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Database: PDB
Entry: 2VDH
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Original site: 2VDH 
HEADER    LYASE                                   09-OCT-07   2VDH              
TITLE     CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII RUBISCO WITH           
TITLE    2 A LARGE-SUBUNIT C172S MUTATION                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;             
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 SYNONYM: RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE LARGE                 
COMPND   5  CHAIN, RUBISCO LARGE SUBUNIT;                                       
COMPND   6 EC: 4.1.1.39;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1;           
COMPND  11 CHAIN: I, J, K, L, M, N, O, P;                                       
COMPND  12 SYNONYM: RUBISCO SMALL SUBUNIT 1,RIBULOSE-1,5-BISPHOSPHATE           
COMPND  13  CARBOXYLASE SMALL CHAIN;                                            
COMPND  14 EC: 4.1.1.39;                                                        
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;                      
SOURCE   3 ORGANISM_TAXID: 3055;                                                
SOURCE   4 STRAIN: 18-7G;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PLS-C172S;                                
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;                      
SOURCE  10 ORGANISM_TAXID: 3055;                                                
SOURCE  11 STRAIN: 18-7G;                                                       
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: PLS-C172S                                 
KEYWDS    VICINAL CYSTEINES, CO2/O2 SPECIFICITY, PHOTOSYNTHESIS,                
KEYWDS   2 TRANSIT PEPTIDE, PHOTORESPIRATION, METAL-BINDING,                    
KEYWDS   3 HYDROXYLATION, OXIDOREDUCTASE, METHYLATION, CHLOROPLAST,             
KEYWDS   4 CALVIN CYCLE, MONOOXYGENASE, LYASE, RUBISCO, PLASTID,                
KEYWDS   5 MAGNESIUM, ACETYLATION, CARBON DIOXIDE FIXATION                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.-J.GARCIA-MURRIA,S.KARKEHABADI,J.MARIN-NAVARRO,                     
AUTHOR   2 S.SATAGOPAN,I.ANDERSSON,R.J.SPREITZER,J.MORENO                       
REVDAT   3   24-FEB-09 2VDH    1       VERSN                                    
REVDAT   2   11-NOV-08 2VDH    1       JRNL   REMARK                            
REVDAT   1   04-NOV-08 2VDH    0                                                
JRNL        AUTH   M.-J.GARCIA-MURRIA,S.KARKEHABADI,J.MARIN-NAVARRO,            
JRNL        AUTH 2 S.SATAGOPAN,I.ANDERSSON,R.J.SPREITZER,J.MORENO               
JRNL        TITL   STRUCTURAL AND FUNCTIONAL CONSEQUENCES OF THE                
JRNL        TITL 2 REPLACEMENT OF PROXIMAL RESIDUES CYS-172 AND CYS-            
JRNL        TITL 3 192 IN THE LARGE SUBUNIT OF RIBULOSE 1,5-                    
JRNL        TITL 4 BISPHOSPHATE CARBOXYLASE/OXYGENASE FROM                      
JRNL        TITL 5 CHLAMYDOMONAS REINHARDTII                                    
JRNL        REF    BIOCHEM.J.                    V. 411   241 2008              
JRNL        REFN                   ISSN 0264-6021                               
JRNL        PMID   18072944                                                     
JRNL        DOI    10.1042/BJ20071422                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.3  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
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        (%) : 88.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 169202                         
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) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
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      : 8936                            
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) : 12724                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2130                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 646                          
REMARK   3   BIN FREE R VALUE                    : 0.2570                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 37804                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 812                                     
REMARK   3   SOLVENT ATOMS            : 1800                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.62000                                              
REMARK   3    B22 (A**2) : 0.18000                                              
REMARK   3    B33 (A**2) : -0.65000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.16000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.960         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.242         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.145         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.958         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 39507 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 53491 ; 1.217 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4833 ; 5.974 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1840 ;32.332 ;23.174       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  6308 ;15.047 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   312 ;15.190 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  5677 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 30352 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A): 18714 ; 0.192 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 26839 ; 0.304 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  2447 ; 0.138 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   139 ; 0.321 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.250 ; 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): 24666 ; 0.566 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 38662 ; 0.876 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 16964 ; 1.446 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 14829 ; 2.307 ; 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):   3630 ;   .00 ;   .05           
REMARK   3   TIGHT THERMAL      1    A (A**2):   3630 ;   .00 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B     13       B     438      1                      
REMARK   3           1     A     13       A     438      1                      
REMARK   3           2     B    440       B     477      1                      
REMARK   3           2     A    440       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    B    (A):   3630 ;   .03 ;   .05           
REMARK   3   TIGHT THERMAL      2    B (A**2):   3630 ;   .11 ;   .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     438      1                      
REMARK   3           1     A     13       A     438      1                      
REMARK   3           2     C    440       C     477      1                      
REMARK   3           2     A    440       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    C    (A):   3630 ;   .04 ;   .05           
REMARK   3   TIGHT THERMAL      3    C (A**2):   3630 ;   .14 ;   .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):   3630 ;   .03 ;   .05           
REMARK   3   TIGHT THERMAL      4    D (A**2):   3630 ;   .12 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 5                                  
REMARK   3     CHAIN NAMES                    : E A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     E     13       E      31      1                      
REMARK   3           1     A     13       A      31      1                      
REMARK   3           2     E     33       E     438      1                      
REMARK   3           2     A     33       A     438      1                      
REMARK   3           3     E    440       E     477      1                      
REMARK   3           3     A    440       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   5    E    (A):   3618 ;   .03 ;   .05           
REMARK   3   TIGHT THERMAL      5    E (A**2):   3618 ;   .11 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 6                                  
REMARK   3     CHAIN NAMES                    : F A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     F     13       F      31      1                      
REMARK   3           1     A     13       A      31      1                      
REMARK   3           2     F     33       F     438      1                      
REMARK   3           2     A     33       A     438      1                      
REMARK   3           3     F    440       F     477      1                      
REMARK   3           3     A    440       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   6    F    (A):   3619 ;   .04 ;   .05           
REMARK   3   TIGHT THERMAL      6    F (A**2):   3619 ;   .12 ;   .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):   3630 ;   .04 ;   .05           
REMARK   3   TIGHT THERMAL      7    G (A**2):   3630 ;   .11 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 8                                  
REMARK   3     CHAIN NAMES                    : H A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     H     13       H     438      1                      
REMARK   3           1     A     13       A     438      1                      
REMARK   3           2     H    440       H     477      1                      
REMARK   3           2     A    440       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   8    H    (A):   3630 ;   .03 ;   .05           
REMARK   3   TIGHT THERMAL      8    H (A**2):   3630 ;   .11 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 9                                  
REMARK   3     CHAIN NAMES                    : I                               
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
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           3     I    131       I     140      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   9    I    (A):   1121 ;   .00 ;   .05           
REMARK   3   TIGHT THERMAL      9    I (A**2):   1121 ;   .00 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 10                                 
REMARK   3     CHAIN NAMES                    : J I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
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           3     J    131       J     140      1                      
REMARK   3           3     I    131       I     140      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  10    J    (A):   1121 ;   .03 ;   .05           
REMARK   3   TIGHT THERMAL     10    J (A**2):   1121 ;   .10 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 11                                 
REMARK   3     CHAIN NAMES                    : K I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
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           3     K    131       K     140      1                      
REMARK   3           3     I    131       I     140      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  11    K    (A):   1121 ;   .03 ;   .05           
REMARK   3   TIGHT THERMAL     11    K (A**2):   1121 ;   .11 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 12                                 
REMARK   3     CHAIN NAMES                    : L I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
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           3     L    131       L     140      1                      
REMARK   3           3     I    131       I     140      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  12    L    (A):   1121 ;   .04 ;   .05           
REMARK   3   TIGHT THERMAL     12    L (A**2):   1121 ;   .11 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 13                                 
REMARK   3     CHAIN NAMES                    : M I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
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           3     M    131       M     140      1                      
REMARK   3           3     I    131       I     140      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  13    M    (A):   1121 ;   .04 ;   .05           
REMARK   3   TIGHT THERMAL     13    M (A**2):   1121 ;   .10 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 14                                 
REMARK   3     CHAIN NAMES                    : N I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
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           3     N    131       N     140      1                      
REMARK   3           3     I    131       I     140      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  14    N    (A):   1121 ;   .03 ;   .05           
REMARK   3   TIGHT THERMAL     14    N (A**2):   1121 ;   .11 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 15                                 
REMARK   3     CHAIN NAMES                    : O I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
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           3     O    131       O     140      1                      
REMARK   3           3     I    131       I     140      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  15    O    (A):   1121 ;   .04 ;   .05           
REMARK   3   TIGHT THERMAL     15    O (A**2):   1121 ;   .10 ;   .50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 16                                 
REMARK   3     CHAIN NAMES                    : P I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
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           3     P    131       P     140      1                      
REMARK   3           3     I    131       I     140      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  16    P    (A):   1121 ;   .04 ;   .05           
REMARK   3   TIGHT THERMAL     16    P (A**2):   1121 ;   .10 ;   .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 2VDH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  09-OCT-07.                 
