GenomeNet

Database: PDB
Entry: 3O4W
LinkDB: 3O4W
Original site: 3O4W 
ANISOU 4599  C   PHE B 131     8187  10707   8897    246    -87   -591       C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
HEADER    LIGASE                                  09-APR-09   3H0L              
TITLE     STRUCTURE OF TRNA-DEPENDENT AMIDOTRANSFERASE GATCAB FROM              
TITLE    2 AQUIFEX AEOLICUS                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT A;             
COMPND   3 CHAIN: A, D, G, J, M, P, S, V;                                       
COMPND   4 SYNONYM: GLU-ADT SUBUNIT A;                                          
COMPND   5 EC: 6.3.5.-;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: ASPARTYL/GLUTAMYL-TRNA(ASN/GLN) AMIDOTRANSFERASE           
COMPND   9 SUBUNIT B;                                                           
COMPND  10 CHAIN: B, E, H, K, N, Q, T, W;                                       
COMPND  11 SYNONYM: ASP/GLU-ADT SUBUNIT B;                                      
COMPND  12 EC: 6.3.5.-;                                                         
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT C;             
COMPND  16 CHAIN: C, F, I, L, O, R, U, X;                                       
COMPND  17 SYNONYM: GLU-ADT SUBUNIT C;                                          
COMPND  18 EC: 6.3.5.-;                                                         
COMPND  19 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;                               
SOURCE   3 ORGANISM_TAXID: 63363;                                               
SOURCE   4 STRAIN: VF5;                                                         
SOURCE   5 GENE: AQ_247, GATA, GATCA;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET17B-CA;                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;                               
SOURCE  13 ORGANISM_TAXID: 63363;                                               
SOURCE  14 STRAIN: VF5;                                                         
SOURCE  15 GENE: AQ_461, GATB;                                                  
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET17B-B;                                 
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;                               
SOURCE  23 ORGANISM_TAXID: 63363;                                               
SOURCE  24 STRAIN: VF5;                                                         
SOURCE  25 GENE: GATC, AQ_2149;                                                 
SOURCE  26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  28 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PET17B-CA                                 
KEYWDS    MULTI PROTEIN COMPLEX, LIGASE, PROTEIN BIOSYNTHESIS                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.WU,W.BU,K.SHEPPARD,M.KITABATAKE,D.SOLL,J.L.SMITH                    
REVDAT   2   25-AUG-09 3H0L    1       JRNL                                     
REVDAT   1   21-JUL-09 3H0L    0                                                
JRNL        AUTH   J.WU,W.BU,K.SHEPPARD,M.KITABATAKE,S.T.KWON,D.SOLL,           
JRNL        AUTH 2 J.L.SMITH                                                    
JRNL        TITL   INSIGHTS INTO TRNA-DEPENDENT AMIDOTRANSFERASE                
JRNL        TITL 2 EVOLUTION AND CATALYSIS FROM THE STRUCTURE OF THE            
JRNL        TITL 3 AQUIFEX AEOLICUS ENZYME                                      
JRNL        REF    J.MOL.BIOL.                   V. 391   703 2009              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   19520089                                                     
JRNL        DOI    10.1016/J.JMB.2009.06.014                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 385553                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.242                           
REMARK   3   R VALUE            (WORKING SET) : 0.240                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 20322                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 22441                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 72.25                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3370                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 1185                         
REMARK   3   BIN FREE R VALUE                    : 0.3840                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 62848                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 296                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.93                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.63000                                             
REMARK   3    B22 (A**2) : 9.07000                                              
REMARK   3    B33 (A**2) : -4.44000                                             
REMARK   3    B12 (A**2) : -0.01000                                             
REMARK   3    B13 (A**2) : -0.26000                                             
REMARK   3    B23 (A**2) : 0.04000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.408         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.268         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.258         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.215        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.923                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 64481 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 87106 ; 1.396 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  7808 ; 6.149 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  2936 ;38.072 ;24.496       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES): 11946 ;18.656 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   400 ;17.933 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  9520 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 48240 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A): 30945 ; 0.220 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 43623 ; 0.309 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  2694 ; 0.166 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    15 ; 0.098 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   122 ; 0.215 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    30 ; 0.206 ; 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): 40352 ; 0.672 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 63456 ; 1.110 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 27450 ; 1.454 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 23650 ; 2.305 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 4                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A D G J M P S V                 
