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Database: PDB
Entry: 2V69
LinkDB: 2V69
Original site: 2V69 
HEADER    OXIDOREDUCTASE                          14-JUL-07   2V69              
TITLE     CRYSTAL STRUCTURE OF CHLAMYDOMONAS REINHARDTII RUBISCO WITH           
TITLE    2 A LARGE-SUBUNIT MUTATION D473E                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;             
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 SYNONYM: RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE LARGE                 
COMPND   5  CHAIN, RUBISCO LARGE SUBUNIT;                                       
COMPND   6 EC: 4.1.1.39;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1;           
COMPND  11 CHAIN: I, J, K, L, M, N, O, P;                                       
COMPND  12 SYNONYM: RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE SMALL                 
COMPND  13  CHAIN, RUBISCO SMALL SUBUNIT 1;                                     
COMPND  14 EC: 4.1.1.39;                                                        
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;                      
SOURCE   3 ORGANISM_TAXID: 3055;                                                
SOURCE   4 STRAIN: 2137;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;                      
SOURCE   9 ORGANISM_TAXID: 3055;                                                
SOURCE  10 STRAIN: 2137;                                                        
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    LARGE SUBUNIT LOOP 6 MUTATION, CO2/O2 SPECIFICITY, CARBON             
KEYWDS   2 DIOXIDE FIXATION, PHOTOSYNTHESIS, TRANSIT PEPTIDE,                   
KEYWDS   3 PHOTORESPIRATION, METAL-BINDING, HYDROXYLATION,                      
KEYWDS   4 OXIDOREDUCTASE, METHYLATION, CHLOROPLAST, CALVIN CYCLE,              
KEYWDS   5 MONOOXYGENASE, LYASE, RUBISCO, PLASTID, MAGNESIUM,                   
KEYWDS   6 ACETYLATION                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.KARKEHABADI,S.SATAGOPAN,T.C.TAYLOR,R.J.SPREITZER,                   
AUTHOR   2 I.ANDERSSON                                                          
REVDAT   7   24-FEB-09 2V69    1       VERSN                                    
REVDAT   6   01-APR-08 2V69    1       REMARK FORMUL LINK   HETATM              
REVDAT   6 2                           ATOM   CONECT MASTER                     
REVDAT   5   23-OCT-07 2V69    1       REMARK                                   
REVDAT   4   02-OCT-07 2V69    1       JRNL   REMARK                            
REVDAT   3   28-AUG-07 2V69    1       AUTHOR                                   
REVDAT   2   07-AUG-07 2V69    1       SOURCE REMARK                            
REVDAT   1   31-JUL-07 2V69    0                                                
JRNL        AUTH   S.KARKEHABADI,S.SATAGOPAN,T.C.TAYLOR,R.J.SPREITZER,          
JRNL        AUTH 2 I.ANDERSSON                                                  
JRNL        TITL   STRUCTURAL ANALYSIS OF ALTERED LARGE-SUBUNIT LOOP-           
JRNL        TITL 2 6-CARBOXY-TERMINUS INTERACTIONS THAT INFLUENCE               
JRNL        TITL 3 CATALYTIC EFFICIENCY AND CO2-O2 SPECIFICITY OF               
JRNL        TITL 4 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE OXYGENASE              
JRNL        REF    BIOCHEMISTRY                  V.  46 11080 2007              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   17824672                                                     
JRNL        DOI    10.1021/BI701063F                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.8  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 118598                         
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) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6228                            
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8556                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3240                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 462                          
REMARK   3   BIN FREE R VALUE                    : 0.3540                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 37429                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 680                                     
REMARK   3   SOLVENT ATOMS            : 395                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.18000                                              
REMARK   3    B22 (A**2) : -2.54000                                             
REMARK   3    B33 (A**2) : -3.08000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -2.01000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.373         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.298         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.453        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
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): 39025 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 52897 ; 1.356 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4785 ; 6.305 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1827 ;33.096 ;23.125       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  6227 ;16.682 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   312 ;15.392 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  5608 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 30080 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A): 19106 ; 0.213 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 26696 ; 0.314 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1489 ; 0.143 ; 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):    57 ; 0.422 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.335 ; 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): 24317 ; 0.612 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 38257 ; 1.080 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 16754 ; 1.240 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 14640 ; 2.044 ; 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     468      1                      
REMARK   3           2     A    476       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   3581 ;  0.00 ;  0.05           
REMARK   3   TIGHT THERMAL      1    A (A**2):   3581 ;  0.00 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B     13       B     468      1                      
REMARK   3           1     A     13       A     468      1                      
REMARK   3           2     B    476       B     477      1                      
REMARK   3           2     A    476       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    B    (A):   3581 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL      2    B (A**2):   3581 ;  0.13 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : C A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C     13       C     468      1                      
REMARK   3           1     A     13       A     468      1                      
REMARK   3           2     C    476       C     477      1                      
REMARK   3           2     A    476       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    C    (A):   3581 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL      3    C (A**2):   3581 ;  0.13 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : D A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     D     13       D     468      1                      
REMARK   3           1     A     13       A     468      1                      
REMARK   3           2     D    476       D     477      1                      
REMARK   3           2     A    476       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   4    D    (A):   3581 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL      4    D (A**2):   3581 ;  0.12 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 5                                  
REMARK   3     CHAIN NAMES                    : E A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     E     13       E     468      1                      
REMARK   3           1     A     13       A     468      1                      
REMARK   3           2     E    476       E     477      1                      
REMARK   3           2     A    476       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   5    E    (A):   3581 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL      5    E (A**2):   3581 ;  0.10 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 6                                  
REMARK   3     CHAIN NAMES                    : F A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     F     13       F     468      1                      
REMARK   3           1     A     13       A     468      1                      
REMARK   3           2     F    476       F     477      1                      
REMARK   3           2     A    476       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   6    F    (A):   3581 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL      6    F (A**2):   3581 ;  0.12 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 7                                  
REMARK   3     CHAIN NAMES                    : G A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     G     13       G     468      1                      
REMARK   3           1     A     13       A     468      1                      
REMARK   3           2     G    476       G     477      1                      
REMARK   3           2     A    476       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   7    G    (A):   3581 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL      7    G (A**2):   3581 ;  0.11 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 8                                  
REMARK   3     CHAIN NAMES                    : H A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     H     13       H     468      1                      
REMARK   3           1     A     13       A     468      1                      
REMARK   3           2     H    476       H     477      1                      
REMARK   3           2     A    476       A     477      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   8    H    (A):   3581 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL      8    H (A**2):   3581 ;  0.10 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 9                                  
REMARK   3     CHAIN NAMES                    : I                               
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     I      1       I     140      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   9    I    (A):   1143 ;  0.00 ;  0.05           
REMARK   3   TIGHT THERMAL      9    I (A**2):   1143 ;  0.00 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 10                                 
REMARK   3     CHAIN NAMES                    : J I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     J      1       J     140      1                      
REMARK   3           1     I      1       I     140      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  10    J    (A):   1143 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL     10    J (A**2):   1143 ;  0.09 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 11                                 
REMARK   3     CHAIN NAMES                    : K I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     K      1       K     140      1                      
REMARK   3           1     I      1       I     140      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  11    K    (A):   1143 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL     11    K (A**2):   1143 ;  0.08 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 12                                 
REMARK   3     CHAIN NAMES                    : L I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     L      1       L     140      1                      
REMARK   3           1     I      1       I     140      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  12    L    (A):   1143 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL     12    L (A**2):   1143 ;  0.11 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 13                                 
REMARK   3     CHAIN NAMES                    : M I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     M      1       M     140      1                      
REMARK   3           1     I      1       I     140      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  13    M    (A):   1143 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL     13    M (A**2):   1143 ;  0.08 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 14                                 
REMARK   3     CHAIN NAMES                    : N I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     N      1       N     140      1                      
REMARK   3           1     I      1       I     140      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  14    N    (A):   1143 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL     14    N (A**2):   1143 ;  0.07 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 15                                 
REMARK   3     CHAIN NAMES                    : O I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     O      1       O     140      1                      
REMARK   3           1     I      1       I     140      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  15    O    (A):   1143 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL     15    O (A**2):   1143 ;  0.07 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 16                                 
REMARK   3     CHAIN NAMES                    : P I                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     P      1       P     140      1                      
REMARK   3           1     I      1       I     140      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL  16    P    (A):   1143 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL     16    P (A**2):   1143 ;  0.07 ;  0.50           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS. VERY WEAK DENSITIES WERE OBSERVED FOR SOME        
REMARK   3  RESIDUE SIDE CHAINS. RESIDUES ARG84, MET87 ARG130, ASN136 AND       
REMARK   3  LYS137 OF THE SMALL SUBUNIT WERE THUS MODELED ON EXISTING HIGH      
REMARK   3  RESOLUTION STRUCTURES AND HAVE HIGH B FACTORS.                      
REMARK   4                                                                      
REMARK   4 2V69 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-JUL-07.                  
