  1.34  
LINK         C   THR F 200                 N   KCX F 201     1555   1555  1.33  
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  1.33  
LINK        MG    MG F1476                 OQ1 KCX F 201     1555   1555  2.04  
LINK        MG    MG F1476                 O3  CAP F1477     1555   1555  2.13  
LINK        MG    MG F1476                 O7  CAP F1477     1555   1555  2.10  
LINK        MG    MG F1476                 O2  CAP F1477     1555   1555  2.21  
LINK        MG    MG F1476                 OE1 GLU F 204     1555   1555  2.07  
LINK        MG    MG F1476                 OD1 ASP F 203     1555   1555  1.96  
LINK         C   TYR G 103                 N   HYP G 104     1555   1555  1.34  
LINK         C   HYP G 104                 N   ILE G 105     1555   1555  1.33  
LINK         C   GLY G 150                 N   HYP G 151     1555   1555  1.33  
LINK         C   HYP G 151                 N   PRO G 152     1555   1555  1.35  
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  1.34  
LINK         C   SMC G 256                 N   ALA G 257     1555   1555  1.34  
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 G1476                 O2  CAP G1477     1555   1555  2.24  
LINK        MG    MG G1476                 O3  CAP G1477     1555   1555  2.14  
LINK        MG    MG G1476                 O7  CAP G1477     1555   1555  2.09  
LINK        MG    MG G1476                 OQ1 KCX G 201     1555   1555  2.04  
LINK        MG    MG G1476                 OD1 ASP G 203     1555   1555  1.98  
LINK        MG    MG G1476                 OE1 GLU G 204     1555   1555  2.00  
LINK         C   TYR H 103                 N   HYP H 104     1555   1555  1.34  
LINK         C   HYP H 104                 N   ILE H 105     1555   1555  1.32  
LINK         C   GLY H 150                 N   HYP H 151     1555   1555  1.34  
LINK         C   HYP H 151                 N   PRO H 152     1555   1555  1.34  
LINK         C   THR H 200                 N   KCX H 201     1555   1555  1.32  
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 H1476                 O2  CAP H1477     1555   1555  2.22  
LINK        MG    MG H1476                 OQ1 KCX H 201     1555   1555  2.03  
LINK        MG    MG H1476                 O3  CAP H1477     1555   1555  2.12  
LINK        MG    MG H1476                 OE1 GLU H 204     1555   1555  2.03  
LINK        MG    MG H1476                 OD1 ASP H 203     1555   1555  1.99  
LINK        MG    MG H1476                 O7  CAP H1477     1555   1555  2.14  
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  
SITE     1 AC1  5 LYS A 177  KCX A 201  ASP A 203  GLU A 204                    
SITE     2 AC1  5 CAP A1477                                                     
SITE     1 AC2 28 THR A 173  LYS A 175  LYS A 177  KCX A 201                    
SITE     2 AC2 28 ASP A 203  GLU A 204  HIS A 294  ARG A 295                    
SITE     3 AC2 28 HIS A 327  LYS A 334  LEU A 335  SER A 379                    
SITE     4 AC2 28 GLY A 380  GLY A 381  GLY A 403  GLY A 404                    
SITE     5 AC2 28 HOH A1139  HOH A1315  HOH A1316  HOH A1317                    
SITE     6 AC2 28 HOH A1318  HOH A1319   MG A1476  GLU B  60                    
SITE     7 AC2 28 THR B  65  TRP B  66  ASN B 123  HOH B1109                    
SITE     1 AC3  5 LYS B 177  KCX B 201  ASP B 203  GLU B 204                    
SITE     2 AC3  5 CAP B1477                                                     
SITE     1 AC4 29 GLU A  60  THR A  65  TRP A  66  ASN A 123                    
SITE     2 AC4 29 HOH A1049  HOH A1103  THR B 173  LYS B 175                    
