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Database: PDB
Entry: 2V68
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Original site: 2V68 
HEADER    OXIDOREDUCTASE                          13-JUL-07   2V68              
TITLE     CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII RUBISCO WITH           
TITLE    2 LARGE-SUBUNIT MUTATIONS V331A, T342I                                 
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: RUBISCO LARGE SUBUNIT, RIBULOSE-1,5-BISPHOSPHATE            
COMPND   5  CARBOXYLASE LARGE CHAIN;                                            
COMPND   6 EC: 4.1.1.39;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1;           
COMPND  11 CHAIN: I, J, K, L, M, N, O, P;                                       
COMPND  12 FRAGMENT: RESIDUES 46-185;                                           
COMPND  13 SYNONYM: RUBISCO SMALL SUBUNIT 1,RIBULOSE-1,5-BISPHOSPHATE           
COMPND  14  CARBOXYLASE SMALL CHAIN;                                            
COMPND  15 EC: 4.1.1.39;                                                        
COMPND  16 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   5   24-FEB-09 2V68    1       VERSN                                    
REVDAT   4   23-OCT-07 2V68    1       REMARK                                   
REVDAT   3   02-OCT-07 2V68    1       JRNL   REMARK                            
REVDAT   2   28-AUG-07 2V68    1       AUTHOR                                   
REVDAT   1   07-AUG-07 2V68    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.    2.3  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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 191997                         
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) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 10153                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 14110                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.34                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2000                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 726                          
REMARK   3   BIN FREE R VALUE                    : 0.2620                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 37909                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 780                                     
REMARK   3   SOLVENT ATOMS            : 2276                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.46                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.27000                                              
REMARK   3    B22 (A**2) : -0.23000                                             
REMARK   3    B33 (A**2) : -0.06000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.03000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.486         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.220         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.143         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.728         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 39580 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 53581 ; 1.230 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4834 ; 6.196 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1866 ;31.745 ;23.183       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  6359 ;14.625 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   320 ;16.232 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  5667 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 30468 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A): 20011 ; 0.190 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 26819 ; 0.302 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  3037 ; 0.137 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    10 ; 0.055 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    99 ; 0.242 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.177 ; 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): 24753 ; 0.562 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 38663 ; 0.901 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 17043 ; 1.509 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 14918 ; 2.424 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 16                                
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A                               
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     13       A     438      1                      
REMARK   3           2     A    440       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   3642 ;  0.00 ;  0.05           
REMARK   3   TIGHT THERMAL      1    A (A**2):   3642 ;  0.00 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B     13       B     438      1                      
REMARK   3           1     A     13       A     438      1                      
REMARK   3           2     B    440       B     477      1                      
REMARK   3           2     A    440       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    B    (A):   3637 ;  0.03 ;  0.05           
REMARK   3   TIGHT THERMAL      2    B (A**2):   3637 ;  0.11 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : C A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C     13       C     437      1                      
REMARK   3           1     A     13       A     437      1                      
REMARK   3           2     C    442       C     477      1                      
REMARK   3           2     A    442       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    C    (A):   3624 ;  0.03 ;  0.05           
REMARK   3   TIGHT THERMAL      3    C (A**2):   3624 ;  0.12 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : D A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     D     13       D     438      1                      
REMARK   3           1     A     13       A     438      1                      
REMARK   3           2     D    440       D     477      1                      
REMARK   3           2     A    440       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   4    D    (A):   3642 ;  0.03 ;  0.05           
REMARK   3   TIGHT THERMAL      4    D (A**2):   3642 ;  0.11 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 5                                  
REMARK   3     CHAIN NAMES                    : E A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     E     13       E     438      1                      
REMARK   3           1     A     13       A     438      1                      
REMARK   3           2     E    440       E     477      1                      
REMARK   3           2     A    440       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   5    E    (A):   3641 ;  0.03 ;  0.05           
REMARK   3   TIGHT THERMAL      5    E (A**2):   3641 ;  0.12 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 6                                  
REMARK   3     CHAIN NAMES                    : F A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     F     13       F     438      1                      
REMARK   3           1     A     13       A     438      1                      
REMARK   3           2     F    440       F     477      1                      
REMARK   3           2     A    440       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   6    F    (A):   3638 ;  0.03 ;  0.05           
REMARK   3   TIGHT THERMAL      6    F (A**2):   3638 ;  0.12 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 7                                  
REMARK   3     CHAIN NAMES                    : G A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     G     13       G     438      1                      
REMARK   3           1     A     13       A     438      1                      
REMARK   3           2     G    440       G     477      1                      
REMARK   3           2     A    440       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   7    G    (A):   3640 ;  0.03 ;  0.05           
REMARK   3   TIGHT THERMAL      7    G (A**2):   3640 ;  0.12 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 8                                  
REMARK   3     CHAIN NAMES                    : H A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     H     13       H     438      1                      
REMARK   3           1     A     13       A     438      1                      
REMARK   3           2     H    440       H     477      1                      
REMARK   3           2     A    440       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   8    H    (A):   3642 ;  0.03 ;  0.05           
REMARK   3   TIGHT THERMAL      8    H (A**2):   3642 ;  0.12 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 9                                  
REMARK   3     CHAIN NAMES                    : I                               
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     I      1       I      83      1                      
REMARK   3           2     I     85       I     129      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   9    I    (A):   1039 ;  0.00 ;  0.05           
REMARK   3   TIGHT THERMAL      9    I (A**2):   1039 ;  0.00 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 10                                 
REMARK   3     CHAIN NAMES                    : J I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     J      1       J      83      1                      
REMARK   3           1     I      1       I      83      1                      
REMARK   3           2     J     85       J     129      1                      
REMARK   3           2     I     85       I     129      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  10    J    (A):   1039 ;  0.03 ;  0.05           
REMARK   3   TIGHT THERMAL     10    J (A**2):   1039 ;  0.11 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 11                                 
REMARK   3     CHAIN NAMES                    : K I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     K      1       K      83      1                      
REMARK   3           1     I      1       I      83      1                      
REMARK   3           2     K     85       K     129      1                      
REMARK   3           2     I     85       I     129      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  11    K    (A):   1037 ;  0.03 ;  0.05           
REMARK   3   TIGHT THERMAL     11    K (A**2):   1037 ;  0.10 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 12                                 
REMARK   3     CHAIN NAMES                    : L I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     L      1       L      83      1                      
REMARK   3           1     I      1       I      83      1                      
REMARK   3           2     L     85       L     129      1                      
REMARK   3           2     I     85       I     129      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  12    L    (A):   1039 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL     12    L (A**2):   1039 ;  0.11 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 13                                 
REMARK   3     CHAIN NAMES                    : M I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     M      1       M      83      1                      
REMARK   3           1     I      1       I      83      1                      
REMARK   3           2     M     85       M     129      1                      
REMARK   3           2     I     85       I     129      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  13    M    (A):   1039 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL     13    M (A**2):   1039 ;  0.13 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 14                                 
REMARK   3     CHAIN NAMES                    : N I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     N      1       N      83      1                      
REMARK   3           1     I      1       I      83      1                      
REMARK   3           2     N     85       N     129      1                      
REMARK   3           2     I     85       I     129      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  14    N    (A):   1037 ;  0.03 ;  0.05           
REMARK   3   TIGHT THERMAL     14    N (A**2):   1037 ;  0.10 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 15                                 
REMARK   3     CHAIN NAMES                    : O I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     O      1       O      83      1                      
REMARK   3           1     I      1       I      83      1                      
REMARK   3           2     O     85       O     129      1                      
REMARK   3           2     I     85       I     129      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  15    O    (A):   1037 ;  0.03 ;  0.05           
REMARK   3   TIGHT THERMAL     15    O (A**2):   1037 ;  0.11 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 16                                 
REMARK   3     CHAIN NAMES                    : P I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     P      1       P      83      1                      
REMARK   3           1     I      1       I      83      1                      
REMARK   3           2     P     85       P     129      1                      
REMARK   3           2     I     85       I     129      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  16    P    (A):   1039 ;  0.03 ;  0.05           
REMARK   3   TIGHT THERMAL     16    P (A**2):   1039 ;  0.11 ;  0.50           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2V68 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-JUL-07.                  