REMARK 100 THE PDBE ID CODE IS EBI-33195.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUN-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               : MAX II                             
REMARK 200  BEAMLINE                       : I711                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0917                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 125065                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.80                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NONE                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 7.9                                
REMARK 200  R MERGE                    (I) : 0.09                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.90                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.63                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1GK8                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):2.44                      
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       84.57000            
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: 124160 ANGSTROM**2                        
REMARK 350 SURFACE AREA OF THE COMPLEX: 155100 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -724.6 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, ASP 473 TO GLU                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ASP 473 TO GLU                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, ASP 473 TO GLU                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, ASP 473 TO GLU                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN E, ASP 473 TO GLU                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, ASP 473 TO GLU                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN G, ASP 473 TO GLU                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN H, ASP 473 TO GLU                        
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     ASP A   470                                                      
REMARK 465     THR A   471                                                      
REMARK 465     ILE A   472                                                      
REMARK 465     GLU A   473                                                      
REMARK 465     LYS A   474                                                      
REMARK 465     LEU A   475                                                      
REMARK 465     MET B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     GLN B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     ALA B     9                                                      
REMARK 465     ASP B   470                                                      
REMARK 465     THR B   471                                                      
REMARK 465     ILE B   472                                                      
REMARK 465     GLU B   473                                                      
REMARK 465     LYS B   474                                                      
REMARK 465     LEU B   475                                                      
REMARK 465     MET C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     PRO C     3                                                      
REMARK 465     GLN C     4                                                      
REMARK 465     THR C     5                                                      
REMARK 465     GLU C     6                                                      
REMARK 465     THR C     7                                                      
REMARK 465     LYS C     8                                                      
REMARK 465     ALA C     9                                                      
REMARK 465     GLY C    10                                                      
REMARK 465     ALA C    11                                                      
REMARK 465     THR C   471                                                      
REMARK 465     ILE C   472                                                      
REMARK 465     GLU C   473                                                      
REMARK 465     LYS C   474                                                      
REMARK 465     LEU C   475                                                      
REMARK 465     MET D     1                                                      
REMARK 465     VAL D     2                                                      
REMARK 465     PRO D     3                                                      
REMARK 465     GLN D     4                                                      
REMARK 465     THR D     5                                                      
REMARK 465     GLU D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     LYS D     8                                                      
REMARK 465     ALA D     9                                                      
REMARK 465     GLY D    10                                                      
REMARK 465     LEU D   475                                                      
REMARK 465     MET E     1                                                      
REMARK 465     VAL E     2                                                      
REMARK 465     PRO E     3                                                      
REMARK 465     GLN E     4                                                      
REMARK 465     THR E     5                                                      
REMARK 465     GLU E     6                                                      
REMARK 465     THR E     7                                                      
REMARK 465     LYS E     8                                                      
REMARK 465     ALA E     9                                                      
REMARK 465     GLY E    10                                                      
REMARK 465     ASP E   470                                                      
REMARK 465     THR E   471                                                      
REMARK 465     ILE E   472                                                      
REMARK 465     GLU E   473                                                      
REMARK 465     LYS E   474                                                      
REMARK 465     LEU E   475                                                      
REMARK 465     MET F     1                                                      
REMARK 465     VAL F     2                                                      
REMARK 465     PRO F     3                                                      
REMARK 465     GLN F     4                                                      
REMARK 465     THR F     5                                                      
REMARK 465     GLU F     6                                                      
REMARK 465     THR F     7                                                      
REMARK 465     LYS F     8                                                      
REMARK 465     ASP F   470                                                      
REMARK 465     THR F   471                                                      
REMARK 465     ILE F   472                                                      
REMARK 465     GLU F   473                                                      
REMARK 465     LYS F   474                                                      
REMARK 465     LEU F   475                                                      
REMARK 465     MET G     1                                                      
REMARK 465     VAL G     2                                                      
REMARK 465     PRO G     3                                                      
REMARK 465     GLN G     4                                                      
REMARK 465     THR G     5                                                      
REMARK 465     GLU G     6                                                      
REMARK 465     THR G     7                                                      
REMARK 465     LYS G     8                                                      
REMARK 465     ASP G   470                                                      
REMARK 465     THR G   471                                                      
REMARK 465     ILE G   472                                                      
REMARK 465     GLU G   473                                                      
REMARK 465     LYS G   474                                                      
REMARK 465     LEU G   475                                                      
REMARK 465     MET H     1                                                      
REMARK 465     VAL H     2                                                      
REMARK 465     PRO H     3                                                      
REMARK 465     GLN H     4                                                      
REMARK 465     THR H     5                                                      
REMARK 465     GLU H     6                                                      
REMARK 465     THR H     7                                                      
REMARK 465     LYS H     8                                                      
REMARK 465     ALA H     9                                                      
REMARK 465     GLY H    10                                                      
REMARK 465     ALA H    11                                                      
REMARK 465     ASP H   470                                                      
REMARK 465     THR H   471                                                      
REMARK 465     ILE H   472                                                      
REMARK 465     GLU H   473                                                      
REMARK 465     LYS H   474                                                      
REMARK 465     LEU H   475                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU D   158  -  NE2  HIS D   325              2.17            
REMARK 500   OE1  GLU H   234  -  O    HOH H  1017              2.13            
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 H  84   CA  -  CB  -  SG  ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    ASN I   8   N   -  CA  -  C   ANGL. DEV. = -16.6 DEGREES          
REMARK 500    ASN L   8   N   -  CA  -  C   ANGL. DEV. = -18.0 DEGREES          
REMARK 500    ASN M   8   N   -  CA  -  C   ANGL. DEV. = -17.0 DEGREES          
REMARK 500    ASN O   8   N   -  CA  -  C   ANGL. DEV. = -16.6 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      -81.65   -146.30                                   
REMARK 500    THR A  65     -169.90   -116.57                                   
REMARK 500    ASP A  86      139.39   -175.88                                   
REMARK 500    ALA A 129        1.20    -66.09                                   
REMARK 500    CYS A 172      118.59   -174.38                                   
REMARK 500    ASN A 207      -96.25   -122.53                                   
REMARK 500    ALA A 296      130.72    -37.58                                   
REMARK 500    MET A 297       -9.58     89.78                                   
REMARK 500    VAL A 331      -57.40     71.00                                   
REMARK 500    SER A 370       -0.93     79.08                                   
REMARK 500    THR A 406      -54.03   -124.98                                   
REMARK 500    SER B  62      -82.85   -143.75                                   
REMARK 500    ASP B  86      135.70   -178.72                                   
REMARK 500    ASN B 207      -92.22   -123.41                                   
REMARK 500    ALA B 296      130.70    -32.16                                   
REMARK 500    MET B 297      -10.61     90.57                                   
REMARK 500    VAL B 331      -57.02     72.37                                   
REMARK 500    ASP B 357       92.18   -160.66                                   
REMARK 500    SER B 370       -0.67     79.87                                   
REMARK 500    THR B 406      -56.60   -126.69                                   
REMARK 500    SER C  62      -78.44   -146.87                                   
REMARK 500    THR C  65     -167.95   -119.38                                   
REMARK 500    ASP C 106      -14.75    -49.29                                   
REMARK 500    ALA C 129        5.29    -67.01                                   
REMARK 500    CYS C 172      114.15   -175.42                                   
REMARK 500    ASN C 207      -95.12   -120.85                                   
REMARK 500    ALA C 296      128.83    -32.32                                   
REMARK 500    MET C 297       -5.23     85.62                                   
REMARK 500    VAL C 331      -60.26     72.78                                   
REMARK 500    THR C 406      -54.80   -127.42                                   
REMARK 500    SER D  62      -83.90   -149.81                                   
REMARK 500    ASP D  86      135.87   -178.50                                   
REMARK 500    CYS D 172      117.20   -172.85                                   
REMARK 500    ASN D 207      -94.40   -123.34                                   
REMARK 500    ALA D 296      134.27    -37.51                                   
REMARK 500    MET D 297       -7.49     84.66                                   