REMARK 100 THE PDBE ID CODE IS EBI-34097.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAY-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.931                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 240796                             
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     (%) : 89.4                               
REMARK 200  DATA REDUNDANCY                : 9.1                                
REMARK 200  R MERGE                    (I) : 0.16                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.70                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.36                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.90                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1GK8                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05                     
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       89.17450            
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: 132050 ANGSTROM**2                        
REMARK 350 SURFACE AREA OF THE COMPLEX: 117550 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -416 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, CYS 172 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 172 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, CYS 172 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, CYS 172 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN E, CYS 172 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, CYS 172 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN G, CYS 172 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN H, CYS 172 TO SER                        
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     LYS A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     GLY A    10                                                      
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     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     GLY E    10                                                      
REMARK 465     MET F     1                                                      
REMARK 465     VAL F     2                                                      
REMARK 465     PRO F     3                                                      
REMARK 465     GLN F     4                                                      
REMARK 465     THR F     5                                                      
REMARK 465     GLU F     6                                                      
REMARK 465     THR F     7                                                      
REMARK 465     LYS F     8                                                      
REMARK 465     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     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 465     GLY H    10                                                      
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   OG1  THR G   471  -  O    HOH G  2172              2.02            
REMARK 500   OG   SER L    53  -  OE2  GLU L    55              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS C 449   CA  -  CB  -  SG  ANGL. DEV. =   7.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  62      -81.85   -141.57                                   
REMARK 500    THR A  65     -166.75   -129.41                                   
REMARK 500    THR A  75     -169.75   -122.22                                   
REMARK 500    ASN A 207      -92.86   -123.86                                   
REMARK 500    MET A 212      113.38   -165.24                                   
REMARK 500    TYR A 239       97.51    -69.82                                   
REMARK 500    MET A 297      -12.42     91.52                                   
REMARK 500    VAL A 331      -52.69     71.82                                   
REMARK 500    ASP A 357       94.55   -160.87                                   
REMARK 500    SER B  62      -78.92   -138.10                                   
REMARK 500    THR B  75     -169.27   -124.95                                   
REMARK 500    ASN B 207      -91.40   -121.88                                   
REMARK 500    MET B 212      106.60   -169.01                                   
REMARK 500    MET B 297      -10.22     91.22                                   
REMARK 500    VAL B 331      -50.15     74.66                                   
REMARK 500    ASP B 357       89.69   -159.65                                   
REMARK 500    SER C  62      -82.57   -138.00                                   
REMARK 500    THR C  65     -165.24   -126.34                                   
REMARK 500    THR C  75     -167.99   -119.49                                   
REMARK 500    ASN C 207      -92.17   -124.27                                   
REMARK 500    MET C 212      117.39   -163.88                                   
REMARK 500    ALA C 296      133.19    -40.00                                   
REMARK 500    MET C 297      -12.49     92.33                                   
REMARK 500    VAL C 331      -55.13     71.13                                   
REMARK 500    ASP C 357       97.06   -160.44                                   
REMARK 500    ARG C 439      -38.53   -136.32                                   
REMARK 500    SER D  62      -79.59   -140.81                                   
REMARK 500    THR D  65     -165.04   -127.31                                   
REMARK 500    THR D  75     -165.26   -120.93                                   
REMARK 500    ASN D 207      -90.33   -125.26                                   
REMARK 500    MET D 212      110.32   -165.35                                   
REMARK 500    ALA D 296      133.99    -36.23                                   
REMARK 500    MET D 297      -16.08     87.31                                   
REMARK 500    VAL D 331      -53.86     73.02                                   
REMARK 500    ASP D 357       92.43   -161.14                                   
REMARK 500    SER E  62      -80.94   -141.87                                   
REMARK 500    THR E  65     -166.27   -127.26                                   
REMARK 500    ASN E 207      -93.83   -124.52                                   
REMARK 500    MET E 212      112.75   -167.19                                   
REMARK 500    MET E 297      -14.94     89.15                                   
REMARK 500    VAL E 331      -51.49     68.77                                   
REMARK 500    ASP E 357       93.84   -164.58                                   
REMARK 500    SER F  62      -80.81   -136.45                                   
REMARK 500    ASN F 207      -94.74   -123.43                                   
REMARK 500    MET F 212      111.83   -165.55                                   
REMARK 500    MET F 297      -12.04     88.35                                   
REMARK 500    VAL F 331      -55.02     71.94                                   
REMARK 500    ASP F 357       89.76   -156.21                                   
REMARK 500    SER G  62      -78.14   -138.76                                   
REMARK 500    THR G  65     -168.28   -128.39                                   
REMARK 500    THR G  75     -169.07   -123.38                                   
REMARK 500    ASN G 207      -91.30   -121.00                                   
REMARK 500    MET G 212      111.70   -160.20                                   
REMARK 500    MET G 297      -13.57     91.02                                   
REMARK 500    VAL G 331      -48.94     71.04                                   
REMARK 500    THR G 406      -52.17   -120.02                                   
REMARK 500    SER H  62      -83.17   -141.31                                   
REMARK 500    ASN H 207      -91.68   -123.32                                   
REMARK 500    MET H 212      113.20   -163.85                                   
REMARK 500    TYR H 239       95.62    -69.49                                   
REMARK 500    MET H 297      -13.68     92.90                                   
REMARK 500    VAL H 331      -51.55     69.00                                   
REMARK 500    ASP H 357       94.27   -161.61                                   
REMARK 500    GLU I  13     -141.30     61.57                                   
REMARK 500    PHE I  15       -0.48     81.44                                   
REMARK 500    SER I  62       58.50    -90.99                                   
REMARK 500    LYS I  77     -119.96     54.51                                   
REMARK 500    GLU J  13     -141.03     62.54                                   
REMARK 500    PHE J  15       -0.60     82.96                                   
REMARK 500    LYS J  77     -122.50     56.24                                   
REMARK 500    PHE K  12       42.76   -140.27                                   
REMARK 500    GLU K  13     -142.57     63.21                                   
REMARK 500    PHE K  15       -3.84     84.20                                   
REMARK 500    LYS K  77     -124.18     60.03                                   
REMARK 500    PHE L  12       45.61   -142.38                                   
REMARK 500    GLU L  13     -143.60     59.42                                   
REMARK 500    PHE L  15       -0.62     83.57                                   
REMARK 500    LYS L  77     -117.51     54.29                                   
REMARK 500    PHE M  12       46.51   -143.53                                   
REMARK 500    GLU M  13     -138.38     57.81                                   
REMARK 500    LYS M  77     -120.67     52.02                                   
REMARK 500    PHE N  12       42.79   -141.78                                   
REMARK 500    GLU N  13     -142.16     61.11                                   
REMARK 500    PHE N  15       -2.36     82.25                                   
REMARK 500    LYS N  77     -122.96     55.70                                   
REMARK 500    GLU O  13     -142.11     62.20                                   
REMARK 500    PHE O  15        0.52     83.44                                   
REMARK 500    SER O  62       52.94    -92.26                                   
REMARK 500    LYS O  77     -119.59     54.71                                   
REMARK 500    GLU P  13     -138.08     66.27                                   
REMARK 500    PHE P  15       -0.26     85.40                                   
REMARK 500    LYS P  77     -118.23     54.92                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 204   OE1                                                    
REMARK 620 2 CAP A1477   O7   97.7                                              
REMARK 620 3 CAP A1477   C   113.7  24.4                                        
REMARK 620 4 ASP A 203   OD1  89.9 101.0 117.6                                  
REMARK 620 5 KCX A 201   OQ1  86.7 166.3 142.8  91.8                            
REMARK 620 6 CAP A1477   O3   84.9  85.5  70.0 172.2  82.0                      
REMARK 620 7 CAP A1477   O2  158.8  77.2  55.7 111.2  94.0  74.2                
REMARK 620 8 CAP A1477   C2  130.5  55.9  31.5 132.4 111.7  55.0  30.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX B 201   OQ1                                                    
REMARK 620 2 CAP B1477   O2   92.0                                              
REMARK 620 3 CAP B1477   O3   82.7  75.3                                        
REMARK 620 4 CAP B1477   C2  109.1  30.4  55.2                                  
REMARK 620 5 CAP B1477   O7  163.9  74.6  85.2  54.9                            
REMARK 620 6 ASP B 203   OD1 100.3 106.6 176.3 125.2  92.3                      
REMARK 620 7 GLU B 204   OE1  90.9 163.4  88.9 134.2  99.5  88.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 203   OD1                                                    
REMARK 620 2 GLU C 204   OE1  94.1                                              
REMARK 620 3 CAP C1477   C   112.3 113.0                                        
REMARK 620 4 CAP C1477   O7   98.1  95.6  24.4                                  
REMARK 620 5 KCX C 201   OQ1  97.4  88.9 140.6 163.5                            
REMARK 620 6 CAP C1477   O3  178.8  85.4  68.8  83.0  81.6                      
REMARK 620 7 CAP C1477   O2  106.8 158.5  54.5  76.8  93.4  73.9                
REMARK 620 8 CAP C1477   C2  126.3 130.2  31.0  55.4 110.1  54.7  30.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAP D1477   C2                                                     
REMARK 620 2 ASP D 203   OD1 128.7                                              
REMARK 620 3 CAP D1477   O2   30.1 107.2                                        
REMARK 620 4 CAP D1477   C    30.8 115.4  53.6                                  
REMARK 620 5 CAP D1477   O7   54.7  97.3  72.7  24.2                            
REMARK 620 6 KCX D 201   OQ1 108.9  91.1  91.0 139.7 163.3                      
REMARK 620 7 GLU D 204   OE1 134.1  89.5 163.0 116.3 102.3  92.2                
REMARK 620 8 CAP D1477   O3   54.1 175.6  73.9  68.8  87.1  84.6  89.8          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX E 201   OQ1                                                    
REMARK 620 2 ASP E 203   OD1  93.7                                              
REMARK 620 3 GLU E 204   OE1  93.7  86.5                                        
REMARK 620 4 CAP E1477   O3   85.8 177.0  90.5                                  
REMARK 620 5 CAP E1477   O2   94.3 109.5 161.5  73.5                            
REMARK 620 6 CAP E1477   C   142.1 114.0 112.4  67.8  53.3                      
REMARK 620 7 CAP E1477   O7  165.8  97.2  96.1  83.8  73.4  23.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 203   OD1                                                    
REMARK 620 2 CAP F1477   C2  136.2                                              
REMARK 620 3 CAP F1477   O2  112.6  31.6                                        
REMARK 620 4 CAP F1477   C   122.1  32.1  56.7                                  
REMARK 620 5 CAP F1477   O7  105.8  57.7  80.1  25.6                            
REMARK 620 6 KCX F 201   OQ1  89.1 112.4  96.1 143.6 164.9                      
REMARK 620 7 GLU F 204   OE1  87.8 131.3 159.4 114.8  96.8  81.6                
REMARK 620 8 CAP F1477   O3  167.7  55.5  76.1  69.7  83.9  81.0  83.4          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 204   OE1                                                    
REMARK 620 2 CAP G1477   O3   85.6                                              
REMARK 620 3 CAP G1477   O7   97.4  84.1                                        
REMARK 620 4 CAP G1477   C2  130.2  54.4  54.9                                  
REMARK 620 5 CAP G1477   C   113.0  68.7  23.9  31.1                            
REMARK 620 6 KCX G 201   OQ1  88.3  79.4 162.1 108.8 139.2                      
REMARK 620 7 ASP G 203   OD1  94.9 175.7 100.0 127.3 114.8  96.3                
REMARK 620 8 CAP G1477   O2  158.7  73.9  75.2  30.2  54.3  93.4 106.0          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX H 201   OQ1                                                    
REMARK 620 2 CAP H1477   O3   90.0                                              
REMARK 620 3 CAP H1477   C2  116.2  55.2                                        
REMARK 620 4 CAP H1477   O2   96.5  75.0  30.4                                  
REMARK 620 5 CAP H1477   C   147.0  68.9  30.8  54.5                            
REMARK 620 6 ASP H 203   OD1  90.5 176.3 127.6 108.7 112.2                      