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     478      2                      
REMARK   3           1     D      1       D     478      2                      
REMARK   3           1     G      1       G     478      2                      
REMARK   3           1     J      1       J     478      2                      
REMARK   3           1     M      1       M     478      2                      
REMARK   3           1     P      1       P     478      2                      
REMARK   3           1     S      1       S     478      2                      
REMARK   3           1     V      1       V     478      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1904 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    D    (A):   1904 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    G    (A):   1904 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    J    (A):   1904 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    M    (A):   1904 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    P    (A):   1904 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    S    (A):   1904 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    V    (A):   1904 ;  0.04 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1864 ;  0.34 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   1864 ;  0.34 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    G    (A):   1864 ;  0.34 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    J    (A):   1864 ;  0.34 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    M    (A):   1864 ;  0.34 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    P    (A):   1864 ;  0.34 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    S    (A):   1864 ;  0.35 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    V    (A):   1864 ;  0.33 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1904 ;  0.09 ;  0.50           
REMARK   3   TIGHT THERMAL      1    D (A**2):   1904 ;  0.09 ;  0.50           
REMARK   3   TIGHT THERMAL      1    G (A**2):   1904 ;  0.09 ;  0.50           
REMARK   3   TIGHT THERMAL      1    J (A**2):   1904 ;  0.10 ;  0.50           
REMARK   3   TIGHT THERMAL      1    M (A**2):   1904 ;  0.09 ;  0.50           
REMARK   3   TIGHT THERMAL      1    P (A**2):   1904 ;  0.10 ;  0.50           
REMARK   3   TIGHT THERMAL      1    S (A**2):   1904 ;  0.10 ;  0.50           
REMARK   3   TIGHT THERMAL      1    V (A**2):   1904 ;  0.09 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1864 ;  0.64 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   1864 ;  0.66 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    G (A**2):   1864 ;  0.61 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    J (A**2):   1864 ;  0.68 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    M (A**2):   1864 ;  0.62 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    P (A**2):   1864 ;  0.69 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    S (A**2):   1864 ;  0.62 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    V (A**2):   1864 ;  0.67 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B E H K N Q T W                 
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      3       B     293      2                      
REMARK   3           1     E      3       E     293      2                      
REMARK   3           1     H      3       H     293      2                      
REMARK   3           1     K      3       K     293      2                      
REMARK   3           1     N      3       N     293      2                      
REMARK   3           1     Q      3       Q     293      2                      
REMARK   3           1     T      3       T     293      2                      
REMARK   3           1     W      3       W     293      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    B    (A):   1164 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    E    (A):   1164 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    H    (A):   1164 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    K    (A):   1164 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    N    (A):   1164 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    Q    (A):   1164 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    T    (A):   1164 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    W    (A):   1164 ;  0.03 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  2    B    (A):   1187 ;  0.37 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    E    (A):   1187 ;  0.35 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    H    (A):   1187 ;  0.37 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    K    (A):   1187 ;  0.36 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    N    (A):   1187 ;  0.37 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    Q    (A):   1187 ;  0.38 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    T    (A):   1187 ;  0.37 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    W    (A):   1187 ;  0.35 ;  0.50           
REMARK   3   TIGHT THERMAL      2    B (A**2):   1164 ;  0.07 ;  0.50           
REMARK   3   TIGHT THERMAL      2    E (A**2):   1164 ;  0.09 ;  0.50           
REMARK   3   TIGHT THERMAL      2    H (A**2):   1164 ;  0.07 ;  0.50           
REMARK   3   TIGHT THERMAL      2    K (A**2):   1164 ;  0.09 ;  0.50           