REMARK 100 THE PDBE ID CODE IS EBI-33193.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-SEP-03                          
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               : MAX II                             
REMARK 200  BEAMLINE                       : I711                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0890                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 1285694                            
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.30                               
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     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 20.3                               
REMARK 200  R MERGE                    (I) : 0.16                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.80                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.29                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.10                               
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  (%): 39.01                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       89.11800            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXADECAMERIC                     
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC              
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 125120 ANGSTROM**2                        
REMARK 350 SURFACE AREA OF THE COMPLEX: 150520 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -731.0 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, THR 342 TO ILE                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, THR 342 TO ILE                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, THR 342 TO ILE                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, THR 342 TO ILE                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN E, THR 342 TO ILE                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, THR 342 TO ILE                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN G, THR 342 TO ILE                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN H, THR 342 TO ILE                        
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     ALA A     9                                                      
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     GLY D    10                                                      
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     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     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     MET H     1                                                      
REMARK 465     VAL H     2                                                      
REMARK 465     PRO H     3                                                      
REMARK 465     GLN H     4                                                      
REMARK 465     THR H     5                                                      
REMARK 465     GLU H     6                                                      
REMARK 465     THR H     7                                                      
REMARK 465     LYS H     8                                                      
REMARK 465     ALA H     9                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH C  2003  -  O    HOH D  2184              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  62      -80.61   -139.11                                   
REMARK 500    THR A  65     -168.46   -128.54                                   
REMARK 500    CYS A 172      125.50   -175.24                                   
REMARK 500    ASN A 207      -95.67   -121.88                                   
REMARK 500    MET A 212      108.85   -163.73                                   
REMARK 500    TYR A 239       98.71    -68.33                                   
REMARK 500    ALA A 296      131.12    -39.41                                   
REMARK 500    MET A 297      -11.68     87.24                                   
REMARK 500    ALA A 331      -49.34     71.51                                   
REMARK 500    ASP A 357       88.73   -157.38                                   
REMARK 500    SER B  62      -76.95   -138.85                                   
REMARK 500    THR B  65     -168.26   -127.40                                   
REMARK 500    CYS B 172      121.81   -171.87                                   
REMARK 500    ASN B 207      -94.18   -118.75                                   
REMARK 500    MET B 212      110.24   -163.98                                   
REMARK 500    MET B 297      -11.17     90.94                                   
REMARK 500    ALA B 331      -49.19     71.12                                   
REMARK 500    ASP B 357       87.91   -157.01                                   
REMARK 500    THR B 406      -55.02   -121.14                                   
REMARK 500    SER C  62      -76.66   -140.06                                   
REMARK 500    THR C  65     -169.00   -126.20                                   
REMARK 500    CYS C 172      123.79   -173.45                                   
REMARK 500    ASN C 207      -94.05   -124.42                                   
REMARK 500    MET C 212      110.07   -165.37                                   
REMARK 500    TYR C 239       97.97    -67.52                                   
REMARK 500    ALA C 296      129.84    -38.38                                   
REMARK 500    MET C 297      -12.73     87.67                                   
REMARK 500    ALA C 331      -48.80     69.94                                   
REMARK 500    ASP C 357       87.77   -160.85                                   
REMARK 500    THR C 406      -54.36   -120.64                                   
REMARK 500    SER D  62      -78.72   -140.82                                   
REMARK 500    CYS D 172      124.51   -175.58                                   
REMARK 500    ASN D 207      -93.73   -121.97                                   
REMARK 500    MET D 212      110.32   -163.32                                   
REMARK 500    TYR D 239       97.57    -68.25                                   
REMARK 500    ALA D 296      132.01    -36.61                                   
REMARK 500    MET D 297      -13.57     85.28                                   
REMARK 500    ALA D 331      -50.45     74.39                                   
REMARK 500    SER E  62      -79.05   -140.71                                   
REMARK 500    CYS E 172      124.67   -173.34                                   
REMARK 500    ASN E 207      -95.30   -126.56                                   
REMARK 500    TYR E 239       99.85    -67.86                                   
REMARK 500    ALA E 296      128.47    -30.38                                   
REMARK 500    MET E 297      -16.05     87.27                                   
REMARK 500    ALA E 331      -49.24     69.71                                   
REMARK 500    SER F  62      -77.40   -142.68                                   
REMARK 500    THR F  65     -166.22   -126.92                                   
REMARK 500    ASP F  86      140.58   -170.08                                   
REMARK 500    CYS F 172      123.98    178.86                                   
REMARK 500    ASN F 207      -96.51   -122.39                                   
REMARK 500    MET F 212      107.96   -166.39                                   
REMARK 500    ALA F 296      129.96    -38.01                                   
REMARK 500    MET F 297       -7.50     86.40                                   
REMARK 500    ALA F 331      -46.82     66.77                                   
REMARK 500    ASP F 357       89.76   -156.68                                   
REMARK 500    THR F 406      -54.92   -120.42                                   
REMARK 500    SER G  62      -79.73   -134.90                                   
REMARK 500    THR G  65     -169.00   -126.13                                   
REMARK 500    CYS G 172      123.55   -176.26                                   
REMARK 500    ASN G 207      -96.84   -123.53                                   
REMARK 500    MET G 212      106.42   -167.19                                   
REMARK 500    TYR G 239       98.65    -68.74                                   
REMARK 500    MET G 297       -8.51     88.27                                   
REMARK 500    ALA G 331      -46.83     71.59                                   
REMARK 500    ASP G 357       86.03   -159.46                                   
REMARK 500    SER H  62      -81.12   -138.37                                   
REMARK 500    CYS H 172      129.34   -175.26                                   
REMARK 500    ASN H 207      -98.11   -122.11                                   
REMARK 500    MET H 212      109.71   -162.89                                   
REMARK 500    MET H 297       -7.99     88.22                                   
REMARK 500    ALA H 331      -46.26     72.19                                   
REMARK 500    ASP H 357       89.16   -157.39                                   
REMARK 500    PHE I  12       45.87   -140.90                                   
REMARK 500    GLU I  13     -139.87     58.40                                   
REMARK 500    PHE I  15        1.16     83.93                                   
REMARK 500    LYS I  77     -123.91     55.59                                   
REMARK 500    PHE J  12       47.55   -143.38                                   
REMARK 500    GLU J  13     -142.40     57.53                                   
REMARK 500    PHE J  15        2.42     86.11                                   
REMARK 500    LYS J  77     -128.49     52.53                                   
REMARK 500    PHE K  12       45.79   -142.15                                   
REMARK 500    GLU K  13     -141.15     60.89                                   
REMARK 500    PHE K  15       -6.68     86.38                                   
REMARK 500    LYS K  77     -123.69     57.00                                   
REMARK 500    PHE L  12       45.71   -141.42                                   
REMARK 500    GLU L  13     -140.84     57.46                                   
REMARK 500    PHE L  15       -0.10     83.31                                   
REMARK 500    LYS L  77     -125.38     58.36                                   
REMARK 500    GLU M  13     -143.67     59.83                                   
REMARK 500    PHE M  15        0.18     80.94                                   
REMARK 500    LYS M  77     -123.44     54.72                                   
REMARK 500    PHE N  12       48.37   -142.40                                   
REMARK 500    GLU N  13     -140.39     55.71                                   
REMARK 500    PHE N  15       -0.21     81.64                                   
REMARK 500    LYS N  77     -124.87     56.89                                   
REMARK 500    PHE O  12       47.70   -145.51                                   
REMARK 500    GLU O  13     -139.28     57.10                                   
REMARK 500    PHE O  15        4.22     81.78                                   
REMARK 500    LYS O  77     -120.32     53.24                                   
REMARK 500    PHE P  12       42.57   -143.12                                   
REMARK 500    GLU P  13     -143.55     62.66                                   
REMARK 500    PHE P  15        2.69     81.54                                   
REMARK 500    SER P  62       54.55    -91.15                                   
REMARK 500    LYS P  77     -127.99     55.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    PHE G 345        24.3      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE)                                            
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX A 201   OQ2                                                    
REMARK 620 2 ASP A 203   OD1  91.9                                              
REMARK 620 3 CAP A 477   O2   94.2 105.9                                        
REMARK 620 4 GLU A 204   OE1  90.5  93.1 160.2                                  
REMARK 620 5 CAP A 477   O3   86.3 177.9  75.3  85.8                            
REMARK 620 6 CAP A 477   O7  166.0  97.8  73.6  98.9  84.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 203   OD1                                                    
REMARK 620 2 GLU B 204   OE1  88.2                                              
REMARK 620 3 KCX B 201   OQ2  86.0  90.1                                        
REMARK 620 4 CAP B 477   O2  108.2 161.6  99.2                                  
REMARK 620 5 CAP B 477   O3  175.8  88.6  91.4  75.4                            
REMARK 620 6 CAP B 477   O7   97.3  97.8 171.5  72.4  85.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAP C 477   O3                                                     
REMARK 620 2 KCX C 201   OQ2  88.8                                              
REMARK 620 3 ASP C 203   OD1 170.3  98.4                                        
REMARK 620 4 CAP C 477   O2   77.6  96.4 107.7                                  
REMARK 620 5 CAP C 477   O7   77.0 163.5  96.7  72.6                            
REMARK 620 6 GLU C 204   OE1  82.5  93.1  90.6 157.8  93.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX D 201   OQ2                                                    
REMARK 620 2 ASP D 203   OD1  90.1                                              
REMARK 620 3 GLU D 204   OE1  91.1  91.7                                        
REMARK 620 4 CAP D 477   O2   96.2 104.9 161.9                                  
REMARK 620 5 CAP D 477   O3   88.1 176.7  85.7  78.0                            
REMARK 620 6 CAP D 477   O7  169.4  95.4  97.8  73.7  86.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAP E 477   O2                                                     
REMARK 620 2 CAP E 477   O3   76.4                                              
REMARK 620 3 CAP E 477   O7   74.4  89.2                                        
REMARK 620 4 ASP E 203   OD1 103.9 176.1  94.7                                  
REMARK 620 5 GLU E 204   OE1 164.2  90.6  97.0  89.7                            
REMARK 620 6 KCX E 201   OQ2  95.9  87.1 170.1  89.0  92.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 203   OD1                                                    
REMARK 620 2 CAP F 477   O2  103.1                                              
REMARK 620 3 CAP F 477   O7  104.1  75.5                                        
REMARK 620 4 KCX F 201   OQ2  89.9  90.4 162.0                                  
REMARK 620 5 GLU F 204   OE1  97.9 159.0 100.8  88.3                            