REMARK 500    VAL D 331      -53.20     68.59                                   
REMARK 500    SER D 370       -5.66     78.90                                   
REMARK 500    THR D 406      -51.74   -124.68                                   
REMARK 500    ASP D 470     -121.11     79.74                                   
REMARK 500    THR D 471      110.53     68.39                                   
REMARK 500    SER E  62      -85.98   -147.89                                   
REMARK 500    THR E  65     -169.76   -118.24                                   
REMARK 500    ASP E  86      134.97   -178.21                                   
REMARK 500    ASN E  95       51.86   -118.53                                   
REMARK 500    ALA E 129        4.20    -65.08                                   
REMARK 500    ASN E 207      -95.92   -125.04                                   
REMARK 500    MET E 212      104.27   -162.03                                   
REMARK 500    ALA E 296      127.45    -29.17                                   
REMARK 500    MET E 297       -5.00     88.71                                   
REMARK 500    VAL E 331      -55.10     72.45                                   
REMARK 500    THR E 406      -54.23   -122.33                                   
REMARK 500    SER F  62      -80.25   -144.14                                   
REMARK 500    ASP F  86      142.33   -174.83                                   
REMARK 500    ALA F 129        2.17    -65.69                                   
REMARK 500    CYS F 172      115.00   -175.72                                   
REMARK 500    ASN F 207      -92.22   -121.04                                   
REMARK 500    MET F 212      113.29   -162.23                                   
REMARK 500    ALA F 296      127.44    -34.67                                   
REMARK 500    MET F 297      -11.51     91.24                                   
REMARK 500    VAL F 331      -58.20     71.41                                   
REMARK 500    ASP F 357       88.67   -160.66                                   
REMARK 500    SER F 370       -1.45     78.89                                   
REMARK 500    THR F 406      -54.45   -122.44                                   
REMARK 500    SER G  62      -77.95   -142.43                                   
REMARK 500    THR G  65     -168.68   -119.41                                   
REMARK 500    ASP G  86      142.05   -174.95                                   
REMARK 500    ASN G  95       59.62   -115.98                                   
REMARK 500    CYS G 172      115.72   -178.40                                   
REMARK 500    ASN G 207      -97.98   -122.86                                   
REMARK 500    ALA G 296      132.99    -38.48                                   
REMARK 500    MET G 297       -3.25     83.76                                   
REMARK 500    VAL G 331      -54.04     66.05                                   
REMARK 500    SER G 370       -3.41     84.98                                   
REMARK 500    THR G 406      -54.63   -125.59                                   
REMARK 500    ARG G 439      -64.47   -104.82                                   
REMARK 500    SER H  62      -79.62   -142.88                                   
REMARK 500    ASP H  86      141.70   -172.39                                   
REMARK 500    ALA H 129        0.53    -67.84                                   
REMARK 500    CYS H 172      117.64   -171.58                                   
REMARK 500    ASN H 207      -99.67   -124.70                                   
REMARK 500    MET H 212      108.04   -160.16                                   
REMARK 500    ALA H 296      127.74    -35.91                                   
REMARK 500    MET H 297       -8.84     90.17                                   
REMARK 500    VAL H 331      -57.37     74.96                                   
REMARK 500    ASP H 357       91.59   -160.18                                   
REMARK 500    SER H 370       -1.65     84.92                                   
REMARK 500    THR H 406      -52.62   -121.01                                   
REMARK 500    ASN I   9       50.43   -112.10                                   
REMARK 500    PHE I  12       43.68   -148.62                                   
REMARK 500    GLU I  13     -145.35     62.93                                   
REMARK 500    PHE I  15       -3.80     79.60                                   
REMARK 500    LYS I  49       19.27    -67.53                                   
REMARK 500    ASN I  54       53.09   -156.40                                   
REMARK 500    LYS I  77     -122.97     55.00                                   
REMARK 500    CYS I  83       95.62    -65.06                                   
REMARK 500    ARG I  84       37.66    -94.01                                   
REMARK 500    PHE J  12       37.98   -148.52                                   
REMARK 500    GLU J  13     -143.57     64.04                                   
REMARK 500    PHE J  15       -9.97     81.20                                   
REMARK 500    LYS J  49       22.23    -67.38                                   
REMARK 500    ASN J  54       49.60   -156.05                                   
REMARK 500    LYS J  77     -120.41     57.26                                   
REMARK 500    CYS J  83       94.80    -65.81                                   
REMARK 500    ARG J  84       37.04    -93.47                                   
REMARK 500    ASN K   9       51.37   -111.06                                   
REMARK 500    PHE K  12       44.87   -150.77                                   
REMARK 500    GLU K  13     -139.51     64.36                                   
REMARK 500    ASN K  54       53.24   -154.71                                   
REMARK 500    LYS K  77     -123.48     55.36                                   
REMARK 500    CYS K  83       95.24    -66.33                                   
REMARK 500    ARG K  84       36.62    -93.30                                   
REMARK 500    ASN L   9       50.41   -114.31                                   
REMARK 500    PHE L  12       39.61   -148.70                                   
REMARK 500    GLU L  13     -145.93     64.34                                   
REMARK 500    LYS L  49       18.28    -69.28                                   
REMARK 500    ASN L  54       55.22   -154.48                                   
REMARK 500    LYS L  77     -126.28     53.71                                   
REMARK 500    CYS L  83       95.05    -65.89                                   
REMARK 500    ARG L  84       41.09    -94.08                                   
REMARK 500    ASN M   9       50.16   -119.65                                   
REMARK 500    PHE M  12       51.47   -148.13                                   
REMARK 500    GLU M  13     -144.95     57.97                                   
REMARK 500    PHE M  15       -4.39     79.81                                   
REMARK 500    LYS M  49       16.78    -63.42                                   
REMARK 500    ASN M  54       54.04   -157.24                                   
REMARK 500    SER M  62       22.27    -76.03                                   
REMARK 500    LYS M  77     -119.64     58.25                                   
REMARK 500    CYS M  83       96.44    -62.60                                   
REMARK 500    ARG M  84       36.12    -92.86                                   
REMARK 500    ASN N   9       51.09   -106.12                                   
REMARK 500    PHE N  12       43.60   -149.45                                   
REMARK 500    GLU N  13     -146.10     66.52                                   
REMARK 500    PHE N  15       -8.99     83.21                                   
REMARK 500    LYS N  49       20.20    -70.78                                   
REMARK 500    ASN N  54       50.50   -154.92                                   
REMARK 500    LYS N  77     -121.98     60.37                                   
REMARK 500    CYS N  83       96.66    -56.99                                   
REMARK 500    ARG N  84       41.32    -95.83                                   
REMARK 500    ASN O   9       53.73   -112.09                                   
REMARK 500    PHE O  12       41.17   -147.56                                   
REMARK 500    GLU O  13     -140.92     65.92                                   
REMARK 500    PHE O  15       -4.22     82.98                                   
REMARK 500    LYS O  49       18.73    -66.33                                   
REMARK 500    ASN O  54       51.16   -152.78                                   
REMARK 500    LYS O  77     -127.33     52.80                                   
REMARK 500    CYS O  83       93.25    -69.06                                   
REMARK 500    ARG O  84       34.81    -91.60                                   
REMARK 500    PHE P  12       46.19   -151.38                                   
REMARK 500    GLU P  13     -150.34     58.94                                   
REMARK 500    PHE P  15       -0.36     80.46                                   
REMARK 500    LYS P  49       19.01    -65.17                                   
REMARK 500    ASN P  54       58.51   -157.80                                   
REMARK 500    SER P  62       24.12    -79.83                                   
REMARK 500    LYS P  77     -120.53     56.69                                   
REMARK 500    ARG P  84       37.44    -94.45                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PHE D  469     ASP D  470                  142.40                    
REMARK 500 ASP D  470     THR D  471                 -149.33                    
REMARK 500 VAL I    7     ASN I    8                  -38.96                    
REMARK 500 VAL J    7     ASN J    8                  -41.04                    
REMARK 500 VAL K    7     ASN K    8                  -37.68                    
REMARK 500 VAL L    7     ASN L    8                  -35.39                    
REMARK 500 VAL M    7     ASN M    8                  -41.01                    
REMARK 500 VAL N    7     ASN N    8                  -39.33                    
REMARK 500 VAL O    7     ASN O    8                  -38.42                    
REMARK 500 VAL P    7     ASN P    8                  -36.76                    
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 A1470  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 203   OD1                                                    
REMARK 620 2 GLU A 204   OE1  91.8                                              
REMARK 620 3 CAP A1471   O7   94.7  92.4                                        
REMARK 620 4 KCX A 201   OQ1 105.9  99.4 155.8                                  
REMARK 620 5 CAP A1471   O2  109.3 153.7  70.9  90.0                            
REMARK 620 6 CAP A1471   O3  171.2  82.6  78.9  81.7  74.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1470  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX B 201   OQ1                                                    
REMARK 620 2 GLU B 204   OE1  98.7                                              
REMARK 620 3 CAP B1471   O3   76.5  78.9                                        
REMARK 620 4 CAP B1471   O7  155.4  90.7  83.2                                  
REMARK 620 5 ASP B 203   OD1 105.2  88.8 167.7  97.7                            
REMARK 620 6 CAP B1471   O2   85.6 150.4  73.6  75.4 118.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C1471  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX C 201   OQ1                                                    
REMARK 620 2 ASP C 203   OD1 106.2                                              
REMARK 620 3 GLU C 204   OE1 103.3  93.0                                        
REMARK 620 4 CAP C1472   O2   86.0 109.9 152.0                                  
REMARK 620 5 CAP C1472   O3   80.0 173.5  83.7  71.7                            
REMARK 620 6 CAP C1472   O7  150.7  98.4  90.9  70.5  76.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D1475  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 203   OD1                                                    
REMARK 620 2 KCX D 201   OQ1 103.9                                              
REMARK 620 3 GLU D 204   OE1  97.2  95.1                                        
REMARK 620 4 CAP D1476   O3  173.3  82.7  81.2                                  
REMARK 620 5 CAP D1476   O2  105.7  94.4 152.3  74.3                            
REMARK 620 6 CAP D1476   O7   95.3 157.3  94.3  78.4  68.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E1470  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAP E1471   O3                                                     
REMARK 620 2 KCX E 201   OQ1  82.2                                              
REMARK 620 3 ASP E 203   OD1 176.6 100.0                                        
REMARK 620 4 GLU E 204   OE1  87.8 105.4  89.1                                  
REMARK 620 5 CAP E1471   O2   73.2  83.5 109.6 157.9                            
REMARK 620 6 CAP E1471   O7   81.3 153.7  97.6  94.2  72.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F1470  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAP F1471   O7                                                     
REMARK 620 2 KCX F 201   OQ1 155.4                                              
REMARK 620 3 ASP F 203   OD1  95.5 106.6                                        
REMARK 620 4 GLU F 204   OE1  95.3  96.3  87.4                                  