REMARK   3   TIGHT THERMAL      2    N (A**2):   1164 ;  0.07 ;  0.50           
REMARK   3   TIGHT THERMAL      2    Q (A**2):   1164 ;  0.09 ;  0.50           
REMARK   3   TIGHT THERMAL      2    T (A**2):   1164 ;  0.09 ;  0.50           
REMARK   3   TIGHT THERMAL      2    W (A**2):   1164 ;  0.07 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    B (A**2):   1187 ;  0.57 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    E (A**2):   1187 ;  0.61 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    H (A**2):   1187 ;  0.55 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    K (A**2):   1187 ;  0.65 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    N (A**2):   1187 ;  0.56 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    Q (A**2):   1187 ;  0.68 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    T (A**2):   1187 ;  0.62 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    W (A**2):   1187 ;  0.59 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : B E H K N Q T W                 
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B    294       B     412      2                      
REMARK   3           1     E    294       E     412      2                      
REMARK   3           1     H    294       H     412      2                      
REMARK   3           1     K    294       K     412      2                      
REMARK   3           1     N    294       N     412      2                      
REMARK   3           1     Q    294       Q     412      2                      
REMARK   3           1     T    294       T     412      2                      
REMARK   3           1     W    294       W     412      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    B    (A):    476 ;  0.02 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    E    (A):    476 ;  0.02 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    H    (A):    476 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    K    (A):    476 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    N    (A):    476 ;  0.02 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    Q    (A):    476 ;  0.02 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    T    (A):    476 ;  0.02 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    W    (A):    476 ;  0.02 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  3    B    (A):    481 ;  0.35 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  3    E    (A):    481 ;  0.36 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  3    H    (A):    481 ;  0.35 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  3    K    (A):    481 ;  0.37 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  3    N    (A):    481 ;  0.32 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  3    Q    (A):    481 ;  0.36 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  3    T    (A):    481 ;  0.33 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  3    W    (A):    481 ;  0.38 ;  0.50           
REMARK   3   TIGHT THERMAL      3    B (A**2):    476 ;  0.04 ;  0.50           
REMARK   3   TIGHT THERMAL      3    E (A**2):    476 ;  0.05 ;  0.50           
REMARK   3   TIGHT THERMAL      3    H (A**2):    476 ;  0.04 ;  0.50           
REMARK   3   TIGHT THERMAL      3    K (A**2):    476 ;  0.04 ;  0.50           
REMARK   3   TIGHT THERMAL      3    N (A**2):    476 ;  0.04 ;  0.50           
REMARK   3   TIGHT THERMAL      3    Q (A**2):    476 ;  0.04 ;  0.50           
REMARK   3   TIGHT THERMAL      3    T (A**2):    476 ;  0.05 ;  0.50           
REMARK   3   TIGHT THERMAL      3    W (A**2):    476 ;  0.04 ;  0.50           
REMARK   3   MEDIUM THERMAL     3    B (A**2):    481 ;  0.35 ;  2.00           
REMARK   3   MEDIUM THERMAL     3    E (A**2):    481 ;  0.37 ;  2.00           
REMARK   3   MEDIUM THERMAL     3    H (A**2):    481 ;  0.32 ;  2.00           
REMARK   3   MEDIUM THERMAL     3    K (A**2):    481 ;  0.35 ;  2.00           
REMARK   3   MEDIUM THERMAL     3    N (A**2):    481 ;  0.28 ;  2.00           
REMARK   3   MEDIUM THERMAL     3    Q (A**2):    481 ;  0.32 ;  2.00           
REMARK   3   MEDIUM THERMAL     3    T (A**2):    481 ;  0.37 ;  2.00           
REMARK   3   MEDIUM THERMAL     3    W (A**2):    481 ;  0.32 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : C F I L O R U X                 
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C      2       C      92      2                      
REMARK   3           1     F      2       F      92      2                      
REMARK   3           1     I      2       I      92      2                      
REMARK   3           1     L      2       L      92      2                      
REMARK   3           1     O      2       O      92      2                      
REMARK   3           1     R      2       R      92      2                      
REMARK   3           1     U      2       U      92      2                      
REMARK   3           1     X      2       X      92      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   4    C    (A):    364 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   4    F    (A):    364 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   4    I    (A):    364 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   4    L    (A):    364 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   4    O    (A):    364 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   4    R    (A):    364 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   4    U    (A):    364 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   4    X    (A):    364 ;  0.03 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  4    C    (A):    400 ;  0.41 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  4    F    (A):    400 ;  0.37 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  4    I    (A):    400 ;  0.36 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  4    L    (A):    400 ;  0.36 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  4    O    (A):    400 ;  0.35 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  4    R    (A):    400 ;  0.56 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  4    U    (A):    400 ;  0.39 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  4    X    (A):    400 ;  0.34 ;  0.50           