REMARK 620 6 CAP F 477   O3  170.6  75.0  84.5  80.9  84.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G 203   OD1                                                    
REMARK 620 2 CAP G 477   O2  103.9                                              
REMARK 620 3 CAP G 477   O7   90.7  69.1                                        
REMARK 620 4 KCX G 201   OQ2  97.6  97.7 165.9                                  
REMARK 620 5 GLU G 204   OE1  95.0 155.8  96.2  94.4                            
REMARK 620 6 CAP G 477   O3  173.2  74.5  82.6  89.2  84.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAP H 477   O3                                                     
REMARK 620 2 KCX H 201   OQ2  85.7                                              
REMARK 620 3 CAP H 477   O2   75.7  93.4                                        
REMARK 620 4 CAP H 477   O7   86.8 165.9  73.2                                  
REMARK 620 5 ASP H 203   OD1 178.5  93.8 105.6  94.0                            
REMARK 620 6 GLU H 204   OE1  86.9  92.5 161.2  99.0  91.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG C 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG D 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG E 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP F 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG F 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG G 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG H 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1484                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1483                 
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 B1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1484                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO I1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO I1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO L1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO N1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO N1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO P1141                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1UW9   RELATED DB: PDB                                   
REMARK 900  L290F-A222T CHLAMYDOMONAS RUBISCO MUTANT                            
REMARK 900 RELATED ID: 1UZH   RELATED DB: PDB                                   
REMARK 900  A CHIMERIC CHLAMYDOMONAS, SPINACH RUBISCO                           
REMARK 900  ENZYME                                                              
REMARK 900 RELATED ID: 1GK8   RELATED DB: PDB                                   
REMARK 900  RUBISCO FROM CHLAMYDOMONAS REINHARDTII                              
REMARK 900 RELATED ID: 1UWA   RELATED DB: PDB                                   
REMARK 900  L290F MUTANT RUBISCO FROM CHLAMYDOMONAS                             
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: 2V69   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII                      
REMARK 900  RUBISCO WITH A LARGE-SUBUNIT MUTATION D473E                         
REMARK 900 RELATED ID: 2V6A   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII                      
REMARK 900  RUBISCO WITH LARGE-SUBUNIT MUTATIONS V331A,                         
REMARK 900  G344S                                                               
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE UNIPROT DATABASE ENTRY FOR THIS SEQUENCE (P00877)                
REMARK 999 HAS A VARIANT (LEU46PRO) WHICH OCCURS IN STRAIN 21GR                 
REMARK 999 AND 2137.                                                            
REMARK 999 THE CHAINS I-P ARE ENCODED BY TWO GENES; RBCS 1, UNP                 
REMARK 999 P00873 AND RBCS 2, UNP P08475, THAT DIFFER IN                        
REMARK 999 POSITIONS 22, 47, 128, AND 132. JUDGING FROM THE                     
REMARK 999 ELECTRON DENSITY, THE TWO GENES ARE EXPRESSED AT                     
REMARK 999 APPROXIMATELY EQUAL LEVEL. SEQUENCE RBCS 1, UNP P00873               
REMARK 999 HAS BEEN USED IN THIS CASE.                                          
DBREF  2V68 A    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V68 B    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V68 C    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V68 D    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V68 E    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V68 F    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V68 G    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V68 H    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V68 I    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V68 J    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V68 K    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V68 L    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V68 M    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V68 N    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V68 O    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V68 P    1   140  UNP    P00873   RBS1_CHLRE      46    185             
SEQADV 2V68 PRO A   46  UNP  P00877    LEU    46 CONFLICT SEE REMARK 999        
SEQADV 2V68 ALA A  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V68 ILE A  342  UNP  P00877    THR   342 ENGINEERED MUTATION            
SEQADV 2V68 PRO B   46  UNP  P00877    LEU    46 CONFLICT SEE REMARK 999        
SEQADV 2V68 ALA B  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V68 ILE B  342  UNP  P00877    THR   342 ENGINEERED MUTATION            
SEQADV 2V68 PRO C   46  UNP  P00877    LEU    46 CONFLICT SEE REMARK 999        
SEQADV 2V68 ALA C  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V68 ILE C  342  UNP  P00877    THR   342 ENGINEERED MUTATION            
SEQADV 2V68 PRO D   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V68 ALA D  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V68 ILE D  342  UNP  P00877    THR   342 ENGINEERED MUTATION            
SEQADV 2V68 PRO E   46  UNP  P00877    LEU    46 CONFLICT SEE REMARK 999        
SEQADV 2V68 ALA E  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V68 ILE E  342  UNP  P00877    THR   342 ENGINEERED MUTATION            
SEQADV 2V68 PRO F   46  UNP  P00877    LEU    46 CONFLICT SEE REMARK 999        
SEQADV 2V68 ALA F  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V68 ILE F  342  UNP  P00877    THR   342 ENGINEERED MUTATION            
SEQADV 2V68 PRO G   46  UNP  P00877    LEU    46 CONFLICT SEE REMARK 999        
SEQADV 2V68 ALA G  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V68 ILE G  342  UNP  P00877    THR   342 ENGINEERED MUTATION            
SEQADV 2V68 PRO H   46  UNP  P00877    LEU    46 CONFLICT SEE REMARK 999        
SEQADV 2V68 ALA H  331  UNP  P00877    VAL   331 ENGINEERED MUTATION            
SEQADV 2V68 ILE H  342  UNP  P00877    THR   342 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 ILE LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 A  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 A  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 A  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 A  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 A  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 A  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 A  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 A  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 A  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 A  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 B  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 B  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 B  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 B  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 B  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 B  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 B  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 B  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 B  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 B  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 B  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 B  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 B  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 B  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 B  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 B  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 B  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 B  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 B  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 B  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 B  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 B  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 B  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 B  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 B  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 B  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 B  475  ARG GLU VAL ILE LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 B  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 B  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 B  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 B  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 B  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 B  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 B  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 B  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 B  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 B  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 C  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 C  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 C  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 C  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 C  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 C  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 C  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 C  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 C  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 C  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 C  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 C  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 C  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 C  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 C  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 C  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 C  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 C  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 C  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 C  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 C  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 C  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 C  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 C  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 C  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 C  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 C  475  ARG GLU VAL ILE LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 C  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 C  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 C  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 C  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 C  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 C  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 C  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 C  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 C  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 C  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 D  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 D  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 D  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 D  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 D  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 D  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 D  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 D  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 D  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 D  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 D  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 D  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 D  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 D  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 D  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 D  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 D  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 D  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 D  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 D  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 D  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 D  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 D  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 D  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 D  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 D  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 D  475  ARG GLU VAL ILE LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 D  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 D  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 D  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 D  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 D  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 D  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 D  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 D  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 D  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 D  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 E  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 E  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 E  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 E  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 E  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 E  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 E  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 E  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 E  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 E  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 E  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 E  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 E  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 E  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 E  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 E  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 E  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 