REMARK 620 7 GLU H 204   OE1  91.5  87.5 130.9 160.6 111.8  88.8                
REMARK 620 8 CAP H1477   O7  170.8  84.9  54.6  74.8  23.9  95.1  95.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG C1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG D1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG E1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG F1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP F1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG G1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG H1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO I1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO L1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO N1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO N1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1483                 
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: 2V68   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII                      
REMARK 900  RUBISCO WITH LARGE-SUBUNIT MUTATIONS V331A,                         
REMARK 900  T342I                                                               
REMARK 900 RELATED ID: 2V69   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII                      
REMARK 900  RUBISCO WITH A LARGE-SUBUNIT MUTATION D473E                         
REMARK 900 RELATED ID: 1GK8   RELATED DB: PDB                                   
REMARK 900  RUBISCO FROM CHLAMYDOMONAS REINHARDTII                              
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: 1UWA   RELATED DB: PDB                                   
REMARK 900  L290F MUTANT RUBISCO FROM CHLAMYDOMONAS                             
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: 2V6A   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII                      
REMARK 900  RUBISCO WITH LARGE-SUBUNIT MUTATIONS V331A,                         
REMARK 900  G344S                                                               
REMARK 900 RELATED ID: 2VDI   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII                      
REMARK 900  RUBISCO WITH A LARGE-SUBUNIT C192S MUTATION                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE UNP P00877 HAS A VARIANT (PRO46LEU)                     
REMARK 999 WHICH OCCURS IN STRAIN 137C                                          
REMARK 999 LARGE CHAIN RESIDUE 46 DIFFERS FROM UNP P00877                       
REMARK 999 AND IS IDENTIFIED AS PRO FROM THE ELECTRON                           
REMARK 999 DENSITY.                                                             
DBREF  2VDH A    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2VDH B    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2VDH C    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2VDH D    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2VDH E    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2VDH F    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2VDH G    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2VDH H    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2VDH I    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2VDH J    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2VDH K    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2VDH L    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2VDH M    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2VDH N    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2VDH O    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2VDH P    1   140  UNP    P00873   RBS1_CHLRE      46    185             
SEQADV 2VDH PRO A   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2VDH SER A  172  UNP  P00877    CYS   172 ENGINEERED MUTATION            
SEQADV 2VDH PRO B   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2VDH SER B  172  UNP  P00877    CYS   172 ENGINEERED MUTATION            
SEQADV 2VDH PRO C   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2VDH SER C  172  UNP  P00877    CYS   172 ENGINEERED MUTATION            
SEQADV 2VDH PRO D   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2VDH SER D  172  UNP  P00877    CYS   172 ENGINEERED MUTATION            
SEQADV 2VDH PRO E   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2VDH SER E  172  UNP  P00877    CYS   172 ENGINEERED MUTATION            
SEQADV 2VDH PRO F   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2VDH SER F  172  UNP  P00877    CYS   172 ENGINEERED MUTATION            
SEQADV 2VDH PRO G   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2VDH SER G  172  UNP  P00877    CYS   172 ENGINEERED MUTATION            
SEQADV 2VDH PRO H   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2VDH SER H  172  UNP  P00877    CYS   172 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 SER 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 VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 A  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 A  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 A  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 A  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 A  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 A  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 A  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 A  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 A  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 A  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 A  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 B  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 B  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 B  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 B  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 B  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 B  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 B  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 B  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 B  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 B  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 B  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 B  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 B  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 B  475  LEU GLY SER 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 VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 B  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 B  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 B  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 B  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 B  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 B  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 B  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 B  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 B  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 B  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 B  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 C  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 C  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 C  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 C  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 C  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 C  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 C  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 C  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 C  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 C  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 C  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 C  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 C  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 C  475  LEU GLY SER 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 VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 C  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 C  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 C  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 C  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 C  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 C  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 C  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 C  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 C  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 C  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 C  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 D  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 D  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 D  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 D  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 D  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 D  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 D  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 D  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 D  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 D  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 D  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 D  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 D  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 D  475  LEU GLY SER 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 VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 D  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 D  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 D  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 D  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 D  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 D  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 D  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 D  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 D  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 D  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 D  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 E  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 E  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 E  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 E  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 E  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 E  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 E  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 E  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 E  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 E  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 E  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 E  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 E  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 E  475  LEU GLY SER 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 VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 E  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 E  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 E  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 E  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 E  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 E  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 E  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 E  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 E  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 E  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 E  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 F  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 F  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 F  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 F  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 F  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 F  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 F  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 F  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 F  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 F  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 F  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 F  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 F  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 F  475  LEU GLY SER 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 VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 F  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 F  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 F  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 F  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 F  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 F  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 F  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 F  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 F  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 F  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 F  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 G  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 G  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 G  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 G  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 G  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 G  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 G  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 G  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 G  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 G  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 G  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 G  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 G  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 G  475  LEU GLY SER 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 VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 G  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 G  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 G  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 G  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 G  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 G  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 G  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 G  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 G  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 G  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 G  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 H  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 H  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 H  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 H  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 H  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 H  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 H  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 H  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 H  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 H  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 H  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 H  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 H  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 H  475  LEU GLY SER 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 VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 H  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 H  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 H  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 H  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 H  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 