SITE     3 AC4 29 LYS B 177  KCX B 201  ASP B 203  GLU B 204                    
SITE     4 AC4 29 HIS B 294  ARG B 295  HIS B 327  LYS B 334                    
SITE     5 AC4 29 LEU B 335  SER B 379  GLY B 380  GLY B 381                    
SITE     6 AC4 29 GLY B 403  GLY B 404  HOH B1264  HOH B1326                    
SITE     7 AC4 29 HOH B1327  HOH B1328  HOH B1329  HOH B1330                    
SITE     8 AC4 29  MG B1476                                                     
SITE     1 AC5  5 LYS C 177  KCX C 201  ASP C 203  GLU C 204                    
SITE     2 AC5  5 CAP C1477                                                     
SITE     1 AC6 29 THR C 173  LYS C 175  LYS C 177  KCX C 201                    
SITE     2 AC6 29 ASP C 203  GLU C 204  HIS C 294  ARG C 295                    
SITE     3 AC6 29 HIS C 327  LYS C 334  LEU C 335  SER C 379                    
SITE     4 AC6 29 GLY C 380  GLY C 381  GLY C 403  GLY C 404                    
SITE     5 AC6 29 HOH C1136  HOH C1308  HOH C1309  HOH C1310                    
SITE     6 AC6 29 HOH C1311  HOH C1312   MG C1476  GLU D  60                    
SITE     7 AC6 29 THR D  65  TRP D  66  ASN D 123  HOH D1038                    
SITE     8 AC6 29 HOH D1098                                                     
SITE     1 AC7  4 KCX D 201  ASP D 203  GLU D 204  CAP D1477                    
SITE     1 AC8 30 GLU C  60  THR C  65  TRP C  66  ASN C 123                    
SITE     2 AC8 30 HOH C1044  HOH C1047  HOH C1105  THR D 173                    
SITE     3 AC8 30 LYS D 175  LYS D 177  KCX D 201  ASP D 203                    
SITE     4 AC8 30 GLU D 204  HIS D 294  ARG D 295  HIS D 327                    
SITE     5 AC8 30 LYS D 334  LEU D 335  SER D 379  GLY D 380                    
SITE     6 AC8 30 GLY D 381  GLY D 403  GLY D 404  HOH D1319                    
SITE     7 AC8 30 HOH D1320  HOH D1321  HOH D1322  HOH D1323                    
SITE     8 AC8 30 HOH D1324   MG D1476                                          
SITE     1 AC9  5 LYS E 177  KCX E 201  ASP E 203  GLU E 204                    
SITE     2 AC9  5 CAP E1477                                                     
SITE     1 BC1 29 THR E 173  LYS E 175  LYS E 177  KCX E 201                    
SITE     2 BC1 29 ASP E 203  GLU E 204  HIS E 294  ARG E 295                    
SITE     3 BC1 29 HIS E 327  LYS E 334  LEU E 335  SER E 379                    
SITE     4 BC1 29 GLY E 380  GLY E 381  GLY E 403  GLY E 404                    
SITE     5 BC1 29 HOH E1270  HOH E1336  HOH E1337  HOH E1338                    
SITE     6 BC1 29 HOH E1339  HOH E1340   MG E1476  GLU F  60                    
SITE     7 BC1 29 THR F  65  TRP F  66  ASN F 123  HOH F1048                    
SITE     8 BC1 29 HOH F1107                                                     
SITE     1 BC2  5 LYS F 177  KCX F 201  ASP F 203  GLU F 204                    
SITE     2 BC2  5 CAP F1477                                                     
SITE     1 BC3 28 GLU E  60  THR E  65  TRP E  66  ASN E 123                    
SITE     2 BC3 28 HOH E1107  THR F 173  LYS F 175  LYS F 177                    
SITE     3 BC3 28 KCX F 201  ASP F 203  GLU F 204  HIS F 294                    
SITE     4 BC3 28 ARG F 295  HIS F 327  LYS F 334  LEU F 335                    
SITE     5 BC3 28 SER F 379  GLY F 380  GLY F 381  GLY F 403                    
SITE     6 BC3 28 GLY F 404  HOH F1264  HOH F1317  HOH F1318                    
SITE     7 BC3 28 HOH F1319  HOH F1320  HOH F1321   MG F1476                    
SITE     1 BC4  4 KCX G 201  ASP G 203  GLU G 204  CAP G1477                    