E  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 E  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 E  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 E  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 E  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 E  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 E  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 E  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 E  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 E  475  ARG GLU VAL ILE LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 E  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 E  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 E  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 E  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 E  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 E  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 E  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 E  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 E  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 E  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 F  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 F  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 F  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 F  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 F  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 F  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 F  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 F  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 F  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 F  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 F  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 F  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 F  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 F  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 F  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 F  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 F  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 F  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 F  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 F  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 F  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 F  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 F  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 F  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 F  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 F  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 F  475  ARG GLU VAL ILE LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 F  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 F  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 F  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 F  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 F  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 F  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 F  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 F  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 F  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 F  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 G  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 G  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 G  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 G  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 G  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 G  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 G  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 G  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 G  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 G  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 G  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 G  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 G  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 G  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 G  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 G  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 G  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 G  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 G  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 G  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 G  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 G  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 G  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 G  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 G  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 G  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 G  475  ARG GLU VAL ILE LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 G  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 G  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 G  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 G  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 G  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 G  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 G  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 G  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 G  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 G  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 H  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 H  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 H  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 H  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 H  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 H  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 H  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 H  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 H  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 H  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 H  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 H  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 H  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 H  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 H  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 H  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 H  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 H  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 H  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 H  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 H  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 H  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 H  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 H  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 H  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 H  475  LEU HIS SER GLY THR ALA VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 H  475  ARG GLU VAL ILE LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 H  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 H  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 H  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 H  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 H  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 H  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 H  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 H  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 H  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 H  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 I  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 I  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 I  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 I  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 I  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 I  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 I  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 I  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 I  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 I  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 I  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 J  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 J  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 J  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 J  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 J  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 J  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 J  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 J  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 J  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 J  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 J  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 K  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 K  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 K  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 K  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 K  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 K  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 K  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 K  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 K  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 K  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 K  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 L  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 L  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 L  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 L  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 L  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 L  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 L  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 L  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 L  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 L  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 L  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 M  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 M  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 M  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 M  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 M  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 M  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 M  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 M  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 M  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 M  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 M  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 N  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 N  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 N  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 N  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 N  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 N  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 N  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 N  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 N  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 N  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 N  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 O  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 O  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 O  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 O  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 O  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 O  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 O  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 O  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 O  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 O  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 O  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 P  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 P  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 P  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 P  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 P  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 P  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 P  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 P  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 P  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 P  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 P  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
MODRES 2V68 HYP A  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V68 HYP A  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V68 KCX A  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V68 SMC A  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V68 SMC A  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V68 HYP B  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V68 HYP B  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V68 KCX B  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V68 SMC B  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V68 SMC B  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V68 HYP C  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V68 HYP C  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V68 KCX C  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V68 SMC C  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V68 SMC C  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V68 HYP D  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V68 HYP D  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V68 KCX D  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V68 SMC D  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V68 SMC D  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V68 HYP E  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V68 HYP E  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V68 KCX E  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V68 SMC E  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V68 SMC E  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V68 HYP F  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V68 HYP F  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V68 KCX F  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V68 SMC F  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V68 SMC F  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V68 HYP G  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V68 HYP G  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V68 KCX G  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V68 SMC G  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V68 SMC G  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V68 HYP H  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V68 HYP H  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V68 KCX H  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V68 SMC H  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2V68 SMC H  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2V68 MME I    1  MET  N-METHYL METHIONINE                                
