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Database: PDB
Entry: 1SVT
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HEADER    CHAPERONE                               29-MAR-04   1SVT              
TITLE     CRYSTAL STRUCTURE OF GROEL14-GROES7-(ADP-ALFX)7                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GROEL PROTEIN;                                             
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N;                     
COMPND   4 SYNONYM: PROTEIN CPN60, 60 KDA CHAPERONIN;                           
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: GROES PROTEIN;                                             
COMPND   8 CHAIN: O, P, Q, R, S, T, U;                                          
COMPND   9 SYNONYM: PROTEIN CPN10, 10 KDA CHAPERONIN;                           
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: GROL, GROEL, MOPA, B4143, C5227, Z5748, ECS5124, SF4297,       
SOURCE   5 S4564;                                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: DH5 ALPHA;                                 
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  11 ORGANISM_TAXID: 562;                                                 
SOURCE  12 GENE: GROS, GROES, MOPB, B4142, C5226, Z5747, ECS5123, SF4296,       
SOURCE  13 S4563;                                                               
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: DH5 ALPHA                                  
KEYWDS    CHAPERONIN, PROTEIN FOLDING, CHAPERONE                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.CHAUDHRY,A.L.HORWICH,A.T.BRUNGER,P.D.ADAMS                          
REVDAT   4   26-MAR-14 1SVT    1       REMARK                                   
REVDAT   3   13-JUL-11 1SVT    1       VERSN                                    
REVDAT   2   24-FEB-09 1SVT    1       VERSN                                    
REVDAT   1   01-MAR-05 1SVT    0                                                
JRNL        AUTH   C.CHAUDHRY,A.L.HORWICH,A.T.BRUNGER,P.D.ADAMS                 
JRNL        TITL   EXPLORING THE STRUCTURAL DYNAMICS OF THE E.COLI CHAPERONIN   
JRNL        TITL 2 GROEL USING TRANSLATION-LIBRATION-SCREW CRYSTALLOGRAPHIC     
JRNL        TITL 3 REFINEMENT OF INTERMEDIATE STATES.                           
JRNL        REF    J.MOL.BIOL.                   V. 342   229 2004              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   15313620                                                     
JRNL        DOI    10.1016/J.JMB.2004.07.015                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.81 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5                                             
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.81                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.39                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 231127                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.248                           
REMARK   3   R VALUE            (WORKING SET) : 0.247                           
REMARK   3   FREE R VALUE                     : 0.274                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.983                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4675                            
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) : 2.81                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.88                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8725                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 161                          
REMARK   3   BIN FREE R VALUE                    : 0.5180                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 59073                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 231                                     
REMARK   3   SOLVENT ATOMS            : 194                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 2.54                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.33100                                             
REMARK   3    B22 (A**2) : -3.72500                                             
REMARK   3    B33 (A**2) : 8.05600                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.983         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.393         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.405         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.496        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.896                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.875                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 59717 ; 0.027 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 80633 ; 2.039 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  7994 ; 6.242 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  9800 ; 0.123 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 43302 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    29 ; 0.264 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    54 ; 0.324 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  1772 ; 0.173 ; 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): 39508 ; 0.218 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 63266 ; 0.386 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 20209 ; 0.840 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 17367 ; 1.235 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : 7                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D E F G                   
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      2       A     135      1                      
REMARK   3           1     B      2       B     135      1                      
REMARK   3           1     C      2       C     135      1                      
REMARK   3           1     D      2       D     135      1                      
REMARK   3           1     E      2       E     135      1                      
REMARK   3           1     F      2       F     135      1                      
REMARK   3           1     G      2       G     135      1                      
REMARK   3           2     A    410       A     525      1                      
REMARK   3           2     B    410       B     525      1                      
REMARK   3           2     C    410       C     525      1                      
REMARK   3           2     D    410       D     525      1                      
REMARK   3           2     E    410       E     525      1                      
REMARK   3           2     F    410       F     525      1                      
REMARK   3           2     G    410       G     525      1                      
REMARK   3           3     A    600       A     603      1                      
REMARK   3           3     B    600       B     603      1                      
REMARK   3           3     C    600       C     603      1                      
REMARK   3           3     D    600       D     603      1                      
REMARK   3           3     E    600       E     603      1                      
REMARK   3           3     F    600       F     603      1                      
REMARK   3           3     G    600       G     603      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1843 ; 0.094 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    B    (A):   1843 ; 0.083 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    C    (A):   1843 ; 0.097 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    D    (A):   1843 ; 0.091 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    E    (A):   1843 ; 0.077 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    F    (A):   1843 ; 0.078 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    G    (A):   1843 ; 0.095 ; 0.050           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1843 ; 0.148 ; 0.500           
REMARK   3   TIGHT THERMAL      1    B (A**2):   1843 ; 0.132 ; 0.500           
REMARK   3   TIGHT THERMAL      1    C (A**2):   1843 ; 0.161 ; 0.500           
REMARK   3   TIGHT THERMAL      1    D (A**2):   1843 ; 0.147 ; 0.500           
REMARK   3   TIGHT THERMAL      1    E (A**2):   1843 ; 0.120 ; 0.500           
REMARK   3   TIGHT THERMAL      1    F (A**2):   1843 ; 0.122 ; 0.500           
REMARK   3   TIGHT THERMAL      1    G (A**2):   1843 ; 0.144 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B C D E F G                   
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    136       A     190      1                      
REMARK   3           1     B    136       B     190      1                      
REMARK   3           1     C    136       C     190      1                      
REMARK   3           1     D    136       D     190      1                      
REMARK   3           1     E    136       E     190      1                      
REMARK   3           1     F    136       F     190      1                      
REMARK   3           1     G    136       G     190      1                      
REMARK   3           2     A    375       A     409      1                      
REMARK   3           2     B    375       B     409      1                      
REMARK   3           2     C    375       C     409      1                      
REMARK   3           2     D    375       D     409      1                      
REMARK   3           2     E    375       E     409      1                      
REMARK   3           2     F    375       F     409      1                      
REMARK   3           2     G    375       G     409      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    A    (A):    647 ; 0.076 ; 0.050           
REMARK   3   TIGHT POSITIONAL   2    B    (A):    647 ; 0.068 ; 0.050           
REMARK   3   TIGHT POSITIONAL   2    C    (A):    647 ; 0.072 ; 0.050           
REMARK   3   TIGHT POSITIONAL   2    D    (A):    647 ; 0.074 ; 0.050           
REMARK   3   TIGHT POSITIONAL   2    E    (A):    647 ; 0.063 ; 0.050           
REMARK   3   TIGHT POSITIONAL   2    F    (A):    647 ; 0.059 ; 0.050           
REMARK   3   TIGHT POSITIONAL   2    G    (A):    647 ; 0.070 ; 0.050           
REMARK   3   TIGHT THERMAL      2    A (A**2):    647 ; 0.109 ; 0.500           
REMARK   3   TIGHT THERMAL      2    B (A**2):    647 ; 0.085 ; 0.500           
REMARK   3   TIGHT THERMAL      2    C (A**2):    647 ; 0.096 ; 0.500           
REMARK   3   TIGHT THERMAL      2    D (A**2):    647 ; 0.096 ; 0.500           
REMARK   3   TIGHT THERMAL      2    E (A**2):    647 ; 0.083 ; 0.500           
REMARK   3   TIGHT THERMAL      2    F (A**2):    647 ; 0.086 ; 0.500           
REMARK   3   TIGHT THERMAL      2    G (A**2):    647 ; 0.092 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A B C D E F G                   
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    191       A     374      1                      
REMARK   3           1     B    191       B     374      1                      
REMARK   3           1     C    191       C     374      1                      
REMARK   3           1     D    191       D     374      1                      
REMARK   3           1     E    191       E     374      1                      
REMARK   3           1     F    191       F     374      1                      
REMARK   3           1     G    191       G     374      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    A    (A):   1398 ; 0.034 ; 0.050           
REMARK   3   TIGHT POSITIONAL   3    B    (A):   1398 ; 0.031 ; 0.050           
REMARK   3   TIGHT POSITIONAL   3    C    (A):   1398 ; 0.033 ; 0.050           
REMARK   3   TIGHT POSITIONAL   3    D    (A):   1398 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   3    E    (A):   1398 ; 0.029 ; 0.050           
REMARK   3   TIGHT POSITIONAL   3    F    (A):   1398 ; 0.026 ; 0.050           
REMARK   3   TIGHT POSITIONAL   3    G    (A):   1398 ; 0.029 ; 0.050           
REMARK   3   TIGHT THERMAL      3    A (A**2):   1398 ; 0.033 ; 0.500           
REMARK   3   TIGHT THERMAL      3    B (A**2):   1398 ; 0.029 ; 0.500           
REMARK   3   TIGHT THERMAL      3    C (A**2):   1398 ; 0.032 ; 0.500           
REMARK   3   TIGHT THERMAL      3    D (A**2):   1398 ; 0.030 ; 0.500           
REMARK   3   TIGHT THERMAL      3    E (A**2):   1398 ; 0.027 ; 0.500           
REMARK   3   TIGHT THERMAL      3    F (A**2):   1398 ; 0.025 ; 0.500           
REMARK   3   TIGHT THERMAL      3    G (A**2):   1398 ; 0.027 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : H I J K L M N                   
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     H      2       H     135      1                      
REMARK   3           1     I      2       I     135      1                      
REMARK   3           1     J      2       J     135      1                      
REMARK   3           1     K      2       K     135      1                      
REMARK   3           1     L      2       L     135      1                      
REMARK   3           1     M      2       M     135      1                      
REMARK   3           1     N      2       N     135      1                      
REMARK   3           2     H    410       H     525      1                      
REMARK   3           2     I    410       I     525      1                      
REMARK   3           2     J    410       J     525      1                      
REMARK   3           2     K    410       K     525      1                      
REMARK   3           2     L    410       L     525      1                      
REMARK   3           2     M    410       M     525      1                      
REMARK   3           2     N    410       N     525      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   4    H    (A):   1811 ; 0.088 ; 0.050           
REMARK   3   TIGHT POSITIONAL   4    I    (A):   1811 ; 0.107 ; 0.050           
REMARK   3   TIGHT POSITIONAL   4    J    (A):   1811 ; 0.092 ; 0.050           
REMARK   3   TIGHT POSITIONAL   4    K    (A):   1811 ; 0.081 ; 0.050           
REMARK   3   TIGHT POSITIONAL   4    L    (A):   1811 ; 0.083 ; 0.050           
REMARK   3   TIGHT POSITIONAL   4    M    (A):   1811 ; 0.099 ; 0.050           
REMARK   3   TIGHT POSITIONAL   4    N    (A):   1811 ; 0.092 ; 0.050           
REMARK   3   TIGHT THERMAL      4    H (A**2):   1811 ; 0.138 ; 0.500           
REMARK   3   TIGHT THERMAL      4    I (A**2):   1811 ; 0.199 ; 0.500           
REMARK   3   TIGHT THERMAL      4    J (A**2):   1811 ; 0.141 ; 0.500           
REMARK   3   TIGHT THERMAL      4    K (A**2):   1811 ; 0.130 ; 0.500           
REMARK   3   TIGHT THERMAL      4    L (A**2):   1811 ; 0.122 ; 0.500           
REMARK   3   TIGHT THERMAL      4    M (A**2):   1811 ; 0.139 ; 0.500           
REMARK   3   TIGHT THERMAL      4    N (A**2):   1811 ; 0.139 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 5                                  
REMARK   3     CHAIN NAMES                    : H I J K L M N                   
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     H    136       H     190      1                      
REMARK   3           1     I    136       I     190      1                      
REMARK   3           1     J    136       J     190      1                      
REMARK   3           1     K    136       K     190      1                      
REMARK   3           1     L    136       L     190      1                      
REMARK   3           1     M    136       M     190      1                      
REMARK   3           1     N    136       N     190      1                      
REMARK   3           2     H    375       H     409      1                      
REMARK   3           2     I    375       I     409      1                      
REMARK   3           2     J    375       J     409      1                      
REMARK   3           2     K    375       K     409      1                      
REMARK   3           2     L    375       L     409      1                      
REMARK   3           2     M    375       M     409      1                      
REMARK   3           2     N    375       N     409      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   5    H    (A):    647 ; 0.054 ; 0.050           
REMARK   3   TIGHT POSITIONAL   5    I    (A):    647 ; 0.064 ; 0.050           
REMARK   3   TIGHT POSITIONAL   5    J    (A):    647 ; 0.060 ; 0.050           
REMARK   3   TIGHT POSITIONAL   5    K    (A):    647 ; 0.049 ; 0.050           
REMARK   3   TIGHT POSITIONAL   5    L    (A):    647 ; 0.046 ; 0.050           
REMARK   3   TIGHT POSITIONAL   5    M    (A):    647 ; 0.060 ; 0.050           
REMARK   3   TIGHT POSITIONAL   5    N    (A):    647 ; 0.059 ; 0.050           
REMARK   3   TIGHT THERMAL      5    H (A**2):    647 ; 0.073 ; 0.500           
REMARK   3   TIGHT THERMAL      5    I (A**2):    647 ; 0.084 ; 0.500           
REMARK   3   TIGHT THERMAL      5    J (A**2):    647 ; 0.083 ; 0.500           
REMARK   3   TIGHT THERMAL      5    K (A**2):    647 ; 0.067 ; 0.500           
REMARK   3   TIGHT THERMAL      5    L (A**2):    647 ; 0.058 ; 0.500           
REMARK   3   TIGHT THERMAL      5    M (A**2):    647 ; 0.080 ; 0.500           
REMARK   3   TIGHT THERMAL      5    N (A**2):    647 ; 0.082 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 6                                  
REMARK   3     CHAIN NAMES                    : H I J K L M N                   
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     H    191       H     374      1                      
REMARK   3           1     I    191       I     374      1                      
REMARK   3           1     J    191       J     374      1                      
REMARK   3           1     K    191       K     374      1                      
REMARK   3           1     L    191       L     374      1                      
REMARK   3           1     M    191       M     374      1                      
REMARK   3           1     N    191       N     374      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   6    H    (A):   1398 ; 0.038 ; 0.050           
REMARK   3   TIGHT POSITIONAL   6    I    (A):   1398 ; 0.040 ; 0.050           
REMARK   3   TIGHT POSITIONAL   6    J    (A):   1398 ; 0.042 ; 0.050           
REMARK   3   TIGHT POSITIONAL   6    K    (A):   1398 ; 0.037 ; 0.050           
REMARK   3   TIGHT POSITIONAL   6    L    (A):   1398 ; 0.036 ; 0.050           
REMARK   3   TIGHT POSITIONAL   6    M    (A):   1398 ; 0.036 ; 0.050           
REMARK   3   TIGHT POSITIONAL   6    N    (A):   1398 ; 0.036 ; 0.050           
REMARK   3   TIGHT THERMAL      6    H (A**2):   1398 ; 0.041 ; 0.500           
REMARK   3   TIGHT THERMAL      6    I (A**2):   1398 ; 0.049 ; 0.500           
REMARK   3   TIGHT THERMAL      6    J (A**2):   1398 ; 0.048 ; 0.500           
REMARK   3   TIGHT THERMAL      6    K (A**2):   1398 ; 0.038 ; 0.500           
REMARK   3   TIGHT THERMAL      6    L (A**2):   1398 ; 0.040 ; 0.500           
REMARK   3   TIGHT THERMAL      6    M (A**2):   1398 ; 0.042 ; 0.500           
REMARK   3   TIGHT THERMAL      6    N (A**2):   1398 ; 0.043 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 7                                  
REMARK   3     CHAIN NAMES                    : O P Q R S T U                   
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     O      1       O      97      1                      
REMARK   3           1     P      1       P      97      1                      
REMARK   3           1     Q      1       Q      97      1                      
REMARK   3           1     R      1       R      97      1                      
REMARK   3           1     S      1       S      97      1                      
REMARK   3           1     T      1       T      97      1                      
REMARK   3           1     U      1       U      97      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   7    O    (A):    728 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   7    P    (A):    728 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   7    Q    (A):    728 ; 0.029 ; 0.050           
REMARK   3   TIGHT POSITIONAL   7    R    (A):    728 ; 0.030 ; 0.050           
REMARK   3   TIGHT POSITIONAL   7    S    (A):    728 ; 0.027 ; 0.050           
REMARK   3   TIGHT POSITIONAL   7    T    (A):    728 ; 0.028 ; 0.050           
REMARK   3   TIGHT POSITIONAL   7    U    (A):    728 ; 0.031 ; 0.050           
REMARK   3   TIGHT THERMAL      7    O (A**2):    728 ; 0.033 ; 0.500           
REMARK   3   TIGHT THERMAL      7    P (A**2):    728 ; 0.031 ; 0.500           
REMARK   3   TIGHT THERMAL      7    Q (A**2):    728 ; 0.029 ; 0.500           
REMARK   3   TIGHT THERMAL      7    R (A**2):    728 ; 0.032 ; 0.500           
REMARK   3   TIGHT THERMAL      7    S (A**2):    728 ; 0.026 ; 0.500           
REMARK   3   TIGHT THERMAL      7    T (A**2):    728 ; 0.027 ; 0.500           
REMARK   3   TIGHT THERMAL      7    U (A**2):    728 ; 0.032 ; 0.500           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 49                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A   135                          
REMARK   3    RESIDUE RANGE :   A   410        A   525                          
REMARK   3    RESIDUE RANGE :   A   600        A   603                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.2740 -53.5180 -12.3710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3516 T22:   0.3814                                     
REMARK   3      T33:   0.3869 T12:  -0.0340                                     
REMARK   3      T13:   0.0061 T23:  -0.0461                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9413 L22:   3.4049                                     
REMARK   3      L33:   0.4307 L12:  -0.5851                                     
REMARK   3      L13:   0.2788 L23:  -0.4602                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0335 S12:   0.0546 S13:  -0.1040                       
REMARK   3      S21:   0.0557 S22:   0.0995 S23:   0.0187                       
REMARK   3      S31:   0.0254 S32:  -0.0874 S33:  -0.0661                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   136        A   190                          
REMARK   3    RESIDUE RANGE :   A   375        A   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.1540 -46.6580 -28.0540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4906 T22:   0.7616                                     
REMARK   3      T33:   0.6163 T12:   0.0237                                     
REMARK   3      T13:  -0.1242 T23:  -0.0450                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.3003 L22:   5.2463                                     
REMARK   3      L33:   2.9806 L12:   6.2404                                     
REMARK   3      L13:   0.3986 L23:  -0.6283                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0040 S12:   0.2691 S13:  -0.2369                       
REMARK   3      S21:  -0.5703 S22:   0.2423 S23:  -0.2565                       
REMARK   3      S31:   0.2917 S32:  -0.7736 S33:  -0.2383                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   191        A   374                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.8820 -35.0130 -48.9510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8854 T22:   1.9684                                     
REMARK   3      T33:   1.4926 T12:  -0.3694                                     
REMARK   3      T13:   0.3299 T23:  -0.6224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1547 L22:   6.4438                                     
REMARK   3      L33:  13.4691 L12:   2.5083                                     
REMARK   3      L13:  -4.4496 L23:   0.1236                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7414 S12:  -1.2187 S13:   0.9749                       
REMARK   3      S21:   1.0424 S22:  -0.9627 S23:   1.1595                       
REMARK   3      S31:  -0.4118 S32:  -0.4474 S33:   0.2213                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     2        B   135                          
REMARK   3    RESIDUE RANGE :   B   410        B   525                          
REMARK   3    RESIDUE RANGE :   B   600        B   603                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.6430 -89.0510 -12.5440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3617 T22:   0.3866                                     
REMARK   3      T33:   0.5085 T12:  -0.0157                                     
REMARK   3      T13:   0.0477 T23:  -0.1293                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2110 L22:   3.1261                                     
REMARK   3      L33:   0.5960 L12:   0.0288                                     
REMARK   3      L13:   0.4883 L23:  -0.3110                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0409 S12:  -0.0844 S13:  -0.0162                       
REMARK   3      S21:  -0.0254 S22:  -0.0154 S23:   0.0039                       
REMARK   3      S31:   0.1782 S32:  -0.0927 S33:   0.0563                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   136        B   190                          
REMARK   3    RESIDUE RANGE :   B   375        B   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.9900 -97.3790 -28.1780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6662 T22:   0.7498                                     
REMARK   3      T33:   0.9582 T12:  -0.1284                                     
REMARK   3      T13:   0.0998 T23:  -0.2076                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1060 L22:  13.3476                                     
REMARK   3      L33:   3.5547 L12:  -1.0690                                     
REMARK   3      L13:   0.6254 L23:  -0.4932                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1439 S12:   0.4175 S13:  -0.6924                       
REMARK   3      S21:  -0.5577 S22:  -0.1793 S23:   0.2772                       
REMARK   3      S31:   0.8849 S32:  -0.3407 S33:   0.0354                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   191        B   374                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.8320 -81.7480 -48.9890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.0339 T22:   2.1476                                     
REMARK   3      T33:   1.8574 T12:   0.0732                                     
REMARK   3      T13:   0.5473 T23:   0.0852                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5233 L22:   9.4789                                     
REMARK   3      L33:  16.4721 L12:   1.3055                                     
REMARK   3      L13:  -1.8687 L23:  -5.7471                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2599 S12:  -0.7547 S13:  -0.7544                       
REMARK   3      S21:   1.6450 S22:   0.3304 S23:   1.3145                       
REMARK   3      S31:   0.5470 S32:  -0.7288 S33:  -0.5903                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     2        C   135                          
REMARK   3    RESIDUE RANGE :   C   410        C   525                          
REMARK   3    RESIDUE RANGE :   C   600        C   603                          
REMARK   3    ORIGIN FOR THE GROUP (A):  91.0140 -96.6650 -12.5790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3691 T22:   0.3838                                     
REMARK   3      T33:   0.1251 T12:   0.0087                                     
REMARK   3      T13:   0.1199 T23:  -0.0116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2231 L22:   5.0094                                     
REMARK   3      L33:   0.2864 L12:   1.0749                                     
REMARK   3      L13:   0.4958 L23:   0.2332                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0803 S12:  -0.0046 S13:   0.0219                       
REMARK   3      S21:   0.0675 S22:  -0.0390 S23:   0.3022                       
REMARK   3      S31:   0.0753 S32:   0.0894 S33:  -0.0413                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   136        C   190                          
REMARK   3    RESIDUE RANGE :   C   375        C   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  87.9080-114.0110 -28.3630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6244 T22:   0.6046                                     