SITE     1 BC5 28 THR G 173  LYS G 175  LYS G 177  KCX G 201                    
SITE     2 BC5 28 ASP G 203  GLU G 204  HIS G 294  ARG G 295                    
SITE     3 BC5 28 HIS G 327  LYS G 334  LEU G 335  SER G 379                    
SITE     4 BC5 28 GLY G 380  GLY G 381  GLY G 403  GLY G 404                    
SITE     5 BC5 28 HOH G1136  HOH G1312  HOH G1313  HOH G1314                    
SITE     6 BC5 28 HOH G1315  HOH G1316   MG G1476  GLU H  60                    
SITE     7 BC5 28 THR H  65  TRP H  66  ASN H 123  HOH H1110                    
SITE     1 BC6  5 LYS H 177  KCX H 201  ASP H 203  GLU H 204                    
SITE     2 BC6  5 CAP H1477                                                     
SITE     1 BC7 30 GLU G  60  THR G  65  TRP G  66  ASN G 123                    
SITE     2 BC7 30 HOH G1043  HOH G1045  HOH G1102  THR H 173                    
SITE     3 BC7 30 LYS H 175  LYS H 177  KCX H 201  ASP H 203                    
SITE     4 BC7 30 GLU H 204  HIS H 294  ARG H 295  HIS H 327                    
SITE     5 BC7 30 LYS H 334  LEU H 335  SER H 379  GLY H 380                    
SITE     6 BC7 30 GLY H 381  GLY H 403  GLY H 404  HOH H1150                    
SITE     7 BC7 30 HOH H1320  HOH H1321  HOH H1322  HOH H1323                    
SITE     8 BC7 30 HOH H1324   MG H1476                                          
SITE     1 BC8  7 TYR A  24  THR A  68  VAL A  69  ASP A  72                    
SITE     2 BC8  7 HOH A1059  HOH A1320  HOH A1321                               
SITE     1 BC9  9 GLY A  16  VAL A  17  LYS A  18  THR A  65                    
SITE     2 BC9  9 TRP A  66  THR A  67  THR A  68  HOH A1023                    
SITE     3 BC9  9 HOH A1321                                                     
SITE     1 CC1  3 GLU A  52  EDO A1484  HOH B1333                               
SITE     1 CC2  6 LYS A 466  PHE A 467  GLU A 468  PHE A 469                    
SITE     2 CC2  6 HOH A1322  HOH A1323                                          
SITE     1 CC3  7 ARG A 295  HIS A 298  PHE A 311  SER A 328                    
SITE     2 CC3  7 GLU A 336  PHE A 345  HOH A1324                               
SITE     1 CC4  8 TYR C  24  GLY C  64  THR C  68  VAL C  69                    
SITE     2 CC4  8 ASP C  72  HOH C1049  HOH C1313  HOH C1314                    
SITE     1 CC5  8 VAL C  17  LYS C  18  THR C  65  TRP C  66                    
SITE     2 CC5  8 THR C  67  THR C  68  HOH C1314  HOH C1315                    
SITE     1 CC6  2 GLU C  52  HOH D1330                                          
SITE     1 CC7  6 LYS C 466  PHE C 467  GLU C 468  PHE C 469                    
SITE     2 CC7  6 HOH C1316  HOH D1328                                          
SITE     1 CC8  5 ARG C 295  PHE C 345  ASP C 473  HOH C1317                    
SITE     2 CC8  5 HOH C1318                                                     
SITE     1 CC9 10 TYR E  24  GLY E  64  THR E  68  VAL E  69                    
SITE     2 CC9 10 ASP E  72  LEU E  77  HOH E1057  HOH E1341                    
SITE     3 CC9 10 HOH E1342  EDO E1479                                          
SITE     1 DC1  8 LYS E  18  THR E  65  TRP E  66  THR E  67                    
SITE     2 DC1  8 THR E  68  HOH E1021  HOH E1342  EDO E1478                    
SITE     1 DC2  3 GLU E  52  HOH E1010  HOH F1328                               
SITE     1 DC3  6 LYS E 466  PHE E 467  GLU E 468  PHE E 469                    
SITE     2 DC3  6 HOH E1343  HOH E1344                                          
SITE     1 DC4  9 TYR G  24  GLY G  64  THR G  68  VAL G  69                    