H  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 H  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 H  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 H  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 H  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 H  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 I  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 I  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 I  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 I  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 I  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 I  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 I  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 I  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 I  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 I  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 I  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 J  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 J  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 J  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 J  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 J  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 J  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 J  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 J  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 J  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 J  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 J  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 K  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 K  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 K  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 K  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 K  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 K  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 K  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 K  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 K  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 K  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 K  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 L  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 L  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 L  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 L  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 L  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 L  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 L  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 L  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 L  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 L  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 L  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 M  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 M  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 M  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 M  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 M  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 M  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 M  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 M  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 M  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 M  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 M  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 N  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 N  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 N  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 N  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 N  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 N  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 N  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 N  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 N  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 N  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 N  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 O  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 O  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 O  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 O  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 O  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 O  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 O  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 O  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 O  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 O  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 O  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 P  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 P  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 P  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 P  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 P  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 P  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 P  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 P  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 P  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 P  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS THR ALA ARG          
SEQRES  11 P  140  ASP PHE GLN PRO ALA ASN LYS ARG SER VAL                      
MODRES 2VDH HYP G  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2VDH SMC C  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2VDH SMC D  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2VDH MME P    1  MET  N-METHYL METHIONINE                                
MODRES 2VDH HYP B  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2VDH HYP H  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2VDH SMC G  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2VDH HYP E  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2VDH SMC A  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2VDH SMC E  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2VDH MME M    1  MET  N-METHYL METHIONINE                                
MODRES 2VDH HYP H  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2VDH MME N    1  MET  N-METHYL METHIONINE                                
MODRES 2VDH SMC E  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2VDH HYP A  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2VDH SMC B  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2VDH KCX D  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2VDH MME L    1  MET  N-METHYL METHIONINE                                
MODRES 2VDH KCX E  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2VDH HYP C  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2VDH HYP D  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2VDH SMC C  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2VDH KCX F  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2VDH SMC A  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2VDH MME J    1  MET  N-METHYL METHIONINE                                
MODRES 2VDH SMC H  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2VDH KCX A  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2VDH MME I    1  MET  N-METHYL METHIONINE                                
MODRES 2VDH KCX H  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2VDH KCX B  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2VDH HYP E  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2VDH SMC B  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2VDH HYP G  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2VDH HYP A  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2VDH SMC H  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2VDH HYP B  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2VDH HYP C  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2VDH SMC D  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2VDH HYP D  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2VDH KCX C  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2VDH HYP F  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2VDH SMC F  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2VDH SMC G  369  CYS  S-METHYLCYSTEINE                                   
MODRES 2VDH MME K    1  MET  N-METHYL METHIONINE                                
MODRES 2VDH SMC F  256  CYS  S-METHYLCYSTEINE                                   
MODRES 2VDH MME O    1  MET  N-METHYL METHIONINE                                
MODRES 2VDH KCX G  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2VDH HYP F  151  PRO  4-HYDROXYPROLINE                                   
HET    HYP  A 104       8                                                       
HET    HYP  A 151       8                                                       
HET    KCX  A 201      12                                                       
HET    SMC  A 256       7                                                       
HET    SMC  A 369       7                                                       
HET     MG  A1476       1                                                       
HET    CAP  A1477      21                                                       
HET    HYP  B 104       8                                                       
HET    HYP  B 151       8                                                       
HET    KCX  B 201      12                                                       
HET    SMC  B 256       7                                                       
HET    SMC  B 369       7                                                       
HET     MG  B1476       1                                                       
HET    CAP  B1477      21                                                       
HET    HYP  C 104       8                                                       
HET    HYP  C 151       8                                                       
HET    KCX  C 201      12                                                       
HET    SMC  C 256       7                                                       
HET    SMC  C 369       7                                                       
HET     MG  C1476       1                                                       
HET    CAP  C1477      21                                                       
HET    HYP  D 104       8                                                       
HET    HYP  D 151       8                                                       
HET    KCX  D 201      12                                                       
HET    SMC  D 256       7                                                       
HET    SMC  D 369       7                                                       
HET     MG  D1476       1                                                       
HET    CAP  D1477      21                                                       
HET    HYP  E 104       8                                                       
HET    HYP  E 151       8                                                       
HET    KCX  E 201      12                                                       
HET    SMC  E 256       7                                                       
HET    SMC  E 369       7                                                       
HET     MG  E1476       1                                                       
HET    CAP  E1477      21                                                       
HET    HYP  F 104       8                                                       
HET    HYP  F 151       8                                                       
HET    KCX  F 201      12                                                       
HET    SMC  F 256       7                                                       
HET    SMC  F 369       7                                                       
HET     MG  F1476       1                                                       
HET    CAP  F1477      21                                                       
HET    HYP  G 104       8                                                       
HET    HYP  G 151       8                                                       
HET    KCX  G 201      12                                                       
HET    SMC  G 256       7                                                       
HET    SMC  G 369       7                                                       
HET     MG  G1476       1                                                       
HET    CAP  G1477      21                                                       
HET    HYP  H 104       8                                                       
HET    HYP  H 151       8                                                       
HET    KCX  H 201      12                                                       
HET    SMC  H 256       7                                                       
HET    SMC  H 369       7                                                       
HET     MG  H1476       1                                                       
HET    CAP  H1477      21                                                       
HET    MME  I   1       9                                                       
HET    MME  J   1       9                                                       
HET    MME  K   1       9                                                       
HET    MME  L   1       9                                                       
HET    MME  M   1       9                                                       
HET    MME  N   1       9                                                       
HET    MME  O   1       9                                                       
HET    MME  P   1       9                                                       
HET    EDO  A1478       4                                                       
HET    EDO  A1479       4                                                       
HET    EDO  A1480       4                                                       
HET    EDO  A1481       4                                                       
HET    EDO  H1478       4                                                       
HET    EDO  H1479       4                                                       
HET    EDO  H1480       4                                                       
HET    EDO  H1481       4                                                       
HET    EDO  H1482       4                                                       
HET    EDO  G1478       4                                                       
HET    EDO  G1479       4                                                       
HET    EDO  A1482       4                                                       
HET    EDO  G1480       4                                                       
HET    EDO  O1141       4                                                       
HET    EDO  O1142       4                                                       
HET    EDO  E1478       4                                                       
HET    EDO  F1478       4                                                       
HET    EDO  F1479       4                                                       
HET    EDO  F1480       4                                                       
HET    EDO  F1481       4                                                       
HET    EDO  C1478       4                                                       
HET    EDO  C1479       4                                                       
HET    EDO  K1141       4                                                       