REMARK   3   TIGHT THERMAL      4    C (A**2):    364 ;  0.07 ;  0.50           
REMARK   3   TIGHT THERMAL      4    F (A**2):    364 ;  0.07 ;  0.50           
REMARK   3   TIGHT THERMAL      4    I (A**2):    364 ;  0.06 ;  0.50           
REMARK   3   TIGHT THERMAL      4    L (A**2):    364 ;  0.07 ;  0.50           
REMARK   3   TIGHT THERMAL      4    O (A**2):    364 ;  0.07 ;  0.50           
REMARK   3   TIGHT THERMAL      4    R (A**2):    364 ;  0.08 ;  0.50           
REMARK   3   TIGHT THERMAL      4    U (A**2):    364 ;  0.07 ;  0.50           
REMARK   3   TIGHT THERMAL      4    X (A**2):    364 ;  0.07 ;  0.50           
REMARK   3   MEDIUM THERMAL     4    C (A**2):    400 ;  0.51 ;  2.00           
REMARK   3   MEDIUM THERMAL     4    F (A**2):    400 ;  0.49 ;  2.00           
REMARK   3   MEDIUM THERMAL     4    I (A**2):    400 ;  0.46 ;  2.00           
REMARK   3   MEDIUM THERMAL     4    L (A**2):    400 ;  0.57 ;  2.00           
REMARK   3   MEDIUM THERMAL     4    O (A**2):    400 ;  0.48 ;  2.00           
REMARK   3   MEDIUM THERMAL     4    R (A**2):    400 ;  0.61 ;  2.00           
REMARK   3   MEDIUM THERMAL     4    U (A**2):    400 ;  0.50 ;  2.00           
REMARK   3   MEDIUM THERMAL     4    X (A**2):    400 ;  0.54 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3H0L COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAY-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB052540.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-MAR-06; 20-MAR-07               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 3                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : APS; APS                           
REMARK 200  BEAMLINE                       : 23-ID-D; 23-ID-D                   
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL                            
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0274,0.9804; 0.97934             
REMARK 200  MONOCHROMATOR                  : MIRRORS; MIRRORS                   
REMARK 200  OPTICS                         : MONOCHROMATOR: MIRRORS;            
REMARK 200                                   MONOCHROMATOR: MIRRORS             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD;              
REMARK 200                                   MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 405875                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.5                               
REMARK 200  DATA REDUNDANCY                : 1.900                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : 0.06000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 73.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.34700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD; SINGLE WAVELENGTH                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 2GI3 AND 2G5H                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1:1 RATIO OF PROTEIN SOLUTION (6-        
REMARK 280  9MG/ML GATCAB,10MM HEPES, 50UM ZN ACETATE,10MM ASN, 0.6MM ATP)      
REMARK 280  MIX WITH WELL SOLUTION (10-12% PEG3350, 10MM MG FORMATE), PH        
REMARK 280  7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8                                  
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11780 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 39390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B                               
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11830 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 39190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, F, E                               
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11870 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 39060 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, I, H                               
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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11740 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 39240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, L, K                               
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 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11800 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 39230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, O, N                               
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 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11820 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 39110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -76.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, R, Q                               
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 350                                                                      
REMARK 350 BIOMOLECULE: 7                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11830 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 39240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, U, T                               
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 350                                                                      
REMARK 350 BIOMOLECULE: 8                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11780 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 39300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: V, X, W                               
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET B     1                                                      
REMARK 465     ASN B     2                                                      
REMARK 465     LYS B   413                                                      
REMARK 465     GLN B   414                                                      