REMARK 620 5 CAP F1471   O2   71.5  90.1 111.4 157.6                            
REMARK 620 6 CAP F1471   O3   82.7  76.7 172.4  85.4  75.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G1470  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAP G1471   O2                                                     
REMARK 620 2 GLU G 204   OE1 159.9                                              
REMARK 620 3 CAP G1471   O3   76.4  88.8                                        
REMARK 620 4 KCX G 201   OQ1  89.6 102.1  83.1                                  
REMARK 620 5 ASP G 203   OD1  97.6  95.3 170.6 104.3                            
REMARK 620 6 CAP G1471   O7   67.5  97.9  83.7 155.6  87.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H1470  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP H 203   OD1                                                    
REMARK 620 2 GLU H 204   OE1  94.0                                              
REMARK 620 3 CAP H1471   O3  170.2  80.6                                        
REMARK 620 4 CAP H1471   O7   93.8  94.9  78.6                                  
REMARK 620 5 KCX H 201   OQ1 101.6 101.1  87.6 156.9                            
REMARK 620 6 CAP H1471   O2  107.8 153.5  75.5  69.4  89.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A1470                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A1471                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B1470                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B1471                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG C1471                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C1472                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG D1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG E1470                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E1471                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG F1470                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP F1471                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG G1470                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G1471                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG H1470                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H1471                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1472                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1473                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1473                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1474                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1472                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1473                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1474                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1472                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1473                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1474                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1472                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1472                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1473                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1473                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1474                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1472                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F1473                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G1474                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1UW9   RELATED DB: PDB                                   
REMARK 900  L290F-A222T CHLAMYDOMONAS RUBISCO MUTANT                            
REMARK 900 RELATED ID: 1UZH   RELATED DB: PDB                                   
REMARK 900  A CHIMERIC CHLAMYDOMONAS, SPINACH RUBISCO                           
REMARK 900  ENZYME                                                              
REMARK 900 RELATED ID: 1GK8   RELATED DB: PDB                                   
REMARK 900  RUBISCO FROM CHLAMYDOMONAS REINHARDTII                              
REMARK 900 RELATED ID: 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 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE UNIPROT DATABASE ENTRY FOR THIS SEQUENCE (P00877)                
REMARK 999 HAS A VARIANT (LEU46PRO) WHICH OCCURS IN STRAIN 21GR                 
REMARK 999 AND 2137.                                                            
DBREF  2V69 A    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V69 B    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V69 C    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V69 D    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V69 E    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V69 F    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V69 G    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V69 H    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  2V69 I    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V69 J    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V69 K    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V69 L    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V69 M    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V69 N    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V69 O    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  2V69 P    1   140  UNP    P00873   RBS1_CHLRE      46    185             
SEQADV 2V69 PRO A   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V69 GLU A  473  UNP  P00877    ASP   473 ENGINEERED MUTATION            
SEQADV 2V69 PRO B   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V69 GLU B  473  UNP  P00877    ASP   473 ENGINEERED MUTATION            
SEQADV 2V69 PRO C   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V69 GLU C  473  UNP  P00877    ASP   473 ENGINEERED MUTATION            
SEQADV 2V69 PRO D   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V69 GLU D  473  UNP  P00877    ASP   473 ENGINEERED MUTATION            
SEQADV 2V69 PRO E   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V69 GLU E  473  UNP  P00877    ASP   473 ENGINEERED MUTATION            
SEQADV 2V69 PRO F   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V69 GLU F  473  UNP  P00877    ASP   473 ENGINEERED MUTATION            
SEQADV 2V69 PRO G   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V69 GLU G  473  UNP  P00877    ASP   473 ENGINEERED MUTATION            
SEQADV 2V69 PRO H   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 2V69 GLU H  473  UNP  P00877    ASP   473 ENGINEERED MUTATION            
SEQRES   1 A  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 A  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 A  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 A  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 A  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 A  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 A  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 A  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 A  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 A  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 A  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 A  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 A  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 A  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 A  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 A  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 A  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 A  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 A  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 A  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 A  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 A  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 A  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 A  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 A  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 A  475  LEU HIS SER GLY THR 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 GLU LYS LEU                                  
SEQRES   1 B  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 B  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 B  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 B  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 B  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 B  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 B  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 B  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 B  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 B  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 B  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 B  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 B  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 B  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 B  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 B  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 B  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 B  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 B  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 B  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 B  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 B  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 B  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 B  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 B  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 B  475  LEU HIS SER GLY THR 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 GLU LYS LEU                                  
SEQRES   1 C  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 C  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 C  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 C  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 C  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 C  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 C  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 C  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 C  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 C  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 C  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 C  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 C  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 C  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 C  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 C  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 C  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 C  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 C  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 C  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 C  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 C  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 C  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 C  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 C  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 C  475  LEU HIS SER GLY THR 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 GLU LYS LEU                                  
SEQRES   1 D  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 D  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 D  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 D  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 D  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 D  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 D  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 D  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 D  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 D  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 D  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 D  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 D  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 D  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 D  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 D  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 D  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 D  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 D  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 D  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 D  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 D  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 D  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 D  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 D  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 D  475  LEU HIS SER GLY THR 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 GLU LYS LEU                                  