SITE     2 DC4  9 ASP G  72  HOH G1317  HOH G1318  HOH G1319                    
SITE     3 DC4  9 EDO G1479                                                     
SITE     1 DC5 10 GLY G  16  VAL G  17  LYS G  18  THR G  65                    
SITE     2 DC5 10 TRP G  66  THR G  67  THR G  68  HOH G1012                    
SITE     3 DC5 10 HOH G1319  EDO G1478                                          
SITE     1 DC6  2 GLU G  52  HOH H1330                                          
SITE     1 DC7  6 LYS G 466  PHE G 467  GLU G 468  PHE G 469                    
SITE     2 DC7  6 HOH G1320  HOH G1321                                          
SITE     1 DC8  7 ARG G 295  HIS G 298  PHE G 345  ASP G 473                    
SITE     2 DC8  7 HOH G1322  HOH G1323  HOH G1324                               
SITE     1 DC9  6 TYR C 226  LYS C 227  HOH C1166  LYS I  49                    
SITE     2 DC9  6 GLU I  55  HOH I1052                                          
SITE     1 EC1  6 TYR E 226  HOH E1176  LYS K  49  GLU K  55                    
SITE     2 EC1  6 HOH K1056  HOH K1057                                          
SITE     1 EC2  6 GLY K  37  TRP K  38  ILE K  39  PHE K  81                    
SITE     2 EC2  6 GLY K  82  CYS K  83                                          
SITE     1 EC3  5 TYR G 226  LYS M  49  GLU M  55  HOH M1054                    
SITE     2 EC3  5 HOH M1112                                                     
SITE     1 EC4  5 GLY M  37  TRP M  38  ILE M  39  GLY M  82                    
SITE     2 EC4  5 CYS M  83                                                     
SITE     1 EC5  5 TYR A 226  LYS O  49  GLU O  55  HOH O1061                    
SITE     2 EC5  5 HOH O1113                                                     
SITE     1 EC6  6 GLY O  37  TRP O  38  ILE O  39  PHE O  81                    
SITE     2 EC6  6 GLY O  82  CYS O  83                                          
SITE     1 EC7  4 LEU E 270  LEU F 270  HOH F1322  HOH F1323                    
SITE     1 EC8  4 LEU A 270  HOH A1325  HOH A1326  LEU B 270                    
SITE     1 EC9  4 LEU G 270  LEU H 270  HOH H1325  HOH H1326                    
SITE     1 FC1  9 TYR B  24  GLY B  64  THR B  68  VAL B  69                    
SITE     2 FC1  9 ASP B  72  HOH B1051  HOH B1057  HOH B1331                    
SITE     3 FC1  9 EDO B1479                                                     
SITE     1 FC2 10 GLY B  16  VAL B  17  LYS B  18  THR B  65                    
SITE     2 FC2 10 TRP B  66  THR B  67  THR B  68  HOH B1331                    
SITE     3 FC2 10 HOH B1332  EDO B1478                                          
SITE     1 FC3  2 HOH A1322  GLU B  52                                          
SITE     1 FC4  5 LYS B 466  PHE B 467  GLU B 468  PHE B 469                    
SITE     2 FC4  5 HOH B1333                                                     
SITE     1 FC5  5 ARG B 295  ASP B 302  GLU B 336  PHE B 345                    
SITE     2 FC5  5 HOH B1334                                                     
SITE     1 FC6  9 TYR H  24  GLY H  64  THR H  68  VAL H  69                    
SITE     2 FC6  9 ASP H  72  HOH H1051  HOH H1056  HOH H1327                    
SITE     3 FC6  9 EDO H1480                                                     
SITE     1 FC7 10 GLY H  16  VAL H  17  LYS H  18  THR H  65                    
SITE     2 FC7 10 TRP H  66  THR H  67  THR H  68  HOH H1327                    
SITE     3 FC7 10 HOH H1328  EDO H1479                                          