HET    EDO  B1478       4                                                       
HET    EDO  B1479       4                                                       
HET    EDO  B1480       4                                                       
HET    EDO  C1480       4                                                       
HET    EDO  J1141       4                                                       
HET    EDO  C1481       4                                                       
HET    EDO  A1483       4                                                       
HET    EDO  D1478       4                                                       
HET    EDO  D1479       4                                                       
HET    EDO  D1480       4                                                       
HET    EDO  E1479       4                                                       
HET    EDO  E1480       4                                                       
HET    EDO  E1481       4                                                       
HET    EDO  E1482       4                                                       
HET    EDO  E1483       4                                                       
HET    EDO  C1482       4                                                       
HET    EDO  M1141       4                                                       
HET    EDO  C1483       4                                                       
HET    EDO  G1481       4                                                       
HET    EDO  G1482       4                                                       
HET    EDO  H1483       4                                                       
HET    EDO  I1141       4                                                       
HET    EDO  K1142       4                                                       
HET    EDO  M1142       4                                                       
HET    EDO  B1481       4                                                       
HET    EDO  B1482       4                                                       
HET    EDO  D1481       4                                                       
HET    EDO  D1482       4                                                       
HET    EDO  L1141       4                                                       
HET    EDO  J1142       4                                                       
HET    EDO  F1482       4                                                       
HET    EDO  N1141       4                                                       
HET    EDO  N1142       4                                                       
HET    EDO  F1483       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                                        
FORMUL  17  EDO    57(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   *1800(H2 O1)                                                  
HELIX    1   1 TYR A   20  TYR A   25  1                                   6    
HELIX    2   2 PRO A   49  SER A   61  1                                  13    
HELIX    3   3 VAL A   69  THR A   75  5                                   7    
HELIX    4   4 SER A   76  LYS A   81  1                                   6    
HELIX    5   5 HYP A  104  PHE A  108  5                                   5    
HELIX    6   6 SER A  112  VAL A  121  1                                  10    
HELIX    7   7 ASN A  123  GLY A  126  5                                   4    
HELIX    8   8 PRO A  141  LYS A  146  1                                   6    
HELIX    9   9 GLY A  154  ASN A  163  1                                  10    
HELIX   10  10 SER A  181  GLY A  195  1                                  15    
HELIX   11  11 ARG A  213  GLY A  233  1                                  21    
HELIX   12  12 THR A  246  GLY A  261  1                                  16    
HELIX   13  13 TYR A  269  GLY A  288  1                                  20    
HELIX   14  14 MET A  297  ARG A  303  1                                   7    
HELIX   15  15 HIS A  310  GLY A  322  1                                  13    
HELIX   16  16 GLU A  338  ASP A  351  1                                  14    
HELIX   17  17 ARG A  358  GLY A  361  5                                   4    
HELIX   18  18 HIS A  383  TRP A  385  5                                   3    
HELIX   19  19 HIS A  386  GLY A  395  1                                  10    
HELIX   20  20 GLY A  403  GLY A  408  1                                   6    
HELIX   21  21 GLY A  412  GLU A  433  1                                  22    
HELIX   22  22 ASP A  436  LYS A  463  1                                  28    
HELIX   23  23 TYR B   20  TYR B   25  1                                   6    
HELIX   24  24 PRO B   49  SER B   61  1                                  13    
HELIX   25  25 VAL B   69  THR B   75  5                                   7    
HELIX   26  26 SER B   76  LYS B   81  1                                   6    
HELIX   27  27 HYP B  104  PHE B  108  5                                   5    
HELIX   28  28 SER B  112  VAL B  121  1                                  10    
HELIX   29  29 ASN B  123  GLY B  126  5                                   4    
HELIX   30  30 PRO B  141  LYS B  146  1                                   6    
HELIX   31  31 GLY B  154  ASN B  163  1                                  10    
HELIX   32  32 SER B  181  GLY B  195  1                                  15    
HELIX   33  33 ARG B  213  GLY B  233  1                                  21    
HELIX   34  34 THR B  246  LEU B  260  1                                  15    
HELIX   35  35 TYR B  269  GLY B  288  1                                  20    
HELIX   36  36 MET B  297  ARG B  303  1                                   7    
HELIX   37  37 HIS B  310  GLY B  322  1                                  13    
HELIX   38  38 GLU B  338  ASP B  351  1                                  14    
HELIX   39  39 ARG B  358  GLY B  361  5                                   4    
HELIX   40  40 HIS B  383  TRP B  385  5                                   3    
HELIX   41  41 HIS B  386  GLY B  395  1                                  10    
HELIX   42  42 GLY B  403  GLY B  408  1                                   6    
HELIX   43  43 GLY B  412  GLU B  433  1                                  22    
HELIX   44  44 ASP B  436  LYS B  463  1                                  28    
HELIX   45  45 TYR C   20  TYR C   25  1                                   6    
HELIX   46  46 PRO C   49  SER C   61  1                                  13    
HELIX   47  47 VAL C   69  THR C   75  5                                   7    
HELIX   48  48 SER C   76  LYS C   81  1                                   6    
HELIX   49  49 HYP C  104  PHE C  108  5                                   5    
HELIX   50  50 SER C  112  GLY C  122  1                                  11    
HELIX   51  51 ASN C  123  GLY C  126  5                                   4    
HELIX   52  52 PRO C  141  LYS C  146  1                                   6    
HELIX   53  53 GLY C  154  ASN C  163  1                                  10    
HELIX   54  54 SER C  181  GLY C  195  1                                  15    
HELIX   55  55 ARG C  213  GLY C  233  1                                  21    
HELIX   56  56 THR C  246  GLY C  261  1                                  16    
HELIX   57  57 TYR C  269  GLY C  288  1                                  20    
HELIX   58  58 MET C  297  ARG C  303  1                                   7    
HELIX   59  59 HIS C  310  GLY C  322  1                                  13    
HELIX   60  60 GLU C  338  ASP C  351  1                                  14    
HELIX   61  61 ARG C  358  GLY C  361  5                                   4    
HELIX   62  62 HIS C  383  TRP C  385  5                                   3    
HELIX   63  63 HIS C  386  GLY C  395  1                                  10    
HELIX   64  64 GLY C  403  GLY C  408  1                                   6    
HELIX   65  65 GLY C  412  GLU C  433  1                                  22    
HELIX   66  66 ASP C  436  LYS C  463  1                                  28    
HELIX   67  67 TYR D   20  TYR D   25  1                                   6    
HELIX   68  68 PRO D   49  SER D   61  1                                  13    
HELIX   69  69 VAL D   69  THR D   75  5                                   7    
HELIX   70  70 SER D   76  LYS D   81  1                                   6    
HELIX   71  71 HYP D  104  PHE D  108  5                                   5    
HELIX   72  72 SER D  112  GLY D  122  1                                  11    
HELIX   73  73 ASN D  123  GLY D  126  5                                   4    
HELIX   74  74 PRO D  141  LYS D  146  1                                   6    
HELIX   75  75 GLY D  154  ASN D  163  1                                  10    
HELIX   76  76 SER D  181  GLY D  195  1                                  15    
HELIX   77  77 ARG D  213  GLY D  233  1                                  21    
HELIX   78  78 THR D  246  GLY D  261  1                                  16    
HELIX   79  79 TYR D  269  GLY D  288  1                                  20    
HELIX   80  80 MET D  297  ARG D  303  1                                   7    
HELIX   81  81 HIS D  310  GLY D  322  1                                  13    
HELIX   82  82 GLU D  338  ASP D  351  1                                  14    
HELIX   83  83 ARG D  358  GLY D  361  5                                   4    
HELIX   84  84 HIS D  383  TRP D  385  5                                   3    
HELIX   85  85 HIS D  386  GLY D  395  1                                  10    
HELIX   86  86 GLY D  403  GLY D  408  1                                   6    
HELIX   87  87 GLY D  412  GLU D  433  1                                  22    
HELIX   88  88 ASP D  436  LYS D  463  1                                  28    
HELIX   89  89 TYR E   20  TYR E   25  1                                   6    
HELIX   90  90 PRO E   49  SER E   61  1                                  13    
HELIX   91  91 VAL E   69  THR E   75  5                                   7    
HELIX   92  92 SER E   76  LYS E   81  1                                   6    
HELIX   93  93 HYP E  104  PHE E  108  5                                   5    
HELIX   94  94 SER E  112  GLY E  122  1                                  11    
HELIX   95  95 ASN E  123  GLY E  126  5                                   4    
HELIX   96  96 PRO E  141  LYS E  146  1                                   6    
HELIX   97  97 GLY E  154  ASN E  163  1                                  10    
HELIX   98  98 SER E  181  GLY E  195  1                                  15    
HELIX   99  99 ARG E  213  GLY E  233  1                                  21    
HELIX  100 100 THR E  246  GLY E  261  1                                  16    
HELIX  101 101 TYR E  269  GLY E  288  1                                  20    
HELIX  102 102 MET E  297  ARG E  303  1                                   7    
HELIX  103 103 HIS E  310  GLY E  322  1                                  13    
HELIX  104 104 GLU E  338  ASP E  351  1                                  14    
HELIX  105 105 ARG E  358  GLY E  361  5                                   4    
HELIX  106 106 HIS E  383  TRP E  385  5                                   3    
HELIX  107 107 HIS E  386  GLY E  395  1                                  10    
HELIX  108 108 GLY E  403  GLY E  408  1                                   6    
HELIX  109 109 GLY E  412  GLU E  433  1                                  22    
HELIX  110 110 ASP E  436  LYS E  463  1                                  28    
HELIX  111 111 TYR F   20  TYR F   25  1                                   6    
HELIX  112 112 PRO F   49  SER F   61  1                                  13    
HELIX  113 113 VAL F   69  THR F   75  5                                   7    
HELIX  114 114 SER F   76  LYS F   81  1                                   6    
HELIX  115 115 HYP F  104  PHE F  108  5                                   5    
HELIX  116 116 SER F  112  VAL F  121  1                                  10    
HELIX  117 117 ASN F  123  GLY F  126  5                                   4    
HELIX  118 118 PRO F  141  LYS F  146  1                                   6    
HELIX  119 119 GLY F  154  ASN F  163  1                                  10    
HELIX  120 120 SER F  181  GLY F  195  1                                  15    
HELIX  121 121 ARG F  213  GLY F  233  1                                  21    
HELIX  122 122 THR F  246  GLY F  261  1                                  16    
HELIX  123 123 TYR F  269  GLY F  288  1                                  20    
HELIX  124 124 MET F  297  ARG F  303  1                                   7    
HELIX  125 125 HIS F  310  GLY F  322  1                                  13    
HELIX  126 126 GLU F  338  ASP F  351  1                                  14    
HELIX  127 127 ARG F  358  GLY F  361  5                                   4    
HELIX  128 128 HIS F  383  TRP F  385  5                                   3    
HELIX  129 129 HIS F  386  GLY F  395  1                                  10    
HELIX  130 130 GLY F  403  GLY F  408  1                                   6    
HELIX  131 131 GLY F  412  GLU F  433  1                                  22    
HELIX  132 132 ASP F  436  LYS F  463  1                                  28    
HELIX  133 133 TYR G   20  TYR G   25  1                                   6    
HELIX  134 134 PRO G   49  SER G   61  1                                  13    
HELIX  135 135 VAL G   69  THR G   75  5                                   7    
HELIX  136 136 SER G   76  LYS G   81  1                                   6    
HELIX  137 137 HYP G  104  PHE G  108  5                                   5    
HELIX  138 138 SER G  112  VAL G  121  1                                  10    
HELIX  139 139 ASN G  123  GLY G  126  5                                   4    
HELIX  140 140 PRO G  141  LYS G  146  1                                   6    
HELIX  141 141 GLY G  154  ASN G  163  1                                  10    
HELIX  142 142 SER G  181  GLY G  195  1                                  15    
HELIX  143 143 ARG G  213  GLY G  233  1                                  21    
HELIX  144 144 THR G  246  GLY G  261  1                                  16    
HELIX  145 145 TYR G  269  GLY G  288  1                                  20    
HELIX  146 146 MET G  297  ARG G  303  1                                   7    
HELIX  147 147 HIS G  310  GLY G  322  1                                  13    
HELIX  148 148 GLU G  338  ASP G  351  1                                  14    
HELIX  149 149 ARG G  358  GLY G  361  5                                   4    
HELIX  150 150 HIS G  383  TRP G  385  5                                   3    
HELIX  151 151 HIS G  386  GLY G  395  1                                  10    
HELIX  152 152 GLY G  403  GLY G  408  1                                   6    
HELIX  153 153 GLY G  412  GLU G  433  1                                  22    
HELIX  154 154 ASP G  436  LYS G  463  1                                  28    
HELIX  155 155 TYR H   20  TYR H   25  1                                   6    
HELIX  156 156 PRO H   49  SER H   61  1                                  13    
HELIX  157 157 VAL H   69  THR H   75  5                                   7    