SEQRES   1 E  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 E  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 E  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 E  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 E  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 E  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 E  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 E  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 E  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 E  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 E  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 E  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 E  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 E  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 E  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 E  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 E  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 E  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 E  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 E  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 E  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 E  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 E  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 E  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 E  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 E  475  LEU HIS SER GLY THR 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 GLU LYS LEU                                  
SEQRES   1 F  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 F  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 F  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 F  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 F  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 F  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 F  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 F  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 F  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 F  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 F  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 F  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 F  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 F  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 F  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 F  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 F  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 F  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 F  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 F  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 F  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 F  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 F  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 F  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 F  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 F  475  LEU HIS SER GLY THR 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 GLU LYS LEU                                  
SEQRES   1 G  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 G  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 G  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 G  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 G  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 G  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 G  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 G  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 G  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 G  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 G  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 G  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 G  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 G  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 G  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 G  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 G  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 G  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 G  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 G  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 G  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 G  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 G  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 G  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 G  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 G  475  LEU HIS SER GLY THR 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 GLU LYS LEU                                  
SEQRES   1 H  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 H  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 H  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 H  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 H  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 H  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 H  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 H  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 H  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 H  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 H  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 H  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 H  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 H  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 H  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 H  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 H  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 H  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 H  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 H  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 H  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 H  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 H  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 H  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 H  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 H  475  LEU HIS SER GLY THR 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 GLU 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 2V69 HYP A  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V69 HYP A  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V69 KCX A  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V69 SMC A  256  MET  S-METHYLCYSTEINE                                   
MODRES 2V69 SMC A  369  MET  S-METHYLCYSTEINE                                   
MODRES 2V69 HYP B  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V69 HYP B  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V69 KCX B  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V69 SMC B  256  MET  S-METHYLCYSTEINE                                   
MODRES 2V69 SMC B  369  MET  S-METHYLCYSTEINE                                   
MODRES 2V69 HYP C  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V69 HYP C  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V69 KCX C  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V69 SMC C  256  MET  S-METHYLCYSTEINE                                   
MODRES 2V69 SMC C  369  MET  S-METHYLCYSTEINE                                   
MODRES 2V69 HYP D  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V69 HYP D  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V69 KCX D  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V69 SMC D  256  MET  S-METHYLCYSTEINE                                   
MODRES 2V69 SMC D  369  MET  S-METHYLCYSTEINE                                   
MODRES 2V69 HYP E  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V69 HYP E  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V69 KCX E  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V69 SMC E  256  MET  S-METHYLCYSTEINE                                   
MODRES 2V69 SMC E  369  MET  S-METHYLCYSTEINE                                   
MODRES 2V69 HYP F  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V69 HYP F  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V69 KCX F  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V69 SMC F  256  MET  S-METHYLCYSTEINE                                   
MODRES 2V69 SMC F  369  MET  S-METHYLCYSTEINE                                   
MODRES 2V69 HYP G  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V69 HYP G  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V69 KCX G  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V69 SMC G  256  MET  S-METHYLCYSTEINE                                   
MODRES 2V69 SMC G  369  MET  S-METHYLCYSTEINE                                   
MODRES 2V69 HYP H  104  PRO  4-HYDROXYPROLINE                                   
MODRES 2V69 HYP H  151  PRO  4-HYDROXYPROLINE                                   
MODRES 2V69 KCX H  201  LYS  LYSYL-CARBAMATE                                    
MODRES 2V69 SMC H  256  MET  S-METHYLCYSTEINE                                   
MODRES 2V69 SMC H  369  MET  S-METHYLCYSTEINE                                   
MODRES 2V69 MME I    1  MET  N-METHYL METHIONINE                                
MODRES 2V69 MME J    1  MET  N-METHYL METHIONINE                                
MODRES 2V69 MME K    1  MET  N-METHYL METHIONINE                                
MODRES 2V69 MME L    1  MET  N-METHYL METHIONINE                                
MODRES 2V69 MME M    1  MET  N-METHYL METHIONINE                                
MODRES 2V69 MME N    1  MET  N-METHYL METHIONINE                                
MODRES 2V69 MME O    1  MET  N-METHYL METHIONINE                                
MODRES 2V69 MME P    1  MET  N-METHYL METHIONINE                                
HET    HYP  A 104       8                                                       
HET    HYP  A 151       8                                                       
HET    KCX  A 201      12                                                       
HET    SMC  A 256       7                                                       
HET    SMC  A 369       7                                                       
HET     MG  A1470       1                                                       
HET    CAP  A1471      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  B1470       1                                                       
HET    CAP  B1471      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  C1471       1                                                       
HET    CAP  C1472      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  D1475       1                                                       
HET    CAP  D1476      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  E1470       1                                                       
HET    CAP  E1471      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  F1470       1                                                       
HET    CAP  F1471      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  G1470       1                                                       
HET    CAP  G1471      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  H1470       1                                                       
HET    CAP  H1471      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  A1472       4                                                       
HET    EDO  A1473       4                                                       
HET    EDO  C1473       4                                                       
HET    EDO  C1474       4                                                       
HET    EDO  C1475       4                                                       
HET    EDO  E1472       4                                                       
HET    EDO  E1473       4                                                       
HET    EDO  E1474       4                                                       
HET    EDO  G1472       4                                                       
HET    EDO  G1473       4                                                       
HET    EDO  E1475       4                                                       
HET    EDO  A1474       4                                                       
HET    EDO  H1472       4                                                       
HET    EDO  B1472       4                                                       
HET    EDO  B1473       4                                                       
HET    EDO  H1473       4                                                       
HET    EDO  H1474       4                                                       
HET    EDO  H1475       4                                                       
HET    EDO  F1472       4                                                       
HET    EDO  F1473       4                                                       
HET    EDO  D1477       4                                                       
HET    EDO  D1478       4                                                       
HET    EDO  D1479       4                                                       
HET    EDO  G1474       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE                              
HETNAM     MME N-METHYL METHIONINE                                              
HETNAM     SMC S-METHYLCYSTEINE                                                 
HETNAM     HYP 4-HYDROXYPROLINE                                                 
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL  17  EDO    24(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   *395(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  VAL A  255  1                                  10    
HELIX   13  13 TYR A  269  GLY A  288  1                                  20    
HELIX   14  14 MET A  297  ARG A  303  1                                   7    
HELIX   15  15 HIS A  310  GLY A  322  1                                  13    
HELIX   16  16 GLU A  338  ASP A  351  1                                  14    
HELIX   17  17 ARG A  358  GLY A  361  5                                   4    
HELIX   18  18 HIS A  383  TRP A  385  5                                   3    