REMARK   3      T33:   1.0680 T12:  -0.0280                                     
REMARK   3      T13:   0.1400 T23:  -0.0937                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2376 L22:  10.4353                                     
REMARK   3      L33:   4.2092 L12:  -4.7754                                     
REMARK   3      L13:   1.1821 L23:  -0.5463                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1033 S12:   1.0712 S13:   0.1916                       
REMARK   3      S21:  -0.4677 S22:  -0.1795 S23:  -1.4869                       
REMARK   3      S31:   0.5847 S32:   0.5770 S33:   0.0762                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   191        C   374                          
REMARK   3    ORIGIN FOR THE GROUP (A):  74.1890-105.8580 -48.8800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9436 T22:   2.0602                                     
REMARK   3      T33:   1.5912 T12:   0.0718                                     
REMARK   3      T13:   0.3423 T23:   0.4206                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.4144 L22:   4.9019                                     
REMARK   3      L33:  13.7942 L12:  -1.5977                                     
REMARK   3      L13:   1.4593 L23:  -4.1173                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3257 S12:  -1.4649 S13:  -1.6741                       
REMARK   3      S21:   0.7331 S22:   0.5651 S23:   0.3363                       
REMARK   3      S31:   0.4060 S32:  -0.4075 S33:  -0.2394                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     2        D   135                          
REMARK   3    RESIDUE RANGE :   D   410        D   525                          
REMARK   3    RESIDUE RANGE :   D   600        D   603                          
REMARK   3    ORIGIN FOR THE GROUP (A): 121.5020 -70.6900 -12.2560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2982 T22:   0.4302                                     
REMARK   3      T33:   0.3444 T12:  -0.0085                                     
REMARK   3      T13:   0.0232 T23:   0.0721                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8078 L22:   4.0793                                     
REMARK   3      L33:   0.4725 L12:  -0.0120                                     
REMARK   3      L13:  -0.0315 L23:   0.1963                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0239 S12:   0.0958 S13:   0.1465                       
REMARK   3      S21:   0.0956 S22:  -0.0011 S23:   0.1378                       
REMARK   3      S31:  -0.0125 S32:   0.0531 S33:   0.0249                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   136        D   190                          
REMARK   3    RESIDUE RANGE :   D   375        D   409                          
REMARK   3    ORIGIN FOR THE GROUP (A): 133.0160 -83.9570 -27.8400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4785 T22:   0.8082                                     
REMARK   3      T33:   0.9688 T12:   0.0233                                     
REMARK   3      T13:   0.1129 T23:   0.0563                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.7910 L22:   4.0960                                     
REMARK   3      L33:   3.3261 L12:   0.1256                                     
REMARK   3      L13:   0.5477 L23:   0.8737                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1293 S12:   0.6492 S13:   1.2725                       
REMARK   3      S21:  -0.3323 S22:   0.2222 S23:  -0.7122                       
REMARK   3      S31:   0.0499 S32:   0.9464 S33:  -0.0929                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   191        D   374                          
REMARK   3    ORIGIN FOR THE GROUP (A): 118.3470 -89.7600 -48.6900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7374 T22:   2.2743                                     
REMARK   3      T33:   1.7910 T12:  -0.2512                                     
REMARK   3      T13:  -0.1926 T23:   0.7876                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5146 L22:   4.8780                                     
REMARK   3      L33:  14.5790 L12:   0.6627                                     
REMARK   3      L13:   4.1777 L23:  -0.9614                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6303 S12:  -1.6305 S13:  -1.5545                       
REMARK   3      S21:   0.7189 S22:  -0.4539 S23:  -0.9617                       
REMARK   3      S31:   0.9001 S32:   0.6046 S33:  -0.1763                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     2        E   135                          
REMARK   3    RESIDUE RANGE :   E   410        E   525                          
REMARK   3    RESIDUE RANGE :   E   600        E   603                          
REMARK   3    ORIGIN FOR THE GROUP (A): 120.4420 -30.6350 -12.4330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3669 T22:   0.4727                                     
REMARK   3      T33:   0.7828 T12:  -0.0477                                     
REMARK   3      T13:  -0.0455 T23:   0.1480                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3975 L22:   3.2221                                     
REMARK   3      L33:   0.6994 L12:  -0.9019                                     
REMARK   3      L13:  -0.3805 L23:   0.4441                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0487 S12:  -0.0112 S13:   0.1598                       
REMARK   3      S21:  -0.0310 S22:   0.0227 S23:  -0.0849                       
REMARK   3      S31:  -0.1603 S32:   0.1310 S33:   0.0260                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   136        E   190                          
REMARK   3    RESIDUE RANGE :   E   375        E   409                          
REMARK   3    ORIGIN FOR THE GROUP (A): 138.1980 -30.0230 -27.9880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6135 T22:   0.9062                                     
REMARK   3      T33:   1.1213 T12:  -0.0474                                     
REMARK   3      T13:   0.0927 T23:   0.2792                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9415 L22:  11.5171                                     
REMARK   3      L33:   4.5528 L12:   5.5779                                     
REMARK   3      L13:  -1.2450 L23:   1.1023                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3959 S12:   0.3470 S13:   0.1762                       
REMARK   3      S21:  -0.8529 S22:  -0.0373 S23:   0.2146                       
REMARK   3      S31:  -0.9274 S32:   0.7219 S33:  -0.3586                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   191        E   374                          
REMARK   3    ORIGIN FOR THE GROUP (A): 133.2630 -45.0750 -48.7940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1852 T22:   2.1504                                     
REMARK   3      T33:   2.0024 T12:  -0.0575                                     
REMARK   3      T13:  -0.5652 T23:   0.2604                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3821 L22:   8.2286                                     
REMARK   3      L33:  15.5491 L12:   1.4727                                     
REMARK   3      L13:   4.7924 L23:   4.4908                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2751 S12:  -0.5882 S13:   0.1408                       
REMARK   3      S21:   1.6266 S22:   0.2852 S23:  -1.9611                       
REMARK   3      S31:  -0.1514 S32:   0.7906 S33:  -0.5603                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     2        F   135                          
REMARK   3    RESIDUE RANGE :   F   410        F   525                          
REMARK   3    RESIDUE RANGE :   F   600        F   603                          
REMARK   3    ORIGIN FOR THE GROUP (A):  88.3940  -6.5470 -12.6060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4585 T22:   0.4258                                     
REMARK   3      T33:   0.7974 T12:  -0.0081                                     
REMARK   3      T13:  -0.1285 T23:   0.1143                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7994 L22:   3.3271                                     
REMARK   3      L33:   0.6312 L12:   0.5400                                     
REMARK   3      L13:  -0.4793 L23:   0.0515                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0036 S12:   0.0105 S13:   0.2515                       
REMARK   3      S21:  -0.0439 S22:  -0.0211 S23:  -0.2698                       
REMARK   3      S31:  -0.2326 S32:   0.0341 S33:   0.0246                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   136        F   190                          
REMARK   3    RESIDUE RANGE :   F   375        F   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  98.9510   7.7850 -28.1850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7498 T22:   0.8368                                     
REMARK   3      T33:   1.6595 T12:  -0.1385                                     
REMARK   3      T13:   0.0217 T23:   0.2724                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6496 L22:  10.5892                                     
REMARK   3      L33:   3.0820 L12:  -4.7686                                     
REMARK   3      L13:  -0.6443 L23:  -1.5025                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2959 S12:   0.6941 S13:   0.9308                       
REMARK   3      S21:  -0.1221 S22:   0.0136 S23:   0.2639                       
REMARK   3      S31:  -0.5635 S32:  -0.1170 S33:  -0.3095                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   191        F   374                          
REMARK   3    ORIGIN FOR THE GROUP (A): 107.8710  -5.3750 -48.9960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.4442 T22:   2.3553                                     
REMARK   3      T33:   2.1005 T12:   0.1436                                     
REMARK   3      T13:  -0.4565 T23:  -0.1018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1776 L22:   4.2686                                     
REMARK   3      L33:   7.9165 L12:  -0.8233                                     
REMARK   3      L13:  -0.5536 L23:   2.3465                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0492 S12:  -0.7498 S13:   0.8852                       
REMARK   3      S21:   1.2256 S22:   0.2974 S23:  -0.8655                       
REMARK   3      S31:  -0.0276 S32:   0.0681 S33:  -0.2481                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G     2        G   135                          
REMARK   3    RESIDUE RANGE :   G   410        G   525                          
REMARK   3    RESIDUE RANGE :   G   600        G   603                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.4820 -16.8680 -12.7860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3427 T22:   0.3829                                     
REMARK   3      T33:   0.4223 T12:   0.0185                                     
REMARK   3      T13:  -0.0833 T23:  -0.0129                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7489 L22:   5.2105                                     
REMARK   3      L33:   0.5696 L12:   0.3579                                     
REMARK   3      L13:  -0.1700 L23:  -0.5039                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0578 S12:   0.0097 S13:   0.1475                       
REMARK   3      S21:   0.0881 S22:   0.0225 S23:  -0.1617                       
REMARK   3      S31:  -0.0567 S32:  -0.0161 S33:  -0.0803                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G   136        G   190                          
REMARK   3    RESIDUE RANGE :   G   375        G   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.7550   0.0030 -28.5930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6943 T22:   0.6113                                     
REMARK   3      T33:   0.9079 T12:   0.0274                                     
REMARK   3      T13:  -0.1386 T23:   0.0649                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.5048 L22:   5.2881                                     
REMARK   3      L33:   4.5629 L12:  -0.6952                                     
REMARK   3      L13:  -2.0299 L23:  -0.6132                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1638 S12:   0.9874 S13:   0.2025                       
REMARK   3      S21:  -0.4386 S22:   0.1306 S23:   0.9769                       
REMARK   3      S31:  -0.2503 S32:  -0.9126 S33:  -0.2944                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G   191        G   374                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.7100  -1.3030 -49.1720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9147 T22:   2.1653                                     
REMARK   3      T33:   1.9767 T12:  -0.1042                                     
REMARK   3      T13:   0.1044 T23:  -0.4730                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3818 L22:   4.0909                                     
REMARK   3      L33:  14.9399 L12:  -0.1647                                     
REMARK   3      L13:  -3.9249 L23:   3.0019                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4214 S12:  -1.4346 S13:   1.7424                       
REMARK   3      S21:   0.6177 S22:   0.0243 S23:   0.3220                       
REMARK   3      S31:  -0.6250 S32:   0.1514 S33:  -0.4456                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     2        H   135                          
REMARK   3    RESIDUE RANGE :   H   410        H   525                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.5550 -76.5050  19.5230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3510 T22:   0.4377                                     
REMARK   3      T33:   0.3435 T12:  -0.0074                                     
REMARK   3      T13:   0.0694 T23:   0.0200                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1563 L22:   5.6801                                     
REMARK   3      L33:   1.2542 L12:   0.3767                                     
REMARK   3      L13:   0.2810 L23:   0.1293                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0611 S12:   0.0399 S13:  -0.2789                       
REMARK   3      S21:  -0.0510 S22:   0.0627 S23:   0.2540                       
REMARK   3      S31:   0.1402 S32:  -0.1883 S33:  -0.0017                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   136        H   190                          
REMARK   3    RESIDUE RANGE :   H   375        H   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.6410 -89.3820  32.5860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8960 T22:   0.8875                                     
REMARK   3      T33:   1.0969 T12:  -0.0804                                     
REMARK   3      T13:   0.0921 T23:  -0.0411                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.1096 L22:   3.5240                                     
REMARK   3      L33:  10.1069 L12:  -3.2770                                     
REMARK   3      L13:   6.6476 L23:  -3.0984                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6026 S12:   0.1085 S13:  -0.1858                       
REMARK   3      S21:  -0.1576 S22:  -0.2875 S23:   0.7161                       
REMARK   3      S31:   0.6685 S32:  -0.4138 S33:  -0.3152                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   191        H   374                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.6250 -83.1120  57.6910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2607 T22:   1.1627                                     
REMARK   3      T33:   1.4790 T12:  -0.0361                                     
REMARK   3      T13:   0.0388 T23:  -0.0412                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.5788 L22:   6.5026                                     
REMARK   3      L33:   4.3451 L12:   1.5039                                     
REMARK   3      L13:  -0.7327 L23:   0.7618                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3370 S12:   0.0980 S13:  -1.2670                       
REMARK   3      S21:   0.3206 S22:  -0.0673 S23:   0.1983                       
REMARK   3      S31:   0.5343 S32:  -0.4586 S33:   0.4043                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I     2        I   135                          
REMARK   3    RESIDUE RANGE :   I   410        I   525                          
REMARK   3    ORIGIN FOR THE GROUP (A):  74.1570 -97.4700  19.5200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3642 T22:   0.4101                                     
REMARK   3      T33:   0.0097 T12:  -0.0053                                     
REMARK   3      T13:   0.0291 T23:   0.0544                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1536 L22:   7.0853                                     
REMARK   3      L33:   0.4577 L12:  -0.9262                                     
REMARK   3      L13:  -0.1295 L23:   0.8617                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0948 S12:   0.0952 S13:   0.0149                       
REMARK   3      S21:  -0.0645 S22:  -0.0062 S23:   0.0851                       
REMARK   3      S31:   0.0719 S32:  -0.0142 S33:  -0.0885                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I   136        I   190                          
REMARK   3    RESIDUE RANGE :   I   375        I   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  75.1780-117.3640  32.3950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6966 T22:   0.6872                                     
REMARK   3      T33:   0.8212 T12:  -0.0496                                     
REMARK   3      T13:   0.1632 T23:  -0.0049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4882 L22:   0.1176                                     
REMARK   3      L33:   9.5438 L12:   0.4319                                     
REMARK   3      L13:   2.5638 L23:   3.1334                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0422 S12:   0.2916 S13:  -0.6659                       
REMARK   3      S21:   0.9948 S22:  -0.3243 S23:  -0.1689                       
REMARK   3      S31:   0.7591 S32:  -0.4453 S33:   0.2820                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I   191        I   374                          
REMARK   3    ORIGIN FOR THE GROUP (A):  74.9030-107.8130  57.6130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1259 T22:   1.2390                                     
REMARK   3      T33:   1.3424 T12:   0.1266                                     
REMARK   3      T13:   0.0800 T23:   0.1339                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.8072 L22:  10.8026                                     
REMARK   3      L33:   5.2234 L12:   0.7689                                     
REMARK   3      L13:  -1.1765 L23:   0.0749                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5080 S12:  -0.6901 S13:  -1.4293                       
REMARK   3      S21:   0.1565 S22:   0.2738 S23:  -1.0577                       
REMARK   3      S31:   0.9242 S32:   0.2007 S33:   0.2343                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J     2        J   135                          
REMARK   3    RESIDUE RANGE :   J   410        J   525                          
REMARK   3    ORIGIN FOR THE GROUP (A): 111.7680 -84.5050  19.7300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3327 T22:   0.4370                                     
REMARK   3      T33:   0.3860 T12:  -0.0008                                     
REMARK   3      T13:   0.0067 T23:   0.0163                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6828 L22:   3.7126                                     
REMARK   3      L33:   0.6673 L12:   0.3233                                     
REMARK   3      L13:  -0.2304 L23:   0.2540                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1588 S12:   0.1550 S13:  -0.2476                       
REMARK   3      S21:   0.0693 S22:   0.1250 S23:  -0.0373                       
REMARK   3      S31:   0.0875 S32:   0.0888 S33:   0.0337                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J   136        J   190                          
REMARK   3    RESIDUE RANGE :   J   375        J   409                          
REMARK   3    ORIGIN FOR THE GROUP (A): 127.3570 -96.2940  33.0190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7902 T22:   0.9531                                     
REMARK   3      T33:   0.9193 T12:   0.1856                                     
REMARK   3      T13:   0.0511 T23:   0.1146                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8787 L22:  10.2318                                     
REMARK   3      L33:   8.7830 L12:  -1.0010                                     
REMARK   3      L13:   1.2370 L23:   4.6902                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3145 S12:  -0.1459 S13:  -0.7142                       
REMARK   3      S21:  -0.9978 S22:  -0.3798 S23:   0.1179                       
REMARK   3      S31:   0.2835 S32:   0.5283 S33:   0.0653                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J   191        J   374                          
REMARK   3    ORIGIN FOR THE GROUP (A): 119.5230 -90.0700  58.1040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8809 T22:   1.6413                                     
REMARK   3      T33:   1.0730 T12:  -0.0242                                     
REMARK   3      T13:   0.1543 T23:   0.0793                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.6016 L22:   8.2545                                     
REMARK   3      L33:   6.6924 L12:  -1.0145                                     
REMARK   3      L13:   0.7650 L23:  -2.2363                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4718 S12:  -0.5607 S13:   0.1754                       
REMARK   3      S21:  -0.1136 S22:  -1.0042 S23:  -0.9359                       
REMARK   3      S31:   0.5127 S32:   1.2685 S33:   0.5323                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K     2        K   135                          
REMARK   3    RESIDUE RANGE :   K   410        K   525                          
REMARK   3    ORIGIN FOR THE GROUP (A): 124.8830 -46.6070  19.6230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3747 T22:   0.4770                                     
REMARK   3      T33:   0.5952 T12:  -0.0081                                     
REMARK   3      T13:  -0.1049 T23:   0.0184                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0331 L22:   4.9276                                     
REMARK   3      L33:   1.1990 L12:   1.3647                                     
REMARK   3      L13:  -0.5406 L23:  -0.4371                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0778 S12:  -0.0474 S13:   0.0726                       
REMARK   3      S21:  -0.0560 S22:  -0.0670 S23:  -0.3552                       
REMARK   3      S31:  -0.0790 S32:   0.2194 S33:   0.1448                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 32                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K   136        K   190                          
REMARK   3    RESIDUE RANGE :   K   375        K   409                          
REMARK   3    ORIGIN FOR THE GROUP (A): 143.7750 -41.4640  32.7640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7257 T22:   1.2377                                     
REMARK   3      T33:   1.5158 T12:  -0.1971                                     
REMARK   3      T13:  -0.1879 T23:   0.0467                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.9246 L22:   0.8107                                     
REMARK   3      L33:   9.3686 L12:  -1.8791                                     
REMARK   3      L13:  -3.8745 L23:   2.8659                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2556 S12:   0.6151 S13:  -0.5096                       
REMARK   3      S21:   0.5885 S22:  -0.1953 S23:  -0.7062                       
REMARK   3      S31:  -0.3741 S32:   0.7910 S33:  -0.0603                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 33                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K   191        K   374                          
REMARK   3    ORIGIN FOR THE GROUP (A): 133.6070 -43.9560  57.8060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2311 T22:   1.3524                                     
REMARK   3      T33:   1.6811 T12:  -0.2690                                     
REMARK   3      T13:  -0.0781 T23:   0.0558                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9147 L22:   6.7298                                     
REMARK   3      L33:   5.8367 L12:  -0.4500                                     
REMARK   3      L13:   0.8440 L23:  -0.7430                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0717 S12:   0.1523 S13:   1.0788                       
REMARK   3      S21:   0.5389 S22:  -0.4266 S23:  -0.7562                       
REMARK   3      S31:  -0.6440 S32:   1.0447 S33:   0.4982                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 34                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     2        L   135                          
REMARK   3    RESIDUE RANGE :   L   410        L   525                          
REMARK   3    ORIGIN FOR THE GROUP (A): 103.6670 -12.8510  19.7300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4455 T22:   0.4896                                     
REMARK   3      T33:   0.6795 T12:  -0.0041                                     
REMARK   3      T13:  -0.1303 T23:  -0.0480                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3476 L22:   7.1433                                     
REMARK   3      L33:   1.6133 L12:  -1.1104                                     
REMARK   3      L13:   0.1384 L23:  -1.0258                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0788 S12:   0.1562 S13:   0.4455                       
REMARK   3      S21:  -0.1237 S22:  -0.1962 S23:  -0.3998                       
REMARK   3      S31:  -0.3853 S32:   0.1533 S33:   0.1174                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 35                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   136        L   190                          
REMARK   3    RESIDUE RANGE :   L   375        L   409                          
REMARK   3    ORIGIN FOR THE GROUP (A): 111.1500   5.1970  32.9040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3097 T22:   1.0048                                     
REMARK   3      T33:   1.5723 T12:  -0.2959                                     
REMARK   3      T13:  -0.4321 T23:  -0.0578                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1219 L22:   0.4185                                     
REMARK   3      L33:   8.9734 L12:  -0.5235                                     
REMARK   3      L13:  -2.9668 L23:   2.7698                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0744 S12:  -0.4185 S13:   0.2863                       
REMARK   3      S21:   0.5995 S22:   0.3980 S23:   0.0581                       
REMARK   3      S31:  -1.3721 S32:   0.9637 S33:  -0.4724                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 36                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   191        L   374                          
REMARK   3    ORIGIN FOR THE GROUP (A): 106.4620  -4.0720  57.7970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9111 T22:   1.1316                                     
REMARK   3      T33:   1.8647 T12:   0.0467                                     
REMARK   3      T13:  -0.2936 T23:  -0.0840                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5378 L22:   6.0616                                     
REMARK   3      L33:   5.3586 L12:   1.9213                                     
REMARK   3      L13:   1.4807 L23:  -0.2832                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7506 S12:  -0.1122 S13:   1.6484                       
REMARK   3      S21:   0.2333 S22:   0.3477 S23:   0.5675                       