HELIX  158 158 SER H   76  LYS H   81  1                                   6    
HELIX  159 159 HYP H  104  PHE H  108  5                                   5    
HELIX  160 160 SER H  112  VAL H  121  1                                  10    
HELIX  161 161 ASN H  123  GLY H  126  5                                   4    
HELIX  162 162 PRO H  141  LYS H  146  1                                   6    
HELIX  163 163 GLY H  154  ASN H  163  1                                  10    
HELIX  164 164 SER H  181  GLY H  195  1                                  15    
HELIX  165 165 ARG H  213  GLY H  233  1                                  21    
HELIX  166 166 THR H  246  GLY H  261  1                                  16    
HELIX  167 167 TYR H  269  GLY H  288  1                                  20    
HELIX  168 168 MET H  297  ARG H  303  1                                   7    
HELIX  169 169 HIS H  310  GLY H  322  1                                  13    
HELIX  170 170 GLU H  338  ASP H  351  1                                  14    
HELIX  171 171 ARG H  358  GLY H  361  5                                   4    
HELIX  172 172 HIS H  383  TRP H  385  5                                   3    
HELIX  173 173 HIS H  386  GLY H  395  1                                  10    
HELIX  174 174 GLY H  403  GLY H  408  1                                   6    
HELIX  175 175 GLY H  412  GLU H  433  1                                  22    
HELIX  176 176 ASP H  436  LYS H  463  1                                  28    
HELIX  177 177 THR I   22  ASN I   36  1                                  15    
HELIX  178 178 GLU I   46  ALA I   50  5                                   5    
HELIX  179 179 ASN I   54  PHE I   60  5                                   7    
HELIX  180 180 ASP I   85  PHE I  100  1                                  16    
HELIX  181 181 PRO I  134  ARG I  138  5                                   5    
HELIX  182 182 THR J   22  GLY J   37  1                                  16    
HELIX  183 183 GLU J   46  ALA J   50  5                                   5    
HELIX  184 184 ASN J   54  PHE J   60  5                                   7    
HELIX  185 185 ASP J   85  PHE J  100  1                                  16    
HELIX  186 186 PRO J  134  ARG J  138  5                                   5    
HELIX  187 187 THR K   22  GLY K   37  1                                  16    
HELIX  188 188 GLU K   46  ALA K   50  5                                   5    
HELIX  189 189 ASN K   54  PHE K   60  5                                   7    
HELIX  190 190 ASP K   85  PHE K  100  1                                  16    
HELIX  191 191 PRO K  134  ARG K  138  5                                   5    
HELIX  192 192 THR L   22  ASN L   36  1                                  15    
HELIX  193 193 GLU L   46  ALA L   50  5                                   5    
HELIX  194 194 ASN L   54  PHE L   60  5                                   7    
HELIX  195 195 ASP L   85  PHE L  100  1                                  16    
HELIX  196 196 PRO L  134  ARG L  138  5                                   5    
HELIX  197 197 THR M   22  ASN M   36  1                                  15    
HELIX  198 198 GLU M   46  ALA M   50  5                                   5    
HELIX  199 199 ASN M   54  PHE M   60  5                                   7    
HELIX  200 200 ASP M   85  PHE M  100  1                                  16    
HELIX  201 201 PRO M  134  ARG M  138  5                                   5    
HELIX  202 202 THR N   22  ASN N   36  1                                  15    
HELIX  203 203 GLU N   46  ALA N   50  5                                   5    
HELIX  204 204 ASN N   54  PHE N   60  5                                   7    
HELIX  205 205 ASP N   85  PHE N  100  1                                  16    
HELIX  206 206 PRO N  134  ARG N  138  5                                   5    
HELIX  207 207 THR O   22  GLY O   37  1                                  16    
HELIX  208 208 GLU O   46  ALA O   50  5                                   5    
HELIX  209 209 ASN O   54  PHE O   60  5                                   7    
HELIX  210 210 ASP O   85  PHE O  100  1                                  16    
HELIX  211 211 PRO O  134  ARG O  138  5                                   5    
HELIX  212 212 THR P   22  ASN P   36  1                                  15    
HELIX  213 213 GLU P   46  ALA P   50  5                                   5    
HELIX  214 214 ASN P   54  PHE P   60  5                                   7    
HELIX  215 215 ASP P   85  PHE P  100  1                                  16    
HELIX  216 216 PRO P  134  ARG P  138  5                                   5    
SHEET    1  AA 5 ARG A  83  PRO A  89  0                                        
SHEET    2  AA 5 TYR A  97  TYR A 103 -1  O  ILE A  98   N  GLU A  88           
SHEET    3  AA 5 ILE A  36  PRO A  44 -1  O  ILE A  36   N  TYR A 103           
SHEET    4  AA 5 LEU A 130  ARG A 139 -1  N  ARG A 131   O  THR A  43           
SHEET    5  AA 5 GLY A 308  ILE A 309  1  O  GLY A 308   N  LEU A 135           
SHEET    1  AB 8 LEU A 169  GLY A 171  0                                        
SHEET    2  AB 8 CYS A 399  GLN A 401  1  O  LEU A 400   N  GLY A 171           
SHEET    3  AB 8 MET A 375  SER A 379  1  O  PRO A 376   N  CYS A 399           
SHEET    4  AB 8 HIS A 325  HIS A 327  1  O  LEU A 326   N  VAL A 377           
SHEET    5  AB 8 LEU A 290  HIS A 294  1  O  ILE A 293   N  HIS A 327           
SHEET    6  AB 8 ILE A 264  ASP A 268  1  O  ILE A 265   N  HIS A 292           
SHEET    7  AB 8 GLY A 237  ASN A 241  1  O  LEU A 240   N  MET A 266           
SHEET    8  AB 8 PHE A 199  KCX A 201  1  O  THR A 200   N  TYR A 239           
SHEET    1  AC 2 TYR A 353  VAL A 354  0                                        
SHEET    2  AC 2 GLN A 366  ASP A 367 -1  O  GLN A 366   N  VAL A 354           
SHEET    1  BA 5 ARG B  83  PRO B  89  0                                        
SHEET    2  BA 5 TYR B  97  TYR B 103 -1  O  ILE B  98   N  GLU B  88           
SHEET    3  BA 5 ILE B  36  PRO B  44 -1  O  ILE B  36   N  TYR B 103           
SHEET    4  BA 5 LEU B 130  ARG B 139 -1  N  ARG B 131   O  THR B  43           
SHEET    5  BA 5 GLY B 308  ILE B 309  1  O  GLY B 308   N  LEU B 135           
SHEET    1  BB 8 LEU B 169  GLY B 171  0                                        
SHEET    2  BB 8 CYS B 399  GLN B 401  1  O  LEU B 400   N  GLY B 171           
SHEET    3  BB 8 MET B 375  SER B 379  1  O  PRO B 376   N  CYS B 399           
SHEET    4  BB 8 HIS B 325  HIS B 327  1  O  LEU B 326   N  VAL B 377           
SHEET    5  BB 8 LEU B 290  HIS B 294  1  O  ILE B 293   N  HIS B 327           
SHEET    6  BB 8 ILE B 264  ASP B 268  1  O  ILE B 265   N  HIS B 292           
SHEET    7  BB 8 GLY B 237  ASN B 241  1  O  LEU B 240   N  MET B 266           
SHEET    8  BB 8 PHE B 199  KCX B 201  1  O  THR B 200   N  TYR B 239           
SHEET    1  BC 2 TYR B 353  VAL B 354  0                                        
SHEET    2  BC 2 GLN B 366  ASP B 367 -1  O  GLN B 366   N  VAL B 354           
SHEET    1  CA 5 ARG C  83  PRO C  89  0                                        
SHEET    2  CA 5 TYR C  97  TYR C 103 -1  O  ILE C  98   N  GLU C  88           
SHEET    3  CA 5 ILE C  36  PRO C  44 -1  O  ILE C  36   N  TYR C 103           
SHEET    4  CA 5 LEU C 130  ARG C 139 -1  N  ARG C 131   O  THR C  43           
SHEET    5  CA 5 GLY C 308  ILE C 309  1  O  GLY C 308   N  LEU C 135           
SHEET    1  CB 8 LEU C 169  GLY C 171  0                                        
SHEET    2  CB 8 CYS C 399  GLN C 401  1  O  LEU C 400   N  GLY C 171           
SHEET    3  CB 8 MET C 375  SER C 379  1  O  PRO C 376   N  CYS C 399           
SHEET    4  CB 8 HIS C 325  HIS C 327  1  O  LEU C 326   N  VAL C 377           
SHEET    5  CB 8 LEU C 290  HIS C 294  1  O  ILE C 293   N  HIS C 327           
SHEET    6  CB 8 ILE C 264  ASP C 268  1  O  ILE C 265   N  HIS C 292           
SHEET    7  CB 8 GLY C 237  ASN C 241  1  O  LEU C 240   N  MET C 266           
SHEET    8  CB 8 PHE C 199  KCX C 201  1  O  THR C 200   N  TYR C 239           
SHEET    1  CC 2 TYR C 353  VAL C 354  0                                        
SHEET    2  CC 2 GLN C 366  ASP C 367 -1  O  GLN C 366   N  VAL C 354           
SHEET    1  DA 5 ARG D  83  PRO D  89  0                                        
SHEET    2  DA 5 TYR D  97  TYR D 103 -1  O  ILE D  98   N  GLU D  88           
SHEET    3  DA 5 ILE D  36  PRO D  44 -1  O  ILE D  36   N  TYR D 103           
SHEET    4  DA 5 LEU D 130  ARG D 139 -1  N  ARG D 131   O  THR D  43           
SHEET    5  DA 5 GLY D 308  ILE D 309  1  O  GLY D 308   N  LEU D 135           
SHEET    1  DB 8 LEU D 169  GLY D 171  0                                        
SHEET    2  DB 8 CYS D 399  GLN D 401  1  O  LEU D 400   N  GLY D 171           
SHEET    3  DB 8 MET D 375  SER D 379  1  O  PRO D 376   N  CYS D 399           
SHEET    4  DB 8 HIS D 325  HIS D 327  1  O  LEU D 326   N  VAL D 377           
SHEET    5  DB 8 LEU D 290  HIS D 294  1  O  ILE D 293   N  HIS D 327           
SHEET    6  DB 8 ILE D 264  ASP D 268  1  O  ILE D 265   N  HIS D 292           
SHEET    7  DB 8 GLY D 237  ASN D 241  1  O  LEU D 240   N  MET D 266           
SHEET    8  DB 8 PHE D 199  KCX D 201  1  O  THR D 200   N  TYR D 239           
SHEET    1  DC 2 TYR D 353  VAL D 354  0                                        
SHEET    2  DC 2 GLN D 366  ASP D 367 -1  O  GLN D 366   N  VAL D 354           
SHEET    1  EA 5 ARG E  83  PRO E  89  0                                        
SHEET    2  EA 5 TYR E  97  TYR E 103 -1  O  ILE E  98   N  GLU E  88           
SHEET    3  EA 5 ILE E  36  PRO E  44 -1  O  ILE E  36   N  TYR E 103           
SHEET    4  EA 5 LEU E 130  ARG E 139 -1  N  ARG E 131   O  THR E  43           
SHEET    5  EA 5 GLY E 308  ILE E 309  1  O  GLY E 308   N  LEU E 135           
SHEET    1  EB 8 LEU E 169  GLY E 171  0                                        
SHEET    2  EB 8 CYS E 399  GLN E 401  1  O  LEU E 400   N  GLY E 171           
SHEET    3  EB 8 MET E 375  SER E 379  1  O  PRO E 376   N  CYS E 399           
SHEET    4  EB 8 HIS E 325  HIS E 327  1  O  LEU E 326   N  VAL E 377           
SHEET    5  EB 8 LEU E 290  HIS E 294  1  O  ILE E 293   N  HIS E 327           
SHEET    6  EB 8 ILE E 264  ASP E 268  1  O  ILE E 265   N  HIS E 292           
SHEET    7  EB 8 GLY E 237  ASN E 241  1  O  LEU E 240   N  MET E 266           
SHEET    8  EB 8 PHE E 199  KCX E 201  1  O  THR E 200   N  TYR E 239           
SHEET    1  EC 2 TYR E 353  VAL E 354  0                                        
SHEET    2  EC 2 GLN E 366  ASP E 367 -1  O  GLN E 366   N  VAL E 354           
SHEET    1  FA 5 ARG F  83  PRO F  89  0                                        
SHEET    2  FA 5 TYR F  97  TYR F 103 -1  O  ILE F  98   N  GLU F  88           
SHEET    3  FA 5 ILE F  36  PRO F  44 -1  O  ILE F  36   N  TYR F 103           
SHEET    4  FA 5 LEU F 130  ARG F 139 -1  N  ARG F 131   O  THR F  43           
SHEET    5  FA 5 GLY F 308  ILE F 309  1  O  GLY F 308   N  LEU F 135           
SHEET    1  FB 8 LEU F 169  GLY F 171  0                                        
SHEET    2  FB 8 CYS F 399  GLN F 401  1  O  LEU F 400   N  GLY F 171           
SHEET    3  FB 8 MET F 375  SER F 379  1  O  PRO F 376   N  CYS F 399           
SHEET    4  FB 8 HIS F 325  HIS F 327  1  O  LEU F 326   N  VAL F 377           
SHEET    5  FB 8 LEU F 290  HIS F 294  1  O  ILE F 293   N  HIS F 327           
SHEET    6  FB 8 ILE F 264  ASP F 268  1  O  ILE F 265   N  HIS F 292           
SHEET    7  FB 8 GLY F 237  ASN F 241  1  O  LEU F 240   N  MET F 266           
SHEET    8  FB 8 PHE F 199  KCX F 201  1  O  THR F 200   N  TYR F 239           
SHEET    1  FC 2 TYR F 353  VAL F 354  0                                        
SHEET    2  FC 2 GLN F 366  ASP F 367 -1  O  GLN F 366   N  VAL F 354           
SHEET    1  GA 5 ARG G  83  PRO G  89  0                                        
SHEET    2  GA 5 TYR G  97  TYR G 103 -1  O  ILE G  98   N  GLU G  88           
SHEET    3  GA 5 ILE G  36  PRO G  44 -1  O  ILE G  36   N  TYR G 103           
SHEET    4  GA 5 LEU G 130  ARG G 139 -1  N  ARG G 131   O  THR G  43           
SHEET    5  GA 5 GLY G 308  ILE G 309  1  O  GLY G 308   N  LEU G 135           
SHEET    1  GB 8 LEU G 169  GLY G 171  0                                        
SHEET    2  GB 8 CYS G 399  GLN G 401  1  O  LEU G 400   N  GLY G 171           
SHEET    3  GB 8 MET G 375  SER G 379  1  O  PRO G 376   N  CYS G 399           
SHEET    4  GB 8 HIS G 325  HIS G 327  1  O  LEU G 326   N  VAL G 377           
SHEET    5  GB 8 LEU G 290  HIS G 294  1  O  ILE G 293   N  HIS G 327           
SHEET    6  GB 8 ILE G 264  ASP G 268  1  O  ILE G 265   N  HIS G 292           
SHEET    7  GB 8 GLY G 237  ASN G 241  1  O  LEU G 240   N  MET G 266           
SHEET    8  GB 8 PHE G 199  KCX G 201  1  O  THR G 200   N  TYR G 239           
SHEET    1  GC 2 TYR G 353  VAL G 354  0                                        
SHEET    2  GC 2 GLN G 366  ASP G 367 -1  O  GLN G 366   N  VAL G 354           
SHEET    1  HA 5 ARG H  83  PRO H  89  0                                        
SHEET    2  HA 5 TYR H  97  TYR H 103 -1  O  ILE H  98   N  GLU H  88           
SHEET    3  HA 5 ILE H  36  PRO H  44 -1  O  ILE H  36   N  TYR H 103           
SHEET    4  HA 5 LEU H 130  ARG H 139 -1  N  ARG H 131   O  THR H  43           
SHEET    5  HA 5 GLY H 308  ILE H 309  1  O  GLY H 308   N  LEU H 135           
SHEET    1  HB 8 LEU H 169  GLY H 171  0                                        
SHEET    2  HB 8 CYS H 399  GLN H 401  1  O  LEU H 400   N  GLY H 171           
SHEET    3  HB 8 MET H 375  SER H 379  1  O  PRO H 376   N  CYS H 399           
SHEET    4  HB 8 HIS H 325  HIS H 327  1  O  LEU H 326   N  VAL H 377           
SHEET    5  HB 8 LEU H 290  HIS H 294  1  O  ILE H 293   N  HIS H 327           
SHEET    6  HB 8 ILE H 264  ASP H 268  1  O  ILE H 265   N  HIS H 292           
SHEET    7  HB 8 GLY H 237  ASN H 241  1  O  LEU H 240   N  MET H 266           
SHEET    8  HB 8 PHE H 199  KCX H 201  1  O  THR H 200   N  TYR H 239           
SHEET    1  HC 2 TYR H 353  VAL H 354  0                                        
SHEET    2  HC 2 GLN H 366  ASP H 367 -1  O  GLN H 366   N  VAL H 354           
SHEET    1  IA 4 THR I  74  TRP I  76  0                                        
SHEET    2  IA 4 ILE I  39  ALA I  45 -1  O  LEU I  42   N  TRP I  76           
SHEET    3  IA 4 TYR I 104  ASP I 111 -1  O  TYR I 104   N  ALA I  45           
SHEET    4  IA 4 VAL I 116  GLN I 124 -1  O  VAL I 116   N  ASP I 111           
SHEET    1  JA 4 THR J  74  TRP J  76  0                                        
SHEET    2  JA 4 ILE J  39  ALA J  45 -1  O  LEU J  42   N  TRP J  76           
SHEET    3  JA 4 TYR J 104  ASP J 111 -1  O  TYR J 104   N  ALA J  45           
SHEET    4  JA 4 VAL J 116  GLN J 124 -1  O  VAL J 116   N  ASP J 111           
SHEET    1  KA 4 THR K  74  TRP K  76  0                                        
SHEET    2  KA 4 ILE K  39  ALA K  45 -1  O  LEU K  42   N  TRP K  76           
SHEET    3  KA 4 TYR K 104  ASP K 111 -1  O  TYR K 104   N  ALA K  45           
SHEET    4  KA 4 VAL K 116  GLN K 124 -1  O  VAL K 116   N  ASP K 111           
SHEET    1  LA 4 THR L  74  TRP L  76  0                                        
SHEET    2  LA 4 ILE L  39  ALA L  45 -1  O  LEU L  42   N  TRP L  76           
SHEET    3  LA 4 TYR L 104  ASP L 111 -1  O  TYR L 104   N  ALA L  45           
SHEET    4  LA 4 VAL L 116  GLN L 124 -1  O  VAL L 116   N  ASP L 111           