HELIX   19  19 HIS A  386  GLY A  395  1                                  10    
HELIX   20  20 GLY A  403  GLY A  408  1                                   6    
HELIX   21  21 GLY A  412  GLY A  434  1                                  23    
HELIX   22  22 GLU A  440  SER A  452  1                                  13    
HELIX   23  23 SER A  452  LYS A  463  1                                  12    
HELIX   24  24 TYR B   20  TYR B   25  1                                   6    
HELIX   25  25 PRO B   49  SER B   61  1                                  13    
HELIX   26  26 VAL B   69  THR B   75  5                                   7    
HELIX   27  27 SER B   76  LYS B   81  1                                   6    
HELIX   28  28 HYP B  104  PHE B  108  5                                   5    
HELIX   29  29 SER B  112  VAL B  121  1                                  10    
HELIX   30  30 ASN B  123  GLY B  126  5                                   4    
HELIX   31  31 PRO B  141  LYS B  146  1                                   6    
HELIX   32  32 GLY B  154  ASN B  163  1                                  10    
HELIX   33  33 SER B  181  GLY B  196  1                                  16    
HELIX   34  34 ARG B  213  GLY B  233  1                                  21    
HELIX   35  35 THR B  246  VAL B  255  1                                  10    
HELIX   36  36 TYR B  269  GLY B  288  1                                  20    
HELIX   37  37 MET B  297  ARG B  303  1                                   7    
HELIX   38  38 HIS B  310  GLY B  322  1                                  13    
HELIX   39  39 GLU B  338  ASP B  351  1                                  14    
HELIX   40  40 ARG B  358  GLY B  361  5                                   4    
HELIX   41  41 HIS B  383  TRP B  385  5                                   3    
HELIX   42  42 HIS B  386  GLY B  395  1                                  10    
HELIX   43  43 GLY B  403  GLY B  408  1                                   6    
HELIX   44  44 GLY B  412  GLU B  433  1                                  22    
HELIX   45  45 GLU B  440  SER B  452  1                                  13    
HELIX   46  46 SER B  452  LYS B  463  1                                  12    
HELIX   47  47 TYR C   20  TYR C   25  1                                   6    
HELIX   48  48 PRO C   49  GLU C   60  1                                  12    
HELIX   49  49 VAL C   69  THR C   75  5                                   7    
HELIX   50  50 SER C   76  LYS C   81  1                                   6    
HELIX   51  51 HYP C  104  PHE C  108  5                                   5    
HELIX   52  52 SER C  112  VAL C  121  1                                  10    
HELIX   53  53 ASN C  123  GLY C  126  5                                   4    
HELIX   54  54 PRO C  141  LYS C  146  1                                   6    
HELIX   55  55 GLY C  154  ASN C  163  1                                  10    
HELIX   56  56 SER C  181  GLY C  195  1                                  15    
HELIX   57  57 ARG C  213  GLY C  233  1                                  21    
HELIX   58  58 THR C  246  VAL C  255  1                                  10    
HELIX   59  59 TYR C  269  GLY C  288  1                                  20    
HELIX   60  60 MET C  297  ARG C  303  1                                   7    
HELIX   61  61 HIS C  310  GLY C  322  1                                  13    
HELIX   62  62 GLU C  338  ASP C  351  1                                  14    
HELIX   63  63 ARG C  358  GLY C  361  5                                   4    
HELIX   64  64 HIS C  383  TRP C  385  5                                   3    
HELIX   65  65 HIS C  386  GLY C  395  1                                  10    
HELIX   66  66 GLY C  403  GLY C  408  1                                   6    
HELIX   67  67 GLY C  412  GLY C  434  1                                  23    
HELIX   68  68 GLU C  440  SER C  452  1                                  13    
HELIX   69  69 SER C  452  TRP C  462  1                                  11    
HELIX   70  70 TYR D   20  TYR D   25  1                                   6    
HELIX   71  71 PRO D   49  GLU D   60  1                                  12    
HELIX   72  72 VAL D   69  THR D   75  5                                   7    
HELIX   73  73 SER D   76  LYS D   81  1                                   6    
HELIX   74  74 HYP D  104  PHE D  108  5                                   5    
HELIX   75  75 SER D  112  VAL D  121  1                                  10    
HELIX   76  76 ASN D  123  GLY D  126  5                                   4    
HELIX   77  77 PRO D  141  LYS D  146  1                                   6    
HELIX   78  78 GLY D  154  ASN D  163  1                                  10    
HELIX   79  79 SER D  181  GLY D  196  1                                  16    
HELIX   80  80 ARG D  213  GLY D  233  1                                  21    
HELIX   81  81 THR D  246  VAL D  255  1                                  10    
HELIX   82  82 TYR D  269  GLY D  288  1                                  20    
HELIX   83  83 MET D  297  ARG D  303  1                                   7    
HELIX   84  84 HIS D  310  GLY D  322  1                                  13    
HELIX   85  85 GLU D  338  ASP D  351  1                                  14    
HELIX   86  86 ARG D  358  GLY D  361  5                                   4    
HELIX   87  87 HIS D  383  TRP D  385  5                                   3    
HELIX   88  88 HIS D  386  GLY D  395  1                                  10    
HELIX   89  89 GLY D  403  GLY D  408  1                                   6    
HELIX   90  90 GLY D  412  GLY D  434  1                                  23    
HELIX   91  91 GLU D  440  SER D  452  1                                  13    
HELIX   92  92 SER D  452  LYS D  463  1                                  12    
HELIX   93  93 TYR E   20  TYR E   25  1                                   6    
HELIX   94  94 PRO E   49  SER E   61  1                                  13    
HELIX   95  95 VAL E   69  THR E   75  5                                   7    
HELIX   96  96 SER E   76  LYS E   81  1                                   6    
HELIX   97  97 HYP E  104  PHE E  108  5                                   5    
HELIX   98  98 SER E  112  GLY E  122  1                                  11    
HELIX   99  99 ASN E  123  GLY E  126  5                                   4    
HELIX  100 100 PRO E  141  LYS E  146  1                                   6    
HELIX  101 101 GLY E  154  ASN E  163  1                                  10    
HELIX  102 102 SER E  181  GLY E  195  1                                  15    
HELIX  103 103 ARG E  213  GLY E  233  1                                  21    
HELIX  104 104 THR E  246  VAL E  255  1                                  10    
HELIX  105 105 TYR E  269  ASN E  287  1                                  19    
HELIX  106 106 MET E  297  ARG E  303  1                                   7    
HELIX  107 107 HIS E  310  GLY E  322  1                                  13    
HELIX  108 108 GLU E  338  ASP E  351  1                                  14    
HELIX  109 109 ARG E  358  GLY E  361  5                                   4    
HELIX  110 110 HIS E  383  TRP E  385  5                                   3    
HELIX  111 111 HIS E  386  GLY E  395  1                                  10    
HELIX  112 112 GLY E  403  GLY E  408  1                                   6    
HELIX  113 113 GLY E  412  GLY E  434  1                                  23    
HELIX  114 114 GLU E  440  SER E  452  1                                  13    
HELIX  115 115 SER E  452  LYS E  463  1                                  12    
HELIX  116 116 TYR F   20  TYR F   25  1                                   6    
HELIX  117 117 PRO F   49  SER F   61  1                                  13    
HELIX  118 118 VAL F   69  THR F   75  5                                   7    
HELIX  119 119 SER F   76  LYS F   81  1                                   6    
HELIX  120 120 HYP F  104  PHE F  108  5                                   5    
HELIX  121 121 SER F  112  VAL F  121  1                                  10    
HELIX  122 122 ASN F  123  GLY F  126  5                                   4    
HELIX  123 123 PRO F  141  LYS F  146  1                                   6    
HELIX  124 124 GLY F  154  ASN F  163  1                                  10    
HELIX  125 125 SER F  181  GLY F  195  1                                  15    
HELIX  126 126 ARG F  213  GLY F  233  1                                  21    
HELIX  127 127 THR F  246  VAL F  255  1                                  10    
HELIX  128 128 TYR F  269  GLY F  288  1                                  20    
HELIX  129 129 MET F  297  ARG F  303  1                                   7    
HELIX  130 130 HIS F  310  GLY F  322  1                                  13    
HELIX  131 131 GLU F  338  ASP F  351  1                                  14    
HELIX  132 132 ARG F  358  GLY F  361  5                                   4    
HELIX  133 133 HIS F  383  TRP F  385  5                                   3    
HELIX  134 134 HIS F  386  GLY F  395  1                                  10    
HELIX  135 135 GLY F  403  GLY F  408  1                                   6    
HELIX  136 136 GLY F  412  GLY F  434  1                                  23    
HELIX  137 137 GLU F  440  LYS F  450  1                                  11    
HELIX  138 138 SER F  452  LYS F  463  1                                  12    
HELIX  139 139 TYR G   20  TYR G   25  1                                   6    
HELIX  140 140 PRO G   49  SER G   61  1                                  13    
HELIX  141 141 VAL G   69  THR G   75  5                                   7    
HELIX  142 142 SER G   76  LYS G   81  1                                   6    
HELIX  143 143 HYP G  104  PHE G  108  5                                   5    
HELIX  144 144 SER G  112  GLY G  122  1                                  11    
HELIX  145 145 ASN G  123  GLY G  126  5                                   4    
HELIX  146 146 PRO G  141  LYS G  146  1                                   6    
HELIX  147 147 GLY G  154  ASN G  163  1                                  10    
HELIX  148 148 SER G  181  GLY G  195  1                                  15    
HELIX  149 149 ARG G  213  GLY G  233  1                                  21    
HELIX  150 150 THR G  246  VAL G  255  1                                  10    
HELIX  151 151 TYR G  269  GLY G  288  1                                  20    
HELIX  152 152 MET G  297  ARG G  303  1                                   7    
HELIX  153 153 HIS G  310  GLY G  322  1                                  13    
HELIX  154 154 GLU G  338  ASP G  351  1                                  14    
HELIX  155 155 ARG G  358  GLY G  361  5                                   4    
HELIX  156 156 HIS G  383  TRP G  385  5                                   3    
HELIX  157 157 HIS G  386  GLY G  395  1                                  10    
HELIX  158 158 GLY G  403  GLY G  408  1                                   6    
HELIX  159 159 GLY G  412  GLY G  434  1                                  23    
HELIX  160 160 GLU G  440  SER G  452  1                                  13    
HELIX  161 161 SER G  452  LYS G  463  1                                  12    
HELIX  162 162 ASP H   19  TYR H   25  1                                   7    
HELIX  163 163 PRO H   49  SER H   61  1                                  13    
HELIX  164 164 VAL H   69  THR H   75  5                                   7    
HELIX  165 165 SER H   76  LYS H   81  1                                   6    
HELIX  166 166 HYP H  104  PHE H  108  5                                   5    
HELIX  167 167 SER H  112  VAL H  121  1                                  10    
HELIX  168 168 ASN H  123  GLY H  126  5                                   4    
HELIX  169 169 PRO H  141  LYS H  146  1                                   6    
HELIX  170 170 GLY H  154  ASN H  163  1                                  10    
HELIX  171 171 SER H  181  GLY H  195  1                                  15    
HELIX  172 172 ARG H  213  GLY H  233  1                                  21    
HELIX  173 173 THR H  246  VAL H  255  1                                  10    
HELIX  174 174 TYR H  269  GLY H  288  1                                  20    
HELIX  175 175 MET H  297  ARG H  303  1                                   7    
HELIX  176 176 HIS H  310  GLY H  322  1                                  13    
HELIX  177 177 GLU H  338  ASP H  351  1                                  14    
HELIX  178 178 ARG H  358  GLY H  361  5                                   4    
HELIX  179 179 HIS H  383  TRP H  385  5                                   3    
HELIX  180 180 HIS H  386  GLY H  395  1                                  10    
HELIX  181 181 GLY H  403  GLY H  408  1                                   6    
HELIX  182 182 GLY H  412  GLY H  434  1                                  23    
HELIX  183 183 GLU H  440  SER H  452  1                                  13    
HELIX  184 184 SER H  452  LYS H  463  1                                  12    
HELIX  185 185 THR I   22  ASN I   36  1                                  15    
HELIX  186 186 GLU I   55  PHE I   60  5                                   6    
HELIX  187 187 ASP I   85  PHE I  100  1                                  16    
HELIX  188 188 THR J   22  ASN J   36  1                                  15    