MODRES 2V68 MME J    1  MET  N-METHYL METHIONINE                                
MODRES 2V68 MME K    1  MET  N-METHYL METHIONINE                                
MODRES 2V68 MME L    1  MET  N-METHYL METHIONINE                                
MODRES 2V68 MME M    1  MET  N-METHYL METHIONINE                                
MODRES 2V68 MME N    1  MET  N-METHYL METHIONINE                                
MODRES 2V68 MME O    1  MET  N-METHYL METHIONINE                                
MODRES 2V68 MME P    1  MET  N-METHYL METHIONINE                                
HET    CAP  A 477      21                                                       
HET     MG  A 476       1                                                       
HET    CAP  B 477      21                                                       
HET     MG  B 476       1                                                       
HET    CAP  C 477      21                                                       
HET     MG  C 476       1                                                       
HET    CAP  D 477      21                                                       
HET     MG  D 476       1                                                       
HET    CAP  E 477      21                                                       
HET     MG  E 476       1                                                       
HET    CAP  F 477      21                                                       
HET     MG  F 476       1                                                       
HET    CAP  G 477      21                                                       
HET     MG  G 476       1                                                       
HET    CAP  H 477      21                                                       
HET     MG  H 476       1                                                       
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    EDO  A1477       4                                                       
HET    EDO  A1484       4                                                       
HET    EDO  A1483       4                                                       
HET    EDO  A1481       4                                                       
HET    EDO  A1482       4                                                       
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    EDO  B1477       4                                                       
HET    EDO  B1479       4                                                       
HET    EDO  B1480       4                                                       
HET    EDO  B1481       4                                                       
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    EDO  C1477       4                                                       
HET    EDO  C1478       4                                                       
HET    EDO  C1480       4                                                       
HET    EDO  C1481       4                                                       
HET    EDO  C1482       4                                                       
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    EDO  D1477       4                                                       
HET    EDO  D1478       4                                                       
HET    EDO  D1480       4                                                       
HET    EDO  D1481       4                                                       
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    EDO  E1476       4                                                       
HET    EDO  E1478       4                                                       
HET    EDO  E1480       4                                                       
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    EDO  F1484       4                                                       
HET    EDO  F1480       4                                                       
HET    EDO  F1481       4                                                       
HET    EDO  F1482       4                                                       
HET    EDO  F1483       4                                                       
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    EDO  G1476       4                                                       
HET    EDO  G1478       4                                                       
HET    EDO  G1480       4                                                       
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    EDO  H1476       4                                                       
HET    EDO  H1478       4                                                       
HET    EDO  H1480       4                                                       
HET    EDO  H1481       4                                                       
HET    EDO  H1482       4                                                       
HET    EDO  H1483       4                                                       
HET    MME  I   1       9                                                       
HET    EDO  I1141       4                                                       
HET    EDO  I1142       4                                                       
HET    MME  J   1       9                                                       
HET    EDO  J1141       4                                                       
HET    EDO  J1142       4                                                       
HET    MME  K   1       9                                                       
HET    EDO  K1141       4                                                       
HET    EDO  K1142       4                                                       
HET    MME  L   1       9                                                       
HET    EDO  L1141       4                                                       
HET    MME  M   1       9                                                       
HET    EDO  M1141       4                                                       
HET    MME  N   1       9                                                       
HET    EDO  N1141       4                                                       
HET    EDO  N1142       4                                                       
HET    MME  O   1       9                                                       
HET    EDO  O1141       4                                                       
HET    EDO  O1142       4                                                       
HET    MME  P   1       9                                                       
HET    EDO  P1141       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    49(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   *2276(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 SER A  112  GLY A  122  1                                  11    
HELIX    6   6 ASN A  123  GLY A  126  5                                   4    
HELIX    7   7 PRO A  141  LYS A  146  1                                   6    
HELIX    8   8 GLY A  154  ASN A  163  1                                  10    
HELIX    9   9 SER A  181  GLY A  195  1                                  15    
HELIX   10  10 ARG A  213  GLY A  233  1                                  21    
HELIX   11  11 THR A  246  ALA A  254  1                                   9    
HELIX   12  12 TYR A  269  GLY A  288  1                                  20    
HELIX   13  13 MET A  297  ARG A  303  1                                   7    
HELIX   14  14 HIS A  310  GLY A  322  1                                  13    
HELIX   15  15 GLU A  338  ASP A  351  1                                  14    
HELIX   16  16 ARG A  358  GLY A  361  5                                   4    
HELIX   17  17 HIS A  383  TRP A  385  5                                   3    
HELIX   18  18 HIS A  386  GLY A  395  1                                  10    
HELIX   19  19 GLY A  403  GLY A  408  1                                   6    
HELIX   20  20 GLY A  412  GLU A  433  1                                  22    
HELIX   21  21 ASP A  436  LYS A  450  1                                  15    
HELIX   22  22 SER A  452  LYS A  463  1                                  12    
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 SER B  112  VAL B  121  1                                  10    
HELIX   28  28 ASN B  123  GLY B  126  5                                   4    
HELIX   29  29 PRO B  141  LYS B  146  1                                   6    
HELIX   30  30 GLY B  154  ASN B  163  1                                  10    
HELIX   31  31 SER B  181  GLY B  195  1                                  15    
HELIX   32  32 ARG B  213  GLY B  233  1                                  21    
HELIX   33  33 THR B  246  ALA B  254  1                                   9    
HELIX   34  34 TYR B  269  GLY B  288  1                                  20    
HELIX   35  35 MET B  297  ARG B  303  1                                   7    
HELIX   36  36 HIS B  310  GLY B  322  1                                  13    
HELIX   37  37 GLU B  338  ASP B  351  1                                  14    
HELIX   38  38 ARG B  358  GLY B  361  5                                   4    
HELIX   39  39 HIS B  383  TRP B  385  5                                   3    
HELIX   40  40 HIS B  386  GLY B  395  1                                  10    
HELIX   41  41 GLY B  403  GLY B  408  1                                   6    
HELIX   42  42 GLY B  412  GLU B  433  1                                  22    
HELIX   43  43 ASP B  436  LYS B  450  1                                  15    
HELIX   44  44 SER B  452  LYS B  463  1                                  12    
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 SER C  112  GLY C  122  1                                  11    
HELIX   50  50 ASN C  123  GLY C  126  5                                   4    
HELIX   51  51 PRO C  141  LYS C  146  1                                   6    
HELIX   52  52 GLY C  154  ASN C  163  1                                  10    
HELIX   53  53 SER C  181  GLY C  195  1                                  15    
HELIX   54  54 ARG C  213  GLY C  233  1                                  21    
HELIX   55  55 THR C  246  ALA C  254  1                                   9    
HELIX   56  56 GLY C  273  GLY C  288  1                                  16    
HELIX   57  57 MET C  297  ARG C  303  1                                   7    
HELIX   58  58 HIS C  310  GLY C  322  1                                  13    
HELIX   59  59 GLU C  338  ASP C  351  1                                  14    
HELIX   60  60 ARG C  358  GLY C  361  5                                   4    
HELIX   61  61 HIS C  383  TRP C  385  5                                   3    
HELIX   62  62 HIS C  386  GLY C  395  1                                  10    
HELIX   63  63 GLY C  403  GLY C  408  1                                   6    
HELIX   64  64 GLY C  412  GLU C  433  1                                  22    
HELIX   65  65 ASP C  436  CYS C  449  1                                  14    
HELIX   66  66 SER C  452  LYS C  463  1                                  12    
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 SER D  112  GLY D  122  1                                  11    
HELIX   72  72 ASN D  123  GLY D  126  5                                   4    
HELIX   73  73 PRO D  141  LYS D  146  1                                   6    
HELIX   74  74 GLY D  154  ASN D  163  1                                  10    
HELIX   75  75 SER D  181  GLY D  195  1                                  15    
HELIX   76  76 ARG D  213  GLY D  233  1                                  21    
HELIX   77  77 THR D  246  ALA D  254  1                                   9    
HELIX   78  78 TYR D  269  GLY D  288  1                                  20    
HELIX   79  79 MET D  297  ARG D  303  1                                   7    
HELIX   80  80 HIS D  310  GLY D  322  1                                  13    
HELIX   81  81 GLU D  338  ASP D  351  1                                  14    
HELIX   82  82 ARG D  358  GLY D  361  5                                   4    
HELIX   83  83 HIS D  383  TRP D  385  5                                   3    
HELIX   84  84 HIS D  386  GLY D  395  1                                  10    
HELIX   85  85 GLY D  403  GLY D  408  1                                   6    
HELIX   86  86 GLY D  412  GLY D  434  1                                  23    
HELIX   87  87 ASP D  436  LYS D  463  1                                  28    
HELIX   88  88 TYR E   20  TYR E   25  1                                   6    
HELIX   89  89 PRO E   49  SER E   61  1                                  13    
HELIX   90  90 VAL E   69  THR E   75  5                                   7    
HELIX   91  91 SER E   76  LYS E   81  1                                   6    
HELIX   92  92 SER E  112  GLY E  122  1                                  11    
HELIX   93  93 ASN E  123  GLY E  126  5                                   4    
HELIX   94  94 PRO E  141  LYS E  146  1                                   6    
HELIX   95  95 GLY E  154  ASN E  163  1                                  10    
HELIX   96  96 SER E  181  GLY E  195  1                                  15    
HELIX   97  97 ARG E  213  GLY E  233  1                                  21    
HELIX   98  98 THR E  246  ALA E  254  1                                   9    
HELIX   99  99 TYR E  269  GLY E  288  1                                  20    
HELIX  100 100 MET E  297  ARG E  303  1                                   7    
HELIX  101 101 HIS E  310  GLY E  322  1                                  13    
HELIX  102 102 GLU E  338  ASP E  351  1                                  14    
HELIX  103 103 ARG E  358  GLY E  361  5                                   4    
HELIX  104 104 HIS E  383  TRP E  385  5                                   3    
HELIX  105 105 HIS E  386  GLY E  395  1                                  10    
HELIX  106 106 GLY E  403  GLY E  408  1                                   6    
HELIX  107 107 GLY E  412  GLU E  433  1                                  22    
HELIX  108 108 ASP E  436  LYS E  463  1                                  28    
HELIX  109 109 TYR F   20  TYR F   25  1                                   6    
HELIX  110 110 PRO F   49  SER F   61  1                                  13    