SHEET    1  MA 4 THR M  74  TRP M  76  0                                        
SHEET    2  MA 4 ILE M  39  ALA M  45 -1  O  LEU M  42   N  TRP M  76           
SHEET    3  MA 4 TYR M 104  ASP M 111 -1  O  TYR M 104   N  ALA M  45           
SHEET    4  MA 4 VAL M 116  GLN M 124 -1  O  VAL M 116   N  ASP M 111           
SHEET    1  NA 4 THR N  74  TRP N  76  0                                        
SHEET    2  NA 4 ILE N  39  ALA N  45 -1  O  LEU N  42   N  TRP N  76           
SHEET    3  NA 4 TYR N 104  ASP N 111 -1  O  TYR N 104   N  ALA N  45           
SHEET    4  NA 4 VAL N 116  GLN N 124 -1  O  VAL N 116   N  ASP N 111           
SHEET    1  OA 4 THR O  74  TRP O  76  0                                        
SHEET    2  OA 4 ILE O  39  ALA O  45 -1  O  LEU O  42   N  TRP O  76           
SHEET    3  OA 4 TYR O 104  ASP O 111 -1  O  TYR O 104   N  ALA O  45           
SHEET    4  OA 4 VAL O 116  GLN O 124 -1  O  VAL O 116   N  ASP O 111           
SHEET    1  PA 4 THR P  74  TRP P  76  0                                        
SHEET    2  PA 4 ILE P  39  ALA P  45 -1  O  LEU P  42   N  TRP P  76           
SHEET    3  PA 4 TYR P 104  ASP P 111 -1  O  TYR P 104   N  ALA P  45           
SHEET    4  PA 4 VAL P 116  GLN P 124 -1  O  VAL P 116   N  ASP P 111           
SSBOND   1 CYS A  247    CYS B  247                          1555   1555  2.09  
SSBOND   2 CYS A  449    CYS A  459                          1555   1555  2.07  
SSBOND   3 CYS B  449    CYS B  459                          1555   1555  2.06  
SSBOND   4 CYS C  247    CYS D  247                          1555   1555  2.06  
SSBOND   5 CYS C  449    CYS C  459                          1555   1555  2.07  
SSBOND   6 CYS D  449    CYS D  459                          1555   1555  2.08  
SSBOND   7 CYS E  247    CYS F  247                          1555   1555  2.06  
SSBOND   8 CYS E  449    CYS E  459                          1555   1555  2.07  
SSBOND   9 CYS F  449    CYS F  459                          1555   1555  2.07  
SSBOND  10 CYS G  247    CYS H  247                          1555   1555  2.09  
SSBOND  11 CYS G  449    CYS G  459                          1555   1555  2.07  
SSBOND  12 CYS H  449    CYS H  459                          1555   1555  2.07  
LINK         C   TYR A 103                 N   HYP A 104     1555   1555  1.36  
LINK         C   HYP A 104                 N   ILE A 105     1555   1555  1.33  
LINK         C   GLY A 150                 N   HYP A 151     1555   1555  1.35  
LINK         C   HYP A 151                 N   PRO A 152     1555   1555  1.35  
LINK         C   THR A 200                 N   KCX A 201     1555   1555  1.33  
LINK         C   KCX A 201                 N   ASP A 202     1555   1555  1.34  
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 A1476                 OE1 GLU A 204     1555   1555  2.10  
LINK        MG    MG A1476                 O7  CAP A1477     1555   1555  2.07  
LINK        MG    MG A1476                 C   CAP A1477     1555   1555  2.80  
LINK        MG    MG A1476                 OD1 ASP A 203     1555   1555  1.94  
LINK        MG    MG A1476                 OQ1 KCX A 201     1555   1555  2.10  
LINK        MG    MG A1476                 O3  CAP A1477     1555   1555  2.24  
LINK        MG    MG A1476                 O2  CAP A1477     1555   1555  2.21  
LINK        MG    MG A1476                 C2  CAP A1477     1555   1555  2.81  
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  1.35  
LINK         C   HYP B 151                 N   PRO B 152     1555   1555  1.35  
LINK         C   THR B 200                 N   KCX B 201     1555   1555  1.32  
LINK         C   KCX B 201                 N   ASP B 202     1555   1555  1.34  
LINK         C   VAL B 255                 N   SMC B 256     1555   1555  1.34  
LINK         C   SMC B 256                 N   ALA B 257     1555   1555  1.33  
LINK         C   TRP B 368                 N   SMC B 369     1555   1555  1.34  
LINK         C   SMC B 369                 N   SER B 370     1555   1555  1.33  
LINK        MG    MG B1476                 OQ1 KCX B 201     1555   1555  1.89  
LINK        MG    MG B1476                 O2  CAP B1477     1555   1555  2.24  
LINK        MG    MG B1476                 O3  CAP B1477     1555   1555  2.16  
LINK        MG    MG B1476                 C2  CAP B1477     1555   1555  2.85  
LINK        MG    MG B1476                 O7  CAP B1477     1555   1555  2.27  
LINK        MG    MG B1476                 OD1 ASP B 203     1555   1555  1.97  
LINK        MG    MG B1476                 OE1 GLU B 204     1555   1555  2.04  
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  1.35  
LINK         C   HYP C 151                 N   PRO C 152     1555   1555  1.35  
LINK         C   THR C 200                 N   KCX C 201     1555   1555  1.33  
LINK         C   KCX C 201                 N   ASP C 202     1555   1555  1.34  
LINK         C   VAL C 255                 N   SMC C 256     1555   1555  1.34  
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 C1476                 OD1 ASP C 203     1555   1555  1.94  
LINK        MG    MG C1476                 OE1 GLU C 204     1555   1555  2.00  
LINK        MG    MG C1476                 C   CAP C1477     1555   1555  2.84  
LINK        MG    MG C1476                 O7  CAP C1477     1555   1555  2.13  
LINK        MG    MG C1476                 OQ1 KCX C 201     1555   1555  1.99  
LINK        MG    MG C1476                 O3  CAP C1477     1555   1555  2.28  
LINK        MG    MG C1476                 O2  CAP C1477     1555   1555  2.16  
LINK        MG    MG C1476                 C2  CAP C1477     1555   1555  2.83  
LINK         C   TYR D 103                 N   HYP D 104     1555   1555  1.35  
LINK         C   HYP D 104                 N   ILE D 105     1555   1555  1.33  
LINK         C   GLY D 150                 N   HYP D 151     1555   1555  1.35  
LINK         C   HYP D 151                 N   PRO D 152     1555   1555  1.35  
LINK         C   THR D 200                 N   KCX D 201     1555   1555  1.33  
LINK         C   KCX D 201                 N   ASP D 202     1555   1555  1.34  
LINK         C   VAL D 255                 N   SMC D 256     1555   1555  1.33  
LINK         C   SMC D 256                 N   ALA D 257     1555   1555  1.33  
LINK         C   TRP D 368                 N   SMC D 369     1555   1555  1.33  
LINK         C   SMC D 369                 N   SER D 370     1555   1555  1.33  
LINK        MG    MG D1476                 O3  CAP D1477     1555   1555  2.16  
LINK        MG    MG D1476                 C   CAP D1477     1555   1555  2.87  
LINK        MG    MG D1476                 O7  CAP D1477     1555   1555  2.16  
LINK        MG    MG D1476                 OQ1 KCX D 201     1555   1555  2.05  
LINK        MG    MG D1476                 O2  CAP D1477     1555   1555  2.28  
LINK        MG    MG D1476                 OD1 ASP D 203     1555   1555  1.97  
LINK        MG    MG D1476                 C2  CAP D1477     1555   1555  2.87  
LINK        MG    MG D1476                 OE1 GLU D 204     1555   1555  1.98  
LINK         C   TYR E 103                 N   HYP E 104     1555   1555  1.34  
LINK         C   HYP E 104                 N   ILE E 105     1555   1555  1.33  
LINK         C   GLY E 150                 N   HYP E 151     1555   1555  1.34  
LINK         C   HYP E 151                 N   PRO E 152     1555   1555  1.34  
LINK         C   THR E 200                 N   KCX E 201     1555   1555  1.33  
LINK         C   KCX E 201                 N   ASP E 202     1555   1555  1.34  
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  1.33  
LINK         C   SMC E 369                 N   SER E 370     1555   1555  1.33  
LINK        MG    MG E1476                 OQ1 KCX E 201     1555   1555  1.96  
LINK        MG    MG E1476                 O7  CAP E1477     1555   1555  2.11  
LINK        MG    MG E1476                 C   CAP E1477     1555   1555  2.86  
LINK        MG    MG E1476                 O2  CAP E1477     1555   1555  2.35  
LINK        MG    MG E1476                 O3  CAP E1477     1555   1555  2.13  
LINK        MG    MG E1476                 OD1 ASP E 203     1555   1555  2.00  
LINK        MG    MG E1476                 OE1 GLU E 204     1555   1555  2.04  
LINK         C   TYR F 103                 N   HYP F 104     1555   1555  1.35  
LINK         C   HYP F 104                 N   ILE F 105     1555   1555  1.34  
LINK         C   GLY F 150                 N   HYP F 151     1555   1555  1.35  
LINK         C   HYP F 151                 N   PRO F 152     1555   1555  1.36  
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  1.33  
LINK         C   TRP F 368                 N   SMC F 369     1555   1555  1.33  
LINK         C   SMC F 369                 N   SER F 370     1555   1555  1.33  
LINK        MG    MG F1476                 O7  CAP F1477     1555   1555  2.10  
LINK        MG    MG F1476                 C   CAP F1477     1555   1555  2.77  
LINK        MG    MG F1476                 O2  CAP F1477     1555   1555  2.16  
LINK        MG    MG F1476                 OD1 ASP F 203     1555   1555  1.90  
LINK        MG    MG F1476                 OE1 GLU F 204     1555   1555  2.15  
LINK        MG    MG F1476                 O3  CAP F1477     1555   1555  2.24  
LINK        MG    MG F1476                 C2  CAP F1477     1555   1555  2.77  
LINK        MG    MG F1476                 OQ1 KCX F 201     1555   1555  2.15  
LINK         C   TYR G 103                 N   HYP G 104     1555   1555  1.34  
LINK         C   HYP G 104                 N   ILE G 105     1555   1555  1.33  
LINK         C   GLY G 150                 N   HYP G 151     1555   1555  1.35  
LINK         C   HYP G 151                 N   PRO G 152     1555   1555  1.35  
LINK         C   THR G 200                 N   KCX G 201     1555   1555  1.33  
LINK         C   KCX G 201                 N   ASP G 202     1555   1555  1.33  
LINK         C   VAL G 255                 N   SMC G 256     1555   1555  1.34  
LINK         C   SMC G 256                 N   ALA G 257     1555   1555  1.34  
LINK         C   TRP G 368                 N   SMC G 369     1555   1555  1.33  
LINK         C   SMC G 369                 N   SER G 370     1555   1555  1.33  
LINK        MG    MG G1476                 O2  CAP G1477     1555   1555  2.30  
LINK        MG    MG G1476                 OE1 GLU G 204     1555   1555  2.05  
LINK        MG    MG G1476                 O3  CAP G1477     1555   1555  2.26  
LINK        MG    MG G1476                 O7  CAP G1477     1555   1555  2.14  
LINK        MG    MG G1476                 C2  CAP G1477     1555   1555  2.88  
LINK        MG    MG G1476                 C   CAP G1477     1555   1555  2.87  
LINK        MG    MG G1476                 OQ1 KCX G 201     1555   1555  2.07  
LINK        MG    MG G1476                 OD1 ASP G 203     1555   1555  1.84  
LINK         C   TYR H 103                 N   HYP H 104     1555   1555  1.35  
LINK         C   HYP H 104                 N   ILE H 105     1555   1555  1.33  
LINK         C   GLY H 150                 N   HYP H 151     1555   1555  1.35  
LINK         C   HYP H 151                 N   PRO H 152     1555   1555  1.34  
LINK         C   THR H 200                 N   KCX H 201     1555   1555  1.33  
LINK         C   KCX H 201                 N   ASP H 202     1555   1555  1.33  
LINK         C   VAL H 255                 N   SMC H 256     1555   1555  1.33  
LINK         C   SMC H 256                 N   ALA H 257     1555   1555  1.33  
LINK         C   TRP H 368                 N   SMC H 369     1555   1555  1.33  
LINK         C   SMC H 369                 N   SER H 370     1555   1555  1.33  
LINK        MG    MG H1476                 O7  CAP H1477     1555   1555  2.18  
LINK        MG    MG H1476                 OE1 GLU H 204     1555   1555  2.03  
LINK        MG    MG H1476                 OD1 ASP H 203     1555   1555  1.95  
LINK        MG    MG H1476                 C   CAP H1477     1555   1555  2.89  
LINK        MG    MG H1476                 O2  CAP H1477     1555   1555  2.25  
LINK        MG    MG H1476                 C2  CAP H1477     1555   1555  2.86  
LINK        MG    MG H1476                 O3  CAP H1477     1555   1555  2.15  
LINK        MG    MG H1476                 OQ1 KCX H 201     1555   1555  2.04  
LINK         C   MME I   1                 N   MET I   2     1555   1555  1.32  
LINK         C   MME J   1                 N   MET J   2     1555   1555  1.33  
LINK         C   MME K   1                 N   MET K   2     1555   1555  1.33  
LINK         C   MME L   1                 N   MET L   2     1555   1555  1.33  
LINK         C   MME M   1                 N   MET M   2     1555   1555  1.33  
LINK         C   MME N   1                 N   MET N   2     1555   1555  1.33  
LINK         C   MME O   1                 N   MET O   2     1555   1555  1.32  
LINK         C   MME P   1                 N   MET P   2     1555   1555  1.32  
CISPEP   1 LYS A  175    PRO A  176          0        -1.98                     
CISPEP   2 LYS B  175    PRO B  176          0        -3.92                     
CISPEP   3 LYS C  175    PRO C  176          0        -2.23                     
CISPEP   4 LYS D  175    PRO D  176          0        -1.05                     
CISPEP   5 LYS E  175    PRO E  176          0        -3.08                     
CISPEP   6 LYS F  175    PRO F  176          0        -0.83                     
CISPEP   7 LYS G  175    PRO G  176          0        -2.28                     
CISPEP   8 LYS H  175    PRO H  176          0        -0.19                     
SITE     1 AC1  5 LYS A 177  KCX A 201  ASP A 203  GLU A 204                    
SITE     2 AC1  5 CAP A1477                                                     
SITE     1 AC2 29 THR A 173  LYS A 175  LYS A 177  KCX A 201                    
SITE     2 AC2 29 ASP A 203  GLU A 204  HIS A 294  ARG A 295                    
SITE     3 AC2 29 HIS A 327  LYS A 334  LEU A 335  SER A 379                    
SITE     4 AC2 29 GLY A 380  GLY A 381  GLY A 403  GLY A 404                    
SITE     5 AC2 29  MG A1476  HOH A2138  HOH A2139  HOH A2166                    
SITE     6 AC2 29 HOH A2167  HOH A2168  HOH A2169  GLU B  60                    
SITE     7 AC2 29 THR B  65  TRP B  66  ASN B 123  HOH B2021                    
SITE     8 AC2 29 HOH B2054                                                     
SITE     1 AC3  4 KCX B 201  ASP B 203  GLU B 204  CAP B1477                    
SITE     1 AC4 31 GLU A  60  THR A  65  TRP A  66  ASN A 123                    
SITE     2 AC4 31 HOH A2017  HOH A2046  THR B 173  LYS B 175                    
SITE     3 AC4 31 LYS B 177  KCX B 201  ASP B 203  GLU B 204                    
SITE     4 AC4 31 HIS B 294  ARG B 295  HIS B 327  LYS B 334                    
SITE     5 AC4 31 LEU B 335  SER B 379  GLY B 380  GLY B 381                    
SITE     6 AC4 31 GLY B 403  GLY B 404   MG B1476  HOH B2079                    
SITE     7 AC4 31 HOH B2122  HOH B2124  HOH B2155  HOH B2157                    
SITE     8 AC4 31 HOH B2186  HOH B2187  HOH B2188                               
SITE     1 AC5  5 LYS C 177  KCX C 201  ASP C 203  GLU C 204                    
SITE     2 AC5  5 CAP C1477                                                     
SITE     1 AC6 28 THR C 173  LYS C 175  LYS C 177  KCX C 201                    
SITE     2 AC6 28 ASP C 203  GLU C 204  HIS C 294  ARG C 295                    
SITE     3 AC6 28 HIS C 327  LYS C 334  LEU C 335  SER C 379                    