REMARK   3      S31:  -1.2897 S32:   0.1311 S33:   0.4029                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 37                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M     2        M   135                          
REMARK   3    RESIDUE RANGE :   M   410        M   525                          
REMARK   3    ORIGIN FOR THE GROUP (A):  64.0700  -8.7060  19.4250              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3679 T22:   0.4312                                     
REMARK   3      T33:   0.2648 T12:  -0.0079                                     
REMARK   3      T13:  -0.0287 T23:  -0.0371                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5201 L22:   5.8969                                     
REMARK   3      L33:   0.5638 L12:  -1.4193                                     
REMARK   3      L13:   0.6260 L23:  -0.5252                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0524 S12:   0.2578 S13:   0.0409                       
REMARK   3      S21:   0.1352 S22:   0.0040 S23:  -0.1717                       
REMARK   3      S31:  -0.0856 S32:   0.0672 S33:  -0.0564                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 38                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M   136        M   190                          
REMARK   3    RESIDUE RANGE :   M   375        M   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  54.1780   8.5160  32.2010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8809 T22:   0.6318                                     
REMARK   3      T33:   0.9310 T12:  -0.0743                                     
REMARK   3      T13:  -0.1324 T23:  -0.1240                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3027 L22:   6.4038                                     
REMARK   3      L33:   7.7422 L12:   4.0299                                     
REMARK   3      L13:  -1.2877 L23:  -4.1309                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7427 S12:  -0.2332 S13:   0.2554                       
REMARK   3      S21:   0.5116 S22:   0.4530 S23:  -0.1347                       
REMARK   3      S31:  -0.4638 S32:  -0.0880 S33:   0.2897                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 39                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M   191        M   374                          
REMARK   3    ORIGIN FOR THE GROUP (A):  58.5000   0.1440  57.4610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4431 T22:   1.4154                                     
REMARK   3      T33:   1.2073 T12:  -0.0123                                     
REMARK   3      T13:  -0.0489 T23:  -0.0772                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1203 L22:   9.0288                                     
REMARK   3      L33:   4.8410 L12:  -1.2768                                     
REMARK   3      L13:   0.7684 L23:   0.5937                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1171 S12:  -0.6757 S13:   0.5572                       
REMARK   3      S21:  -0.0995 S22:  -0.1329 S23:   0.9308                       
REMARK   3      S31:  -0.7157 S32:  -0.5467 S33:   0.2500                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 40                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   N     2        N   135                          
REMARK   3    RESIDUE RANGE :   N   410        N   525                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.9240 -36.7870  19.6420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3939 T22:   0.4197                                     
REMARK   3      T33:   0.3597 T12:   0.0025                                     
REMARK   3      T13:  -0.0549 T23:  -0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8271 L22:   4.1714                                     
REMARK   3      L33:   0.5608 L12:   1.7098                                     
REMARK   3      L13:   0.1136 L23:   0.1601                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2532 S12:   0.0842 S13:   0.3568                       
REMARK   3      S21:  -0.1122 S22:   0.2145 S23:   0.2428                       
REMARK   3      S31:  -0.0857 S32:  -0.0790 S33:   0.0387                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 41                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   N   136        N   190                          
REMARK   3    RESIDUE RANGE :   N   375        N   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.7400 -33.0820  32.9480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7711 T22:   1.2086                                     
REMARK   3      T33:   0.8203 T12:   0.0621                                     
REMARK   3      T13:   0.0341 T23:  -0.1413                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0196 L22:   8.3885                                     
REMARK   3      L33:   8.1619 L12:   0.9663                                     
REMARK   3      L13:  -0.5103 L23:  -3.6769                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0697 S12:   0.3452 S13:   1.0255                       
REMARK   3      S21:  -0.5019 S22:   0.2765 S23:   0.5369                       
REMARK   3      S31:  -0.2258 S32:  -0.8167 S33:  -0.3462                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 42                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   N   191        N   374                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.3770 -35.4300  58.0320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2053 T22:   1.5280                                     
REMARK   3      T33:   1.3762 T12:  -0.2356                                     
REMARK   3      T13:  -0.1818 T23:  -0.1647                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.7949 L22:   9.0637                                     
REMARK   3      L33:   6.2183 L12:  -1.4497                                     
REMARK   3      L13:  -1.7456 L23:   1.3609                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6072 S12:  -0.0621 S13:  -1.1425                       
REMARK   3      S21:   0.4954 S22:  -1.0433 S23:   1.3756                       
REMARK   3      S31:  -0.1158 S32:  -1.0989 S33:   0.4361                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 43                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   O     1        O    97                          
REMARK   3    ORIGIN FOR THE GROUP (A):  65.7220 -29.5560 -98.1260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8145 T22:   1.8394                                     
REMARK   3      T33:   1.3709 T12:  -0.0643                                     
REMARK   3      T13:  -0.0075 T23:  -0.0921                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5122 L22:   4.7923                                     
REMARK   3      L33:   9.8536 L12:   2.7327                                     
REMARK   3      L13:  -3.4755 L23:  -2.8614                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3692 S12:  -0.2787 S13:  -0.4064                       
REMARK   3      S21:   0.5688 S22:  -0.4076 S23:   0.4651                       
REMARK   3      S31:  -0.8752 S32:  -0.4615 S33:   0.0384                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 44                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   P     1        P    97                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.9980 -48.7480 -98.0830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8006 T22:   2.0247                                     
REMARK   3      T33:   1.3726 T12:  -0.0022                                     
REMARK   3      T13:   0.0543 T23:  -0.1902                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2702 L22:  10.1108                                     
REMARK   3      L33:   7.6103 L12:   3.3695                                     
REMARK   3      L13:  -1.8114 L23:  -6.6623                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0032 S12:  -0.2953 S13:  -0.7258                       
REMARK   3      S21:   0.7808 S22:   0.0407 S23:  -0.1251                       
REMARK   3      S31:  -0.4267 S32:  -0.2531 S33:  -0.0375                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 45                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Q     1        Q    97                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.2040 -70.7420 -98.1070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7009 T22:   2.1422                                     
REMARK   3      T33:   1.3907 T12:  -0.1085                                     
REMARK   3      T13:   0.2414 T23:  -0.0113                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2734 L22:   9.7593                                     
REMARK   3      L33:   9.8893 L12:  -3.7833                                     
REMARK   3      L13:   3.5340 L23:  -4.4063                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0276 S12:  -0.6422 S13:  -0.8134                       
REMARK   3      S21:   0.4617 S22:   0.0558 S23:   0.0008                       
REMARK   3      S31:   0.1877 S32:  -0.2073 S33:  -0.0834                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 46                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   R     1        R    97                          
REMARK   3    ORIGIN FOR THE GROUP (A):  81.8750 -78.3980 -98.0250              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9101 T22:   1.9995                                     
REMARK   3      T33:   1.3998 T12:  -0.0506                                     
REMARK   3      T13:   0.1556 T23:   0.1818                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.3647 L22:   1.5795                                     
REMARK   3      L33:   9.6435 L12:  -0.7000                                     
REMARK   3      L13:   5.0271 L23:   0.5128                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3108 S12:  -0.6682 S13:  -0.1589                       
REMARK   3      S21:   0.3830 S22:  -0.0555 S23:  -0.7297                       
REMARK   3      S31:   0.2237 S32:  -0.0180 S33:  -0.2553                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 47                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   S     1        S    97                          
REMARK   3    ORIGIN FOR THE GROUP (A): 101.5240 -66.5430 -97.9680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8330 T22:   1.9518                                     
REMARK   3      T33:   1.5239 T12:   0.1358                                     
REMARK   3      T13:   0.1962 T23:   0.2965                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.4646 L22:   8.0801                                     
REMARK   3      L33:  10.0806 L12:   4.1593                                     
REMARK   3      L13:   5.0036 L23:   5.4218                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3424 S12:  -0.4158 S13:   0.3595                       
REMARK   3      S21:   0.7058 S22:   0.0743 S23:  -0.6861                       
REMARK   3      S31:   0.8432 S32:   0.0683 S33:  -0.4167                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 48                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   T     1        T    97                          
REMARK   3    ORIGIN FOR THE GROUP (A): 104.4370 -43.7020 -98.1440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5758 T22:   2.1504                                     
REMARK   3      T33:   1.5697 T12:   0.0544                                     
REMARK   3      T13:   0.0001 T23:   0.2423                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7537 L22:  14.7623                                     
REMARK   3      L33:   9.8965 L12:  -0.6239                                     
REMARK   3      L13:  -1.2112 L23:   5.6545                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1035 S12:  -0.5262 S13:   0.5457                       
REMARK   3      S21:   1.1387 S22:   0.5111 S23:  -0.5617                       
REMARK   3      S31:   0.2260 S32:   0.4211 S33:  -0.4076                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 49                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   U     1        U    97                          
REMARK   3    ORIGIN FOR THE GROUP (A):  88.5350 -27.0200 -98.3380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6862 T22:   2.0937                                     
REMARK   3      T33:   1.4848 T12:  -0.1774                                     
REMARK   3      T13:  -0.0528 T23:  -0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2215 L22:   3.1239                                     
REMARK   3      L33:  10.1555 L12:  -2.6750                                     
REMARK   3      L13:  -2.3202 L23:   2.5592                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1382 S12:  -0.9569 S13:   0.4174                       
REMARK   3      S21:   0.6255 S22:   0.1529 S23:   0.6524                       
REMARK   3      S31:  -0.0594 S32:   0.3336 S33:  -0.0147                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK BULK SOLVENT                                    
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: NULL                                      
REMARK   4                                                                      
REMARK   4 1SVT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB022035.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 231127                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.77                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3000, CACODYLIC ACID, POTASSIUM       
REMARK 280  CHLORIDE, PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000      127.77300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      133.42750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      127.77300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      133.42750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 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: 21-MERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 21-MERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 78620 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 317280 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -466.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,            
REMARK 350                    AND CHAINS: J, K, L, M, N, O, P, Q, R,            
REMARK 350                    AND CHAINS: S, T, U                               
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 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   NH1  ARG A   452     O    HOH A   614              1.88            
REMARK 500   OH   TYR G   478     O    HOH G   611              1.88            
REMARK 500   NZ   LYS I   425     O    HOH I   540              1.90            
REMARK 500   N    GLU H   434     O    HOH H   536              1.93            
REMARK 500   OE1  GLU G   409     O    HOH G   619              1.95            
REMARK 500   NZ   LYS M   425     O    HOH M   532              2.06            
REMARK 500   O3B  ADP D   600     F2   AF3 D   602              2.08            
REMARK 500   O2A  ADP C   600     F1   AF3 C   602              2.10            
REMARK 500   NH2  ARG L   421     O    HOH L   537              2.10            
REMARK 500   O2A  ADP E   600     F1   AF3 E   602              2.11            
REMARK 500   O    THR C   125     O    HOH C   609              2.12            
REMARK 500   O2A  ADP A   600     F1   AF3 A   602              2.12            
REMARK 500   O3B  ADP B   600     F2   AF3 B   602              2.15            
REMARK 500   OD2  ASP N    87     O    HOH N   530              2.17            
REMARK 500   O    ASP B   359     OE2  GLU B   363              2.18            
REMARK 500   O    ASP E   359     OE2  GLU E   363              2.18            
REMARK 500   NH1  ARG D   452     O    HOH D   609              2.18            
REMARK 500   O1B  ADP D   600     F2   AF3 D   602              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PHE A  44   CE1   PHE A  44   CZ      0.114                       
REMARK 500    MET A  73   SD    MET A  73   CE      0.493                       
REMARK 500    GLU A  76   CD    GLU A  76   OE1     0.114                       
REMARK 500    GLU A  76   CD    GLU A  76   OE2     0.114                       
REMARK 500    MET A 111   SD    MET A 111   CE      0.355                       
REMARK 500    GLU A 129   CG    GLU A 129   CD      0.114                       
REMARK 500    GLU A 129   CD    GLU A 129   OE1     0.089                       
REMARK 500    GLU A 129   CD    GLU A 129   OE2     0.093                       
REMARK 500    GLU A 130   CD    GLU A 130   OE1     0.084                       
REMARK 500    GLU A 391   CD    GLU A 391   OE1     0.074                       
REMARK 500    GLU A 434   CG    GLU A 434   CD      0.104                       
REMARK 500    GLU A 434   CD    GLU A 434   OE1     0.074                       
REMARK 500    GLU A 484   CD    GLU A 484   OE2     0.086                       
REMARK 500    TYR A 506   CG    TYR A 506   CD1    -0.092                       
REMARK 500    VAL A 510   CB    VAL A 510   CG1    -0.137                       
REMARK 500    GLU B  76   CD    GLU B  76   OE1     0.089                       
REMARK 500    GLU B 102   CG    GLU B 102   CD      0.096                       
REMARK 500    MET B 111   SD    MET B 111   CE      0.368                       
REMARK 500    GLU B 129   CG    GLU B 129   CD      0.093                       
REMARK 500    GLU B 391   CD    GLU B 391   OE1     0.073                       
REMARK 500    GLU B 483   CD    GLU B 483   OE1     0.098                       
REMARK 500    GLU B 484   CD    GLU B 484   OE2     0.071                       
REMARK 500    MET B 514   SD    MET B 514   CE      0.433                       
REMARK 500    MET C  73   SD    MET C  73   CE      0.547                       
REMARK 500    GLU C  76   CD    GLU C  76   OE1     0.131                       
REMARK 500    ASP C  83   C     ASP C  83   O       0.156                       
REMARK 500    VAL C  94   C     VAL C  94   O       0.163                       
REMARK 500    GLN C  97   CB    GLN C  97   CG     -0.197                       
REMARK 500    GLU C 102   CG    GLU C 102   CD      0.145                       
REMARK 500    GLU C 102   CD    GLU C 102   OE1     0.082                       
REMARK 500    LYS C 105   CD    LYS C 105   CE      0.164                       
REMARK 500    LYS C 105   C     LYS C 105   O       0.114                       
REMARK 500    LYS C 117   CB    LYS C 117   CG     -0.203                       
REMARK 500    GLU C 129   CG    GLU C 129   CD      0.111                       
REMARK 500    GLU C 129   CD    GLU C 129   OE1     0.079                       
REMARK 500    GLU C 391   CD    GLU C 391   OE1     0.071                       
REMARK 500    GLU C 397   CD    GLU C 397   OE2     0.070                       
REMARK 500    ASP C 398   CB    ASP C 398   CG      0.172                       
REMARK 500    ASP C 398   CG    ASP C 398   OD1     0.138                       
REMARK 500    GLN C 432   CG    GLN C 432   CD      0.141                       
REMARK 500    CYS C 458   CB    CYS C 458   SG     -0.112                       
REMARK 500    ALA C 511   CA    ALA C 511   CB      0.140                       
REMARK 500    MET C 514   SD    MET C 514   CE      0.356                       
REMARK 500    PHE D  44   CE1   PHE D  44   CZ      0.125                       
REMARK 500    MET D  73   SD    MET D  73   CE      0.394                       
REMARK 500    VAL D  74   CB    VAL D  74   CG1    -0.130                       
REMARK 500    GLU D  76   CD    GLU D  76   OE1     0.090                       
REMARK 500    GLU D 102   CG    GLU D 102   CD      0.107                       
REMARK 500    GLU D 102   CD    GLU D 102   OE1     0.078                       
REMARK 500    GLU D 102   CD    GLU D 102   OE2     0.068                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     147 BOND DEVIATIONS.                              
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    ASP A  11   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ILE A  49   CG1 -  CB  -  CG2 ANGL. DEV. = -15.2 DEGREES          
REMARK 500    ASP A  64   CB  -  CG  -  OD2 ANGL. DEV. =   8.4 DEGREES          
REMARK 500    LYS A  65   CD  -  CE  -  NZ  ANGL. DEV. = -14.0 DEGREES          
REMARK 500    ASP A  87   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP A 115   CB  -  CG  -  OD2 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    LEU A 116   CB  -  CG  -  CD1 ANGL. DEV. = -11.0 DEGREES          
REMARK 500    ASP A 121   CB  -  CG  -  OD1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    CYS A 138   CA  -  CB  -  SG  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ASP A 188   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP A 328   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A 398   CB  -  CG  -  OD1 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    LEU A 419   CB  -  CG  -  CD2 ANGL. DEV. = -10.2 DEGREES          
REMARK 500    ASP A 435   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    LEU A 444   CB  -  CG  -  CD1 ANGL. DEV. = -11.4 DEGREES          
REMARK 500    ARG A 452   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ASP A 523   CB  -  CG  -  OD2 ANGL. DEV. =   8.2 DEGREES          
REMARK 500    ASP B  11   CB  -  CG  -  OD1 ANGL. DEV. =  -7.6 DEGREES          
REMARK 500    ASP B  11   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP B  25   CB  -  CG  -  OD1 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ILE B  49   CG1 -  CB  -  CG2 ANGL. DEV. = -13.2 DEGREES          
REMARK 500    LEU B  62   CB  -  CG  -  CD2 ANGL. DEV. = -14.2 DEGREES          
REMARK 500    ASP B 115   CB  -  CG  -  OD2 ANGL. DEV. =   7.8 DEGREES          
REMARK 500    ARG B 118   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP B 140   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP B 328   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP B 398   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    LEU B 419   CB  -  CG  -  CD2 ANGL. DEV. = -12.2 DEGREES          
REMARK 500    ASP B 435   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP C  41   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ILE C  49   CG1 -  CB  -  CG2 ANGL. DEV. = -14.5 DEGREES          
REMARK 500    LEU C  62   CB  -  CG  -  CD2 ANGL. DEV. = -12.7 DEGREES          
REMARK 500    ASP C  64   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP C  87   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ILE C 100   CG1 -  CB  -  CG2 ANGL. DEV. = -14.8 DEGREES          
REMARK 500    ASP C 121   CB  -  CG  -  OD1 ANGL. DEV. =   8.4 DEGREES          
REMARK 500    LEU C 131   CB  -  CG  -  CD2 ANGL. DEV. = -13.2 DEGREES          
REMARK 500    LEU C 134   CB  -  CG  -  CD2 ANGL. DEV. = -10.7 DEGREES          
REMARK 500    ASP C 398   CB  -  CG  -  OD1 ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ASP C 490   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG C 501   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    LEU C 513   CA  -  CB  -  CG  ANGL. DEV. = -16.0 DEGREES          
REMARK 500    MET C 514   CG  -  SD  -  CE  ANGL. DEV. = -11.9 DEGREES          
REMARK 500    ASP C 523   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ASP D  11   CB  -  CG  -  OD1 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    ASP D  11   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ASP D  64   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP D 121   CB  -  CG  -  OD1 ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ASP D 121   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    ASP D 188   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     155 ANGLE DEVIATIONS.                             
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                                                                      
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    LYS A  34       31.11    -96.06                                   
REMARK 500    PHE A  44      -94.13      8.83                                   
REMARK 500    ARG A  58      -15.61    -49.92                                   
REMARK 500    ALA A  84      -61.29   -103.46                                   
REMARK 500    ALA A  85      -72.81    -63.18                                   
REMARK 500    SER A 139      -31.95   -132.62                                   
REMARK 500    ALA A 152       39.19    -84.35                                   
REMARK 500    PRO A 202        3.04    -52.91                                   
REMARK 500    LYS A 225      159.41    160.34                                   
REMARK 500    ARG A 268       21.10    -75.30                                   
REMARK 500    LYS A 311       53.68    -93.09                                   
REMARK 500    ASP A 328       26.14   -155.60                                   
REMARK 500    ASP A 334       84.51     61.77                                   
REMARK 500    ALA A 356       99.76    -66.18                                   
REMARK 500    ALA A 373     -107.64    -77.45                                   
REMARK 500    THR A 385     -150.48   -109.68                                   
REMARK 500    PHE B  44      -95.04      8.26                                   
REMARK 500    ALA B  85      -74.70    -72.57                                   
REMARK 500    SER B 139      -35.61   -132.08                                   
REMARK 500    ALA B 152       44.09    -88.06                                   
REMARK 500    PRO B 202        4.67    -53.40                                   
REMARK 500    PHE B 204      -35.86    -39.94                                   
REMARK 500    LYS B 225      164.62    162.55                                   
REMARK 500    GLU B 257      -70.25    -47.64                                   
REMARK 500    ARG B 268       21.95    -74.92                                   
REMARK 500    LYS B 311       54.97    -94.67                                   
REMARK 500    ASP B 328       24.98   -151.40                                   
REMARK 500    ASP B 334       83.42     61.51                                   
REMARK 500    ALA B 356       99.22    -66.83                                   
REMARK 500    ALA B 373     -105.18    -78.34                                   
REMARK 500    THR B 385     -145.60   -103.68                                   
REMARK 500    SER B 463      -53.94    -28.47                                   
REMARK 500    LEU C  23      -74.05    -54.12                                   
REMARK 500    LYS C  28      -40.87    -28.93                                   
REMARK 500    PHE C  44      -96.48      4.53                                   
REMARK 500    ARG C  58      -17.92    -42.81                                   
REMARK 500    ALA C  84      -60.27   -101.51                                   
REMARK 500    ALA C  85      -84.38    -69.73                                   
REMARK 500    SER C 139      -32.58   -132.27                                   
REMARK 500    ALA C 152       42.25    -87.93                                   
REMARK 500    PRO C 202        3.20    -54.23                                   
REMARK 500    LYS C 225      164.28    162.46                                   
REMARK 500    ARG C 268       22.35    -75.22                                   
REMARK 500    ILE C 270      -72.14    -69.02                                   
REMARK 500    LYS C 311       51.35    -91.56                                   
REMARK 500    ASP C 328       25.44   -151.54                                   
REMARK 500    ASP C 334       86.03     61.93                                   
REMARK 500    ALA C 356       99.57    -66.72                                   
REMARK 500    ALA C 373     -103.54    -77.62                                   
REMARK 500    THR C 385     -150.35   -112.28                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     377 RAMACHANDRAN OUTLIERS.                        