HELIX  111 111 VAL F   69  THR F   75  5                                   7    
HELIX  112 112 SER F   76  LYS F   81  1                                   6    
HELIX  113 113 SER F  112  GLY F  122  1                                  11    
HELIX  114 114 ASN F  123  GLY F  126  5                                   4    
HELIX  115 115 PRO F  141  LYS F  146  1                                   6    
HELIX  116 116 GLY F  154  ASN F  163  1                                  10    
HELIX  117 117 SER F  181  GLY F  195  1                                  15    
HELIX  118 118 ARG F  213  GLY F  233  1                                  21    
HELIX  119 119 THR F  246  ALA F  254  1                                   9    
HELIX  120 120 TYR F  269  GLY F  288  1                                  20    
HELIX  121 121 MET F  297  ARG F  303  1                                   7    
HELIX  122 122 HIS F  310  GLY F  322  1                                  13    
HELIX  123 123 GLU F  338  ASP F  351  1                                  14    
HELIX  124 124 ARG F  358  GLY F  361  5                                   4    
HELIX  125 125 HIS F  383  TRP F  385  5                                   3    
HELIX  126 126 HIS F  386  GLY F  395  1                                  10    
HELIX  127 127 GLY F  403  GLY F  408  1                                   6    
HELIX  128 128 GLY F  412  GLU F  433  1                                  22    
HELIX  129 129 ASP F  436  CYS F  449  1                                  14    
HELIX  130 130 SER F  452  LYS F  463  1                                  12    
HELIX  131 131 TYR G   20  TYR G   25  1                                   6    
HELIX  132 132 PRO G   49  SER G   61  1                                  13    
HELIX  133 133 VAL G   69  THR G   75  5                                   7    
HELIX  134 134 SER G   76  LYS G   81  1                                   6    
HELIX  135 135 SER G  112  GLY G  122  1                                  11    
HELIX  136 136 ASN G  123  GLY G  126  5                                   4    
HELIX  137 137 PRO G  141  LYS G  146  1                                   6    
HELIX  138 138 GLY G  154  ASN G  163  1                                  10    
HELIX  139 139 SER G  181  GLY G  195  1                                  15    
HELIX  140 140 ARG G  213  GLY G  233  1                                  21    
HELIX  141 141 THR G  246  ALA G  254  1                                   9    
HELIX  142 142 TYR G  269  GLY G  288  1                                  20    
HELIX  143 143 MET G  297  ARG G  303  1                                   7    
HELIX  144 144 HIS G  310  GLY G  322  1                                  13    
HELIX  145 145 GLU G  338  ASP G  351  1                                  14    
HELIX  146 146 ARG G  358  GLY G  361  5                                   4    
HELIX  147 147 HIS G  383  TRP G  385  5                                   3    
HELIX  148 148 HIS G  386  GLY G  395  1                                  10    
HELIX  149 149 GLY G  403  GLY G  408  1                                   6    
HELIX  150 150 GLY G  412  GLU G  433  1                                  22    
HELIX  151 151 ASP G  436  LYS G  463  1                                  28    
HELIX  152 152 TYR H   20  TYR H   25  1                                   6    
HELIX  153 153 PRO H   49  SER H   61  1                                  13    
HELIX  154 154 VAL H   69  THR H   75  5                                   7    
HELIX  155 155 SER H   76  LYS H   81  1                                   6    
HELIX  156 156 SER H  112  GLY H  122  1                                  11    
HELIX  157 157 ASN H  123  GLY H  126  5                                   4    
HELIX  158 158 PRO H  141  LYS H  146  1                                   6    
HELIX  159 159 GLY H  154  ASN H  163  1                                  10    
HELIX  160 160 SER H  181  GLY H  195  1                                  15    
HELIX  161 161 ARG H  213  GLY H  233  1                                  21    
HELIX  162 162 THR H  246  ALA H  254  1                                   9    
HELIX  163 163 TYR H  269  GLY H  288  1                                  20    
HELIX  164 164 MET H  297  ARG H  303  1                                   7    
HELIX  165 165 HIS H  310  GLY H  322  1                                  13    
HELIX  166 166 GLU H  338  ASP H  351  1                                  14    
HELIX  167 167 ARG H  358  GLY H  361  5                                   4    
HELIX  168 168 HIS H  383  TRP H  385  5                                   3    
HELIX  169 169 HIS H  386  GLY H  395  1                                  10    
HELIX  170 170 GLY H  403  GLY H  408  1                                   6    
HELIX  171 171 GLY H  412  GLU H  433  1                                  22    
HELIX  172 172 ASP H  436  LYS H  463  1                                  28    
HELIX  173 173 THR I   22  GLY I   37  1                                  16    
HELIX  174 174 GLU I   46  ALA I   50  5                                   5    
HELIX  175 175 ASN I   54  PHE I   60  5                                   7    
HELIX  176 176 ASP I   85  PHE I  100  1                                  16    
HELIX  177 177 PRO I  134  ARG I  138  5                                   5    
HELIX  178 178 THR J   22  GLY J   37  1                                  16    
HELIX  179 179 GLU J   46  ALA J   50  5                                   5    
HELIX  180 180 ASN J   54  PHE J   60  5                                   7    
HELIX  181 181 ASP J   85  PHE J  100  1                                  16    
HELIX  182 182 PRO J  134  ARG J  138  5                                   5    
HELIX  183 183 THR K   22  ASN K   36  1                                  15    
HELIX  184 184 GLU K   46  ALA K   50  5                                   5    
HELIX  185 185 ASN K   54  PHE K   60  5                                   7    
HELIX  186 186 ASP K   85  PHE K  100  1                                  16    
HELIX  187 187 PRO K  134  ARG K  138  5                                   5    
HELIX  188 188 THR L   22  ASN L   36  1                                  15    
HELIX  189 189 GLU L   46  ALA L   50  5                                   5    
HELIX  190 190 ASN L   54  PHE L   60  5                                   7    
HELIX  191 191 ASP L   85  PHE L  100  1                                  16    
HELIX  192 192 PRO L  134  ARG L  138  5                                   5    
HELIX  193 193 THR M   22  ASN M   36  1                                  15    
HELIX  194 194 GLU M   46  ALA M   50  5                                   5    
HELIX  195 195 ASN M   54  PHE M   60  5                                   7    
HELIX  196 196 ASP M   85  PHE M  100  1                                  16    
HELIX  197 197 PRO M  134  ARG M  138  5                                   5    
HELIX  198 198 THR N   22  GLY N   37  1                                  16    
HELIX  199 199 GLU N   46  ALA N   50  5                                   5    
HELIX  200 200 ASN N   54  PHE N   60  5                                   7    
HELIX  201 201 ASP N   85  PHE N  100  1                                  16    
HELIX  202 202 PRO N  134  ARG N  138  5                                   5    
HELIX  203 203 THR O   22  GLY O   37  1                                  16    
HELIX  204 204 GLU O   46  ALA O   50  5                                   5    
HELIX  205 205 ASN O   54  PHE O   60  5                                   7    
HELIX  206 206 ASP O   85  PHE O  100  1                                  16    
HELIX  207 207 PRO O  134  ARG O  138  5                                   5    
HELIX  208 208 THR P   22  GLY P   37  1                                  16    
HELIX  209 209 GLU P   46  ALA P   50  5                                   5    
HELIX  210 210 ASN P   54  PHE P   60  5                                   7    
HELIX  211 211 ASP P   85  PHE P  100  1                                  16    
HELIX  212 212 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  ALA A 102 -1  O  ILE A  98   N  GLU A  88           
SHEET    3  AA 5 LEU A  37  PRO A  44 -1  O  ALA A  38   N  VAL A 101           
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 7 LEU A 169  GLY A 171  0                                        
SHEET    2  AB 7 CYS A 399  GLN A 401  1  O  LEU A 400   N  GLY A 171           
SHEET    3  AB 7 MET A 375  SER A 379  1  O  PRO A 376   N  CYS A 399           
SHEET    4  AB 7 HIS A 325  HIS A 327  1  O  LEU A 326   N  VAL A 377           
SHEET    5  AB 7 LEU A 290  HIS A 294  1  O  ILE A 293   N  HIS A 327           
SHEET    6  AB 7 ILE A 264  ASP A 268  1  O  ILE A 265   N  HIS A 292           
SHEET    7  AB 7 LEU A 240  ASN A 241  1  O  LEU A 240   N  MET A 266           
SHEET    1  BA 5 ARG B  83  PRO B  89  0                                        
SHEET    2  BA 5 TYR B  97  ALA B 102 -1  O  ILE B  98   N  GLU B  88           
SHEET    3  BA 5 LEU B  37  PRO B  44 -1  O  ALA B  38   N  VAL B 101           
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 7 LEU B 169  GLY B 171  0                                        
SHEET    2  BB 7 CYS B 399  GLN B 401  1  O  LEU B 400   N  GLY B 171           
SHEET    3  BB 7 MET B 375  SER B 379  1  O  PRO B 376   N  CYS B 399           
SHEET    4  BB 7 HIS B 325  HIS B 327  1  O  LEU B 326   N  VAL B 377           
SHEET    5  BB 7 LEU B 290  HIS B 294  1  O  ILE B 293   N  HIS B 327           
SHEET    6  BB 7 ILE B 264  ASP B 268  1  O  ILE B 265   N  HIS B 292           
SHEET    7  BB 7 LEU B 240  ASN B 241  1  O  LEU B 240   N  MET B 266           
SHEET    1  CA 5 ARG C  83  PRO C  89  0                                        
SHEET    2  CA 5 TYR C  97  ALA C 102 -1  O  ILE C  98   N  GLU C  88           
SHEET    3  CA 5 LEU C  37  PRO C  44 -1  O  ALA C  38   N  VAL C 101           
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 7 LEU C 169  GLY C 171  0                                        
SHEET    2  CB 7 CYS C 399  GLN C 401  1  O  LEU C 400   N  GLY C 171           
SHEET    3  CB 7 MET C 375  SER C 379  1  O  PRO C 376   N  CYS C 399           
SHEET    4  CB 7 HIS C 325  HIS C 327  1  O  LEU C 326   N  VAL C 377           
SHEET    5  CB 7 LEU C 290  HIS C 294  1  O  ILE C 293   N  HIS C 327           
SHEET    6  CB 7 ILE C 264  ASP C 268  1  O  ILE C 265   N  HIS C 292           
SHEET    7  CB 7 LEU C 240  ASN C 241  1  O  LEU C 240   N  MET C 266           
SHEET    1  DA 5 ARG D  83  PRO D  89  0                                        
SHEET    2  DA 5 TYR D  97  ALA D 102 -1  O  ILE D  98   N  GLU D  88           
SHEET    3  DA 5 LEU D  37  PRO D  44 -1  O  ALA D  38   N  VAL D 101           
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 7 LEU D 169  GLY D 171  0                                        
SHEET    2  DB 7 CYS D 399  GLN D 401  1  O  LEU D 400   N  GLY D 171           
SHEET    3  DB 7 MET D 375  SER D 379  1  O  PRO D 376   N  CYS D 399           
SHEET    4  DB 7 HIS D 325  HIS D 327  1  O  LEU D 326   N  VAL D 377           
SHEET    5  DB 7 LEU D 290  HIS D 294  1  O  ILE D 293   N  HIS D 327           
SHEET    6  DB 7 ILE D 264  ASP D 268  1  O  ILE D 265   N  HIS D 292           
SHEET    7  DB 7 LEU D 240  ASN D 241  1  O  LEU D 240   N  MET D 266           
SHEET    1  EA 5 ARG E  83  PRO E  89  0                                        
SHEET    2  EA 5 TYR E  97  ALA E 102 -1  O  ILE E  98   N  GLU E  88           
SHEET    3  EA 5 LEU E  37  PRO E  44 -1  O  ALA E  38   N  VAL E 101           
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 7 LEU E 169  GLY E 171  0                                        
SHEET    2  EB 7 CYS E 399  GLN E 401  1  O  LEU E 400   N  GLY E 171           
SHEET    3  EB 7 MET E 375  SER E 379  1  O  PRO E 376   N  CYS E 399           
SHEET    4  EB 7 HIS E 325  HIS E 327  1  O  LEU E 326   N  VAL E 377           
SHEET    5  EB 7 LEU E 290  HIS E 294  1  O  ILE E 293   N  HIS E 327           
SHEET    6  EB 7 ILE E 264  ASP E 268  1  O  ILE E 265   N  HIS E 292           
SHEET    7  EB 7 LEU E 240  ASN E 241  1  O  LEU E 240   N  MET E 266           
SHEET    1  FA 5 ARG F  83  PRO F  89  0                                        
SHEET    2  FA 5 TYR F  97  ALA F 102 -1  O  ILE F  98   N  GLU F  88           
SHEET    3  FA 5 LEU F  37  PRO F  44 -1  O  ALA F  38   N  VAL F 101           
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 7 LEU F 169  GLY F 171  0                                        
SHEET    2  FB 7 CYS F 399  GLN F 401  1  O  LEU F 400   N  GLY F 171           
SHEET    3  FB 7 MET F 375  SER F 379  1  O  PRO F 376   N  CYS F 399           
SHEET    4  FB 7 HIS F 325  HIS F 327  1  O  LEU F 326   N  VAL F 377           
SHEET    5  FB 7 LEU F 290  HIS F 294  1  O  ILE F 293   N  HIS F 327           
SHEET    6  FB 7 ILE F 264  ASP F 268  1  O  ILE F 265   N  HIS F 292           
SHEET    7  FB 7 LEU F 240  ASN F 241  1  O  LEU F 240   N  MET F 266           
SHEET    1  GA 5 ARG G  83  PRO G  89  0                                        
SHEET    2  GA 5 TYR G  97  ALA G 102 -1  O  ILE G  98   N  GLU G  88           
SHEET    3  GA 5 LEU G  37  PRO G  44 -1  O  ALA G  38   N  VAL G 101           
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 7 LEU G 169  GLY G 171  0                                        
SHEET    2  GB 7 CYS G 399  GLN G 401  1  O  LEU G 400   N  GLY G 171           
SHEET    3  GB 7 MET G 375  SER G 379  1  O  PRO G 376   N  CYS G 399           
SHEET    4  GB 7 HIS G 325  HIS G 327  1  O  LEU G 326   N  VAL G 377           
SHEET    5  GB 7 LEU G 290  HIS G 294  1  O  ILE G 293   N  HIS G 327           
SHEET    6  GB 7 ILE G 264  ASP G 268  1  O  ILE G 265   N  HIS G 292           
SHEET    7  GB 7 LEU G 240  ASN G 241  1  O  LEU G 240   N  MET G 266           
SHEET    1  HA 5 ARG H  83  PRO H  89  0                                        
SHEET    2  HA 5 TYR H  97  ALA H 102 -1  O  ILE H  98   N  GLU H  88           
SHEET    3  HA 5 LEU H  37  PRO H  44 -1  O  ALA H  38   N  VAL H 101           
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 7 LEU H 169  GLY H 171  0                                        
SHEET    2  HB 7 CYS H 399  GLN H 401  1  O  LEU H 400   N  GLY H 171           
SHEET    3  HB 7 MET H 375  SER H 379  1  O  PRO H 376   N  CYS H 399           
SHEET    4  HB 7 HIS H 325  HIS H 327  1  O  LEU H 326   N  VAL H 377           
SHEET    5  HB 7 LEU H 290  HIS H 294  1  O  ILE H 293   N  HIS H 327           
SHEET    6  HB 7 ILE H 264  ASP H 268  1  O  ILE H 265   N  HIS H 292           
SHEET    7  HB 7 LEU H 240  ASN H 241  1  O  LEU H 240   N  MET H 266           