SITE     4 AC6 28 GLY C 380  GLY C 381  GLY C 403  GLY C 404                    
SITE     5 AC6 28  MG C1476  HOH C2062  HOH C2063  HOH C2131                    
SITE     6 AC6 28 HOH C2139  HOH C2154  HOH C2155  HOH C2156                    
SITE     7 AC6 28 GLU D  60  THR D  65  TRP D  66  ASN D 123                    
SITE     1 AC7  5 LYS D 177  KCX D 201  ASP D 203  GLU D 204                    
SITE     2 AC7  5 CAP D1477                                                     
SITE     1 AC8 27 GLU C  60  THR C  65  TRP C  66  ASN C 123                    
SITE     2 AC8 27 THR D 173  LYS D 175  LYS D 177  KCX D 201                    
SITE     3 AC8 27 ASP D 203  GLU D 204  HIS D 294  ARG D 295                    
SITE     4 AC8 27 HIS D 327  LYS D 334  LEU D 335  SER D 379                    
SITE     5 AC8 27 GLY D 380  GLY D 381  GLY D 403  GLY D 404                    
SITE     6 AC8 27  MG D1476  HOH D2060  HOH D2134  HOH D2135                    
SITE     7 AC8 27 HOH D2141  HOH D2167  HOH D2168                               
SITE     1 AC9  5 LYS E 177  KCX E 201  ASP E 203  GLU E 204                    
SITE     2 AC9  5 CAP E1477                                                     
SITE     1 BC1 27 THR E 173  LYS E 175  LYS E 177  KCX E 201                    
SITE     2 BC1 27 ASP E 203  GLU E 204  HIS E 294  ARG E 295                    
SITE     3 BC1 27 HIS E 327  LYS E 334  LEU E 335  SER E 379                    
SITE     4 BC1 27 GLY E 380  GLY E 381  GLY E 403  GLY E 404                    
SITE     5 BC1 27  MG E1476  HOH E2140  HOH E2173  HOH E2174                    
SITE     6 BC1 27 HOH E2175  HOH E2176  GLU F  60  THR F  65                    
SITE     7 BC1 27 TRP F  66  ASN F 123  HOH F2022                               
SITE     1 BC2  5 LYS F 177  KCX F 201  ASP F 203  GLU F 204                    
SITE     2 BC2  5 CAP F1477                                                     
SITE     1 BC3 28 GLU E  60  THR E  65  TRP E  66  ASN E 123                    
SITE     2 BC3 28 HOH E2025  THR F 173  LYS F 175  LYS F 177                    
SITE     3 BC3 28 KCX F 201  ASP F 203  GLU F 204  HIS F 294                    
SITE     4 BC3 28 ARG F 295  HIS F 327  LYS F 334  LEU F 335                    
SITE     5 BC3 28 SER F 379  GLY F 380  GLY F 381  GLY F 403                    
SITE     6 BC3 28 GLY F 404   MG F1476  HOH F2071  HOH F2146                    
SITE     7 BC3 28 HOH F2171  HOH F2172  HOH F2173  HOH F2174                    
SITE     1 BC4  5 LYS G 177  KCX G 201  ASP G 203  GLU G 204                    
SITE     2 BC4  5 CAP G1477                                                     
SITE     1 BC5 29 THR G 173  LYS G 175  LYS G 177  KCX G 201                    
SITE     2 BC5 29 ASP G 203  GLU G 204  HIS G 294  ARG G 295                    
SITE     3 BC5 29 HIS G 327  LYS G 334  LEU G 335  SER G 379                    
SITE     4 BC5 29 GLY G 380  GLY G 381  GLY G 403  GLY G 404                    
SITE     5 BC5 29  MG G1476  HOH G2073  HOH G2116  HOH G2149                    
SITE     6 BC5 29 HOH G2174  HOH G2175  HOH G2176  GLU H  60                    
SITE     7 BC5 29 THR H  65  TRP H  66  ASN H 123  HOH H2023                    
SITE     8 BC5 29 HOH H2056                                                     
SITE     1 BC6  5 LYS H 177  KCX H 201  ASP H 203  GLU H 204                    
SITE     2 BC6  5 CAP H1477                                                     
SITE     1 BC7 29 GLU G  60  THR G  65  TRP G  66  ASN G 123                    
SITE     2 BC7 29 HOH G2022  HOH G2049  THR H 173  LYS H 175                    
SITE     3 BC7 29 LYS H 177  KCX H 201  ASP H 203  GLU H 204                    
SITE     4 BC7 29 HIS H 294  ARG H 295  HIS H 327  LYS H 334                    
SITE     5 BC7 29 LEU H 335  SER H 379  GLY H 380  GLY H 381                    
SITE     6 BC7 29 GLY H 403  GLY H 404   MG H1476  HOH H2156                    
SITE     7 BC7 29 HOH H2166  HOH H2181  HOH H2182  HOH H2183                    
SITE     8 BC7 29 HOH H2184                                                     
SITE     1 BC8  8 THR A  65  THR A  67  THR A  68  VAL A  69                    
SITE     2 BC8  8 ASP A  72  HOH A2022  HOH A2170  HOH A2171                    
SITE     1 BC9  7 LYS A  18  THR A  65  TRP A  66  THR A  67                    
SITE     2 BC9  7 THR A  68  HOH A2006  HOH A2171                               
SITE     1 CC1  2 GLU A  52  HOH B2192                                          
SITE     1 CC2  7 PHE A 311  GLU A 336  GLY A 337  PHE A 345                    
SITE     2 CC2  7 ASP A 473  HOH A2172  HOH A2173                               
SITE     1 CC3  6 TYR H  24  THR H  68  VAL H  69  ASP H  72                    
SITE     2 CC3  6 HOH H2185  HOH H2186                                          
SITE     1 CC4  7 GLY H  16  LYS H  18  THR H  65  TRP H  66                    
SITE     2 CC4  7 THR H  67  THR H  68  HOH H2187                               
SITE     1 CC5  1 GLU H  52                                                     
SITE     1 CC6  5 LYS H 466  PHE H 467  GLU H 468  PHE H 469                    
SITE     2 CC6  5 HOH H2188                                                     
SITE     1 CC7  4 ARG H 295  GLU H 336  PHE H 345  ASP H 473                    
SITE     1 CC8  7 TYR G  24  THR G  68  VAL G  69  ASP G  72                    
SITE     2 CC8  7 HOH G2030  HOH G2177  HOH G2178                               
SITE     1 CC9  7 LYS G  18  THR G  65  TRP G  66  THR G  67                    
SITE     2 CC9  7 THR G  68  HOH G2178  HOH G2179                               
SITE     1 DC1  5 LYS A 466  PHE A 467  GLU A 468  PHE A 469                    
SITE     2 DC1  5 HOH A2174                                                     
SITE     1 DC2  6 ARG G 295  SER G 328  GLY G 329  GLU G 336                    
SITE     2 DC2  6 PHE G 345  HOH G2134                                          
SITE     1 DC3  5 TYR A 226  LYS A 227  LYS O  49  GLU O  55                    
SITE     2 DC3  5 ASP O  69                                                     
SITE     1 DC4  5 GLY O  37  TRP O  38  ILE O  39  PHE O  81                    
SITE     2 DC4  5 GLY O  82                                                     
SITE     1 DC5  4 LEU E 270  HOH E2177  HOH E2178  LEU F 270                    
SITE     1 DC6  7 TYR F  24  THR F  68  VAL F  69  ASP F  72                    
SITE     2 DC6  7 HOH F2023  HOH F2028  HOH F2175                               
SITE     1 DC7  9 GLY F  16  VAL F  17  LYS F  18  THR F  65                    
SITE     2 DC7  9 TRP F  66  THR F  67  THR F  68  HOH F2023                    
SITE     3 DC7  9 HOH F2176                                                     
SITE     1 DC8  3 LYS F 466  GLU F 468  PHE F 469                               
SITE     1 DC9  5 ARG F 295  SER F 328  GLU F 336  ASP F 473                    
SITE     2 DC9  5 HOH F2177                                                     
SITE     1 EC1  7 TYR C  24  THR C  68  VAL C  69  ASP C  72                    
SITE     2 EC1  7 HOH C2018  HOH C2020  HOH C2027                               
SITE     1 EC2  7 VAL C  17  LYS C  18  TRP C  66  THR C  67                    
SITE     2 EC2  7 THR C  68  HOH C2018  HOH C2157                               
SITE     1 EC3  6 GLY K  37  TRP K  38  ILE K  39  PHE K  81                    
SITE     2 EC3  6 GLY K  82  CYS K  83                                          
SITE     1 EC4  6 TYR B  24  THR B  68  VAL B  69  ASP B  72                    
SITE     2 EC4  6 HOH B2189  HOH B2190                                          
SITE     1 EC5  8 VAL B  17  LYS B  18  THR B  65  TRP B  66                    
SITE     2 EC5  8 THR B  67  THR B  68  HOH B2007  HOH B2190                    
SITE     1 EC6  3 HOH A2174  GLU B  52  ALA B 129                               
SITE     1 EC7  2 GLU C  52  PHE D 469                                          
SITE     1 EC8  5 LYS H 227  LYS J  49  GLU J  55  ASP J  69                    
SITE     2 EC8  5 HOH J2019                                                     
SITE     1 EC9  4 LEU C 270  HOH C2159  LEU D 270  HOH D2096                    
SITE     1 FC1  4 LEU A 270  HOH A2175  HOH A2176  LEU B 270                    
SITE     1 FC2  8 GLY D  16  LYS D  18  TRP D  66  THR D  67                    
SITE     2 FC2  8 THR D  68  EDO D1481  HOH D2016  HOH D2169                    
SITE     1 FC3  2 TYR D  20  GLU D  52                                          
SITE     1 FC4  5 LYS D 466  PHE D 467  GLU D 468  PHE D 469                    
SITE     2 FC4  5 HOH D2170                                                     
SITE     1 FC5  7 TYR E  24  THR E  68  VAL E  69  ASP E  72                    
SITE     2 FC5  7 EDO E1480  HOH E2029  HOH E2035                               
SITE     1 FC6  7 LYS E  18  TYR E  20  THR E  65  TRP E  66                    
SITE     2 FC6  7 THR E  67  THR E  68  EDO E1479                               
SITE     1 FC7  2 TYR E  20  GLU E  52                                          
SITE     1 FC8  3 LYS E 466  GLU E 468  PHE E 469                               
SITE     1 FC9  6 ARG E 295  GLU E 336  PHE E 345  ASP E 473                    
SITE     2 FC9  6 HOH E2122  HOH E2180                                          
SITE     1 GC1  3 LYS C 466  GLU C 468  PHE C 469                               
SITE     1 GC2  4 GLY M  37  TRP M  38  ILE M  39  GLY M  82                    
SITE     1 GC3  5 ARG C 295  HIS C 298  PHE C 345  ASP C 473                    
SITE     2 GC3  5 HOH C2106                                                     
SITE     1 GC4  3 GLU G  52  ALA G 129  HOH H2188                               
SITE     1 GC5  5 LYS G 466  PHE G 467  GLU G 468  PHE G 469                    
SITE     2 GC5  5 HOH G2180                                                     
SITE     1 GC6  4 LEU G 270  LEU H 270  HOH H2189  HOH H2190                    
SITE     1 GC7  5 TYR C 226  LYS I  49  GLU I  55  SER I  56                    
SITE     2 GC7  5 ASP I  69                                                     
SITE     1 GC8  4 LYS K  49  GLU K  55  ASN K  70  HOH K2022                    
SITE     1 GC9  5 TYR G 226  HOH G2093  LYS M  49  GLU M  55                    
SITE     2 GC9  5 HOH M2030                                                     
SITE     1 HC1  4 LYS B 466  PHE B 467  GLU B 468  HOH B2192                    
SITE     1 HC2  3 ARG B 295  GLY B 337  ASP B 473                               
SITE     1 HC3 10 TYR D  24  GLY D  64  THR D  68  VAL D  69                    
SITE     2 HC3 10 ASP D  72  LEU D  77  EDO D1478  HOH D2016                    
SITE     3 HC3 10 HOH D2018  HOH D2020                                          
SITE     1 HC4  4 ARG D 295  GLU D 336  ASP D 473  HOH D2171                    
SITE     1 HC5  5 TYR B 226  LYS B 227  LYS L  49  GLU L  55                    
SITE     2 HC5  5 HOH L2024                                                     
SITE     1 HC6  5 GLY J  37  TRP J  38  ILE J  39  PHE J  81                    
SITE     2 HC6  5 GLY J  82                                                     
SITE     1 HC7  1 GLU F  52                                                     
SITE     1 HC8  6 LYS D 227  LYS N  49  GLU N  55  ASP N  69                    
SITE     2 HC8  6 HOH N2028  HOH N2029                                          
SITE     1 HC9  3 ILE N  39  GLY N  82  CYS N  83                               
SITE     1 IC1  6 TYR F 226  LYS F 227  ALA F 230  LYS P  49                    
SITE     2 IC1  6 GLU P  55  HOH P2027                                          
CRYST1  120.190  178.349  122.561  90.00 117.87  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      0.008320  0.000000  0.004400        0.00000                         
SCALE2      0.000000  0.005607  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009230        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 -0.777200  0.291900 -0.557500       53.62000    1                    
MTRIX2   2  0.291900 -0.617700 -0.730200        9.92100    1                    
MTRIX3   2 -0.557500 -0.730300  0.394900       26.67000    1                    
MTRIX1   3  0.095300 -0.295100  0.950700       -0.80700    1                    
MTRIX2   3  0.776800  0.619300  0.114400      -20.55000    1                    
MTRIX3   3 -0.622500  0.727600  0.288200       30.50000    1                    
MTRIX1   4 -0.691000 -0.486300  0.534900       26.83000    1                    
MTRIX2   4 -0.484200 -0.238100  0.842000       30.37000    1                    
MTRIX3   4  0.536800 -0.840700 -0.070970       12.08000    1                    
MTRIX1   5 -0.810700  0.483700  0.329900       34.23000    1                    
MTRIX2   5  0.484800  0.238800  0.841400      -30.50000    1                    
MTRIX3   5  0.328200  0.842000 -0.428100       24.92000    1                    
MTRIX1   6  0.586600 -0.777400  0.227100        4.43400    1                    
MTRIX2   6 -0.776200 -0.619700 -0.116300       20.48000    1                    
MTRIX3   6  0.231100 -0.108100 -0.966900       39.48000    1                    
MTRIX1   7  0.092760  0.778400 -0.620900       35.12000    1                    
MTRIX2   7 -0.292200  0.617500  0.730300      -10.07000    1                    
MTRIX3   7  0.951900  0.113700  0.284700       -5.50000    1                    
MTRIX1   8  0.500600 -0.000151 -0.865700       31.35000    1                    
MTRIX2   8 -0.000197 -1.000000  0.000061       -0.14380    1                    
MTRIX3   8 -0.865700  0.000140 -0.500600       54.21000    1                    
MTRIX1   9  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   9  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   9  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  10 -0.779000  0.287000 -0.557500       53.73000    1                    
MTRIX2  10  0.295100 -0.616600 -0.729800        9.70300    1                    
MTRIX3  10 -0.553300 -0.733100  0.395600       26.55000    1                    
MTRIX1  11  0.097580 -0.295300  0.950400       -0.79660    1                    
MTRIX2  11  0.769500  0.628000  0.116100      -20.51000    1                    
MTRIX3  11 -0.631100  0.720000  0.288500       30.85000    1                    
MTRIX1  12 -0.694600 -0.485100  0.531200       27.14000    1                    
MTRIX2  12 -0.482400 -0.233700 -0.844200       30.35000    1                    
MTRIX3  12  0.533600 -0.842700 -0.071660       12.20000    1                    
MTRIX1  13 -0.808400  0.489900  0.326300       34.35000    1                    
MTRIX2  13  0.481700  0.231900  0.845100      -30.49000    1                    
MTRIX3  13  0.338300  0.840400 -0.423500       24.42000    1                    
MTRIX1  14  0.592700 -0.773200  0.225600        4.27900    1                    
MTRIX2  14 -0.771100 -0.625600 -0.118200       20.48000    1                    
MTRIX3  14  0.232500 -0.103900 -0.967000       39.32000    1                    
MTRIX1  15  0.088690  0.779200 -0.620400       35.16000    1                    
MTRIX2  15 -0.296400  0.615300  0.730400       -9.81800    1                    
MTRIX3  15  0.950900  0.119100  0.285600       -5.56600    1                    
MTRIX1  16  0.500300  0.000189 -0.865900       31.33000    1                    
MTRIX2  16 -0.001347 -1.000000 -0.000996       -0.04693    1                    
MTRIX3  16 -0.865900  0.001665 -0.500300       54.15000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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