HELIX  189 189 ALA J   47  TYR J   51  5                                   5    
HELIX  190 190 ASN J   54  PHE J   60  5                                   7    
HELIX  191 191 ASP J   85  PHE J  100  1                                  16    
HELIX  192 192 THR K   22  ASN K   36  1                                  15    
HELIX  193 193 ALA K   47  TYR K   51  5                                   5    
HELIX  194 194 ASN K   54  PHE K   60  5                                   7    
HELIX  195 195 ASP K   85  PHE K  100  1                                  16    
HELIX  196 196 THR L   22  ASN L   36  1                                  15    
HELIX  197 197 GLU L   55  PHE L   60  5                                   6    
HELIX  198 198 ASP L   85  PHE L  100  1                                  16    
HELIX  199 199 THR M   22  ASN M   36  1                                  15    
HELIX  200 200 ALA M   47  TYR M   51  5                                   5    
HELIX  201 201 GLU M   55  PHE M   60  5                                   6    
HELIX  202 202 ASP M   85  PHE M  100  1                                  16    
HELIX  203 203 THR N   22  GLY N   37  1                                  16    
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 THR O   22  ASN O   36  1                                  15    
HELIX  207 207 ASN O   54  PHE O   60  5                                   7    
HELIX  208 208 ASP O   85  PHE O  100  1                                  16    
HELIX  209 209 THR P   22  ASN P   36  1                                  15    
HELIX  210 210 SER P   56  PHE P   60  5                                   5    
HELIX  211 211 ASP P   85  PHE P  100  1                                  16    
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 ARG D 134  ARG D 139 -1  O  ARG D 134   N  ARG D  41           
SHEET    5  DA 5 GLY D 308  ILE D 309  1  O  GLY D 308   N  LEU D 135           
SHEET    1  DB 4 ARG D  83  PRO D  89  0                                        
SHEET    2  DB 4 TYR D  97  TYR D 103 -1  O  ILE D  98   N  GLU D  88           
SHEET    3  DB 4 ILE D  36  PRO D  44 -1  O  ILE D  36   N  TYR D 103           
SHEET    4  DB 4 LEU D 130  ALA D 132 -1  N  ARG D 131   O  THR D  43           
SHEET    1  DC 8 LEU D 169  GLY D 171  0                                        
SHEET    2  DC 8 CYS D 399  GLN D 401  1  O  LEU D 400   N  GLY D 171           
SHEET    3  DC 8 MET D 375  SER D 379  1  O  PRO D 376   N  CYS D 399           
SHEET    4  DC 8 HIS D 325  HIS D 327  1  O  LEU D 326   N  VAL D 377           
SHEET    5  DC 8 LEU D 290  HIS D 294  1  O  ILE D 293   N  HIS D 327           
SHEET    6  DC 8 ILE D 264  ASP D 268  1  O  ILE D 265   N  HIS D 292           
SHEET    7  DC 8 GLY D 237  ASN D 241  1  O  LEU D 240   N  MET D 266           
SHEET    8  DC 8 PHE D 199  KCX D 201  1  O  THR D 200   N  TYR D 239           
SHEET    1  DD 2 TYR D 353  VAL D 354  0                                        
SHEET    2  DD 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 ARG G 134  ARG G 139 -1  O  ARG G 134   N  ARG G  41           
SHEET    5  GA 5 GLY G 308  ILE G 309  1  O  GLY G 308   N  LEU G 135           
SHEET    1  GB 4 ARG G  83  PRO G  89  0                                        
SHEET    2  GB 4 TYR G  97  TYR G 103 -1  O  ILE G  98   N  GLU G  88           
SHEET    3  GB 4 ILE G  36  PRO G  44 -1  O  ILE G  36   N  TYR G 103           
SHEET    4  GB 4 LEU G 130  ALA G 132 -1  N  ARG G 131   O  THR G  43           
SHEET    1  GC 8 LEU G 169  GLY G 171  0                                        
SHEET    2  GC 8 CYS G 399  GLN G 401  1  O  LEU G 400   N  GLY G 171           
SHEET    3  GC 8 MET G 375  SER G 379  1  O  PRO G 376   N  CYS G 399           
SHEET    4  GC 8 HIS G 325  HIS G 327  1  O  LEU G 326   N  VAL G 377           
SHEET    5  GC 8 LEU G 290  HIS G 294  1  O  ILE G 293   N  HIS G 327           
SHEET    6  GC 8 ILE G 264  ASP G 268  1  O  ILE G 265   N  HIS G 292           
SHEET    7  GC 8 GLY G 237  ASN G 241  1  O  LEU G 240   N  MET G 266           
SHEET    8  GC 8 PHE G 199  KCX G 201  1  O  THR G 200   N  TYR G 239           
SHEET    1  GD 2 TYR G 353  VAL G 354  0                                        
SHEET    2  GD 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  2.10  
SSBOND   2 CYS C  247    CYS D  247                          1555   1555  2.14  
SSBOND   3 CYS E  247    CYS F  247                          1555   1555  2.10  
SSBOND   4 CYS G  247    CYS H  247                          1555   1555  2.12  
LINK         C   TYR A 103                 N   HYP A 104     1555   1555  1.34  
LINK         C   HYP A 104                 N   ILE A 105     1555   1555  1.33  
LINK         C   GLY A 150                 N   HYP A 151     1555   1555  1.33  
LINK         C   HYP A 151                 N   PRO A 152     1555   1555  1.34  
LINK         C   THR A 200                 N   KCX A 201     1555   1555  1.32  
LINK         C   KCX A 201                 N   ASP A 202     1555   1555  1.33  
LINK         C   VAL A 255                 N   SMC A 256     1555   1555  1.33  
LINK         C   SMC A 256                 N   ALA A 257     1555   1555  1.33  
LINK         C   TRP A 368                 N   SMC A 369     1555   1555  1.33  
LINK         C   SMC A 369                 N   SER A 370     1555   1555  1.34  
LINK        MG    MG A1470                 OD1 ASP A 203     1555   1555  1.91  
LINK        MG    MG A1470                 OE1 GLU A 204     1555   1555  2.05  
LINK        MG    MG A1470                 O7  CAP A1471     1555   1555  2.28  
LINK        MG    MG A1470                 OQ1 KCX A 201     1555   1555  1.87  
LINK        MG    MG A1470                 O2  CAP A1471     1555   1555  2.25  
LINK        MG    MG A1470                 O3  CAP A1471     1555   1555  2.21  
LINK         C   TYR B 103                 N   HYP B 104     1555   1555  1.33  
LINK         C   HYP B 104                 N   ILE B 105     1555   1555  1.32  
LINK         C   GLY B 150                 N   HYP B 151     1555   1555  1.35  
LINK         C   HYP B 151                 N   PRO B 152     1555   1555  1.34  
LINK         C   THR B 200                 N   KCX B 201     1555   1555  1.33  
LINK         C   KCX B 201                 N   ASP B 202     1555   1555  1.33  
LINK         C   VAL B 255                 N   SMC B 256     1555   1555  1.33  
LINK         C   SMC B 256                 N   ALA B 257     1555   1555  1.33  
LINK         C   TRP B 368                 N   SMC B 369     1555   1555  1.32  
LINK         C   SMC B 369                 N   SER B 370     1555   1555  1.33  
LINK        MG    MG B1470                 OQ1 KCX B 201     1555   1555  1.99  
LINK        MG    MG B1470                 OE1 GLU B 204     1555   1555  2.10  
LINK        MG    MG B1470                 O3  CAP B1471     1555   1555  2.25  
LINK        MG    MG B1470                 O7  CAP B1471     1555   1555  2.17  
LINK        MG    MG B1470                 OD1 ASP B 203     1555   1555  2.00  
LINK        MG    MG B1470                 O2  CAP B1471     1555   1555  2.32  
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  1.33  
LINK         C   HYP C 151                 N   PRO C 152     1555   1555  1.34  
LINK         C   THR C 200                 N   KCX C 201     1555   1555  1.33  
LINK         OQ1 KCX C 201                MG    MG C1471     1555   1555  1.76  
LINK         C   KCX C 201                 N   ASP C 202     1555   1555  1.33  
LINK         C   VAL C 255                 N   SMC C 256     1555   1555  1.34  
LINK         C   SMC C 256                 N   ALA C 257     1555   1555  1.32  
LINK         C   TRP C 368                 N   SMC C 369     1555   1555  1.34  
LINK         C   SMC C 369                 N   SER C 370     1555   1555  1.33  
LINK        MG    MG C1471                 OD1 ASP C 203     1555   1555  1.88  
LINK        MG    MG C1471                 OE1 GLU C 204     1555   1555  2.05  
LINK        MG    MG C1471                 O2  CAP C1472     1555   1555  2.27  
LINK        MG    MG C1471                 O3  CAP C1472     1555   1555  2.24  
LINK        MG    MG C1471                 O7  CAP C1472     1555   1555  2.32  
LINK         C   TYR D 103                 N   HYP D 104     1555   1555  1.34  
LINK         C   HYP D 104                 N   ILE D 105     1555   1555  1.33  
LINK         C   GLY D 150                 N   HYP D 151     1555   1555  1.34  
LINK         C   HYP D 151                 N   PRO D 152     1555   1555  1.34  
LINK         C   THR D 200                 N   KCX D 201     1555   1555  1.32  
LINK         C   KCX D 201                 N   ASP D 202     1555   1555  1.33  
LINK         C   VAL D 255                 N   SMC D 256     1555   1555  1.34  
LINK         C   SMC D 256                 N   ALA D 257     1555   1555  1.33  
LINK         C   TRP D 368                 N   SMC D 369     1555   1555  1.33  
LINK         C   SMC D 369                 N   SER D 370     1555   1555  1.35  
LINK        MG    MG D1475                 O7  CAP D1476     1555   1555  2.31  
LINK        MG    MG D1475                 OD1 ASP D 203     1555   1555  1.78  
LINK        MG    MG D1475                 OE1 GLU D 204     1555   1555  2.03  
LINK        MG    MG D1475                 O3  CAP D1476     1555   1555  2.38  
LINK        MG    MG D1475                 O2  CAP D1476     1555   1555  2.32  
LINK        MG    MG D1475                 OQ1 KCX D 201     1555   1555  1.95  
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  1.33  
LINK         C   THR E 200                 N   KCX E 201     1555   1555  1.32  
LINK         C   KCX E 201                 N   ASP E 202     1555   1555  1.33  
LINK         C   VAL E 255                 N   SMC E 256     1555   1555  1.33  
LINK         C   SMC E 256                 N   ALA E 257     1555   1555  1.34  
LINK         C   TRP E 368                 N   SMC E 369     1555   1555  1.33  
LINK         C   SMC E 369                 N   SER E 370     1555   1555  1.33  
LINK        MG    MG E1470                 O7  CAP E1471     1555   1555  2.13  
LINK        MG    MG E1470                 O2  CAP E1471     1555   1555  2.30  
LINK        MG    MG E1470                 OE1 GLU E 204     1555   1555  1.98  
LINK        MG    MG E1470                 OD1 ASP E 203     1555   1555  2.05  
LINK        MG    MG E1470                 OQ1 KCX E 201     1555   1555  2.01  
LINK        MG    MG E1470                 O3  CAP E1471     1555   1555  2.23  
LINK         C   TYR F 103                 N   HYP F 104     1555   1555  1.34  
LINK         C   HYP F 104                 N   ILE F 105     1555   1555  1.34  
LINK         C   GLY F 150                 N   HYP F 151     1555   1555  1.33  
LINK         C   HYP F 151                 N   PRO F 152     1555   1555  1.34  
LINK         C   THR F 200                 N   KCX F 201     1555   1555  1.32  
LINK         C   KCX F 201                 N   ASP F 202     1555   1555  1.33  
LINK         C   VAL F 255                 N   SMC F 256     1555   1555  1.33  
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  1.34  
LINK        MG    MG F1470                 O7  CAP F1471     1555   1555  2.34  
LINK        MG    MG F1470                 O3  CAP F1471     1555   1555  2.24  
LINK        MG    MG F1470                 O2  CAP F1471     1555   1555  2.08  
LINK        MG    MG F1470                 OE1 GLU F 204     1555   1555  1.98  
LINK        MG    MG F1470                 OD1 ASP F 203     1555   1555  1.95  
LINK        MG    MG F1470                 OQ1 KCX F 201     1555   1555  2.02  
LINK         C   TYR G 103                 N   HYP G 104     1555   1555  1.35  
LINK         C   HYP G 104                 N   ILE G 105     1555   1555  1.33  
LINK         C   GLY G 150                 N   HYP G 151     1555   1555  1.34  
LINK         C   HYP G 151                 N   PRO G 152     1555   1555  1.36  
LINK         C   THR G 200                 N   KCX G 201     1555   1555  1.32  
LINK         C   KCX G 201                 N   ASP G 202     1555   1555  1.33  
LINK         C   VAL G 255                 N   SMC G 256     1555   1555  1.32  
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  1.34  
LINK        MG    MG G1470                 O2  CAP G1471     1555   1555  2.30  
LINK        MG    MG G1470                 OE1 GLU G 204     1555   1555  1.93  
LINK        MG    MG G1470                 O3  CAP G1471     1555   1555  2.00  
LINK        MG    MG G1470                 OQ1 KCX G 201     1555   1555  1.82  
LINK        MG    MG G1470                 OD1 ASP G 203     1555   1555  1.96  
LINK        MG    MG G1470                 O7  CAP G1471     1555   1555  2.34  
LINK         C   TYR H 103                 N   HYP H 104     1555   1555  1.35  
LINK         C   HYP H 104                 N   ILE H 105     1555   1555  1.32  
LINK         C   GLY H 150                 N   HYP H 151     1555   1555  1.34  
LINK         C   HYP H 151                 N   PRO H 152     1555   1555  1.34  
LINK         C   THR H 200                 N   KCX H 201     1555   1555  1.34  
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  1.32  
LINK         C   TRP H 368                 N   SMC H 369     1555   1555  1.33  
LINK         C   SMC H 369                 N   SER H 370     1555   1555  1.34  
LINK        MG    MG H1470                 O2  CAP H1471     1555   1555  2.31  
LINK        MG    MG H1470                 OQ1 KCX H 201     1555   1555  1.89  
LINK        MG    MG H1470                 O7  CAP H1471     1555   1555  2.27  