SHEET    1  IA 4 THR I  74  TRP I  76  0                                        
SHEET    2  IA 4 ILE I  39  ALA I  45 -1  O  LEU I  42   N  TRP I  76           
SHEET    3  IA 4 TYR I 104  ASP I 111 -1  O  TYR I 104   N  ALA I  45           
SHEET    4  IA 4 VAL I 116  GLN I 124 -1  O  VAL I 116   N  ASP I 111           
SHEET    1  JA 4 THR J  74  TRP J  76  0                                        
SHEET    2  JA 4 ILE J  39  ALA J  45 -1  O  LEU J  42   N  TRP J  76           
SHEET    3  JA 4 TYR J 104  ASP J 111 -1  O  TYR J 104   N  ALA J  45           
SHEET    4  JA 4 VAL J 116  GLN J 124 -1  O  VAL J 116   N  ASP J 111           
SHEET    1  KA 4 THR K  74  TRP K  76  0                                        
SHEET    2  KA 4 ILE K  39  ALA K  45 -1  O  LEU K  42   N  TRP K  76           
SHEET    3  KA 4 TYR K 104  ASP K 111 -1  O  TYR K 104   N  ALA K  45           
SHEET    4  KA 4 VAL K 116  GLN K 124 -1  O  VAL K 116   N  ASP K 111           
SHEET    1  LA 4 THR L  74  TRP L  76  0                                        
SHEET    2  LA 4 ILE L  39  ALA L  45 -1  O  LEU L  42   N  TRP L  76           
SHEET    3  LA 4 TYR L 104  ASP L 111 -1  O  TYR L 104   N  ALA L  45           
SHEET    4  LA 4 VAL L 116  GLN L 124 -1  O  VAL L 116   N  ASP L 111           
SHEET    1  MA 4 THR M  74  TRP M  76  0                                        
SHEET    2  MA 4 ILE M  39  ALA M  45 -1  O  LEU M  42   N  TRP M  76           
SHEET    3  MA 4 TYR M 104  ASP M 111 -1  O  TYR M 104   N  ALA M  45           
SHEET    4  MA 4 VAL M 116  GLN M 124 -1  O  VAL M 116   N  ASP M 111           
SHEET    1  NA 4 THR N  74  TRP N  76  0                                        
SHEET    2  NA 4 ILE N  39  ALA N  45 -1  O  LEU N  42   N  TRP N  76           
SHEET    3  NA 4 TYR N 104  ASP N 111 -1  O  TYR N 104   N  ALA N  45           
SHEET    4  NA 4 VAL N 116  GLN N 124 -1  O  VAL N 116   N  ASP N 111           
SHEET    1  OA 4 THR O  74  TRP O  76  0                                        
SHEET    2  OA 4 ILE O  39  ALA O  45 -1  O  LEU O  42   N  TRP O  76           
SHEET    3  OA 4 TYR O 104  ASP O 111 -1  O  TYR O 104   N  ALA O  45           
SHEET    4  OA 4 VAL O 116  GLN O 124 -1  O  VAL O 116   N  ASP O 111           
SHEET    1  PA 4 THR P  74  TRP P  76  0                                        
SHEET    2  PA 4 ILE P  39  ALA P  45 -1  O  LEU P  42   N  TRP P  76           
SHEET    3  PA 4 TYR P 104  ASP P 111 -1  O  TYR P 104   N  ALA P  45           
SHEET    4  PA 4 VAL P 116  GLN P 124 -1  O  VAL P 116   N  ASP P 111           
SSBOND   1 CYS A  247    CYS B  247                          1555   1555  2.10  
SSBOND   2 CYS C  247    CYS D  247                          1555   1555  2.07  
SSBOND   3 CYS E  247    CYS F  247                          1555   1555  2.09  
SSBOND   4 CYS G  247    CYS H  247                          1555   1555  2.09  
LINK         C   TYR A 103                 N   HYP A 104     1555   1555  1.34  
LINK         C   HYP A 104                 N   ILE A 105     1555   1555  1.33  
LINK         C   GLY A 150                 N   HYP A 151     1555   1555  1.34  
LINK         C   HYP A 151                 N   PRO A 152     1555   1555  1.36  
LINK         C   THR A 200                 N   KCX A 201     1555   1555  1.33  
LINK         C   KCX A 201                 N   ASP A 202     1555   1555  1.34  
LINK         C   VAL A 255                 N   SMC A 256     1555   1555  1.34  
LINK         C   SMC A 256                 N   ALA A 257     1555   1555  1.33  
LINK         C   TRP A 368                 N   SMC A 369     1555   1555  1.34  
LINK         C   SMC A 369                 N   SER A 370     1555   1555  1.33  
LINK        MG    MG A 476                 OQ2 KCX A 201     1555   1555  2.06  
LINK        MG    MG A 476                 OD1 ASP A 203     1555   1555  1.93  
LINK        MG    MG A 476                 O2  CAP A 477     1555   1555  2.24  
LINK        MG    MG A 476                 OE1 GLU A 204     1555   1555  2.01  
LINK        MG    MG A 476                 O3  CAP A 477     1555   1555  2.22  
LINK        MG    MG A 476                 O7  CAP A 477     1555   1555  2.22  
LINK         C   TYR B 103                 N   HYP B 104     1555   1555  1.35  
LINK         C   HYP B 104                 N   ILE B 105     1555   1555  1.33  
LINK         C   GLY B 150                 N   HYP B 151     1555   1555  1.34  
LINK         C   HYP B 151                 N   PRO B 152     1555   1555  1.35  
LINK         C   THR B 200                 N   KCX B 201     1555   1555  1.33  
LINK         C   KCX B 201                 N   ASP B 202     1555   1555  1.34  
LINK         C   VAL B 255                 N   SMC B 256     1555   1555  1.33  
LINK         C   SMC B 256                 N   ALA B 257     1555   1555  1.34  
LINK         C   TRP B 368                 N   SMC B 369     1555   1555  1.34  
LINK         C   SMC B 369                 N   SER B 370     1555   1555  1.33  
LINK        MG    MG B 476                 OD1 ASP B 203     1555   1555  1.99  
LINK        MG    MG B 476                 OE1 GLU B 204     1555   1555  2.08  
LINK        MG    MG B 476                 OQ2 KCX B 201     1555   1555  2.02  
LINK        MG    MG B 476                 O2  CAP B 477     1555   1555  2.16  
LINK        MG    MG B 476                 O3  CAP B 477     1555   1555  2.23  
LINK        MG    MG B 476                 O7  CAP B 477     1555   1555  2.27  
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  1.34  
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  1.33  
LINK         C   TRP C 368                 N   SMC C 369     1555   1555  1.33  
LINK         C   SMC C 369                 N   SER C 370     1555   1555  1.34  
LINK        MG    MG C 476                 O3  CAP C 477     1555   1555  2.21  
LINK        MG    MG C 476                 OQ2 KCX C 201     1555   1555  1.92  
LINK        MG    MG C 476                 OD1 ASP C 203     1555   1555  1.91  
LINK        MG    MG C 476                 O2  CAP C 477     1555   1555  2.16  
LINK        MG    MG C 476                 O7  CAP C 477     1555   1555  2.35  
LINK        MG    MG C 476                 OE1 GLU C 204     1555   1555  2.07  
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  1.35  
LINK         C   THR D 200                 N   KCX D 201     1555   1555  1.33  
LINK         C   KCX D 201                 N   ASP D 202     1555   1555  1.33  
LINK         C   VAL D 255                 N   SMC D 256     1555   1555  1.34  
LINK         C   SMC D 256                 N   ALA D 257     1555   1555  1.33  
LINK         C   TRP D 368                 N   SMC D 369     1555   1555  1.34  
LINK         C   SMC D 369                 N   SER D 370     1555   1555  1.33  
LINK        MG    MG D 476                 OD1 ASP D 203     1555   1555  2.01  
LINK        MG    MG D 476                 OQ2 KCX D 201     1555   1555  1.98  
LINK        MG    MG D 476                 O3  CAP D 477     1555   1555  2.11  
LINK        MG    MG D 476                 O7  CAP D 477     1555   1555  2.18  
LINK        MG    MG D 476                 O2  CAP D 477     1555   1555  2.31  
LINK        MG    MG D 476                 OE1 GLU D 204     1555   1555  2.12  
LINK         C   TYR E 103                 N   HYP E 104     1555   1555  1.35  
LINK         C   HYP E 104                 N   ILE E 105     1555   1555  1.34  
LINK         C   GLY E 150                 N   HYP E 151     1555   1555  1.34  
LINK         C   HYP E 151                 N   PRO E 152     1555   1555  1.35  
LINK         C   THR E 200                 N   KCX E 201     1555   1555  1.33  
LINK         C   KCX E 201                 N   ASP E 202     1555   1555  1.34  
LINK         C   VAL E 255                 N   SMC E 256     1555   1555  1.33  
LINK         C   SMC E 256                 N   ALA E 257     1555   1555  1.33  
LINK         C   TRP E 368                 N   SMC E 369     1555   1555  1.34  
LINK         C   SMC E 369                 N   SER E 370     1555   1555  1.33  
LINK        MG    MG E 476                 OD1 ASP E 203     1555   1555  1.99  
LINK        MG    MG E 476                 O7  CAP E 477     1555   1555  2.29  
LINK        MG    MG E 476                 O3  CAP E 477     1555   1555  2.14  
LINK        MG    MG E 476                 O2  CAP E 477     1555   1555  2.20  
LINK        MG    MG E 476                 OQ2 KCX E 201     1555   1555  2.12  
LINK        MG    MG E 476                 OE1 GLU E 204     1555   1555  2.05  
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  1.34  
LINK         C   HYP F 151                 N   PRO F 152     1555   1555  1.35  
LINK         C   THR F 200                 N   KCX F 201     1555   1555  1.33  
LINK         C   KCX F 201                 N   ASP F 202     1555   1555  1.33  
LINK         C   VAL F 255                 N   SMC F 256     1555   1555  1.33  
LINK         C   SMC F 256                 N   ALA F 257     1555   1555  1.34  
LINK         C   TRP F 368                 N   SMC F 369     1555   1555  1.34  
LINK         C   SMC F 369                 N   SER F 370     1555   1555  1.33  
LINK        MG    MG F 476                 OE1 GLU F 204     1555   1555  2.05  
LINK        MG    MG F 476                 O3  CAP F 477     1555   1555  2.19  
LINK        MG    MG F 476                 OQ2 KCX F 201     1555   1555  2.11  
LINK        MG    MG F 476                 O7  CAP F 477     1555   1555  2.10  
LINK        MG    MG F 476                 O2  CAP F 477     1555   1555  2.23  
LINK        MG    MG F 476                 OD1 ASP F 203     1555   1555  1.89  
LINK         C   TYR G 103                 N   HYP G 104     1555   1555  1.35  
LINK         C   HYP G 104                 N   ILE G 105     1555   1555  1.34  
LINK         C   GLY G 150                 N   HYP G 151     1555   1555  1.35  
LINK         C   HYP G 151                 N   PRO G 152     1555   1555  1.34  
LINK         C   THR G 200                 N   KCX G 201     1555   1555  1.33  
LINK         C   KCX G 201                 N   ASP G 202     1555   1555  1.34  
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  1.34  
LINK         C   SMC G 369                 N   SER G 370     1555   1555  1.34  
LINK        MG    MG G 476                 O3  CAP G 477     1555   1555  2.18  
LINK        MG    MG G 476                 OD1 ASP G 203     1555   1555  1.97  
LINK        MG    MG G 476                 O2  CAP G 477     1555   1555  2.24  
LINK        MG    MG G 476                 O7  CAP G 477     1555   1555  2.30  
LINK        MG    MG G 476                 OQ2 KCX G 201     1555   1555  1.95  
LINK        MG    MG G 476                 OE1 GLU G 204     1555   1555  2.07  
LINK         C   TYR H 103                 N   HYP H 104     1555   1555  1.34  
LINK         C   HYP H 104                 N   ILE H 105     1555   1555  1.33  
LINK         C   GLY H 150                 N   HYP H 151     1555   1555  1.36  
LINK         C   HYP H 151                 N   PRO H 152     1555   1555  1.35  
LINK         C   THR H 200                 N   KCX H 201     1555   1555  1.33  
LINK         C   KCX H 201                 N   ASP H 202     1555   1555  1.33  
LINK         C   VAL H 255                 N   SMC H 256     1555   1555  1.32  
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  1.34  
LINK        MG    MG H 476                 OE1 GLU H 204     1555   1555  1.97  
LINK        MG    MG H 476                 OD1 ASP H 203     1555   1555  1.94  
LINK        MG    MG H 476                 O7  CAP H 477     1555   1555  2.20  
LINK        MG    MG H 476                 O2  CAP H 477     1555   1555  2.28  
LINK        MG    MG H 476                 OQ2 KCX H 201     1555   1555  2.03  
LINK        MG    MG H 476                 O3  CAP H 477     1555   1555  2.22  
LINK         C   MME I   1                 N   MET I   2     1555   1555  1.33  
LINK         C   MME J   1                 N   MET J   2     1555   1555  1.32  
LINK         C   MME K   1                 N   MET K   2     1555   1555  1.33  
LINK         C   MME L   1                 N   MET L   2     1555   1555  1.33  
LINK         C   MME M   1                 N   MET M   2     1555   1555  1.33  
LINK         C   MME N   1                 N   MET N   2     1555   1555  1.33  
LINK         C   MME O   1                 N   MET O   2     1555   1555  1.33  
LINK         C   MME P   1                 N   MET P   2     1555   1555  1.33  
CISPEP   1 LYS A  175    PRO A  176          0        -0.85                     
CISPEP   2 LYS B  175    PRO B  176          0        -1.92                     
CISPEP   3 LYS C  175    PRO C  176          0         0.16                     
CISPEP   4 LYS D  175    PRO D  176          0        -2.66                     
CISPEP   5 LYS E  175    PRO E  176          0        -2.09                     
CISPEP   6 LYS F  175    PRO F  176          0         0.35                     
CISPEP   7 LYS G  175    PRO G  176          0        -1.70                     
CISPEP   8 LYS H  175    PRO H  176          0         0.79                     
SITE     1 AC1 28 THR A 173  LYS A 175  LYS A 177  KCX A 201                    
SITE     2 AC1 28 ASP A 203  GLU A 204  HIS A 294  ARG A 295                    
SITE     3 AC1 28 HIS A 327  LYS A 334  LEU A 335  SER A 379                    
SITE     4 AC1 28 GLY A 380  GLY A 381  GLY A 403  GLY A 404                    
SITE     5 AC1 28  MG A 476  HOH A2157  HOH A2192  HOH A2204                    
SITE     6 AC1 28 HOH A2231  HOH A2232  HOH A2233  HOH A2234                    
SITE     7 AC1 28 GLU B  60  THR B  65  TRP B  66  ASN B 123                    
SITE     1 AC2  5 LYS A 177  KCX A 201  ASP A 203  GLU A 204                    
SITE     2 AC2  5 CAP A 477                                                     
SITE     1 AC3 30 GLU A  60  THR A  65  TRP A  66  ASN A 123                    
SITE     2 AC3 30 HOH A2028  THR B 173  LYS B 175  LYS B 177                    
SITE     3 AC3 30 KCX B 201  ASP B 203  GLU B 204  HIS B 294                    
SITE     4 AC3 30 ARG B 295  HIS B 327  LYS B 334  LEU B 335                    
SITE     5 AC3 30 SER B 379  GLY B 380  GLY B 381  GLY B 403                    
SITE     6 AC3 30 GLY B 404   MG B 476  HOH B2086  HOH B2088                    
SITE     7 AC3 30 HOH B2133  HOH B2208  HOH B2209  HOH B2210                    
SITE     8 AC3 30 HOH B2211  HOH B2212                                          
SITE     1 AC4  4 KCX B 201  ASP B 203  GLU B 204  CAP B 477                    
SITE     1 AC5 29 THR C 173  LYS C 175  LYS C 177  KCX C 201                    
SITE     2 AC5 29 ASP C 203  GLU C 204  HIS C 294  ARG C 295                    
SITE     3 AC5 29 HIS C 327  LYS C 334  LEU C 335  SER C 379                    