SITE     1 FC8  2 HOH G1321  GLU H  52                                          
SITE     1 FC9  5 LYS H 466  PHE H 467  GLU H 468  PHE H 469                    
SITE     2 FC9  5 HOH H1330                                                     
SITE     1 GC1  9 TYR F  24  GLY F  64  THR F  68  VAL F  69                    
SITE     2 GC1  9 ASP F  72  HOH F1058  HOH F1324  HOH F1326                    
SITE     3 GC1  9 EDO F1480                                                     
SITE     1 GC2  9 GLY F  16  LYS F  18  THR F  65  TRP F  66                    
SITE     2 GC2  9 THR F  67  THR F  68  HOH F1325  HOH F1326                    
SITE     3 GC2  9 EDO F1479                                                     
SITE     1 GC3  2 HOH E1343  GLU F  52                                          
SITE     1 GC4  5 LYS F 466  PHE F 467  GLU F 468  PHE F 469                    
SITE     2 GC4  5 HOH F1328                                                     
SITE     1 GC5  6 ARG F 295  HIS F 298  GLU F 336  PHE F 345                    
SITE     2 GC5  6 HOH F1329  HOH F1330                                          
SITE     1 GC6  9 TYR D  24  GLY D  64  THR D  68  VAL D  69                    
SITE     2 GC6  9 ASP D  72  HOH D1325  HOH D1326  HOH D1327                    
SITE     3 GC6  9 EDO D1479                                                     
SITE     1 GC7  9 GLY D  16  LYS D  18  THR D  65  TRP D  66                    
SITE     2 GC7  9 THR D  67  THR D  68  HOH D1016  HOH D1327                    
SITE     3 GC7  9 EDO D1478                                                     
SITE     1 GC8  3 GLU D  52  HOH D1006  HOH D1328                               
SITE     1 GC9  6 LYS D 466  PHE D 467  GLU D 468  PHE D 469                    
SITE     2 GC9  6 HOH D1329  HOH D1330                                          
SITE     1 HC1  6 TYR H 226  HOH H1180  LYS J  49  GLU J  55                    
SITE     2 HC1  6 HOH J1057  HOH J1059                                          
SITE     1 HC2  7 GLY J  37  TRP J  38  ILE J  39  PHE J  81                    
SITE     2 HC2  7 GLY J  82  CYS J  83  HOH J1106                               
SITE     1 HC3  5 TYR F 226  HOH F1173  LYS P  49  GLU P  55                    
SITE     2 HC3  5 HOH P1058                                                     
SITE     1 HC4  7 GLY P  37  TRP P  38  ILE P  39  PHE P  81                    
SITE     2 HC4  7 GLY P  82  CYS P  83  HOH P1100                               
SITE     1 HC5  7 TYR D 226  LYS D 227  LYS N  49  GLU N  55                    
SITE     2 HC5  7 HOH N1058  HOH N1059  HOH N1110                               
SITE     1 HC6  7 GLY N  37  TRP N  38  ILE N  39  PHE N  81                    
SITE     2 HC6  7 GLY N  82  CYS N  83  HOH N1111                               
SITE     1 HC7  4 LEU C 270  HOH C1319  HOH C1320  LEU D 270                    
SITE     1 HC8  4 GLY A  47  PRO A  49  HOH A1327  EDO A1480                    
SITE     1 HC9  4 GLY I  37  TRP I  38  ILE I  39  GLY I  82                    
SITE     1 IC1  6 ARG D 295  HIS D 298  PHE D 345  ASP D 473                    
SITE     2 IC1  6 HOH D1331  HOH D1332                                          
SITE     1 IC2  6 TYR B 226  HOH B1181  LYS L  49  GLU L  55                    
SITE     2 IC2  6 HOH L1059  HOH L1060                                          
SITE     1 IC3  7 GLY L  37  TRP L  38  ILE L  39  PHE L  81                    
SITE     2 IC3  7 GLY L  82  CYS L  83  HOH L1111                               