LINK        MG    MG H1470                 O3  CAP H1471     1555   1555  2.24  
LINK        MG    MG H1470                 OE1 GLU H 204     1555   1555  2.07  
LINK        MG    MG H1470                 OD1 ASP H 203     1555   1555  1.89  
LINK         C   MME I   1                 N   MET I   2     1555   1555  1.33  
LINK         C   MME J   1                 N   MET J   2     1555   1555  1.33  
LINK         C   MME K   1                 N   MET K   2     1555   1555  1.33  
LINK         C   MME L   1                 N   MET L   2     1555   1555  1.34  
LINK         C   MME M   1                 N   MET M   2     1555   1555  1.33  
LINK         C   MME N   1                 N   MET N   2     1555   1555  1.33  
LINK         C   MME O   1                 N   MET O   2     1555   1555  1.33  
LINK         C   MME P   1                 N   MET P   2     1555   1555  1.33  
CISPEP   1 LYS A  175    PRO A  176          0        -0.37                     
CISPEP   2 LYS B  175    PRO B  176          0         1.09                     
CISPEP   3 LYS C  175    PRO C  176          0         1.50                     
CISPEP   4 LYS D  175    PRO D  176          0        -4.07                     
CISPEP   5 LYS E  175    PRO E  176          0        -0.54                     
CISPEP   6 LYS F  175    PRO F  176          0        -0.77                     
CISPEP   7 LYS G  175    PRO G  176          0        -0.21                     
CISPEP   8 LYS H  175    PRO H  176          0        -2.12                     
SITE     1 AC1  5 LYS A 177  KCX A 201  ASP A 203  GLU A 204                    
SITE     2 AC1  5 CAP A1471                                                     
SITE     1 AC2 23 THR A 173  LYS A 175  LYS A 177  KCX A 201                    
SITE     2 AC2 23 ASP A 203  GLU A 204  HIS A 294  ARG A 295                    
SITE     3 AC2 23 HIS A 327  LYS A 334  LEU A 335  SER A 379                    
SITE     4 AC2 23 GLY A 380  GLY A 381  GLY A 403  GLY A 404                    
SITE     5 AC2 23 HOH A1049  HOH A1050   MG A1470  GLU B  60                    
SITE     6 AC2 23 THR B  65  TRP B  66  ASN B 123                               
SITE     1 AC3  5 LYS B 177  KCX B 201  ASP B 203  GLU B 204                    
SITE     2 AC3  5 CAP B1471                                                     
SITE     1 AC4 22 GLU A  60  THR A  65  TRP A  66  ASN A 123                    
SITE     2 AC4 22 THR B 173  LYS B 175  LYS B 177  KCX B 201                    
SITE     3 AC4 22 ASP B 203  GLU B 204  HIS B 294  ARG B 295                    
SITE     4 AC4 22 HIS B 327  LYS B 334  LEU B 335  SER B 379                    
SITE     5 AC4 22 GLY B 380  GLY B 381  GLY B 403  GLY B 404                    
SITE     6 AC4 22 HOH B1029   MG B1470                                          
SITE     1 AC5  5 LYS C 177  KCX C 201  ASP C 203  GLU C 204                    
SITE     2 AC5  5 CAP C1472                                                     
SITE     1 AC6 23 THR C 173  LYS C 175  LYS C 177  KCX C 201                    
SITE     2 AC6 23 ASP C 203  GLU C 204  HIS C 294  ARG C 295                    
SITE     3 AC6 23 HIS C 327  LYS C 334  LEU C 335  SER C 379                    
SITE     4 AC6 23 GLY C 380  GLY C 381  GLY C 403  GLY C 404                    
SITE     5 AC6 23 HOH C1051  HOH C1056   MG C1471  GLU D  60                    
SITE     6 AC6 23 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 D1476                                                     
SITE     1 AC8 25 GLU C  60  THR C  65  TRP C  66  ASN C 123                    
SITE     2 AC8 25 HOH C1015  THR D 173  LYS D 175  LYS D 177                    
SITE     3 AC8 25 KCX D 201  ASP D 203  GLU D 204  HIS D 294                    
SITE     4 AC8 25 ARG D 295  HIS D 327  LYS D 334  LEU D 335                    
SITE     5 AC8 25 SER D 379  GLY D 380  GLY D 381  GLY D 403                    
SITE     6 AC8 25 GLY D 404  HOH D1029  HOH D1035  HOH D1036                    
SITE     7 AC8 25  MG D1475                                                     
SITE     1 AC9  5 LYS E 177  KCX E 201  ASP E 203  GLU E 204                    
SITE     2 AC9  5 CAP E1471                                                     
SITE     1 BC1 23 THR E 173  LYS E 175  LYS E 177  KCX E 201                    
SITE     2 BC1 23 ASP E 203  GLU E 204  HIS E 294  ARG E 295                    
SITE     3 BC1 23 HIS E 327  LYS E 334  LEU E 335  SER E 379                    
SITE     4 BC1 23 GLY E 380  GLY E 381  GLY E 403  GLY E 404                    
SITE     5 BC1 23 HOH E1048  HOH E1049   MG E1470  GLU F  60                    
SITE     6 BC1 23 THR F  65  TRP F  66  ASN F 123                               
SITE     1 BC2  5 LYS F 177  KCX F 201  ASP F 203  GLU F 204                    
SITE     2 BC2  5 CAP F1471                                                     
SITE     1 BC3 23 GLU E  60  THR E  65  TRP E  66  ASN E 123                    
SITE     2 BC3 23 THR F 173  LYS F 175  LYS F 177  KCX F 201                    
SITE     3 BC3 23 ASP F 203  GLU F 204  HIS F 294  ARG F 295                    
SITE     4 BC3 23 HIS F 327  LYS F 334  LEU F 335  SER F 379                    
SITE     5 BC3 23 GLY F 380  GLY F 381  GLY F 403  GLY F 404                    
SITE     6 BC3 23 HOH F1039  HOH F1040   MG F1470                               
SITE     1 BC4  5 LYS G 177  KCX G 201  ASP G 203  GLU G 204                    
SITE     2 BC4  5 CAP G1471                                                     
SITE     1 BC5 23 THR G 173  LYS G 175  LYS G 177  KCX G 201                    
SITE     2 BC5 23 ASP G 203  GLU G 204  HIS G 294  ARG G 295                    
SITE     3 BC5 23 HIS G 327  LYS G 334  LEU G 335  SER G 379                    
SITE     4 BC5 23 GLY G 380  GLY G 381  GLY G 403  GLY G 404                    
SITE     5 BC5 23 HOH G1035  HOH G1041   MG G1470  GLU H  60                    
SITE     6 BC5 23 THR H  65  TRP H  66  ASN H 123                               
SITE     1 BC6  5 LYS H 177  KCX H 201  ASP H 203  GLU H 204                    
SITE     2 BC6  5 CAP H1471                                                     
SITE     1 BC7 22 GLU G  60  THR G  65  TRP G  66  ASN G 123                    
SITE     2 BC7 22 THR H 173  LYS H 175  LYS H 177  KCX H 201                    
SITE     3 BC7 22 ASP H 203  GLU H 204  HIS H 294  ARG H 295                    
SITE     4 BC7 22 HIS H 327  LYS H 334  LEU H 335  SER H 379                    
SITE     5 BC7 22 GLY H 380  GLY H 381  GLY H 403  GLY H 404                    
SITE     6 BC7 22 HOH H1040   MG H1470                                          
SITE     1 BC8  5 LYS A  18  ASP A  19  TRP A  66  THR A  67                    
SITE     2 BC8  5 THR A  68                                                     
SITE     1 BC9  4 LYS A 466  PHE A 467  GLU A 468  PHE A 469                    
SITE     1 CC1  6 TYR C  24  THR C  68  VAL C  69  ASP C  72                    
SITE     2 CC1  6 HOH C1057  EDO C1474                                          
SITE     1 CC2  8 LYS C  18  TYR C  20  THR C  65  TRP C  66                    
SITE     2 CC2  8 THR C  67  THR C  68  HOH C1057  EDO C1473                    
SITE     1 CC3  3 ARG C 295  GLU C 336  HOH C1043                               
SITE     1 CC4  5 TYR E  24  THR E  68  VAL E  69  ASP E  72                    
SITE     2 CC4  5 HOH E1053                                                     
SITE     1 CC5  7 LYS E  18  TYR E  20  THR E  65  TRP E  66                    
SITE     2 CC5  7 THR E  67  THR E  68  HOH E1002                               
SITE     1 CC6  1 GLU E  52                                                     
SITE     1 CC7  4 TYR G  24  THR G  68  VAL G  69  ASP G  72                    
SITE     1 CC8  7 LYS G  18  ASP G  19  TYR G  20  THR G  65                    
SITE     2 CC8  7 TRP G  66  THR G  67  THR G  68                               
SITE     1 CC9  4 LEU E 270  HOH E1054  LEU F 270  HOH F1028                    
SITE     1 DC1  4 LEU A 270  HOH A1051  HOH A1052  LEU B 270                    
SITE     1 DC2  4 LEU G 270  LEU H 270  HOH H1041  HOH H1042                    
SITE     1 DC3  6 TYR B  24  GLY B  64  THR B  68  VAL B  69                    
SITE     2 DC3  6 ASP B  72  EDO B1473                                          
SITE     1 DC4  7 LYS B  18  TYR B  20  THR B  65  TRP B  66                    
SITE     2 DC4  7 THR B  67  THR B  68  EDO B1472                               
SITE     1 DC5  7 TYR H  24  GLY H  64  THR H  68  VAL H  69                    
SITE     2 DC5  7 ASP H  72  HOH H1043  EDO H1474                               
SITE     1 DC6  6 LYS H  18  ASP H  19  TRP H  66  THR H  67                    
SITE     2 DC6  6 THR H  68  EDO H1473                                          
SITE     1 DC7  3 LYS H 466  PHE H 467  GLU H 468                               
SITE     1 DC8  7 TYR F  24  THR F  68  VAL F  69  ASP F  72                    
SITE     2 DC8  7 LEU F  77  HOH F1041  EDO F1473                               
SITE     1 DC9  7 LYS F  18  ASP F  19  THR F  65  TRP F  66                    
SITE     2 DC9  7 THR F  67  THR F  68  EDO F1472                               
SITE     1 EC1  6 TYR D  24  GLY D  64  THR D  68  VAL D  69                    
SITE     2 EC1  6 ASP D  72  HOH D1002                                          
SITE     1 EC2  6 LYS D  18  ASP D  19  THR D  65  TRP D  66                    
SITE     2 EC2  6 THR D  67  THR D  68                                          
SITE     1 EC3  5 LEU C 270  THR C 271  LEU D 270  GLY D 273                    
SITE     2 EC3  5 PHE D 274                                                     
SITE     1 EC4  7 ASP E 286  ASN E 287  HOH E1039  ARG G 215                    
SITE     2 EC4  7 LYS G 252  SMC G 256  VAL M  63                               
CRYST1  114.242  169.140  137.179  90.00  96.24  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      0.008753  0.000000  0.000957        0.00000                         
SCALE2      0.000000  0.005912  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007333        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  0.196500 -0.671300 -0.714700       46.21000    1                    
MTRIX2   2 -0.672900 -0.622500  0.399700       17.25000    1                    
MTRIX3   2 -0.713200  0.402400 -0.574000       61.18000    1                    
MTRIX1   3  0.001170 -0.584100 -0.811700       51.24000    1                    
MTRIX2   3  0.676900  0.597900 -0.429300       11.42000    1                    
MTRIX3   3  0.736100 -0.548900  0.396100       19.08000    1                    
MTRIX1   4  0.971300  0.036830  0.234900       -8.49600    1                    
MTRIX2   4  0.036310 -0.999300  0.006565       26.60000    1                    
MTRIX3   4  0.235000  0.002153 -0.972000       67.72000    1                    
MTRIX1   5 -0.992800  0.090970 -0.077940       29.31000    1                    
MTRIX2   5  0.094830  0.199300 -0.975300       44.72000    1                    
MTRIX3   5 -0.073190 -0.975700 -0.206500       57.91000    1                    
MTRIX1   6 -0.200800  0.580400  0.789200      -19.77000    1                    
MTRIX2   6  0.579200 -0.579400  0.573500       -7.22000    1                    
MTRIX3   6  0.790100  0.572200 -0.219800       25.08000    1                    
MTRIX1   7  0.002765  0.674500  0.738300      -22.00000    1                    
MTRIX2   7 -0.582600  0.601100 -0.547000       33.33000    1                    
MTRIX3   7 -0.812700 -0.428700  0.394600       39.05000    1                    
MTRIX1   8 -0.979500 -0.125300 -0.157600       34.96000    1                    
MTRIX2   8 -0.130700 -0.199900  0.971100      -16.71000    1                    
MTRIX3   8 -0.153200  0.971800  0.179400       18.38000    1                    
MTRIX1   9  0.196900 -0.670100 -0.715700       46.20000    1                    
MTRIX2   9 -0.674600 -0.622300  0.397000       17.35000    1                    
MTRIX3   9 -0.711500  0.404600 -0.574600       61.14000    1                    
MTRIX1  10  0.004787 -0.584300 -0.811500       51.19000    1                    
MTRIX2  10  0.678700  0.597900 -0.426500       11.36000    1                    
MTRIX3  10  0.734400 -0.548700  0.399400       19.02000    1                    
MTRIX1  11  0.972200  0.031730  0.231800       -8.49500    1                    
MTRIX2  11  0.030840 -0.999500  0.007487       26.75000    1                    
MTRIX3  11  0.231900 -0.000130 -0.972700       67.83000    1                    
MTRIX1  12 -0.992300  0.094590 -0.079520       29.44000    1                    
MTRIX2  12  0.097310  0.201600 -0.974600       44.75000    1                    
MTRIX3  12 -0.076170 -0.974900 -0.209200       58.12000    1                    
MTRIX1  13 -0.203200  0.584000  0.785900      -19.49000    1                    
MTRIX2  13  0.574100 -0.579100  0.578800       -7.27400    1                    
MTRIX3  13  0.793100  0.568900 -0.217600       24.95000    1                    
MTRIX1  14  0.003392  0.678100  0.734900      -21.79000    1                    
MTRIX2  14 -0.578300  0.600900 -0.551800       33.41000    1                    
MTRIX3  14 -0.815800 -0.423100  0.394200       39.17000    1                    
MTRIX1  15 -0.979500 -0.121000 -0.161300       35.14000    1                    
MTRIX2  15 -0.134900 -0.201500  0.970200      -16.67000    1                    
MTRIX3  15 -0.149900  0.972000  0.181100       18.24000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system