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 SER A   43     PHE A   44                  149.78                    
REMARK 500 GLY H   32     PRO H   33                  143.83                    
REMARK 500 GLY I   32     PRO I   33                  138.93                    
REMARK 500 GLY J   32     PRO J   33                  148.19                    
REMARK 500 GLY K   32     PRO K   33                  147.25                    
REMARK 500 GLY L   32     PRO L   33                  146.83                    
REMARK 500 GLY M   32     PRO M   33                  145.16                    
REMARK 500 GLY N   32     PRO N   33                  148.58                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL A 422        24.1      L          L   OUTSIDE RANGE           
REMARK 500    ALA A 449        24.2      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 499        23.2      L          L   OUTSIDE RANGE           
REMARK 500    THR B 468        24.2      L          L   OUTSIDE RANGE           
REMARK 500    VAL B 499        20.4      L          L   OUTSIDE RANGE           
REMARK 500    ALA C 449        24.3      L          L   OUTSIDE RANGE           
REMARK 500    THR C 468        25.0      L          L   OUTSIDE RANGE           
REMARK 500    VAL C 499        22.3      L          L   OUTSIDE RANGE           
REMARK 500    VAL D 422        22.0      L          L   OUTSIDE RANGE           
REMARK 500    ALA D 423        23.4      L          L   OUTSIDE RANGE           
REMARK 500    VAL E 499        24.0      L          L   OUTSIDE RANGE           
REMARK 500    VAL F 422        24.9      L          L   OUTSIDE RANGE           
REMARK 500    THR F 468        23.4      L          L   OUTSIDE RANGE           
REMARK 500    VAL F 499        21.6      L          L   OUTSIDE RANGE           
REMARK 500    VAL G 499        20.8      L          L   OUTSIDE RANGE           
REMARK 500    THR H 468        21.6      L          L   OUTSIDE RANGE           
REMARK 500    ALA I  78        22.4      L          L   OUTSIDE RANGE           
REMARK 500    LEU I 426        24.7      L          L   OUTSIDE RANGE           
REMARK 500    THR I 468        24.0      L          L   OUTSIDE RANGE           
REMARK 500    THR J 468        21.5      L          L   OUTSIDE RANGE           
REMARK 500    THR K 468        23.8      L          L   OUTSIDE RANGE           
REMARK 500    THR L 468        22.1      L          L   OUTSIDE RANGE           
REMARK 500    THR M 468        23.6      L          L   OUTSIDE RANGE           
REMARK 500    THR N 468        19.2      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A 600   O1B                                                    
REMARK 620 2 ADP A 600   O2A  80.3                                              
REMARK 620 3 AF3 A 602   F1   97.5  74.8                                        
REMARK 620 4 ASP A  87   OD1  90.5 158.2  87.0                                  
REMARK 620 5 AF3 A 602  AL    67.3  89.7  36.4  68.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             AF3 A 602  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  87   OD1                                                    
REMARK 620 2 AF3 A 602   F1   66.8                                              
REMARK 620 3 AF3 A 602   F2   55.7 113.5                                        
REMARK 620 4 AF3 A 602   F3  143.6 135.1 111.2                                  
REMARK 620 5 ADP A 600   O1B  58.5  62.1  61.0 150.9                            
REMARK 620 6 ADP A 600   O3B 106.9 114.5  61.0  89.8  61.5                      
REMARK 620 7 ADP A 600   O2A  76.9  33.2  99.5 138.6  38.6  81.3                
REMARK 620 8 ADP A 600   O3A 103.9  73.4  89.8 110.2  45.7  43.6  41.2          
REMARK 620 9 THR A  89   OG1 107.5 172.9  64.2  47.2 119.4  70.8 151.9 112.8    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 603   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A 600   O3A                                                    
REMARK 620 2 THR A  30   O   104.1                                              
REMARK 620 3 ADP A 600   O1A  47.1  64.4                                        
REMARK 620 4 LYS A  51   O   156.5  93.6 134.4                                  
REMARK 620 5 AF3 A 602   F3   79.5 172.8 115.9  81.3                            
REMARK 620 6 THR A  30   OG1 134.2  67.1 127.2  67.0 114.9                      
REMARK 620 7 THR A  90   OG1  78.3 124.6 121.1 104.4  61.9  72.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP B 600   O1B                                                    
REMARK 620 2 ADP B 600   O2A  87.9                                              
REMARK 620 3 ASP B  87   OD1  79.0 154.7                                        
REMARK 620 4 AF3 B 602   F1   83.7  74.2  82.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             AF3 B 602  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP B 600   O3B                                                    
REMARK 620 2 AF3 B 602   F1  113.7                                              
REMARK 620 3 AF3 B 602   F2   68.4 122.2                                        
REMARK 620 4 AF3 B 602   F3   82.3 136.4 101.3                                  
REMARK 620 5  MG B 601  MG    96.3  26.7  97.7 158.8                            
REMARK 620 6 ADP B 600   O2A  88.0  26.0 118.3 132.1  27.0                      
REMARK 620 7 ASP B  87   OD1 106.7  64.6  60.6 152.5  48.0  74.9                
REMARK 620 8 THR B  89   OG1  69.4 165.4  44.3  57.1 141.9 155.1 100.9          
REMARK 620 9 ADP B 600   O1B  65.7  56.2  78.4 145.9  31.9  40.4  55.7 116.9    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B 603   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP B 600   O1A                                                    
REMARK 620 2 ADP B 600   O3A  47.4                                              
REMARK 620 3 LYS B  51   O   141.4 158.4                                        
REMARK 620 4 AF3 B 602   F3  117.2  75.9  84.6                                  
REMARK 620 5 THR B  30   O    65.4 103.9  96.4 173.7                            
REMARK 620 6 THR B  30   OG1 122.9 123.4  71.5 108.6  66.0                      
REMARK 620 7 THR B  90   OG1 113.9  70.3 104.6  51.4 122.5  71.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP C 600   O1B                                                    
REMARK 620 2 ADP C 600   O2A  86.4                                              
REMARK 620 3 ASP C  87   OD1  73.5 156.0                                        
REMARK 620 4 AF3 C 602   F1   94.9  74.7  93.7                                  
REMARK 620 5 AF3 C 602  AL    64.2  85.7  73.9  33.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             AF3 C 602  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP C 600   O3B                                                    
REMARK 620 2 AF3 C 602   F1  120.4                                              
REMARK 620 3 AF3 C 602   F2   55.8 114.8                                        
REMARK 620 4 AF3 C 602   F3   84.2 139.2 105.9                                  
REMARK 620 5 ADP C 600   O3A  50.1  76.3  94.1 103.8                            
REMARK 620 6 ADP C 600   O2A  89.5  33.2 108.8 132.5  43.2                      
REMARK 620 7 ASP C  87   OD1  96.4  62.4  55.0 153.2  96.8  74.2                
REMARK 620 8 ADP C 600   O1B  63.3  62.4  63.3 146.5  49.6  45.5  47.6          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C 603   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP C 600   O3A                                                    
REMARK 620 2 ADP C 600   O1A  46.0                                              
REMARK 620 3 AF3 C 602   F3   74.6 113.6                                        
REMARK 620 4 THR C  90   OG1  69.8 112.5  52.6                                  
REMARK 620 5 THR C  30   OG1 129.2 132.3 105.5  71.4                            
REMARK 620 6 LYS C  51   NZ   95.4  52.3 128.6 164.8 118.3                      
REMARK 620 7 LYS C  51   O   150.0 143.6  77.7 101.8  69.6  92.9                
REMARK 620 8 THR C  30   O   107.8  69.0 177.4 126.9  72.2  52.7 100.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP D 600   O2A                                                    
REMARK 620 2 ADP D 600   O1B 102.3                                              
REMARK 620 3 ASP D  87   OD1 165.0  77.2                                        
REMARK 620 4 AF3 D 602   F1   73.7 100.6  91.6                                  
REMARK 620 5 AF3 D 602  AL    94.2  66.1  71.8  37.0                            
REMARK 620 6 AF3 D 602   F2  119.6  41.6  50.6  71.4  35.1                      
REMARK 620 7 HOH D 611   O   124.8 127.3  51.1  74.7  86.4  90.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             AF3 D 602  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP D 600   O3B                                                    
REMARK 620 2 AF3 D 602   F1  116.5                                              
REMARK 620 3 AF3 D 602   F2   63.9 110.2                                        
REMARK 620 4 AF3 D 602   F3   84.1 137.2 112.5                                  
REMARK 620 5 ADP D 600   O3A  46.4  71.7  89.8 109.4                            
REMARK 620 6 THR D  89   OG1  70.0 172.4  68.3  44.7 115.5                      
REMARK 620 7 ADP D 600   O2A  88.6  27.9  98.1 141.0  45.0 158.0                
REMARK 620 8 ADP D 600   O1B  65.4  64.6  53.4 149.5  50.3 117.3  45.1          
REMARK 620 9 ASP D  87   OD1 106.5  68.8  49.8 144.5 101.7 106.2  74.2  52.1    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K D 603   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP D 600   O3A                                                    
REMARK 620 2 THR D  90   OG1  69.7                                              
REMARK 620 3 AF3 D 602   F3   76.2  57.6                                        
REMARK 620 4 ADP D 600   O1A  45.9 111.7 113.9                                  
REMARK 620 5 THR D  30   O   100.6 116.9 174.2  65.6                            
REMARK 620 6 THR D  30   OG1 120.9  68.7 112.3 122.7  65.0                      
REMARK 620 7 LYS D  51   O   160.4 104.2  84.8 144.0  98.7  70.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP E 600   O1B                                                    
REMARK 620 2 ADP E 600   O2A  95.0                                              
REMARK 620 3 HOH E 608   O   143.0 121.7                                        
REMARK 620 4 AF3 E 602   F1  101.9  75.8  84.6                                  
REMARK 620 5 ASP E  87   OD1  83.2 166.9  60.0  91.8                            
REMARK 620 6 AF3 E 602  AL    69.3  95.2 100.4  36.7  71.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             AF3 E 602  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E  87   OD1                                                    
REMARK 620 2 AF3 E 602   F1   68.1                                              
REMARK 620 3 AF3 E 602   F2   52.2 118.7                                        
REMARK 620 4 AF3 E 602   F3  153.9 133.4 107.8                                  
REMARK 620 5 ADP E 600   O2A  74.0  29.7 111.3 132.1                            
REMARK 620 6 ADP E 600   O1B  53.4  64.4  69.8 142.4  43.0                      
REMARK 620 7 ADP E 600   O3A 101.6  72.1 105.0 100.0  43.7  48.8                
REMARK 620 8 THR E  89   OG1 103.6 169.9  54.9  53.2 155.8 115.8 116.1          
REMARK 620 9 ADP E 600   O3B 105.1 116.1  72.5  79.9  86.4  63.4  46.1  70.8    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E 603   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP E 600   O1A                                                    
REMARK 620 2 ADP E 600   O3A  44.4                                              
REMARK 620 3 THR E  90   OG1 108.3  68.1                                        
REMARK 620 4 THR E  30   OG1 124.0 124.2  72.1                                  
REMARK 620 5 THR E  30   O    63.4 100.4 122.0  70.0                            
REMARK 620 6 AF3 E 602   F3  109.9  70.9  52.4 111.7 170.7                      
REMARK 620 7 LYS E  51   O   139.3 155.5 111.8  76.2  99.8  89.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP F 600   O2A                                                    
REMARK 620 2 ADP F 600   O1B  84.3                                              
REMARK 620 3 AF3 F 602   F1   74.5  97.5                                        
REMARK 620 4 ASP F  87   OD1 155.3  78.1  90.7                                  
REMARK 620 5 AF3 F 602  AL    88.6  65.4  36.4  68.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             AF3 F 602  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F  87   OD1                                                    
REMARK 620 2 AF3 F 602   F1   69.1                                              
REMARK 620 3 AF3 F 602   F2   51.0 117.4                                        
REMARK 620 4 AF3 F 602   F3  150.8 134.9 107.6                                  
REMARK 620 5 ADP F 600   O1B  53.4  64.1  66.6 143.9                            
REMARK 620 6 ADP F 600   O3B 100.8 116.1  66.0  83.5  61.3                      
REMARK 620 7 ADP F 600   O2A  74.7  32.1 106.8 134.4  40.9  84.0                
REMARK 620 8 ADP F 600   O3A  98.8  73.8  97.0 104.0  45.6  44.6  42.6          
REMARK 620 9 THR F  89   OG1 106.2 172.9  60.0  47.9 117.9  69.5 153.3 112.7    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K F 603   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP F 600   O1A                                                    
REMARK 620 2 ADP F 600   O3A  46.1                                              
REMARK 620 3 THR F  90   OG1 112.1  71.5                                        
REMARK 620 4 THR F  30   OG1 118.8 119.2  66.1                                  
REMARK 620 5 THR F  30   O    64.5  99.2 111.8  61.7                            
REMARK 620 6 AF3 F 602   F3  117.1  78.3  59.9 112.4 171.7                      
REMARK 620 7 LYS F  51   O   144.6 166.8 101.7  65.6  93.8  88.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP G 600   O2A                                                    
REMARK 620 2 ADP G 600   O1B  87.7                                              
REMARK 620 3 AF3 G 602   F1   73.5  98.6                                        
REMARK 620 4 ASP G  87   OD1 162.4  85.8  91.4                                  
REMARK 620 5 AF3 G 602  AL    89.7  66.3  36.7  72.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             AF3 G 602  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR G  89   OG1                                                    
REMARK 620 2 AF3 G 602   F1  169.3                                              
REMARK 620 3 AF3 G 602   F2   53.5 118.5                                        
REMARK 620 4 AF3 G 602   F3   55.8 132.7 108.8                                  
REMARK 620 5 ADP G 600   O3B  70.9 114.5  69.2  81.4                            
REMARK 620 6 ADP G 600   O3A 115.2  72.0 101.5  99.7  45.0                      
REMARK 620 7 ASP G  87   OD1 106.4  63.4  58.2 157.1 107.7 101.4                
REMARK 620 8 ADP G 600   O1B 115.4  62.8  69.3 142.1  62.1  47.2  55.4          
REMARK 620 9 HOH G 618   O    51.7 120.0  65.6  78.8 120.6 165.1  78.6 127.7    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G 603   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR G  30   OG1                                                    
REMARK 620 2 THR G  30   O    64.3                                              
REMARK 620 3 LYS G  51   O    72.8  95.0                                        
REMARK 620 4 ADP G 600   O1A 120.3  62.7 136.1                                  
REMARK 620 5 AF3 G 602   F3  118.3 176.8  87.7 114.1                            
REMARK 620 6 ADP G 600   O3A 125.1 100.0 160.5  45.7  77.0                      
REMARK 620 7 THR G  90   OG1  77.0 123.7 111.2 112.6  56.5  70.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 603                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 603                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 603                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D 603                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 603                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K F 603                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 603                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 D 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 E 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP F 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 F 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 G 602                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1PCQ   RELATED DB: PDB                                   
REMARK 900 THIS ENTRY 1SVT, DETERMINED BY THE SAME AUTHORS OF THE PDB           
REMARK 900 ENTRY 1PCQ, REFLECTS AN ALTERNATIVE MODELING OF 1PCQ.                
DBREF  1SVT A    2   525  UNP    P0A6F5   CH60_ECOLI       1    524             
DBREF  1SVT B    2   525  UNP    P0A6F5   CH60_ECOLI       1    524             
DBREF  1SVT C    2   525  UNP    P0A6F5   CH60_ECOLI       1    524             
DBREF  1SVT D    2   525  UNP    P0A6F5   CH60_ECOLI       1    524             
DBREF  1SVT E    2   525  UNP    P0A6F5   CH60_ECOLI       1    524             
DBREF  1SVT F    2   525  UNP    P0A6F5   CH60_ECOLI       1    524             
DBREF  1SVT G    2   525  UNP    P0A6F5   CH60_ECOLI       1    524             
DBREF  1SVT H    2   525  UNP    P0A6F5   CH60_ECOLI       1    524             
DBREF  1SVT I    2   525  UNP    P0A6F5   CH60_ECOLI       1    524             
DBREF  1SVT J    2   525  UNP    P0A6F5   CH60_ECOLI       1    524             
DBREF  1SVT K    2   525  UNP    P0A6F5   CH60_ECOLI       1    524             
DBREF  1SVT L    2   525  UNP    P0A6F5   CH60_ECOLI       1    524             
DBREF  1SVT M    2   525  UNP    P0A6F5   CH60_ECOLI       1    524             
DBREF  1SVT N    2   525  UNP    P0A6F5   CH60_ECOLI       1    524             
DBREF  1SVT O    1    97  UNP    P0A6F9   CH10_ECOLI       1     97             
DBREF  1SVT P    1    97  UNP    P0A6F9   CH10_ECOLI       1     97             
DBREF  1SVT Q    1    97  UNP    P0A6F9   CH10_ECOLI       1     97             
DBREF  1SVT R    1    97  UNP    P0A6F9   CH10_ECOLI       1     97             
DBREF  1SVT S    1    97  UNP    P0A6F9   CH10_ECOLI       1     97             
DBREF  1SVT T    1    97  UNP    P0A6F9   CH10_ECOLI       1     97             
DBREF  1SVT U    1    97  UNP    P0A6F9   CH10_ECOLI       1     97             
SEQRES   1 A  524  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 A  524  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 A  524  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 A  524  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 A  524  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 A  524  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 A  524  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 A  524  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 A  524  ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 A  524  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 A  524  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 A  524  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 A  524  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 A  524  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 A  524  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 A  524  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 A  524  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 A  524  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 A  524  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 A  524  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 A  524  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 A  524  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 A  524  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 A  524  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 A  524  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 A  524  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 A  524  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 A  524  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 A  524  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 A  524  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 A  524  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 A  524  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 A  524  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 A  524  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 A  524  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 A  524  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 A  524  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 A  524  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 A  524  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 A  524  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 A  524  THR ASP LEU PRO                                              
SEQRES   1 B  524  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 B  524  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 B  524  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 B  524  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 B  524  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 B  524  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 B  524  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 B  524  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 B  524  ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 B  524  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 B  524  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 B  524  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 B  524  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 B  524  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 B  524  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 B  524  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 B  524  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 B  524  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 B  524  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 B  524  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 B  524  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 B  524  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 B  524  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 B  524  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 B  524  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 B  524  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 B  524  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 B  524  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 B  524  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 B  524  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 B  524  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 B  524  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 B  524  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 B  524  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 B  524  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 B  524  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 B  524  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 B  524  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 B  524  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 B  524  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 B  524  THR ASP LEU PRO                                              
SEQRES   1 C  524  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 C  524  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 C  524  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 C  524  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 C  524  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 C  524  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 C  524  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 C  524  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 C  524  ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 C  524  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 C  524  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 C  524  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 C  524  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 C  524  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 C  524  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 C  524  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 C  524  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 C  524  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 C  524  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 C  524  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 C  524  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 C  524  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 C  524  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 C  524  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 C  524  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 C  524  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 C  524  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 C  524  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 C  524  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 C  524  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 C  524  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 C  524  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 C  524  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 C  524  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 C  524  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 C  524  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 C  524  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 C  524  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 C  524  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 C  524  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 C  524  THR ASP LEU PRO                                              