CRYST1  129.906  196.629  201.950  90.00  90.00  90.00 P 21 21 21   32          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007698  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005086  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004952        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2  0.105300  0.704300 -0.702100       51.25000    1                    
MTRIX2   2  0.703600 -0.551700 -0.447900      150.00000    1                    
MTRIX3   2 -0.702800 -0.446800 -0.553600      231.00000    1                    
MTRIX1   3  0.430900 -0.058090  0.900500      -43.37000    1                    
MTRIX2   3 -0.802900  0.430800  0.412000       66.21000    1                    
MTRIX3   3 -0.411900 -0.900600  0.139000      193.10000    1                    
MTRIX1   4 -0.628700 -0.067550 -0.774700      178.00000    1                    
MTRIX2   4 -0.068450 -0.987500  0.141700      184.90000    1                    
MTRIX3   4 -0.774600  0.142100  0.616200       69.14000    1                    
MTRIX1   5 -0.139400 -0.860600  0.489800      107.80000    1                    
MTRIX2   5 -0.860600 -0.139400 -0.489800      209.20000    1                    
MTRIX3   5  0.489800 -0.489800 -0.721300      178.10000    1                    
MTRIX1   6 -0.964600  0.156200  0.212700       84.80000    1                    
MTRIX2   6  0.156400 -0.310700  0.937500       31.03000    1                    
MTRIX3   6  0.212500  0.937600  0.275300      -36.92000    1                    
MTRIX1   7  0.430300 -0.803400 -0.411700      151.30000    1                    
MTRIX2   7 -0.055740  0.431500 -0.900400      142.50000    1                    
MTRIX3   7  0.901000  0.410400  0.140900      -15.06000    1                    
MTRIX1   8 -0.232200  0.929300  0.287300      -42.22000    1                    
MTRIX2   8  0.930300  0.125900  0.344600       -3.61500    1                    
MTRIX3   8  0.284100  0.347300 -0.893700      125.00000    1                    
MTRIX1   9  0.103700  0.705100 -0.701500       51.09000    1                    
MTRIX2   9  0.704600 -0.549900 -0.448500      149.90000    1                    
MTRIX3   9 -0.701900 -0.447800 -0.553900      231.10000    1                    
MTRIX1  10  0.429500 -0.059760  0.901100      -43.19000    1                    
MTRIX2  10 -0.803800  0.429500  0.411600       66.39000    1                    
MTRIX3  10 -0.411600 -0.901100  0.136500      193.40000    1                    
MTRIX1  11 -0.629100 -0.067810 -0.774400      178.00000    1                    
MTRIX2  11 -0.068930 -0.987400  0.142500      184.70000    1                    
MTRIX3  11 -0.774300  0.143000  0.616500       69.03000    1                    
MTRIX1  12 -0.139100 -0.860300  0.490500      107.70000    1                    
MTRIX2  12 -0.861000 -0.139600 -0.489100      209.10000    1                    
MTRIX3  12  0.489300 -0.490300 -0.721200      178.20000    1                    
MTRIX1  13 -0.964500  0.157000  0.212300       84.77000    1                    
MTRIX2  13  0.156000 -0.310000  0.937800       30.94000    1                    
MTRIX3  13  0.213000  0.937700  0.274500      -36.88000    1                    
MTRIX1  14  0.430500 -0.802400 -0.413300      151.40000    1                    
MTRIX2  14 -0.054840  0.433800 -0.899300      142.20000    1                    
MTRIX3  14  0.900900  0.409800  0.142800      -15.17000    1                    
MTRIX1  15 -0.230400  0.929300  0.288500      -42.37000    1                    
MTRIX2  15  0.930100  0.123300  0.345900       -3.38100    1                    
MTRIX3  15  0.285900  0.348100 -0.892800      124.70000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system