SITE     4 AC5 29 GLY C 380  GLY C 381  GLY C 403  GLY C 404                    
SITE     5 AC5 29  MG C 476  HOH C2099  HOH C2100  HOH C2154                    
SITE     6 AC5 29 HOH C2225  HOH C2226  HOH C2227  HOH C2228                    
SITE     7 AC5 29 GLU D  60  THR D  65  TRP D  66  ASN D 123                    
SITE     8 AC5 29 HOH D2066                                                     
SITE     1 AC6  4 KCX C 201  ASP C 203  GLU C 204  CAP C 477                    
SITE     1 AC7 28 GLU C  60  THR C  65  TRP C  66  ASN C 123                    
SITE     2 AC7 28 THR D 173  LYS D 175  LYS D 177  KCX D 201                    
SITE     3 AC7 28 ASP D 203  GLU D 204  HIS D 294  ARG D 295                    
SITE     4 AC7 28 HIS D 327  LYS D 334  LEU D 335  SER D 379                    
SITE     5 AC7 28 GLY D 380  GLY D 381  GLY D 403  GLY D 404                    
SITE     6 AC7 28  MG D 476  HOH D2142  HOH D2172  HOH D2181                    
SITE     7 AC7 28 HOH D2205  HOH D2206  HOH D2207  HOH D2208                    
SITE     1 AC8  4 KCX D 201  ASP D 203  GLU D 204  CAP D 477                    
SITE     1 AC9 28 THR E 173  LYS E 175  LYS E 177  KCX E 201                    
SITE     2 AC9 28 ASP E 203  GLU E 204  HIS E 294  ARG E 295                    
SITE     3 AC9 28 HIS E 327  LYS E 334  LEU E 335  SER E 379                    
SITE     4 AC9 28 GLY E 380  GLY E 381  GLY E 403  GLY E 404                    
SITE     5 AC9 28  MG E 476  HOH E2146  HOH E2179  HOH E2220                    
SITE     6 AC9 28 HOH E2221  HOH E2222  HOH E2223  HOH E2224                    
SITE     7 AC9 28 GLU F  60  THR F  65  TRP F  66  ASN F 123                    
SITE     1 BC1  4 KCX E 201  ASP E 203  GLU E 204  CAP E 477                    
SITE     1 BC2 29 GLU E  60  THR E  65  TRP E  66  ASN E 123                    
SITE     2 BC2 29 HOH E2063  THR F 173  LYS F 175  LYS F 177                    
SITE     3 BC2 29 KCX F 201  ASP F 203  GLU F 204  HIS F 294                    
SITE     4 BC2 29 ARG F 295  HIS F 327  LYS F 334  LEU F 335                    
SITE     5 BC2 29 SER F 379  GLY F 380  GLY F 381  GLY F 403                    
SITE     6 BC2 29 GLY F 404   MG F 476  HOH F2088  HOH F2205                    
SITE     7 BC2 29 HOH F2206  HOH F2207  HOH F2208  HOH F2209                    
SITE     8 BC2 29 HOH F2210                                                     
SITE     1 BC3  5 LYS F 177  KCX F 201  ASP F 203  GLU F 204                    
SITE     2 BC3  5 CAP F 477                                                     
SITE     1 BC4 30 THR G 173  LYS G 175  LYS G 177  KCX G 201                    
SITE     2 BC4 30 ASP G 203  GLU G 204  HIS G 294  ARG G 295                    
SITE     3 BC4 30 HIS G 327  LYS G 334  LEU G 335  SER G 379                    
SITE     4 BC4 30 GLY G 380  GLY G 381  GLY G 403  GLY G 404                    
SITE     5 BC4 30  MG G 476  HOH G2085  HOH G2142  HOH G2181                    
SITE     6 BC4 30 HOH G2217  HOH G2218  HOH G2219  GLU H  60                    
SITE     7 BC4 30 THR H  65  TRP H  66  ASN H 123  HOH H2025                    
SITE     8 BC4 30 HOH H2027  HOH H2067                                          
SITE     1 BC5  4 KCX G 201  ASP G 203  GLU G 204  CAP G 477                    
SITE     1 BC6 28 GLU G  60  THR G  65  TRP G  66  ASN G 123                    
SITE     2 BC6 28 HOH G2058  THR H 173  LYS H 175  LYS H 177                    
SITE     3 BC6 28 KCX H 201  ASP H 203  GLU H 204  HIS H 294                    
SITE     4 BC6 28 ARG H 295  HIS H 327  LYS H 334  LEU H 335                    
SITE     5 BC6 28 SER H 379  GLY H 380  GLY H 381  GLY H 403                    
SITE     6 BC6 28 GLY H 404   MG H 476  HOH H2183  HOH H2195                    
SITE     7 BC6 28 HOH H2227  HOH H2228  HOH H2229  HOH H2230                    
SITE     1 BC7  5 LYS H 177  KCX H 201  ASP H 203  GLU H 204                    
SITE     2 BC7  5 CAP H 477                                                     
SITE     1 BC8  6 LYS A 466  PHE A 467  GLU A 468  PHE A 469                    
SITE     2 BC8  6 HOH A2237  HOH B2213                                          
SITE     1 BC9  6 ARG A 295  SER A 328  GLY A 329  GLU A 336                    
SITE     2 BC9  6 GLY A 337  PHE A 345                                          
SITE     1 CC1  8 LYS A  18  THR A  65  TRP A  66  THR A  67                    
SITE     2 CC1  8 THR A  68  EDO A1481  HOH A2011  HOH A2235                    
SITE     1 CC2  8 TYR A  24  THR A  68  VAL A  69  ASP A  72                    
SITE     2 CC2  8 EDO A1483  HOH A2035  HOH A2235  HOH A2236                    
SITE     1 CC3  3 TYR A  20  GLU A  52  HOH B2216                               
SITE     1 CC4  7 TYR B  24  THR B  68  VAL B  69  ASP B  72                    
SITE     2 CC4  7 HOH B2027  HOH B2032  HOH B2214                               
SITE     1 CC5  5 LYS B 466  PHE B 467  GLU B 468  PHE B 469                    
SITE     2 CC5  5 HOH B2216                                                     
SITE     1 CC6  3 TYR B  20  GLU B  52  HOH B2213                               
SITE     1 CC7  7 LYS B  18  THR B  65  TRP B  66  THR B  67                    
SITE     2 CC7  7 THR B  68  HOH B2214  HOH B2215                               
SITE     1 CC8  1 GLU C  52                                                     
SITE     1 CC9  7 LYS C  18  THR C  65  TRP C  66  THR C  67                    
SITE     2 CC9  7 THR C  68  HOH C2030  HOH C2230                               
SITE     1 DC1  8 TYR C  24  GLY C  64  THR C  68  VAL C  69                    
SITE     2 DC1  8 ASP C  72  HOH C2030  HOH C2231  HOH C2232                    
SITE     1 DC2  5 LYS C 466  PHE C 467  GLU C 468  PHE C 469                    
SITE     2 DC2  5 HOH C2229                                                     
SITE     1 DC3  5 GLU C 336  GLY C 337  ASP C 473  HOH C2165                    
SITE     2 DC3  5 HOH C2233                                                     
SITE     1 DC4  7 TYR D  24  THR D  68  VAL D  69  ASP D  72                    
SITE     2 DC4  7 EDO D1480  HOH D2031  HOH D2211                               
SITE     1 DC5  5 LYS D 466  PHE D 467  GLU D 468  PHE D 469                    
SITE     2 DC5  5 HOH D2209                                                     
SITE     1 DC6  9 GLY D  16  LYS D  18  THR D  65  TRP D  66                    
SITE     2 DC6  9 THR D  67  THR D  68  EDO D1477  HOH D2210                    
SITE     3 DC6  9 HOH D2211                                                     
SITE     1 DC7  2 HOH C2229  GLU D  52                                          
SITE     1 DC8  8 TYR E  24  THR E  68  VAL E  69  ASP E  72                    
SITE     2 DC8  8 LEU E  77  HOH E2031  HOH E2035  HOH E2225                    
SITE     1 DC9  7 LYS E  18  THR E  65  TRP E  66  THR E  67                    
SITE     2 DC9  7 THR E  68  HOH E2009  HOH E2225                               
SITE     1 EC1  1 GLU E  52                                                     
SITE     1 EC2  8 TYR F  24  THR F  68  VAL F  69  ASP F  72                    
SITE     2 EC2  8 LEU F  77  HOH F2027  HOH F2029  HOH F2033                    
SITE     1 EC3  2 TYR F  20  GLU F  52                                          
SITE     1 EC4  6 ARG F 295  HIS F 298  PHE F 311  SER F 328                    
SITE     2 EC4  6 GLU F 336  PHE F 345                                          
SITE     1 EC5  4 LYS F 466  PHE F 467  GLU F 468  PHE F 469                    
SITE     1 EC6  9 GLY F  16  VAL F  17  LYS F  18  THR F  65                    
SITE     2 EC6  9 TRP F  66  THR F  67  THR F  68  HOH F2011                    
SITE     3 EC6  9 HOH F2027                                                     
SITE     1 EC7  7 TYR G  24  THR G  68  VAL G  69  ASP G  72                    
SITE     2 EC7  7 HOH G2025  HOH G2027  HOH G2220                               
SITE     1 EC8  6 LYS G  18  THR G  65  TRP G  66  THR G  67                    
SITE     2 EC8  6 THR G  68  HOH G2220                                          
SITE     1 EC9  5 LYS G 466  PHE G 467  GLU G 468  PHE G 469                    
SITE     2 EC9  5 HOH G2221                                                     
SITE     1 FC1  8 TYR H  24  THR H  68  VAL H  69  ASP H  72                    
SITE     2 FC1  8 EDO H1482  HOH H2033  HOH H2231  HOH H2232                    
SITE     1 FC2  5 LYS H 466  PHE H 467  GLU H 468  PHE H 469                    
SITE     2 FC2  5 EDO H1483                                                     
SITE     1 FC3  3 HOH G2221  TYR H  20  GLU H  52                               
SITE     1 FC4  5 ARG H 295  SER H 328  GLY H 329  GLU H 336                    
SITE     2 FC4  5 PHE H 345                                                     
SITE     1 FC5  9 GLY H  16  LYS H  18  THR H  65  TRP H  66                    
SITE     2 FC5  9 THR H  67  THR H  68  EDO H1476  HOH H2007                    
SITE     3 FC5  9 HOH H2231                                                     
SITE     1 FC6  3 PHE H 469  EDO H1478  HOH H2234                               
SITE     1 FC7  7 TYR C 226  LYS C 227  ALA C 230  LYS I  49                    
SITE     2 FC7  7 GLU I  55  HOH I2057  HOH I2058                               
SITE     1 FC8  6 GLY I  37  ILE I  39  GLY I  82  CYS I  83                    
SITE     2 FC8  6 ARG I  84  HOH I2017                                          
SITE     1 FC9  6 TYR H 226  LYS H 227  HOH H2113  LYS J  49                    
SITE     2 FC9  6 GLU J  55  HOH J2031                                          
SITE     1 GC1  5 GLY J  37  TRP J  38  PHE J  81  GLY J  82                    
SITE     2 GC1  5 CYS J  83                                                     
SITE     1 GC2  6 GLY K  37  TRP K  38  ILE K  39  PHE K  81                    
SITE     2 GC2  6 GLY K  82  CYS K  83                                          
SITE     1 GC3  6 TYR E 226  HOH E2113  LYS K  49  GLU K  55                    
SITE     2 GC3  6 HOH K2034  HOH K2036                                          
SITE     1 GC4  5 TYR B 226  ALA B 230  HOH B2111  LYS L  49                    
SITE     2 GC4  5 GLU L  55                                                     
SITE     1 GC5  5 TYR G 226  LYS G 227  LYS M  49  GLU M  55                    
SITE     2 GC5  5 SER M  56                                                     
SITE     1 GC6  2 ILE N  39  GLY N  82                                          
SITE     1 GC7  4 LYS N  49  GLU N  55  ASP N  69  HOH N2031                    
SITE     1 GC8  5 TYR A 226  HOH A2120  LYS O  49  GLU O  55                    
SITE     2 GC8  5 HOH O2030                                                     
SITE     1 GC9  6 GLY O  37  TRP O  38  ILE O  39  PHE O  81                    
SITE     2 GC9  6 GLY O  82  CYS O  83                                          
SITE     1 HC1  5 GLY E  10  GLY P  37  TRP P  38  ILE P  39                    
SITE     2 HC1  5 GLY P  82                                                     
CRYST1  120.421  178.236  122.758  90.00 117.72  90.00 P 1 21 1     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008304  0.000000  0.004363        0.00000                         
SCALE2      0.000000  0.005611  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009202        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  0.599000  0.765800  0.233900      -93.34000    1                    
MTRIX2   2  0.766100 -0.633100  0.111000      145.00000    1                    
MTRIX3   2  0.233100  0.112700 -0.965900      163.70000    1                    
MTRIX1   3  0.092550 -0.771000 -0.630100      101.40000    1                    
MTRIX2   3  0.292500  0.626000 -0.722900       99.72000    1                    
MTRIX3   3  0.095180 -0.117400  0.283400       90.63000    1                    
MTRIX1   4 -0.682000  0.488000  0.544700     -122.10000    1                    
MTRIX2   4  0.487500 -0.251800  0.836000       44.69000    1                    
MTRIX3   4  0.545200  0.835700 -0.066160       31.28000    1                    
MTRIX1   5 -0.818300 -0.476800  0.321000      -23.45000    1                    
MTRIX2   5 -0.477100  0.252100 -0.841900      126.30000    1                    
MTRIX3   5  0.320500 -0.842100 -0.433800      201.20000    1                    
MTRIX1   6 -0.780800 -0.290900 -0.552900       36.42000    1                    
MTRIX2   6 -0.287300 -0.618800  0.731100       69.41000    1                    
MTRIX3   6 -0.554800  0.729700  0.399600      -21.71000    1                    
MTRIX1   7  0.088920  0.293300  0.951900     -124.80000    1                    
MTRIX2   7 -0.771100  0.625200 -0.120700       26.83000    1                    
MTRIX3   7 -0.630500 -0.723200  0.281800      110.60000    1                    
MTRIX1   8  0.500000 -0.011880 -0.865900       65.28000    1                    
MTRIX2   8 -0.011420 -0.999900  0.007126      169.60000    1                    
MTRIX3   8 -0.865900  0.006323 -0.500100      110.80000    1                    
MTRIX1   9  0.596600  0.766900  0.236500      -93.66000    1                    
MTRIX2   9  0.768200 -0.631000  0.108000      145.20000    1                    
MTRIX3   9  0.232100  0.117300 -0.965600      163.30000    1                    
MTRIX1  10  0.095440 -0.770300 -0.630500      101.40000    1                    
MTRIX2  10  0.287200  0.627800 -0.723500       99.69000    1                    
MTRIX3  10  0.953100 -0.112000  0.281100       90.50000    1                    
MTRIX1  11 -0.680600  0.492400  0.542500     -122.20000    1                    
MTRIX2  11  0.491300 -0.242400  0.836500       43.92000    1                    
MTRIX3  11  0.543400  0.835900 -0.076900       32.40000    1                    
MTRIX1  12 -0.815700 -0.477800  0.326200      -23.94000    1                    
MTRIX2  12 -0.480700  0.246100 -0.841700      126.80000    1                    
MTRIX3  12  0.321800 -0.843300 -0.430400      200.90000    1                    
MTRIX1  13 -0.780800 -0.291600 -0.552600       36.39000    1                    
MTRIX2  13 -0.282900 -0.623500  0.728900       69.98000    1                    
MTRIX3  13 -0.557100  0.725400  0.404300      -21.90000    1                    
MTRIX1  14  0.088380  0.291500  0.952500     -124.80000    1                    
MTRIX2  14 -0.773900  0.622200 -0.118600       26.83000    1                    
MTRIX3  14 -0.627200 -0.726600  0.280600      110.90000    1                    
MTRIX1  15  0.499900 -0.011290 -0.866000       65.25000    1                    
MTRIX2  15 -0.010380 -0.999900  0.007043      169.50000    1                    
MTRIX3  15 -0.866000  0.005470 -0.499900      110.80000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system