SEQRES   1 D  524  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 D  524  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 D  524  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 D  524  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 D  524  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 D  524  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 D  524  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 D  524  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 D  524  ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 D  524  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 D  524  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 D  524  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 D  524  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 D  524  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 D  524  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 D  524  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 D  524  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 D  524  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 D  524  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 D  524  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 D  524  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 D  524  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 D  524  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 D  524  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 D  524  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 D  524  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 D  524  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 D  524  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 D  524  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 D  524  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 D  524  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 D  524  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 D  524  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 D  524  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 D  524  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 D  524  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 D  524  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 D  524  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 D  524  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 D  524  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 D  524  THR ASP LEU PRO                                              
SEQRES   1 E  524  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 E  524  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 E  524  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 E  524  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 E  524  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 E  524  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 E  524  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 E  524  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 E  524  ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 E  524  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 E  524  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 E  524  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 E  524  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 E  524  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 E  524  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 E  524  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 E  524  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 E  524  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 E  524  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 E  524  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 E  524  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 E  524  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 E  524  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 E  524  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 E  524  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 E  524  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 E  524  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 E  524  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 E  524  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 E  524  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 E  524  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 E  524  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 E  524  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 E  524  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 E  524  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 E  524  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 E  524  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 E  524  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 E  524  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 E  524  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 E  524  THR ASP LEU PRO                                              
SEQRES   1 F  524  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 F  524  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 F  524  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 F  524  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 F  524  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 F  524  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 F  524  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 F  524  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 F  524  ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 F  524  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 F  524  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 F  524  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 F  524  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 F  524  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 F  524  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 F  524  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 F  524  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 F  524  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 F  524  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 F  524  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 F  524  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 F  524  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 F  524  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 F  524  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 F  524  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 F  524  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 F  524  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 F  524  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 F  524  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 F  524  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 F  524  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 F  524  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 F  524  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 F  524  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 F  524  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 F  524  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 F  524  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 F  524  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 F  524  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 F  524  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 F  524  THR ASP LEU PRO                                              
SEQRES   1 G  524  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 G  524  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 G  524  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 G  524  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 G  524  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 G  524  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 G  524  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 G  524  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 G  524  ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 G  524  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 G  524  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 G  524  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 G  524  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 G  524  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 G  524  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 G  524  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 G  524  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 G  524  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 G  524  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 G  524  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 G  524  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 G  524  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 G  524  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 G  524  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 G  524  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 G  524  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 G  524  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 G  524  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 G  524  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 G  524  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 G  524  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 G  524  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 G  524  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 G  524  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 G  524  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 G  524  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 G  524  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 G  524  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 G  524  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 G  524  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 G  524  THR ASP LEU PRO                                              
SEQRES   1 H  524  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 H  524  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 H  524  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 H  524  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 H  524  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 H  524  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 H  524  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 H  524  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 H  524  ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 H  524  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 H  524  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 H  524  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 H  524  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 H  524  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 H  524  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 H  524  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 H  524  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 H  524  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 H  524  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 H  524  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 H  524  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 H  524  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 H  524  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 H  524  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 H  524  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 H  524  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 H  524  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 H  524  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 H  524  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 H  524  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 H  524  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 H  524  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 H  524  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 H  524  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 H  524  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 H  524  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 H  524  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 H  524  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 H  524  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 H  524  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 H  524  THR ASP LEU PRO                                              
SEQRES   1 I  524  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 I  524  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 I  524  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 I  524  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 I  524  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 I  524  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 I  524  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 I  524  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 I  524  ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 I  524  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 I  524  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 I  524  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 I  524  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 I  524  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 I  524  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 I  524  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 I  524  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 I  524  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 I  524  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 I  524  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 I  524  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 I  524  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 I  524  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 I  524  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 I  524  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 I  524  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 I  524  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 I  524  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 I  524  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 I  524  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 I  524  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 I  524  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 I  524  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 I  524  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 I  524  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 I  524  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 I  524  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 I  524  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 I  524  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 I  524  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 I  524  THR ASP LEU PRO                                              
SEQRES   1 J  524  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 J  524  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 J  524  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 J  524  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 J  524  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 J  524  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 J  524  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 J  524  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 J  524  ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 J  524  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 J  524  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 J  524  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 J  524  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 J  524  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 J  524  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 J  524  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 J  524  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 J  524  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 J  524  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 J  524  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 J  524  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 J  524  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 J  524  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 J  524  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 J  524  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 J  524  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 J  524  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 J  524  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 J  524  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 J  524  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 J  524  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 J  524  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 J  524  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 J  524  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 J  524  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 J  524  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 J  524  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 J  524  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 J  524  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 J  524  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 J  524  THR ASP LEU PRO                                              
SEQRES   1 K  524  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 K  524  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 K  524  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 K  524  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 K  524  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 K  524  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 K  524  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 K  524  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 K  524  ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 K  524  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 K  524  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 K  524  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 K  524  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 K  524  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 K  524  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 K  524  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 K  524  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 K  524  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 K  524  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 K  524  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 K  524  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 K  524  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 K  524  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 K  524  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 K  524  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 K  524  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 K  524  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 K  524  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 K  524  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 K  524  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 K  524  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 K  524  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 K  524  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 K  524  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 K  524  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 K  524  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 K  524  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 K  524  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 K  524  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 K  524  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 K  524  THR ASP LEU PRO                                              
SEQRES   1 L  524  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 L  524  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 L  524  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 L  524  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 L  524  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 L  524  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 L  524  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 L  524  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 L  524  ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 L  524  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 L  524  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 L  524  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 L  524  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 L  524  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 L  524  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 L  524  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 L  524  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 L  524  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 L  524  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 L  524  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 L  524  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 L  524  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 L  524  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 L  524  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 L  524  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 L  524  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 L  524  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 L  524  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 L  524  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 L  524  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 L  524  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 L  524  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 L  524  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 L  524  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 L  524  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 L  524  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 L  524  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 L  524  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 L  524  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 L  524  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 L  524  THR ASP LEU PRO                                              
SEQRES   1 M  524  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 M  524  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 M  524  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 M  524  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 M  524  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 M  524  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 M  524  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 M  524  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 M  524  ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 M  524  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 M  524  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 M  524  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 M  524  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 M  524  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 M  524  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 M  524  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 M  524  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 M  524  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 M  524  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 M  524  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 M  524  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 M  524  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 M  524  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 M  524  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 M  524  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 M  524  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 M  524  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 M  524  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 M  524  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 M  524  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 M  524  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 M  524  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 M  524  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 M  524  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 M  524  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 M  524  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 M  524  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 M  524  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 M  524  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 M  524  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 M  524  THR ASP LEU PRO                                              
SEQRES   1 N  524  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 N  524  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 N  524  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 N  524  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 N  524  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 N  524  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 N  524  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 N  524  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 N  524  ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 N  524  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 N  524  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 N  524  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 N  524  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 N  524  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 N  524  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 N  524  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 N  524  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 N  524  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 N  524  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 N  524  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 N  524  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 N  524  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 N  524  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 N  524  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 N  524  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 N  524  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 N  524  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 N  524  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 N  524  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 N  524  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 N  524  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 N  524  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 N  524  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 N  524  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 N  524  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 N  524  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 N  524  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 N  524  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 N  524  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 N  524  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 N  524  THR ASP LEU PRO                                              
SEQRES   1 O   97  MET ASN ILE ARG PRO LEU HIS ASP ARG VAL ILE VAL LYS          
SEQRES   2 O   97  ARG LYS GLU VAL GLU THR LYS SER ALA GLY GLY ILE VAL          
SEQRES   3 O   97  LEU THR GLY SER ALA ALA ALA LYS SER THR ARG GLY GLU          
SEQRES   4 O   97  VAL LEU ALA VAL GLY ASN GLY ARG ILE LEU GLU ASN GLY          
SEQRES   5 O   97  GLU VAL LYS PRO LEU ASP VAL LYS VAL GLY ASP ILE VAL          
SEQRES   6 O   97  ILE PHE ASN ASP GLY TYR GLY VAL LYS SER GLU LYS ILE          
SEQRES   7 O   97  ASP ASN GLU GLU VAL LEU ILE MET SER GLU SER ASP ILE          
SEQRES   8 O   97  LEU ALA ILE VAL GLU ALA                                      
SEQRES   1 P   97  MET ASN ILE ARG PRO LEU HIS ASP ARG VAL ILE VAL LYS          
SEQRES   2 P   97  ARG LYS GLU VAL GLU THR LYS SER ALA GLY GLY ILE VAL          
SEQRES   3 P   97  LEU THR GLY SER ALA ALA ALA LYS SER THR ARG GLY GLU          
SEQRES   4 P   97  VAL LEU ALA VAL GLY ASN GLY ARG ILE LEU GLU ASN GLY          
SEQRES   5 P   97  GLU VAL LYS PRO LEU ASP VAL LYS VAL GLY ASP ILE VAL          
SEQRES   6 P   97  ILE PHE ASN ASP GLY TYR GLY VAL LYS SER GLU LYS ILE          
SEQRES   7 P   97  ASP ASN GLU GLU VAL LEU ILE MET SER GLU SER ASP ILE          
SEQRES   8 P   97  LEU ALA ILE VAL GLU ALA                                      
SEQRES   1 Q   97  MET ASN ILE ARG PRO LEU HIS ASP ARG VAL ILE VAL LYS          
SEQRES   2 Q   97  ARG LYS GLU VAL GLU THR LYS SER ALA GLY GLY ILE VAL          
SEQRES   3 Q   97  LEU THR GLY SER ALA ALA ALA LYS SER THR ARG GLY GLU          
SEQRES   4 Q   97  VAL LEU ALA VAL GLY ASN GLY ARG ILE LEU GLU ASN GLY          
SEQRES   5 Q   97  GLU VAL LYS PRO LEU ASP VAL LYS VAL GLY ASP ILE VAL          
SEQRES   6 Q   97  ILE PHE ASN ASP GLY TYR GLY VAL LYS SER GLU LYS ILE          
SEQRES   7 Q   97  ASP ASN GLU GLU VAL LEU ILE MET SER GLU SER ASP ILE          
SEQRES   8 Q   97  LEU ALA ILE VAL GLU ALA                                      
SEQRES   1 R   97  MET ASN ILE ARG PRO LEU HIS ASP ARG VAL ILE VAL LYS          
SEQRES   2 R   97  ARG LYS GLU VAL GLU THR LYS SER ALA GLY GLY ILE VAL          
SEQRES   3 R   97  LEU THR GLY SER ALA ALA ALA LYS SER THR ARG GLY GLU          
SEQRES   4 R   97  VAL LEU ALA VAL GLY ASN GLY ARG ILE LEU GLU ASN GLY          
SEQRES   5 R   97  GLU VAL LYS PRO LEU ASP VAL LYS VAL GLY ASP ILE VAL          
SEQRES   6 R   97  ILE PHE ASN ASP GLY TYR GLY VAL LYS SER GLU LYS ILE          
SEQRES   7 R   97  ASP ASN GLU GLU VAL LEU ILE MET SER GLU SER ASP ILE          
SEQRES   8 R   97  LEU ALA ILE VAL GLU ALA                                      
SEQRES   1 S   97  MET ASN ILE ARG PRO LEU HIS ASP ARG VAL ILE VAL LYS          
SEQRES   2 S   97  ARG LYS GLU VAL GLU THR LYS SER ALA GLY GLY ILE VAL          
SEQRES   3 S   97  LEU THR GLY SER ALA ALA ALA LYS SER THR ARG GLY GLU          
SEQRES   4 S   97  VAL LEU ALA VAL GLY ASN GLY ARG ILE LEU GLU ASN GLY          
SEQRES   5 S   97  GLU VAL LYS PRO LEU ASP VAL LYS VAL GLY ASP ILE VAL          
SEQRES   6 S   97  ILE PHE ASN ASP GLY TYR GLY VAL LYS SER GLU LYS ILE          
SEQRES   7 S   97  ASP ASN GLU GLU VAL LEU ILE MET SER GLU SER ASP ILE          
SEQRES   8 S   97  LEU ALA ILE VAL GLU ALA                                      
SEQRES   1 T   97  MET ASN ILE ARG PRO LEU HIS ASP ARG VAL ILE VAL LYS          
SEQRES   2 T   97  ARG LYS GLU VAL GLU THR LYS SER ALA GLY GLY ILE VAL          
SEQRES   3 T   97  LEU THR GLY SER ALA ALA ALA LYS SER THR ARG GLY GLU          
SEQRES   4 T   97  VAL LEU ALA VAL GLY ASN GLY ARG ILE LEU GLU ASN GLY          
SEQRES   5 T   97  GLU VAL LYS PRO LEU ASP VAL LYS VAL GLY ASP ILE VAL          
SEQRES   6 T   97  ILE PHE ASN ASP GLY TYR GLY VAL LYS SER GLU LYS ILE          
SEQRES   7 T   97  ASP ASN GLU GLU VAL LEU ILE MET SER GLU SER ASP ILE          
SEQRES   8 T   97  LEU ALA ILE VAL GLU ALA                                      
SEQRES   1 U   97  MET ASN ILE ARG PRO LEU HIS ASP ARG VAL ILE VAL LYS          
SEQRES   2 U   97  ARG LYS GLU VAL GLU THR LYS SER ALA GLY GLY ILE VAL          
SEQRES   3 U   97  LEU THR GLY SER ALA ALA ALA LYS SER THR ARG GLY GLU          
SEQRES   4 U   97  VAL LEU ALA VAL GLY ASN GLY ARG ILE LEU GLU ASN GLY          
SEQRES   5 U   97  GLU VAL LYS PRO LEU ASP VAL LYS VAL GLY ASP ILE VAL          
SEQRES   6 U   97  ILE PHE ASN ASP GLY TYR GLY VAL LYS SER GLU LYS ILE          
SEQRES   7 U   97  ASP ASN GLU GLU VAL LEU ILE MET SER GLU SER ASP ILE          
SEQRES   8 U   97  LEU ALA ILE VAL GLU ALA                                      
HET     MG  A 601       1                                                       
HET      K  A 603       1                                                       
HET     MG  B 601       1                                                       
HET      K  B 603       1                                                       
HET     MG  C 601       1                                                       
HET      K  C 603       1                                                       
HET     MG  D 601       1                                                       
HET      K  D 603       1                                                       
HET     MG  E 601       1                                                       
HET      K  E 603       1                                                       
HET     MG  F 601       1                                                       
HET      K  F 603       1                                                       
HET     MG  G 601       1                                                       
HET      K  G 603       1                                                       
HET    ADP  A 600      27                                                       
HET    AF3  A 602       4                                                       
HET    ADP  B 600      27                                                       
HET    AF3  B 602       4                                                       
HET    ADP  C 600      27                                                       
HET    AF3  C 602       4                                                       
HET    ADP  D 600      27                                                       
HET    AF3  D 602       4                                                       
HET    ADP  E 600      27                                                       
HET    AF3  E 602       4                                                       
HET    ADP  F 600      27                                                       
HET    AF3  F 602       4                                                       
HET    ADP  G 600      27                                                       
HET    AF3  G 602       4                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM       K POTASSIUM ION                                                    
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     AF3 ALUMINUM FLUORIDE                                                
FORMUL  22   MG    7(MG 2+)                                                     
FORMUL  23    K    7(K 1+)                                                      
FORMUL  36  ADP    7(C10 H15 N5 O10 P2)                                         
FORMUL  37  AF3    7(AL F3)                                                     
FORMUL  50  HOH   *194(H2 O)                                                    
HELIX    1   1 GLY A    9  VAL A   29  1                                  21    
HELIX    2   2 ASP A   52  ARG A   58  1                                   7    
HELIX    3   3 ASP A   64  ALA A   85  1                                  22    
HELIX    4   4 GLY A   88  ALA A  108  1                                  21    
HELIX    5   5 ASN A  112  SER A  135  1                                  24    
HELIX    6   6 ASP A  140  ALA A  152  1                                  13    
HELIX    7   7 ASP A  155  GLY A  170  1                                  16    
HELIX    8   8 ASN A  229  GLU A  232  5                                   4    
HELIX    9   9 MET A  233  GLY A  244  1                                  12    
HELIX   10  10 GLU A  255  ARG A  268  1                                  14    
HELIX   11  11 PHE A  281  GLY A  297  1                                  17    
HELIX   12  12 GLU A  304  GLY A  306  5                                   3    
HELIX   13  13 GLU A  308  ALA A  312  5                                   5    
HELIX   14  14 THR A  313  LEU A  317  5                                   5    
HELIX   15  15 GLU A  338  GLU A  355  1                                  18    
HELIX   16  16 ASP A  359  ALA A  373  1                                  15    
HELIX   17  17 GLU A  386  GLY A  410  1                                  25    
HELIX   18  18 GLY A  416  LEU A  426  1                                  11    
HELIX   19  19 ALA A  427  LEU A  429  5                                   3    
HELIX   20  20 ASN A  433  MET A  447  1                                  15    
HELIX   21  21 GLU A  448  ASN A  457  1                                  10    
HELIX   22  22 GLU A  461  GLY A  472  1                                  12    
HELIX   23  23 THR A  497  ILE A  515  1                                  19    
HELIX   24  24 GLY B    9  VAL B   29  1                                  21    
HELIX   25  25 ASP B   52  ILE B   60  1                                   9    
HELIX   26  26 ASP B   64  ALA B   85  1                                  22    
HELIX   27  27 GLY B   88  ALA B  108  1                                  21    
HELIX   28  28 ASN B  112  SER B  135  1                                  24    
HELIX   29  29 ASP B  140  ALA B  152  1                                  13    
HELIX   30  30 ASP B  155  GLY B  170  1                                  16    
HELIX   31  31 ASN B  229  GLU B  232  5                                   4    
HELIX   32  32 MET B  233  GLY B  244  1                                  12    
HELIX   33  33 GLU B  255  ARG B  268  1                                  14    
HELIX   34  34 PHE B  281  GLY B  297  1                                  17    
HELIX   35  35 GLU B  304  GLY B  306  5                                   3    
HELIX   36  36 GLU B  308  ALA B  312  5                                   5    
HELIX   37  37 THR B  313  LEU B  317  5                                   5    
HELIX   38  38 GLU B  338  GLU B  355  1                                  18    
HELIX   39  39 ASP B  359  ALA B  373  1                                  15    
HELIX   40  40 GLU B  386  GLY B  410  1                                  25    
HELIX   41  41 GLY B  416  LEU B  426  1                                  11    
HELIX   42  42 ALA B  427  LEU B  429  5                                   3    
HELIX   43  43 ASN B  433  MET B  447  1                                  15    
HELIX   44  44 GLU B  448  ASN B  457  1                                  10    
HELIX   45  45 GLU B  461  GLY B  472  1                                  12    
HELIX   46  46 THR B  497  ILE B  515  1                                  19    
HELIX   47  47 GLY C    9  VAL C   29  1                                  21    
HELIX   48  48 ASP C   52  ARG C   58  1                                   7    
HELIX   49  49 ASP C   64  ALA C   85  1                                  22    
HELIX   50  50 GLY C   88  ALA C  108  1                                  21    
HELIX   51  51 ASN C  112  SER C  135  1                                  24    
HELIX   52  52 ASP C  140  ALA C  152  1                                  13    
HELIX   53  53 ASP C  155  GLY C  170  1                                  16    
HELIX   54  54 ASN C  229  GLU C  232  5                                   4    
HELIX   55  55 MET C  233  GLY C  244  1                                  12    
HELIX   56  56 GLU C  255  ARG C  268  1                                  14    
HELIX   57  57 PHE C  281  GLY C  297  1                                  17    
HELIX   58  58 GLU C  304  GLY C  306  5                                   3    
HELIX   59  59 GLU C  308  ALA C  312  5                                   5    
HELIX   60  60 THR C  313  LEU C  317  5                                   5    
HELIX   61  61 GLU C  338  ALA C  356  1                                  19    
HELIX   62  62 ASP C  359  ALA C  373  1                                  15    
HELIX   63  63 GLU C  386  GLY C  410  1                                  25    
HELIX   64  64 GLY C  416  LEU C  426  1                                  11    
HELIX   65  65 ALA C  427  LEU C  429  5                                   3    
HELIX   66  66 ASN C  433  MET C  447  1                                  15    
HELIX   67  67 GLU C  448  CYS C  458  1                                  11    
HELIX   68  68 GLU C  461  GLY C  472  1                                  12    
HELIX   69  69 THR C  497  ILE C  515  1                                  19    
HELIX   70  70 GLY D    9  LYS D   28  1                                  20    
HELIX   71  71 VAL D   29  LEU D   31  5                                   3    
HELIX   72  72 ASP D   52  ARG D   58  1                                   7    
HELIX   73  73 ASP D   64  ALA D   85  1                                  22    
HELIX   74  74 GLY D   88  ALA D  108  1                                  21    
HELIX   75  75 ASN D  112  SER D  135  1                                  24    
HELIX   76  76 ASP D  140  ALA D  152  1                                  13    
HELIX   77  77 ASP D  155  GLY D  170  1                                  16    
HELIX   78  78 ASN D  229  GLU D  232  5                                   4    
HELIX   79  79 MET D  233  GLY D  244  1                                  12    
HELIX   80  80 GLU D  255  ARG D  268  1                                  14    
HELIX   81  81 PHE D  281  GLY D  297  1                                  17    
HELIX   82  82 GLU D  304  GLY D  306  5                                   3    
HELIX   83  83 GLU D  308  ALA D  312  5                                   5    
HELIX   84  84 THR D  313  LEU D  317  5                                   5    
HELIX   85  85 GLU D  338  GLU D  355  1                                  18    
HELIX   86  86 ASP D  359  ALA D  373  1                                  15    
HELIX   87  87 GLU D  386  GLY D  410  1                                  25    
HELIX   88  88 GLY D  416  LEU D  426  1                                  11    
HELIX   89  89 ALA D  427  LEU D  429  5                                   3    
HELIX   90  90 ASN D  433  MET D  447  1                                  15    
HELIX   91  91 GLU D  448  ASN D  457  1                                  10    
HELIX   92  92 GLU D  461  GLY D  471  1                                  11    
HELIX   93  93 THR D  497  ILE D  515  1                                  19    
HELIX   94  94 GLY E    9  VAL E   29  1                                  21    
HELIX   95  95 ASP E   52  ARG E   58  1                                   7    
HELIX   96  96 ASP E   64  ALA E   85  1                                  22    
HELIX   97  97 GLY E   88  ALA E  108  1                                  21    
HELIX   98  98 ASN E  112  SER E  135  1                                  24    
HELIX   99  99 ASP E  140  ALA E  152  1                                  13    
HELIX  100 100 ASP E  155  GLY E  170  1                                  16    
HELIX  101 101 ASN E  229  GLU E  232  5                                   4    
HELIX  102 102 MET E  233  GLY E  244  1                                  12    
HELIX  103 103 GLU E  255  ARG E  268  1                                  14    
HELIX  104 104 PHE E  281  GLY E  297  1                                  17    
HELIX  105 105 GLU E  304  GLY E  306  5                                   3    
HELIX  106 106 GLU E  308  ALA E  312  5                                   5    
HELIX  107 107 THR E  313  LEU E  317  5                                   5    
HELIX  108 108 GLU E  338  GLU E  355  1                                  18    
HELIX  109 109 ASP E  359  ALA E  373  1                                  15    
HELIX  110 110 GLU E  386  GLY E  410  1                                  25    
HELIX  111 111 GLY E  416  LEU E  426  1                                  11    
HELIX  112 112 ALA E  427  LEU E  429  5                                   3    
HELIX  113 113 ASN E  433  GLU E  448  1                                  16    
HELIX  114 114 GLU E  448  ASN E  457  1                                  10    
HELIX  115 115 GLU E  461  GLY E  472  1                                  12    
HELIX  116 116 THR E  497  ILE E  515  1                                  19    
HELIX  117 117 GLY F    9  VAL F   29  1                                  21    
HELIX  118 118 ASP F   52  ARG F   58  1                                   7    
HELIX  119 119 ASP F   64  ALA F   85  1                                  22    
HELIX  120 120 GLY F   88  ALA F  108  1                                  21    
HELIX  121 121 ASN F  112  SER F  135  1                                  24    
HELIX  122 122 ASP F  140  ALA F  152  1                                  13    
HELIX  123 123 ASP F  155  GLY F  170  1                                  16    
HELIX  124 124 ASN F  229  GLU F  232  5                                   4    
HELIX  125 125 MET F  233  GLY F  244  1                                  12    
HELIX  126 126 GLU F  255  ARG F  268  1                                  14    
HELIX  127 127 PHE F  281  GLY F  297  1                                  17    
HELIX  128 128 GLU F  304  GLY F  306  5                                   3    
HELIX  129 129 GLU F  308  ALA F  312  5                                   5    
HELIX  130 130 THR F  313  LEU F  317  5                                   5    
HELIX  131 131 GLU F  338  GLU F  355  1                                  18    
HELIX  132 132 ASP F  359  ALA F  373  1                                  15    
HELIX  133 133 GLU F  386  GLY F  410  1                                  25    
HELIX  134 134 GLY F  416  LEU F  426  1                                  11    
HELIX  135 135 ALA F  427  LEU F  429  5                                   3    
HELIX  136 136 ASN F  433  MET F  447  1                                  15    
HELIX  137 137 GLU F  448  ASN F  457  1                                  10    
HELIX  138 138 GLU F  461  GLY F  471  1                                  11    
HELIX  139 139 THR F  497  ILE F  515  1                                  19    
HELIX  140 140 GLY G    9  VAL G   29  1                                  21    
HELIX  141 141 ASP G   52  ARG G   58  1                                   7    
HELIX  142 142 ASP G   64  ALA G   85  1                                  22    
HELIX  143 143 GLY G   88  ALA G  108  1                                  21    
HELIX  144 144 ASN G  112  SER G  135  1                                  24    
HELIX  145 145 ASP G  140  ALA G  152  1                                  13    
HELIX  146 146 ASP G  155  GLY G  170  1                                  16    
HELIX  147 147 ASN G  229  GLU G  232  5                                   4    
HELIX  148 148 MET G  233  GLY G  244  1                                  12    
HELIX  149 149 GLU G  255  ARG G  268  1                                  14    
HELIX  150 150 PHE G  281  GLY G  297  1                                  17    
HELIX  151 151 GLU G  304  GLY G  306  5                                   3    
HELIX  152 152 GLU G  308  ALA G  312  5                                   5    
HELIX  153 153 THR G  313  LEU G  317  5                                   5    
HELIX  154 154 GLU G  338  GLU G  355  1                                  18    
HELIX  155 155 ASP G  359  ALA G  373  1                                  15    
HELIX  156 156 GLU G  386  GLY G  410  1                                  25    
HELIX  157 157 GLY G  416  LEU G  426  1                                  11    
HELIX  158 158 ALA G  427  LEU G  429  5                                   3    
HELIX  159 159 ASN G  433  MET G  447  1                                  15    
HELIX  160 160 GLU G  448  ASN G  457  1                                  10    
HELIX  161 161 GLU G  461  GLY G  471  1                                  11    
HELIX  162 162 THR G  497  ILE G  515  1                                  19    
HELIX  163 163 GLY H    9  LYS H   28  1                                  20    
HELIX  164 164 VAL H   29  LEU H   31  5                                   3    
HELIX  165 165 ASP H   52  ILE H   60  1                                   9    
HELIX  166 166 PHE H   66  ALA H   84  1                                  19    
HELIX  167 167 GLY H   88  ALA H  108  1                                  21    
HELIX  168 168 ASN H  112  SER H  135  1                                  24    
HELIX  169 169 ASP H  140  ALA H  152  1                                  13    
HELIX  170 170 ASP H  155  GLY H  170  1                                  16    
HELIX  171 171 MET H  233  ALA H  243  1                                  11    
HELIX  172 172 GLU H  255  ARG H  268  1                                  14    
HELIX  173 173 PHE H  281  GLY H  297  1                                  17    
HELIX  174 174 THR H  313  LEU H  317  5                                   5    
HELIX  175 175 GLU H  338  ILE H  353  1                                  16    
HELIX  176 176 SER H  358  GLY H  375  1                                  18    
HELIX  177 177 THR H  385  GLY H  410  1                                  26    
HELIX  178 178 GLY H  416  LEU H  426  1                                  11    
HELIX  179 179 ASN H  433  MET H  447  1                                  15    
HELIX  180 180 GLU H  448  CYS H  458  1                                  11    
HELIX  181 181 GLU H  461  GLY H  471  1                                  11    
HELIX  182 182 THR H  497  THR H  516  1                                  20    
HELIX  183 183 GLY I    9  LYS I   28  1                                  20    
HELIX  184 184 VAL I   29  LEU I   31  5                                   3    
HELIX  185 185 ASP I   52  ILE I   60  1                                   9    
HELIX  186 186 PHE I   66  ALA I   84  1                                  19    
HELIX  187 187 GLY I   88  ALA I  108  1                                  21    
HELIX  188 188 ASN I  112  SER I  135  1                                  24    
HELIX  189 189 ASP I  140  ALA I  152  1                                  13    
HELIX  190 190 ASP I  155  GLY I  170  1                                  16    
HELIX  191 191 MET I  233  ALA I  241  1                                   9    
HELIX  192 192 GLU I  255  ARG I  268  1                                  14    
HELIX  193 193 PHE I  281  GLY I  297  1                                  17    
HELIX  194 194 THR I  313  LEU I  317  5                                   5    
HELIX  195 195 GLU I  338  ILE I  353  1                                  16    
HELIX  196 196 SER I  358  GLY I  375  1                                  18    
HELIX  197 197 THR I  385  GLY I  410  1                                  26    
HELIX  198 198 GLY I  416  LEU I  426  1                                  11    
HELIX  199 199 ASN I  433  MET I  447  1                                  15    
HELIX  200 200 GLU I  448  CYS I  458  1                                  11    
HELIX  201 201 GLU I  461  GLY I  472  1                                  12    
HELIX  202 202 THR I  497  THR I  516  1                                  20    
HELIX  203 203 GLY J    9  LYS J   28  1                                  20    
HELIX  204 204 VAL J   29  LEU J   31  5                                   3    
HELIX  205 205 ASP J   52  ILE J   60  1                                   9    
HELIX  206 206 PHE J   66  ALA J   84  1                                  19    
HELIX  207 207 GLY J   88  ALA J  108  1                                  21    
HELIX  208 208 ASN J  112  SER J  135  1                                  24    
HELIX  209 209 ASP J  140  ALA J  152  1                                  13    
HELIX  210 210 ASP J  155  GLY J  170  1                                  16    
HELIX  211 211 MET J  233  ALA J  241  1                                   9    
HELIX  212 212 GLU J  255  ARG J  268  1                                  14    
HELIX  213 213 PHE J  281  GLY J  297  1                                  17    
HELIX  214 214 THR J  313  LEU J  317  5                                   5    
HELIX  215 215 GLU J  338  ILE J  353  1                                  16    
HELIX  216 216 SER J  358  GLY J  375  1                                  18    
HELIX  217 217 THR J  385  GLY J  410  1                                  26    
HELIX  218 218 GLY J  416  LEU J  426  1                                  11    
HELIX  219 219 ASN J  433  MET J  447  1                                  15    
HELIX  220 220 GLU J  448  ASN J  457  1                                  10    
HELIX  221 221 GLU J  461  GLY J  471  1                                  11    
HELIX  222 222 THR J  497  THR J  516  1                                  20    
HELIX  223 223 GLY K    9  LYS K   28  1                                  20    
HELIX  224 224 VAL K   29  LEU K   31  5                                   3    
HELIX  225 225 ASP K   52  ILE K   60  1                                   9    
HELIX  226 226 PHE K   66  ALA K   84  1                                  19    
HELIX  227 227 GLY K   88  ALA K  108  1                                  21    
HELIX  228 228 ASN K  112  SER K  135  1                                  24    
HELIX  229 229 ASP K  140  ALA K  152  1                                  13    
HELIX  230 230 ASP K  155  GLY K  170  1                                  16    
HELIX  231 231 MET K  233  ALA K  243  1                                  11    
HELIX  232 232 GLU K  255  ARG K  268  1                                  14    
HELIX  233 233 PHE K  281  GLY K  297  1                                  17    
HELIX  234 234 THR K  313  LEU K  317  5                                   5    
HELIX  235 235 GLU K  338  ILE K  353  1                                  16    
HELIX  236 236 SER K  358  GLY K  375  1                                  18    
HELIX  237 237 THR K  385  GLY K  410  1                                  26    
HELIX  238 238 GLY K  416  LEU K  426  1                                  11    
HELIX  239 239 ASN K  433  ALA K  446  1                                  14    
HELIX  240 240 GLU K  448  CYS K  458  1                                  11    
HELIX  241 241 GLU K  461  GLY K  471  1                                  11    
HELIX  242 242 THR K  497  THR K  516  1                                  20    
HELIX  243 243 GLY L    9  LYS L   28  1                                  20    
HELIX  244 244 VAL L   29  LEU L   31  5                                   3    
HELIX  245 245 ASP L   52  ILE L   60  1                                   9    
HELIX  246 246 PHE L   66  ALA L   84  1                                  19    
HELIX  247 247 GLY L   88  ALA L  108  1                                  21    
HELIX  248 248 ASN L  112  SER L  135  1                                  24    
HELIX  249 249 ASP L  140  ALA L  152  1                                  13    
HELIX  250 250 ASP L  155  GLY L  170  1                                  16    
HELIX  251 251 MET L  233  ALA L  241  1                                   9    
HELIX  252 252 GLU L  255  ARG L  268  1                                  14    
HELIX  253 253 PHE L  281  GLY L  297  1                                  17    
HELIX  254 254 THR L  313  LEU L  317  5                                   5    
HELIX  255 255 GLU L  338  ILE L  353  1                                  16    
HELIX  256 256 SER L  358  GLY L  375  1                                  18    
HELIX  257 257 THR L  385  GLY L  410  1                                  26    
HELIX  258 258 GLY L  416  LEU L  426  1                                  11    
HELIX  259 259 ASN L  433  MET L  447  1                                  15    
HELIX  260 260 GLU L  448  CYS L  458  1                                  11    
HELIX  261 261 GLU L  461  GLY L  472  1                                  12    
HELIX  262 262 THR L  497  THR L  516  1                                  20    
HELIX  263 263 GLY M    9  LYS M   28  1                                  20    
HELIX  264 264 VAL M   29  LEU M   31  5                                   3    
HELIX  265 265 ASP M   52  ILE M   60  1                                   9    
HELIX  266 266 PHE M   66  ALA M   84  1                                  19    
HELIX  267 267 GLY M   88  ALA M  108  1                                  21    
HELIX  268 268 ASN M  112  SER M  135  1                                  24    
HELIX  269 269 ASP M  140  ALA M  152  1                                  13    
HELIX  270 270 ASP M  155  GLY M  170  1                                  16    
HELIX  271 271 MET M  233  ALA M  241  1                                   9    
HELIX  272 272 GLU M  255  ARG M  268  1                                  14    
HELIX  273 273 PHE M  281  GLY M  297  1                                  17    
HELIX  274 274 THR M  313  LEU M  317  5                                   5    
HELIX  275 275 GLU M  338  ILE M  353  1                                  16    
HELIX  276 276 SER M  358  GLY M  375  1                                  18    
HELIX  277 277 THR M  385  GLY M  410  1                                  26    
HELIX  278 278 GLY M  416  LEU M  426  1                                  11    
HELIX  279 279 ASN M  433  MET M  447  1                                  15    
HELIX  280 280 GLU M  448  ASN M  457  1                                  10    
HELIX  281 281 GLU M  461  GLY M  471  1                                  11    
HELIX  282 282 THR M  497  THR M  516  1                                  20    
HELIX  283 283 GLY N    9  LYS N   28  1                                  20    
HELIX  284 284 VAL N   29  LEU N   31  5                                   3    
HELIX  285 285 ASP N   52  ILE N   60  1                                   9    
HELIX  286 286 PHE N   66  ALA N   84  1                                  19    
HELIX  287 287 GLY N   88  ALA N  108  1                                  21    
HELIX  288 288 ASN N  112  SER N  135  1                                  24    
HELIX  289 289 ASP N  140  ALA N  152  1                                  13    
HELIX  290 290 ASP N  155  GLY N  170  1                                  16    
HELIX  291 291 MET N  233  ALA N  243  1                                  11    
HELIX  292 292 GLU N  255  ARG N  268  1                                  14    
HELIX  293 293 PHE N  281  GLY N  297  1                                  17    
HELIX  294 294 THR N  313  LEU N  317  5                                   5    
HELIX  295 295 GLU N  338  ILE N  353  1                                  16    
HELIX  296 296 SER N  358  GLY N  375  1                                  18    
HELIX  297 297 THR N  385  GLY N  410  1                                  26    
HELIX  298 298 GLY N  416  LEU N  426  1                                  11    
HELIX  299 299 ASN N  433  MET N  447  1                                  15    
HELIX  300 300 GLU N  448  CYS N  458  1                                  11    
HELIX  301 301 GLU N  461  GLY N  471  1                                  11    
HELIX  302 302 THR N  497  THR N  516  1                                  20    
SHEET    1   A 4 LYS A   4  PHE A   8  0                                        
SHEET    2   A 4 THR A 517  ASP A 523 -1  O  THR A 522   N  ASP A   5           
SHEET    3   A 4 ASN B  37  LEU B  40  1  O  ASN B  37   N  GLU A 518           
SHEET    4   A 4 THR B  48  THR B  50 -1  O  THR B  48   N  LEU B  40           
SHEET    1   B 4 THR A  48  THR A  50  0                                        
SHEET    2   B 4 ASN A  37  LEU A  40 -1  N  VAL A  38   O  THR A  50           
SHEET    3   B 4 THR G 517  ASP G 523  1  O  CYS G 519   N  VAL A  39           
SHEET    4   B 4 LYS G   4  PHE G   8 -1  N  ASP G   5   O  THR G 522           
SHEET    1   C 3 ILE A 175  ASP A 179  0                                        
SHEET    2   C 3 VAL A 376  VAL A 381  1  O  ILE A 379   N  THR A 176           
SHEET    3   C 3 GLU A 186  VAL A 190 -1  N  GLU A 186   O  LYS A 380           
SHEET    1   D 6 MET A 193  PHE A 195  0                                        
SHEET    2   D 6 THR A 330  GLY A 335 -1  O  THR A 330   N  PHE A 195           
SHEET    3   D 6 GLY A 318  ILE A 325 -1  N  VAL A 324   O  THR A 331           
SHEET    4   D 6 PHE A 219  ILE A 227 -1  N  ILE A 220   O  GLY A 318           
SHEET    5   D 6 LEU A 247  VAL A 254  1  O  LEU A 248   N  LEU A 221           
SHEET    6   D 6 VAL A 273  LYS A 277  1  O  ALA A 274   N  ILE A 249           
SHEET    1   E 4 VAL A 213  GLU A 216  0                                        
SHEET    2   E 4 GLY A 318  ILE A 325 -1  O  VAL A 323   N  LEU A 215           
SHEET    3   E 4 PHE A 219  ILE A 227 -1  N  ILE A 220   O  GLY A 318           
SHEET    4   E 4 ILE A 301  SER A 302  1  O  ILE A 301   N  LEU A 222           
SHEET    1   F 2 VAL A 411  ALA A 413  0                                        
SHEET    2   F 2 LEU A 494  PRO A 496 -1  O  ASP A 495   N  VAL A 412           
SHEET    1   G 2 TYR A 476  ASN A 479  0                                        
SHEET    2   G 2 GLU A 484  ASN A 487 -1  O  GLY A 486   N  GLY A 477           
SHEET    1   H 4 LYS B   4  PHE B   8  0                                        
SHEET    2   H 4 THR B 517  ASP B 523 -1  O  THR B 522   N  ASP B   5           
SHEET    3   H 4 ASN C  37  LEU C  40  1  O  ASN C  37   N  GLU B 518           
SHEET    4   H 4 THR C  48  THR C  50 -1  O  THR C  48   N  LEU C  40           
SHEET    1   I 3 ILE B 175  ASP B 179  0                                        
SHEET    2   I 3 VAL B 376  VAL B 381  1  O  ILE B 379   N  THR B 176           
SHEET    3   I 3 GLU B 186  VAL B 190 -1  N  GLU B 186   O  LYS B 380           
SHEET    1   J 6 MET B 193  PHE B 195  0                                        
SHEET    2   J 6 THR B 330  GLY B 335 -1  O  THR B 330   N  PHE B 195           
SHEET    3   J 6 GLY B 318  ILE B 325 -1  N  VAL B 324   O  THR B 331           
SHEET    4   J 6 PHE B 219  ILE B 227 -1  N  ILE B 220   O  GLY B 318           
SHEET    5   J 6 LEU B 247  VAL B 254  1  O  LEU B 248   N  LEU B 221           
SHEET    6   J 6 VAL B 273  LYS B 277  1  O  ALA B 274   N  ILE B 249           
SHEET    1   K 4 VAL B 213  GLU B 216  0                                        
SHEET    2   K 4 GLY B 318  ILE B 325 -1  O  ILE B 325   N  VAL B 213           
SHEET    3   K 4 PHE B 219  ILE B 227 -1  N  ILE B 220   O  GLY B 318           
SHEET    4   K 4 ILE B 301  SER B 302  1  O  ILE B 301   N  LEU B 222           
SHEET    1   L 2 VAL B 411  ALA B 413  0                                        
SHEET    2   L 2 LEU B 494  PRO B 496 -1  O  ASP B 495   N  VAL B 412           
SHEET    1   M 2 TYR B 476  ASN B 479  0                                        
SHEET    2   M 2 GLU B 484  ASN B 487 -1  O  GLY B 486   N  GLY B 477           
SHEET    1   N 4 LYS C   4  PHE C   8  0                                        
SHEET    2   N 4 THR C 517  ASP C 523 -1  O  THR C 522   N  ASP C   5           
SHEET    3   N 4 ASN D  37  LEU D  40  1  O  ASN D  37   N  GLU C 518           
SHEET    4   N 4 THR D  48  THR D  50 -1  O  THR D  50   N  VAL D  38           
SHEET    1   O 3 ILE C 175  ASP C 179  0                                        
SHEET    2   O 3 VAL C 376  VAL C 381  1  O  ILE C 379   N  THR C 176           
SHEET    3   O 3 GLU C 186  VAL C 190 -1  N  GLU C 186   O  LYS C 380           
SHEET    1   P 6 MET C 193  PHE C 195  0                                        
SHEET    2   P 6 THR C 330  GLY C 335 -1  O  THR C 330   N  PHE C 195           
SHEET    3   P 6 GLY C 318  ILE C 325 -1  N  VAL C 324   O  THR C 331           
SHEET    4   P 6 PHE C 219  ILE C 227 -1  N  ILE C 220   O  GLY C 318           
SHEET    5   P 6 LEU C 247  VAL C 254  1  O  ILE C 250   N  LEU C 221           
SHEET    6   P 6 VAL C 273  LYS C 277  1  O  ALA C 274   N  ILE C 249           
SHEET    1   Q 4 VAL C 213  GLU C 216  0                                        
SHEET    2   Q 4 GLY C 318  ILE C 325 -1  O  ILE C 325   N  VAL C 213           
SHEET    3   Q 4 PHE C 219  ILE C 227 -1  N  ILE C 220   O  GLY C 318           
SHEET    4   Q 4 ILE C 301  SER C 302  1  O  ILE C 301   N  LEU C 222           
SHEET    1   R 2 VAL C 411  ALA C 413  0                                        
SHEET    2   R 2 LEU C 494  PRO C 496 -1  O  ASP C 495   N  VAL C 412           
SHEET    1   S 2 TYR C 476  ASN C 479  0                                        
SHEET    2   S 2 GLU C 484  ASN C 487 -1  O  GLY C 486   N  GLY C 477           
SHEET    1   T 4 LYS D   4  PHE D   8  0                                        
SHEET    2   T 4 THR D 517  ASP D 523 -1  O  THR D 522   N  ASP D   5           
SHEET    3   T 4 ASN E  37  LEU E  40  1  O  ASN E  37   N  GLU D 518           
SHEET    4   T 4 THR E  48  THR E  50 -1  O  THR E  50   N  VAL E  38           
SHEET    1   U 3 ILE D 175  ASP D 179  0                                        
SHEET    2   U 3 VAL D 376  VAL D 381  1  O  ILE D 379   N  THR D 176           
SHEET    3   U 3 GLU D 186  VAL D 190 -1  N  GLU D 186   O  LYS D 380           
SHEET    1   V 6 MET D 193  PHE D 195  0                                        
SHEET    2   V 6 THR D 330  GLY D 335 -1  O  THR D 330   N  PHE D 195           
SHEET    3   V 6 GLY D 318  ILE D 325 -1  N  VAL D 324   O  THR D 331           
SHEET    4   V 6 PHE D 219  ILE D 227 -1  N  ILE D 220   O  GLY D 318           
SHEET    5   V 6 LEU D 247  VAL D 254  1  O  ILE D 250   N  LEU D 221           
SHEET    6   V 6 VAL D 273  LYS D 277  1  O  ALA D 274   N  ILE D 249           
SHEET    1   W 4 VAL D 213  GLU D 216  0                                        
SHEET    2   W 4 GLY D 318  ILE D 325 -1  O  ILE D 325   N  VAL D 213           
SHEET    3   W 4 PHE D 219  ILE D 227 -1  N  ILE D 220   O  GLY D 318           
SHEET    4   W 4 ILE D 301  SER D 302  1  O  ILE D 301   N  LEU D 222           
SHEET    1   X 2 VAL D 411  ALA D 413  0                                        
SHEET    2   X 2 LEU D 494  PRO D 496 -1  O  ASP D 495   N  VAL D 412           
SHEET    1   Y 2 TYR D 476  ASN D 479  0                                        
SHEET    2   Y 2 GLU D 484  ASN D 487 -1  O  GLY D 486   N  GLY D 477           
SHEET    1   Z 4 LYS E   4  PHE E   8  0                                        
SHEET    2   Z 4 THR E 517  ASP E 523 -1  O  THR E 522   N  ASP E   5           
SHEET    3   Z 4 ASN F  37  LEU F  40  1  O  ASN F  37   N  GLU E 518           
SHEET    4   Z 4 THR F  48  THR F  50 -1  O  THR F  48   N  LEU F  40           
SHEET    1  AA 3 VAL E 174  ASP E 179  0                                        
SHEET    2  AA 3 VAL E 376  VAL E 381  1  O  ILE E 379   N  THR E 176           
SHEET    3  AA 3 GLU E 186  VAL E 190 -1  N  GLU E 186   O  LYS E 380           
SHEET    1  AB 6 MET E 193  PHE E 195  0                                        
SHEET    2  AB 6 THR E 330  GLY E 335 -1  O  THR E 330   N  PHE E 195           
SHEET    3  AB 6 GLY E 318  ILE E 325 -1  N  VAL E 324   O  THR E 331           
SHEET    4  AB 6 PHE E 219  ILE E 227 -1  N  ILE E 220   O  GLY E 318           
SHEET    5  AB 6 LEU E 247  VAL E 254  1  O  LEU E 248   N  LEU E 221           
SHEET    6  AB 6 VAL E 273  LYS E 277  1  O  ALA E 274   N  ILE E 249           
SHEET    1  AC 4 VAL E 213  GLU E 216  0                                        
SHEET    2  AC 4 GLY E 318  ILE E 325 -1  O  ILE E 325   N  VAL E 213           
SHEET    3  AC 4 PHE E 219  ILE E 227 -1  N  ILE E 220   O  GLY E 318           
SHEET    4  AC 4 ILE E 301  SER E 302  1  O  ILE E 301   N  LEU E 222           
SHEET    1  AD 2 VAL E 411  ALA E 413  0                                        
SHEET    2  AD 2 LEU E 494  PRO E 496 -1  O  ASP E 495   N  VAL E 412           
SHEET    1  AE 2 TYR E 476  ASN E 479  0                                        
SHEET    2  AE 2 GLU E 484  ASN E 487 -1  O  GLY E 486   N  GLY E 477           
SHEET    1  AF 4 LYS F   4  PHE F   8  0                                        
SHEET    2  AF 4 THR F 517  ASP F 523 -1  O  THR F 522   N  ASP F   5           
SHEET    3  AF 4 ASN G  37  LEU G  40  1  O  ASN G  37   N  GLU F 518           
SHEET    4  AF 4 THR G  48  THR G  50 -1  O  THR G  48   N  LEU G  40           
SHEET    1  AG 3 ILE F 175  ASP F 179  0                                        
SHEET    2  AG 3 VAL F 376  VAL F 381  1  O  ILE F 379   N  THR F 176           
SHEET    3  AG 3 GLU F 186  VAL F 190 -1  N  GLU F 186   O  LYS F 380           
SHEET    1  AH 6 MET F 193  PHE F 195  0                                        
SHEET    2  AH 6 THR F 330  GLY F 335 -1  O  THR F 330   N  PHE F 195           
SHEET    3  AH 6 GLY F 318  ILE F 325 -1  N  VAL F 324   O  THR F 331           
SHEET    4  AH 6 PHE F 219  ILE F 227 -1  N  ILE F 220   O  GLY F 318           
SHEET    5  AH 6 LEU F 247  VAL F 254  1  O  LEU F 248   N  LEU F 221           
SHEET    6  AH 6 VAL F 273  LYS F 277  1  O  ALA F 274   N  ILE F 249           
SHEET    1  AI 4 VAL F 213  GLU F 216  0                                        
SHEET    2  AI 4 GLY F 318  ILE F 325 -1  O  ILE F 325   N  VAL F 213           
SHEET    3  AI 4 PHE F 219  ILE F 227 -1  N  ILE F 220   O  GLY F 318           
SHEET    4  AI 4 ILE F 301  SER F 302  1  O  ILE F 301   N  LEU F 222           
SHEET    1  AJ 2 VAL F 411  ALA F 413  0                                        
SHEET    2  AJ 2 LEU F 494  PRO F 496 -1  O  ASP F 495   N  VAL F 412           
SHEET    1  AK 2 TYR F 476  ASN F 479  0                                        
SHEET    2  AK 2 GLU F 484  ASN F 487 -1  O  GLY F 486   N  GLY F 477           
SHEET    1  AL 3 VAL G 174  ASP G 179  0                                        
SHEET    2  AL 3 VAL G 376  VAL G 381  1  O  ILE G 379   N  THR G 176           
SHEET    3  AL 3 GLU G 186  VAL G 190 -1  N  GLU G 186   O  LYS G 380           
SHEET    1  AM 6 MET G 193  PHE G 195  0                                        
SHEET    2  AM 6 THR G 330  GLY G 335 -1  O  THR G 330   N  PHE G 195           
SHEET    3  AM 6 GLY G 318  ILE G 325 -1  N  VAL G 324   O  THR G 331           
SHEET    4  AM 6 PHE G 219  ILE G 227 -1  N  ILE G 220   O  GLY G 318           
SHEET    5  AM 6 LEU G 247  VAL G 254  1  O  LEU G 248   N  LEU G 221           
SHEET    6  AM 6 VAL G 273  LYS G 277  1  O  ALA G 274   N  ILE G 249           
SHEET    1  AN 4 VAL G 213  GLU G 216  0                                        
SHEET    2  AN 4 GLY G 318  ILE G 325 -1  O  ILE G 325   N  VAL G 213           
SHEET    3  AN 4 PHE G 219  ILE G 227 -1  N  ILE G 220   O  GLY G 318           
SHEET    4  AN 4 ILE G 301  SER G 302  1  O  ILE G 301   N  LEU G 222           
SHEET    1  AO 2 VAL G 411  ALA G 413  0                                        
SHEET    2  AO 2 LEU G 494  PRO G 496 -1  O  ASP G 495   N  VAL G 412           
SHEET    1  AP 2 TYR G 476  ASN G 479  0                                        
SHEET    2  AP 2 GLU G 484  ASN G 487 -1  O  GLY G 486   N  GLY G 477           
SHEET    1  AQ 4 LYS H   4  PHE H   8  0                                        
SHEET    2  AQ 4 THR H 517  ASP H 523 -1  O  THR H 522   N  ASP H   5           
SHEET    3  AQ 4 ASN N  37  LEU N  40  1  O  VAL N  39   N  VAL H 521           
SHEET    4  AQ 4 THR N  48  THR N  50 -1  O  THR N  48   N  LEU N  40           
SHEET    1  AR 4 THR H  48  THR H  50  0                                        
SHEET    2  AR 4 ASN H  37  LEU H  40 -1  N  LEU H  40   O  THR H  48           
SHEET    3  AR 4 THR I 517  ASP I 523  1  O  CYS I 519   N  VAL H  39           
SHEET    4  AR 4 LYS I   4  PHE I   8 -1  N  ASP I   5   O  THR I 522           
SHEET    1  AS 3 VAL H 174  ASP H 179  0                                        
SHEET    2  AS 3 VAL H 376  VAL H 381  1  O  ALA H 377   N  VAL H 174           
SHEET    3  AS 3 ASP H 188  VAL H 190 -1  N  VAL H 190   O  VAL H 376           
SHEET    1  AT 6 MET H 193  PHE H 195  0                                        
SHEET    2  AT 6 THR H 330  GLY H 335 -1  O  ILE H 332   N  MET H 193           
SHEET    3  AT 6 GLY H 318  ILE H 325 -1  N  ARG H 322   O  ILE H 333           
SHEET    4  AT 6 PHE H 219  ILE H 227 -1  N  ILE H 220   O  GLY H 318           
SHEET    5  AT 6 LEU H 247  VAL H 254  1  O  LEU H 248   N  LEU H 221           
SHEET    6  AT 6 VAL H 273  LYS H 277  1  O  VAL H 276   N  ILE H 249           
SHEET    1  AU 4 VAL H 213  GLU H 216  0                                        
SHEET    2  AU 4 GLY H 318  ILE H 325 -1  O  ILE H 325   N  VAL H 213           
SHEET    3  AU 4 PHE H 219  ILE H 227 -1  N  ILE H 220   O  GLY H 318           
SHEET    4  AU 4 VAL H 300  SER H 302  1  O  ILE H 301   N  LEU H 222           
SHEET    1  AV 2 VAL H 411  ALA H 413  0                                        
SHEET    2  AV 2 LEU H 494  PRO H 496 -1  O  ASP H 495   N  VAL H 412           
SHEET    1  AW 2 TYR H 476  ASN H 479  0                                        
SHEET    2  AW 2 GLU H 484  ASN H 487 -1  O  GLY H 486   N  GLY H 477           
SHEET    1  AX 4 THR I  48  THR I  50  0                                        
SHEET    2  AX 4 ASN I  37  LEU I  40 -1  N  LEU I  40   O  THR I  48           
SHEET    3  AX 4 THR J 517  ASP J 523  1  O  GLU J 518   N  ASN I  37           
SHEET    4  AX 4 LYS J   4  PHE J   8 -1  N  ASP J   5   O  THR J 522           
SHEET    1  AY 3 VAL I 174  ASP I 179  0                                        
SHEET    2  AY 3 VAL I 376  VAL I 381  1  O  ALA I 377   N  THR I 176           
SHEET    3  AY 3 GLU I 186  VAL I 190 -1  N  VAL I 190   O  VAL I 376           
SHEET    1  AZ 6 MET I 193  PHE I 195  0                                        
SHEET    2  AZ 6 THR I 330  GLY I 335 -1  O  ILE I 332   N  MET I 193           
SHEET    3  AZ 6 GLY I 318  ILE I 325 -1  N  ARG I 322   O  ILE I 333           
SHEET    4  AZ 6 PHE I 219  ILE I 227 -1  N  ILE I 220   O  GLY I 318           
SHEET    5  AZ 6 LEU I 247  VAL I 254  1  O  LEU I 248   N  LEU I 221           
SHEET    6  AZ 6 VAL I 273  LYS I 277  1  O  VAL I 276   N  ILE I 249           
SHEET    1  BA 4 VAL I 213  GLU I 216  0                                        
SHEET    2  BA 4 GLY I 318  ILE I 325 -1  O  ILE I 325   N  VAL I 213           
SHEET    3  BA 4 PHE I 219  ILE I 227 -1  N  ILE I 220   O  GLY I 318           
SHEET    4  BA 4 VAL I 300  SER I 302  1  O  ILE I 301   N  LEU I 222           
SHEET    1  BB 2 VAL I 411  ALA I 413  0                                        
SHEET    2  BB 2 LEU I 494  PRO I 496 -1  O  ASP I 495   N  VAL I 412           
SHEET    1  BC 2 TYR I 476  ASN I 479  0                                        
SHEET    2  BC 2 GLU I 484  ASN I 487 -1  O  GLU I 484   N  ASN I 479           
SHEET    1  BD 4 THR J  48  THR J  50  0                                        
SHEET    2  BD 4 ASN J  37  LEU J  40 -1  N  LEU J  40   O  THR J  48           
SHEET    3  BD 4 THR K 517  ASP K 523  1  O  CYS K 519   N  VAL J  39           
SHEET    4  BD 4 LYS K   4  PHE K   8 -1  N  ASP K   5   O  THR K 522           
SHEET    1  BE 3 VAL J 174  ASP J 179  0                                        
SHEET    2  BE 3 VAL J 376  VAL J 381  1  O  ALA J 377   N  VAL J 174           
SHEET    3  BE 3 GLU J 186  VAL J 190 -1  N  VAL J 190   O  VAL J 376           
SHEET    1  BF 6 MET J 193  PHE J 195  0                                        
SHEET    2  BF 6 THR J 330  GLY J 335 -1  O  THR J 330   N  PHE J 195           
SHEET    3  BF 6 GLY J 318  ILE J 325 -1  N  ARG J 322   O  ILE J 333           
SHEET    4  BF 6 PHE J 219  ILE J 227 -1  N  ILE J 220   O  GLY J 318           
SHEET    5  BF 6 LEU J 247  VAL J 254  1  O  LEU J 248   N  LEU J 221           
SHEET    6  BF 6 VAL J 273  LYS J 277  1  O  VAL J 276   N  ILE J 249           
SHEET    1  BG 4 VAL J 213  GLU J 216  0                                        
SHEET    2  BG 4 GLY J 318  ILE J 325 -1  O  ILE J 325   N  VAL J 213           
SHEET    3  BG 4 PHE J 219  ILE J 227 -1  N  ILE J 220   O  GLY J 318           
SHEET    4  BG 4 VAL J 300  SER J 302  1  O  ILE J 301   N  ASP J 224           
SHEET    1  BH 2 VAL J 411  ALA J 413  0                                        
SHEET    2  BH 2 LEU J 494  PRO J 496 -1  O  ASP J 495   N  VAL J 412           
SHEET    1  BI 2 TYR J 476  ASN J 479  0                                        
SHEET    2  BI 2 GLU J 484  ASN J 487 -1  O  GLY J 486   N  GLY J 477           
SHEET    1  BJ 4 THR K  48  THR K  50  0                                        
SHEET    2  BJ 4 ASN K  37  LEU K  40 -1  N  LEU K  40   O  THR K  48           
SHEET    3  BJ 4 THR L 517  ASP L 523  1  O  VAL L 521   N  VAL K  39           
SHEET    4  BJ 4 LYS L   4  PHE L   8 -1  N  ASP L   5   O  THR L 522           
SHEET    1  BK 3 VAL K 174  ASP K 179  0                                        
SHEET    2  BK 3 VAL K 376  VAL K 381  1  O  ALA K 377   N  VAL K 174           
SHEET    3  BK 3 GLU K 186  VAL K 190 -1  N  VAL K 190   O  VAL K 376           
SHEET    1  BL 6 MET K 193  PHE K 195  0                                        
SHEET    2  BL 6 THR K 330  GLY K 335 -1  O  ILE K 332   N  MET K 193           
SHEET    3  BL 6 GLY K 318  ILE K 325 -1  N  ARG K 322   O  ILE K 333           
SHEET    4  BL 6 PHE K 219  ILE K 227 -1  N  ILE K 220   O  GLY K 318           
SHEET    5  BL 6 LEU K 247  VAL K 254  1  O  LEU K 248   N  LEU K 221           
SHEET    6  BL 6 VAL K 273  LYS K 277  1  O  VAL K 276   N  ILE K 249           
SHEET    1  BM 4 VAL K 213  GLU K 216  0                                        
SHEET    2  BM 4 GLY K 318  ILE K 325 -1  O  ILE K 325   N  VAL K 213           
SHEET    3  BM 4 PHE K 219  ILE K 227 -1  N  ILE K 220   O  GLY K 318           
SHEET    4  BM 4 VAL K 300  SER K 302  1  O  ILE K 301   N  ASP K 224           
SHEET    1  BN 2 VAL K 411  ALA K 413  0                                        
SHEET    2  BN 2 LEU K 494  PRO K 496 -1  O  ASP K 495   N  VAL K 412           
SHEET    1  BO 2 TYR K 476  ASN K 479  0                                        
SHEET    2  BO 2 GLU K 484  ASN K 487 -1  O  GLY K 486   N  GLY K 477           
SHEET    1  BP 4 THR L  48  THR L  50  0                                        
SHEET    2  BP 4 ASN L  37  LEU L  40 -1  N  LEU L  40   O  THR L  48           
SHEET    3  BP 4 THR M 517  ASP M 523  1  O  GLU M 518   N  ASN L  37           
SHEET    4  BP 4 LYS M   4  PHE M   8 -1  N  ASP M   5   O  THR M 522           
SHEET    1  BQ 3 VAL L 174  ASP L 179  0                                        
SHEET    2  BQ 3 VAL L 376  VAL L 381  1  O  ALA L 377   N  VAL L 174           
SHEET    3  BQ 3 GLU L 186  VAL L 190 -1  N  VAL L 190   O  VAL L 376           
SHEET    1  BR 6 MET L 193  PHE L 195  0                                        
SHEET    2  BR 6 THR L 330  GLY L 335 -1  O  ILE L 332   N  MET L 193           
SHEET    3  BR 6 GLY L 318  ILE L 325 -1  N  ARG L 322   O  ILE L 333           
SHEET    4  BR 6 PHE L 219  ILE L 227 -1  N  ILE L 220   O  GLY L 318           
SHEET    5  BR 6 LEU L 247  VAL L 254  1  O  LEU L 248   N  LEU L 221           
SHEET    6  BR 6 VAL L 273  LYS L 277  1  O  VAL L 276   N  ILE L 249           
SHEET    1  BS 4 VAL L 213  GLU L 216  0                                        
SHEET    2  BS 4 GLY L 318  ILE L 325 -1  O  ILE L 325   N  VAL L 213           
SHEET    3  BS 4 PHE L 219  ILE L 227 -1  N  ILE L 220   O  GLY L 318           
SHEET    4  BS 4 VAL L 300  SER L 302  1  O  ILE L 301   N  LEU L 222           
SHEET    1  BT 2 VAL L 411  ALA L 413  0                                        
SHEET    2  BT 2 LEU L 494  PRO L 496 -1  O  ASP L 495   N  VAL L 412           
SHEET    1  BU 2 TYR L 476  ASN L 479  0                                        
SHEET    2  BU 2 GLU L 484  ASN L 487 -1  O  GLY L 486   N  GLY L 477           
SHEET    1  BV 4 THR M  48  THR M  50  0                                        
SHEET    2  BV 4 ASN M  37  LEU M  40 -1  N  LEU M  40   O  THR M  48           
SHEET    3  BV 4 THR N 517  ASP N 523  1  O  GLU N 518   N  ASN M  37           
SHEET    4  BV 4 LYS N   4  PHE N   8 -1  N  ASP N   5   O  THR N 522           
SHEET    1  BW 3 VAL M 174  ASP M 179  0                                        
SHEET    2  BW 3 VAL M 376  VAL M 381  1  O  ALA M 377   N  VAL M 174           
SHEET    3  BW 3 ASP M 188  VAL M 190 -1  N  VAL M 190   O  VAL M 376           
SHEET    1  BX 6 MET M 193  PHE M 195  0                                        
SHEET    2  BX 6 THR M 330  GLY M 335 -1  O  ILE M 332   N  MET M 193           
SHEET    3  BX 6 GLY M 318  ILE M 325 -1  N  ARG M 322   O  ILE M 333           
SHEET    4  BX 6 PHE M 219  ILE M 227 -1  N  ILE M 220   O  GLY M 318           
SHEET    5  BX 6 LEU M 247  VAL M 254  1  O  LEU M 248   N  LEU M 221           
SHEET    6  BX 6 VAL M 273  LYS M 277  1  O  VAL M 276   N  ILE M 249           
SHEET    1  BY 4 VAL M 213  GLU M 216  0                                        
SHEET    2  BY 4 GLY M 318  ILE M 325 -1  O  VAL M 323   N  LEU M 215           
SHEET    3  BY 4 PHE M 219  ILE M 227 -1  N  ILE M 220   O  GLY M 318           
SHEET    4  BY 4 VAL M 300  SER M 302  1  O  ILE M 301   N  LEU M 222           
SHEET    1  BZ 2 VAL M 411  ALA M 413  0                                        
SHEET    2  BZ 2 LEU M 494  PRO M 496 -1  O  ASP M 495   N  VAL M 412           
SHEET    1  CA 2 TYR M 476  ASN M 479  0                                        
SHEET    2  CA 2 GLU M 484  ASN M 487 -1  O  GLU M 484   N  ASN M 479           
SHEET    1  CB 3 VAL N 174  ASP N 179  0                                        
SHEET    2  CB 3 VAL N 376  VAL N 381  1  O  ALA N 377   N  VAL N 174           
SHEET    3  CB 3 ASP N 188  VAL N 190 -1  N  VAL N 190   O  VAL N 376           
SHEET    1  CC 6 MET N 193  PHE N 195  0                                        
SHEET    2  CC 6 THR N 330  GLY N 335 -1  O  ILE N 332   N  MET N 193           
SHEET    3  CC 6 GLY N 318  ILE N 325 -1  N  ARG N 322   O  ILE N 333           
SHEET    4  CC 6 PHE N 219  ILE N 227 -1  N  ILE N 220   O  GLY N 318           
SHEET    5  CC 6 LEU N 247  VAL N 254  1  O  LEU N 248   N  LEU N 221           
SHEET    6  CC 6 VAL N 273  LYS N 277  1  O  VAL N 276   N  ILE N 249           
SHEET    1  CD 4 VAL N 213  GLU N 216  0                                        
SHEET    2  CD 4 GLY N 318  ILE N 325 -1  O  ILE N 325   N  VAL N 213           
SHEET    3  CD 4 PHE N 219  ILE N 227 -1  N  ILE N 220   O  GLY N 318           
SHEET    4  CD 4 VAL N 300  SER N 302  1  O  ILE N 301   N  LEU N 222           
SHEET    1  CE 2 VAL N 411  ALA N 413  0                                        
SHEET    2  CE 2 LEU N 494  PRO N 496 -1  O  ASP N 495   N  VAL N 412           
SHEET    1  CF 2 TYR N 476  ASN N 479  0                                        
SHEET    2  CF 2 GLU N 484  ASN N 487 -1  O  GLY N 486   N  GLY N 477           
SHEET    1  CG 7 ILE O   3  PRO O   5  0                                        
SHEET    2  CG 7 ILE U  91  VAL U  95 -1  O  ILE U  94   N  ARG O   4           
SHEET    3  CG 7 ILE U  64  PHE U  67 -1  N  ILE U  64   O  VAL U  95           
SHEET    4  CG 7 ARG U  37  VAL U  43 -1  N  GLY U  38   O  VAL U  65           
SHEET    5  CG 7 ARG U   9  ARG U  14 -1  N  ILE U  11   O  LEU U  41           
SHEET    6  CG 7 GLU U  81  SER U  87 -1  O  MET U  86   N  VAL U  10           
SHEET    7  CG 7 LYS U  74  ILE U  78 -1  N  GLU U  76   O  VAL U  83           
SHEET    1  CH 7 LYS O  74  ILE O  78  0                                        
SHEET    2  CH 7 GLU O  81  SER O  87 -1  O  VAL O  83   N  GLU O  76           
SHEET    3  CH 7 ARG O   9  ARG O  14 -1  N  VAL O  10   O  MET O  86           
SHEET    4  CH 7 ARG O  37  VAL O  43 -1  O  LEU O  41   N  ILE O  11           
SHEET    5  CH 7 ILE O  64  PHE O  67 -1  O  VAL O  65   N  GLY O  38           
SHEET    6  CH 7 ILE O  91  VAL O  95 -1  O  VAL O  95   N  ILE O  64           
SHEET    7  CH 7 ILE P   3  PRO P   5 -1  O  ARG P   4   N  ILE O  94           
SHEET    1  CI 2 GLY O  46  ARG O  47  0                                        
SHEET    2  CI 2 LYS O  55  PRO O  56 -1  O  LYS O  55   N  ARG O  47           
SHEET    1  CJ 7 LYS P  74  ILE P  78  0                                        
SHEET    2  CJ 7 GLU P  81  SER P  87 -1  O  VAL P  83   N  GLU P  76           
SHEET    3  CJ 7 ARG P   9  ARG P  14 -1  N  VAL P  10   O  MET P  86           
SHEET    4  CJ 7 ARG P  37  VAL P  43 -1  O  LEU P  41   N  ILE P  11           
SHEET    5  CJ 7 ILE P  64  PHE P  67 -1  O  VAL P  65   N  GLY P  38           
SHEET    6  CJ 7 ILE P  91  VAL P  95 -1  O  VAL P  95   N  ILE P  64           
SHEET    7  CJ 7 ILE Q   3  PRO Q   5 -1  O  ARG Q   4   N  ILE P  94           
SHEET    1  CK 2 GLY P  46  ARG P  47  0                                        
SHEET    2  CK 2 LYS P  55  PRO P  56 -1  O  LYS P  55   N  ARG P  47           
SHEET    1  CL 7 LYS Q  74  ILE Q  78  0                                        
SHEET    2  CL 7 GLU Q  81  SER Q  87 -1  O  VAL Q  83   N  GLU Q  76           
SHEET    3  CL 7 ARG Q   9  ARG Q  14 -1  N  VAL Q  10   O  MET Q  86           
SHEET    4  CL 7 ARG Q  37  VAL Q  43 -1  O  LEU Q  41   N  ILE Q  11           
SHEET    5  CL 7 ILE Q  64  PHE Q  67 -1  O  VAL Q  65   N  GLY Q  38           
SHEET    6  CL 7 ILE Q  91  VAL Q  95 -1  O  VAL Q  95   N  ILE Q  64           
SHEET    7  CL 7 ILE R   3  PRO R   5 -1  O  ARG R   4   N  ILE Q  94           
SHEET    1  CM 2 GLY Q  46  ARG Q  47  0                                        
SHEET    2  CM 2 LYS Q  55  PRO Q  56 -1  O  LYS Q  55   N  ARG Q  47           
SHEET    1  CN 7 LYS R  74  ILE R  78  0                                        
SHEET    2  CN 7 GLU R  81  SER R  87 -1  O  VAL R  83   N  GLU R  76           
SHEET    3  CN 7 ARG R   9  ARG R  14 -1  N  VAL R  10   O  MET R  86           
SHEET    4  CN 7 ARG R  37  VAL R  43 -1  O  LEU R  41   N  ILE R  11           
SHEET    5  CN 7 ILE R  64  PHE R  67 -1  O  VAL R  65   N  GLY R  38           
SHEET    6  CN 7 ILE R  91  VAL R  95 -1  O  VAL R  95   N  ILE R  64           
SHEET    7  CN 7 ILE S   3  PRO S   5 -1  O  ARG S   4   N  ILE R  94           
SHEET    1  CO 2 GLY R  46  ARG R  47  0                                        
SHEET    2  CO 2 LYS R  55  PRO R  56 -1  O  LYS R  55   N  ARG R  47           
SHEET    1  CP 7 LYS S  74  ILE S  78  0                                        
SHEET    2  CP 7 GLU S  81  SER S  87 -1  O  VAL S  83   N  GLU S  76           
SHEET    3  CP 7 ARG S   9  ARG S  14 -1  N  VAL S  10   O  MET S  86           
SHEET    4  CP 7 ARG S  37  VAL S  43 -1  O  LEU S  41   N  ILE S  11           
SHEET    5  CP 7 ILE S  64  PHE S  67 -1  O  VAL S  65   N  GLY S  38           
SHEET    6  CP 7 ILE S  91  VAL S  95 -1  O  VAL S  95   N  ILE S  64           
SHEET    7  CP 7 ILE T   3  PRO T   5 -1  O  ARG T   4   N  ILE S  94           
SHEET    1  CQ 2 GLY S  46  ARG S  47  0                                        
SHEET    2  CQ 2 LYS S  55  PRO S  56 -1  O  LYS S  55   N  ARG S  47           
SHEET    1  CR 7 LYS T  74  ILE T  78  0                                        
SHEET    2  CR 7 GLU T  81  SER T  87 -1  O  VAL T  83   N  GLU T  76           
SHEET    3  CR 7 ARG T   9  ARG T  14 -1  N  VAL T  10   O  MET T  86           
SHEET    4  CR 7 ARG T  37  VAL T  43 -1  O  LEU T  41   N  ILE T  11           
SHEET    5  CR 7 ILE T  64  PHE T  67 -1  O  VAL T  65   N  GLY T  38           
SHEET    6  CR 7 ILE T  91  VAL T  95 -1  O  VAL T  95   N  ILE T  64           
SHEET    7  CR 7 ILE U   3  PRO U   5 -1  O  ARG U   4   N  ILE T  94           
SHEET    1  CS 2 GLY T  46  ARG T  47  0                                        
SHEET    2  CS 2 LYS T  55  PRO T  56 -1  O  LYS T  55   N  ARG T  47           
SHEET    1  CT 2 GLY U  46  ARG U  47  0                                        
SHEET    2  CT 2 LYS U  55  PRO U  56 -1  O  LYS U  55   N  ARG U  47           
LINK         O1B ADP A 600                MG    MG A 601     1555   1555  1.56  
LINK         O3B ADP A 600                 F2  AF3 A 602     1555   1555  2.01  
LINK         O2A ADP A 600                MG    MG A 601     1555   1555  1.74  
LINK        MG    MG A 601                 F1  AF3 A 602     1555   1555  1.76  
LINK        MG    MG A 601                 OD1 ASP A  87     1555   1555  2.35  
LINK        MG    MG A 601                AL   AF3 A 602     1555   1555  2.95  
LINK        AL   AF3 A 602                 OD1 ASP A  87     1555   1555  3.02  
LINK        AL   AF3 A 602                 O1B ADP A 600     1555   1555  2.75  
LINK        AL   AF3 A 602                 O3B ADP A 600     1555   1555  2.13  
LINK        AL   AF3 A 602                 O2A ADP A 600     1555   1555  3.42  
LINK        AL   AF3 A 602                 O3A ADP A 600     1555   1555  3.49  
LINK        AL   AF3 A 602                 OG1 THR A  89     1555   1555  3.59  
LINK         K     K A 603                 O3A ADP A 600     1555   1555  3.30  
LINK         K     K A 603                 O   THR A  30     1555   1555  3.16  
LINK         K     K A 603                 O1A ADP A 600     1555   1555  2.90  
LINK         K     K A 603                 O   LYS A  51     1555   1555  2.79  
LINK         K     K A 603                 F3  AF3 A 602     1555   1555  3.61  
LINK         K     K A 603                 OG1 THR A  30     1555   1555  2.90  
LINK         K     K A 603                 OG1 THR A  90     1555   1555  2.81  
LINK         O1B ADP B 600                MG    MG B 601     1555   1555  1.71  
LINK         O3B ADP B 600                AL   AF3 B 602     1555   1555  2.01  
LINK         O2A ADP B 600                MG    MG B 601     1555   1555  1.61  
LINK         O2A ADP B 600                 F1  AF3 B 602     1555   1555  2.05  
LINK        MG    MG B 601                 OD1 ASP B  87     1555   1555  2.64  
LINK        MG    MG B 601                 F1  AF3 B 602     1555   1555  1.77  
LINK        AL   AF3 B 602                MG    MG B 601     1555   1555  3.23  
LINK        AL   AF3 B 602                 O2A ADP B 600     1555   1555  3.55  
LINK        AL   AF3 B 602                 OD1 ASP B  87     1555   1555  3.28  
LINK        AL   AF3 B 602                 OG1 THR B  89     1555   1555  3.57  
LINK        AL   AF3 B 602                 O1B ADP B 600     1555   1555  2.77  
LINK        AL   AF3 B 602                 O3A ADP B 600     1555   1555  3.40  
LINK        AL   AF3 B 602                 K     K B 603     1555   1555  3.69  
LINK         K     K B 603                 O1A ADP B 600     1555   1555  2.97  
LINK         K     K B 603                 O3A ADP B 600     1555   1555  3.51  
LINK         K     K B 603                 O   LYS B  51     1555   1555  2.75  
LINK         K     K B 603                 F3  AF3 B 602     1555   1555  3.19  
LINK         K     K B 603                 O   THR B  30     1555   1555  3.20  
LINK         K     K B 603                 OG1 THR B  30     1555   1555  3.04  
LINK         K     K B 603                 OG1 THR B  90     1555   1555  3.00  
LINK         O3B ADP C 600                 F2  AF3 C 602     1555   1555  1.90  
LINK         O1B ADP C 600                MG    MG C 601     1555   1555  1.76  
LINK         O2A ADP C 600                MG    MG C 601     1555   1555  1.81  
LINK        MG    MG C 601                 OD1 ASP C  87     1555   1555  2.27  
LINK        MG    MG C 601                 F1  AF3 C 602     1555   1555  1.63  
LINK        MG    MG C 601                AL   AF3 C 602     1555   1555  3.00  
LINK        AL   AF3 C 602                 O3B ADP C 600     1555   1555  2.18  
LINK        AL   AF3 C 602                 O3A ADP C 600     1555   1555  3.46  
LINK        AL   AF3 C 602                 O2A ADP C 600     1555   1555  3.39  
LINK        AL   AF3 C 602                 OD1 ASP C  87     1555   1555  3.22  
LINK        AL   AF3 C 602                 O1B ADP C 600     1555   1555  2.74  
LINK         K     K C 603                 O3A ADP C 600     1555   1555  3.62  
LINK         K     K C 603                 O1A ADP C 600     1555   1555  2.83  
LINK         K     K C 603                 F3  AF3 C 602     1555   1555  3.41  
LINK         K     K C 603                 OG1 THR C  90     1555   1555  3.01  
LINK         K     K C 603                 OG1 THR C  30     1555   1555  2.89  
LINK         K     K C 603                 NZ  LYS C  51     1555   1555  3.68  
LINK         K     K C 603                 O   LYS C  51     1555   1555  2.78  
LINK         K     K C 603                 O   THR C  30     1555   1555  2.92  
LINK         O2A ADP D 600                MG    MG D 601     1555   1555  1.54  
LINK         O2A ADP D 600                 F1  AF3 D 602     1555   1555  1.96  
LINK         O1B ADP D 600                MG    MG D 601     1555   1555  1.59  
LINK        MG    MG D 601                 OD1 ASP D  87     1555   1555  2.48  
LINK        MG    MG D 601                 F1  AF3 D 602     1555   1555  1.73  
LINK        MG    MG D 601                AL   AF3 D 602     1555   1555  2.93  
LINK        MG    MG D 601                 F2  AF3 D 602     1555   1555  3.10  
LINK        MG    MG D 601                 O   HOH D 611     1555   1555  3.11  
LINK        AL   AF3 D 602                 O3B ADP D 600     1555   1555  2.08  
LINK        AL   AF3 D 602                 O3A ADP D 600     1555   1555  3.47  
LINK        AL   AF3 D 602                 OG1 THR D  89     1555   1555  3.63  
LINK        AL   AF3 D 602                 O2A ADP D 600     1555   1555  3.41  
LINK        AL   AF3 D 602                 O1B ADP D 600     1555   1555  2.71  
LINK        AL   AF3 D 602                 OD1 ASP D  87     1555   1555  3.19  
LINK         K     K D 603                 O3A ADP D 600     1555   1555  3.53  
LINK         K     K D 603                 OG1 THR D  90     1555   1555  2.99  
LINK         K     K D 603                 F3  AF3 D 602     1555   1555  3.63  
LINK         K     K D 603                 O1A ADP D 600     1555   1555  2.83  
LINK         K     K D 603                 O   THR D  30     1555   1555  3.19  
LINK         K     K D 603                 OG1 THR D  30     1555   1555  3.12  
LINK         K     K D 603                 O   LYS D  51     1555   1555  2.67  
LINK         O1B ADP E 600                MG    MG E 601     1555   1555  1.59  
LINK         O2A ADP E 600                MG    MG E 601     1555   1555  1.67  
LINK        MG    MG E 601                 O   HOH E 608     1555   1555  2.20  
LINK        MG    MG E 601                 F1  AF3 E 602     1555   1555  1.76  
LINK        MG    MG E 601                 OD1 ASP E  87     1555   1555  2.36  
LINK        MG    MG E 601                AL   AF3 E 602     1555   1555  2.93  
LINK        AL   AF3 E 602                 OD1 ASP E  87     1555   1555  3.14  
LINK        AL   AF3 E 602                 O2A ADP E 600     1555   1555  3.50  
LINK        AL   AF3 E 602                 O1B ADP E 600     1555   1555  2.80  
LINK        AL   AF3 E 602                 O3A ADP E 600     1555   1555  3.36  
LINK        AL   AF3 E 602                 OG1 THR E  89     1555   1555  3.56  
LINK        AL   AF3 E 602                 O3B ADP E 600     1555   1555  2.07  
LINK         K     K E 603                 O1A ADP E 600     1555   1555  3.17  
LINK         K     K E 603                 O3A ADP E 600     1555   1555  3.69  
LINK         K     K E 603                 OG1 THR E  90     1555   1555  3.01  
LINK         K     K E 603                 OG1 THR E  30     1555   1555  2.76  
LINK         K     K E 603                 O   THR E  30     1555   1555  3.18  
LINK         K     K E 603                 F3  AF3 E 602     1555   1555  3.32  
LINK         K     K E 603                 O   LYS E  51     1555   1555  2.48  
LINK         O2A ADP F 600                 F1  AF3 F 602     1555   1555  2.00  
LINK         O2A ADP F 600                MG    MG F 601     1555   1555  1.58  
LINK         O1B ADP F 600                MG    MG F 601     1555   1555  1.67  
LINK        MG    MG F 601                 F1  AF3 F 602     1555   1555  1.71  
LINK        MG    MG F 601                 OD1 ASP F  87     1555   1555  2.36  
LINK        MG    MG F 601                AL   AF3 F 602     1555   1555  2.95  
LINK        AL   AF3 F 602                 OD1 ASP F  87     1555   1555  3.03  
LINK        AL   AF3 F 602                 O1B ADP F 600     1555   1555  2.72  
LINK        AL   AF3 F 602                 O3B ADP F 600     1555   1555  2.32  
LINK        AL   AF3 F 602                 O2A ADP F 600     1555   1555  3.32  
LINK        AL   AF3 F 602                 O3A ADP F 600     1555   1555  3.56  
LINK        AL   AF3 F 602                 OG1 THR F  89     1555   1555  3.57  
LINK        AL   AF3 F 602                 K     K F 603     1555   1555  3.71  
LINK         K     K F 603                 O1A ADP F 600     1555   1555  3.06  
LINK         K     K F 603                 O3A ADP F 600     1555   1555  3.58  
LINK         K     K F 603                 OG1 THR F  90     1555   1555  3.04  
LINK         K     K F 603                 OG1 THR F  30     1555   1555  3.38  
LINK         K     K F 603                 O   THR F  30     1555   1555  3.29  
LINK         K     K F 603                 F3  AF3 F 602     1555   1555  3.34  
LINK         K     K F 603                 O   LYS F  51     1555   1555  2.77  
LINK         O2A ADP G 600                 F1  AF3 G 602     1555   1555  2.00  
LINK         O2A ADP G 600                MG    MG G 601     1555   1555  1.72  
LINK         O1B ADP G 600                MG    MG G 601     1555   1555  1.68  
LINK        MG    MG G 601                 F1  AF3 G 602     1555   1555  1.63  
LINK        MG    MG G 601                 OD1 ASP G  87     1555   1555  2.30  
LINK        MG    MG G 601                AL   AF3 G 602     1555   1555  2.93  
LINK        AL   AF3 G 602                 OG1 THR G  89     1555   1555  3.61  
LINK        AL   AF3 G 602                 O3B ADP G 600     1555   1555  2.31  
LINK        AL   AF3 G 602                 O3A ADP G 600     1555   1555  3.49  
LINK        AL   AF3 G 602                 OD1 ASP G  87     1555   1555  3.14  
LINK        AL   AF3 G 602                 O1B ADP G 600     1555   1555  2.73  
LINK        AL   AF3 G 602                 O   HOH G 618     1555   1555  3.69  
LINK        AL   AF3 G 602                 O2A ADP G 600     1555   1555  3.39  
LINK         K     K G 603                 OG1 THR G  30     1555   1555  2.90  
LINK         K     K G 603                 O   THR G  30     1555   1555  3.21  
LINK         K     K G 603                 O   LYS G  51     1555   1555  2.69  
LINK         K     K G 603                 O1A ADP G 600     1555   1555  3.06  
LINK         K     K G 603                 F3  AF3 G 602     1555   1555  3.20  
LINK         K     K G 603                 O3A ADP G 600     1555   1555  3.52  
LINK         K     K G 603                 OG1 THR G  90     1555   1555  2.79  
SITE     1 AC1  3 ASP A  87  ADP A 600  AF3 A 602                               
SITE     1 AC2  5 THR A  30  LYS A  51  THR A  90  ADP A 600                    
SITE     2 AC2  5 AF3 A 602                                                     
SITE     1 AC3  3 ASP B  87  ADP B 600  AF3 B 602                               
SITE     1 AC4  5 THR B  30  LYS B  51  THR B  90  ADP B 600                    
SITE     2 AC4  5 AF3 B 602                                                     
SITE     1 AC5  3 ASP C  87  ADP C 600  AF3 C 602                               
SITE     1 AC6  5 THR C  30  LYS C  51  THR C  90  ADP C 600                    
SITE     2 AC6  5 AF3 C 602                                                     
SITE     1 AC7  3 ASP D  87  ADP D 600  AF3 D 602                               
SITE     1 AC8  5 THR D  30  LYS D  51  THR D  90  ADP D 600                    
SITE     2 AC8  5 AF3 D 602                                                     
SITE     1 AC9  4 ASP E  87  ADP E 600  AF3 E 602  HOH E 608                    
SITE     1 BC1  5 THR E  30  LYS E  51  THR E  90  ADP E 600                    
SITE     2 BC1  5 AF3 E 602                                                     
SITE     1 BC2  3 ASP F  87  ADP F 600  AF3 F 602                               
SITE     1 BC3  5 THR F  30  LYS F  51  THR F  90  ADP F 600                    
SITE     2 BC3  5 AF3 F 602                                                     
SITE     1 BC4  3 ASP G  87  ADP G 600  AF3 G 602                               
SITE     1 BC5  5 THR G  30  LYS G  51  THR G  90  ADP G 600                    
SITE     2 BC5  5 AF3 G 602                                                     
SITE     1 BC6 23 THR A  30  LEU A  31  GLY A  32  PRO A  33                    
SITE     2 BC6 23 LYS A  51  ASP A  87  GLY A  88  THR A  89                    
SITE     3 BC6 23 THR A  90  THR A  91  ILE A 150  GLY A 414                    
SITE     4 BC6 23 GLY A 415  ILE A 454  TYR A 478  ASN A 479                    
SITE     5 BC6 23 ALA A 480  ALA A 481  ILE A 493  ASP A 495                    
SITE     6 BC6 23  MG A 601  AF3 A 602    K A 603                               
SITE     1 BC7  9 ASP A  52  GLY A  53  ASP A  87  GLY A  88                    
SITE     2 BC7  9 THR A  89  THR A  90  ADP A 600   MG A 601                    
SITE     3 BC7  9   K A 603                                                     
SITE     1 BC8 23 THR B  30  LEU B  31  GLY B  32  PRO B  33                    
SITE     2 BC8 23 LYS B  51  ASP B  87  GLY B  88  THR B  89                    
SITE     3 BC8 23 THR B  90  THR B  91  ILE B 150  GLY B 414                    
SITE     4 BC8 23 GLY B 415  ILE B 454  TYR B 478  ASN B 479                    
SITE     5 BC8 23 ALA B 480  ALA B 481  ILE B 493  ASP B 495                    
SITE     6 BC8 23  MG B 601  AF3 B 602    K B 603                               
SITE     1 BC9  8 GLY B  53  ASP B  87  GLY B  88  THR B  89                    
SITE     2 BC9  8 THR B  90  ADP B 600   MG B 601    K B 603                    
SITE     1 CC1 22 THR C  30  LEU C  31  GLY C  32  PRO C  33                    
SITE     2 CC1 22 LYS C  51  ASP C  87  GLY C  88  THR C  89                    
SITE     3 CC1 22 THR C  90  THR C  91  ILE C 150  GLY C 414                    
SITE     4 CC1 22 GLY C 415  ILE C 454  TYR C 478  ASN C 479                    
SITE     5 CC1 22 ALA C 480  ALA C 481  ASP C 495   MG C 601                    
SITE     6 CC1 22 AF3 C 602    K C 603                                          
SITE     1 CC2  9 ASP C  52  GLY C  53  ASP C  87  GLY C  88                    
SITE     2 CC2  9 THR C  89  THR C  90  ADP C 600   MG C 601                    
SITE     3 CC2  9   K C 603                                                     
SITE     1 CC3 23 THR D  30  LEU D  31  GLY D  32  PRO D  33                    
SITE     2 CC3 23 LYS D  51  ASP D  87  GLY D  88  THR D  89                    
SITE     3 CC3 23 THR D  90  THR D  91  ILE D 150  GLY D 414                    
SITE     4 CC3 23 GLY D 415  ILE D 454  TYR D 478  ASN D 479                    
SITE     5 CC3 23 ALA D 480  ALA D 481  ILE D 493  ASP D 495                    
SITE     6 CC3 23  MG D 601  AF3 D 602    K D 603                               
SITE     1 CC4  9 ASP D  52  GLY D  53  ASP D  87  GLY D  88                    
SITE     2 CC4  9 THR D  89  THR D  90  ADP D 600   MG D 601                    
SITE     3 CC4  9   K D 603                                                     
SITE     1 CC5 23 THR E  30  LEU E  31  GLY E  32  PRO E  33                    
SITE     2 CC5 23 LYS E  51  ASP E  87  GLY E  88  THR E  89                    
SITE     3 CC5 23 THR E  90  THR E  91  ILE E 150  GLY E 414                    
SITE     4 CC5 23 GLY E 415  ILE E 454  TYR E 478  ASN E 479                    
SITE     5 CC5 23 ALA E 480  ALA E 481  ILE E 493  ASP E 495                    
SITE     6 CC5 23  MG E 601  AF3 E 602    K E 603                               
SITE     1 CC6  9 GLY E  53  ASP E  87  GLY E  88  THR E  89                    
SITE     2 CC6  9 THR E  90  ADP E 600   MG E 601    K E 603                    
SITE     3 CC6  9 HOH E 608                                                     
SITE     1 CC7 23 THR F  30  LEU F  31  GLY F  32  PRO F  33                    
SITE     2 CC7 23 LYS F  51  ASP F  87  GLY F  88  THR F  89                    
SITE     3 CC7 23 THR F  90  THR F  91  ILE F 150  GLY F 414                    
SITE     4 CC7 23 GLY F 415  ILE F 454  TYR F 478  ASN F 479                    
SITE     5 CC7 23 ALA F 480  ALA F 481  ILE F 493  ASP F 495                    
SITE     6 CC7 23  MG F 601  AF3 F 602    K F 603                               
SITE     1 CC8  8 GLY F  53  ASP F  87  GLY F  88  THR F  89                    
SITE     2 CC8  8 THR F  90  ADP F 600   MG F 601    K F 603                    
SITE     1 CC9 22 THR G  30  LEU G  31  GLY G  32  PRO G  33                    
SITE     2 CC9 22 LYS G  51  ASP G  87  GLY G  88  THR G  89                    
SITE     3 CC9 22 THR G  90  THR G  91  ILE G 150  GLY G 414                    
SITE     4 CC9 22 GLY G 415  ILE G 454  TYR G 478  ASN G 479                    
SITE     5 CC9 22 ALA G 480  ALA G 481  ASP G 495   MG G 601                    
SITE     6 CC9 22 AF3 G 602    K G 603                                          
SITE     1 DC1  8 GLY G  53  ASP G  87  GLY G  88  THR G  89                    
SITE     2 DC1  8 THR G  90  ADP G 600   MG G 601    K G 603                    
CRYST1  255.546  266.855  187.049  90.00  90.00  90.00 P 21 21 2    56          
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      0.003913  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.003747  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005346        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system