REMARK 465     ILE B   415                                                      
REMARK 465     THR B   416                                                      
REMARK 465     ASP B   417                                                      
REMARK 465     GLU B   418                                                      
REMARK 465     ASN B   419                                                      
REMARK 465     GLN B   420                                                      
REMARK 465     ILE B   421                                                      
REMARK 465     LYS B   422                                                      
REMARK 465     GLU B   423                                                      
REMARK 465     LEU B   424                                                      
REMARK 465     VAL B   425                                                      
REMARK 465     LYS B   426                                                      
REMARK 465     LYS B   427                                                      
REMARK 465     ILE B   428                                                      
REMARK 465     PHE B   429                                                      
REMARK 465     GLU B   430                                                      
REMARK 465     LYS B   431                                                      
REMARK 465     HIS B   432                                                      
REMARK 465     PRO B   433                                                      
REMARK 465     LYS B   434                                                      
REMARK 465     GLU B   435                                                      
REMARK 465     VAL B   436                                                      
REMARK 465     GLU B   437                                                      
REMARK 465     ARG B   438                                                      
REMARK 465     LEU B   439                                                      
REMARK 465     LYS B   440                                                      
REMARK 465     GLN B   441                                                      
REMARK 465     GLY B   442                                                      
REMARK 465     GLU B   443                                                      
REMARK 465     GLU B   444                                                      
REMARK 465     LYS B   445                                                      
REMARK 465     LEU B   446                                                      
REMARK 465     ILE B   447                                                      
REMARK 465     GLY B   448                                                      
REMARK 465     PHE B   449                                                      
REMARK 465     PHE B   450                                                      
REMARK 465     VAL B   451                                                      
REMARK 465     GLY B   452                                                      
REMARK 465     GLN B   453                                                      
REMARK 465     VAL B   454                                                      
REMARK 465     MET B   455                                                      
REMARK 465     ARG B   456                                                      
REMARK 465     GLU B   457                                                      
REMARK 465     THR B   458                                                      
REMARK 465     ARG B   459                                                      
REMARK 465     GLY B   460                                                      
REMARK 465     LYS B   461                                                      
REMARK 465     ALA B   462                                                      
REMARK 465     ASN B   463                                                      
REMARK 465     PRO B   464                                                      
REMARK 465     GLN B   465                                                      
REMARK 465     VAL B   466                                                      
REMARK 465     VAL B   467                                                      
REMARK 465     ASN B   468                                                      
REMARK 465     LYS B   469                                                      
REMARK 465     VAL B   470                                                      
REMARK 465     ILE B   471                                                      
REMARK 465     ARG B   472                                                      
REMARK 465     GLU B   473                                                      
REMARK 465     LEU B   474                                                      
REMARK 465     VAL B   475                                                      
REMARK 465     LYS B   476                                                      
REMARK 465     GLU B   477                                                      
REMARK 465     VAL B   478                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLU C    93                                                      
REMARK 465     VAL C    94                                                      
REMARK 465     MET E     1                                                      
REMARK 465     ASN E     2                                                      
REMARK 465     LYS E   413                                                      
REMARK 465     GLN E   414                                                      
REMARK 465     ILE E   415                                                      
REMARK 465     THR E   416                                                      
REMARK 465     ASP E   417                                                      
REMARK 465     GLU E   418                                                      
REMARK 465     ASN E   419                                                      
REMARK 465     GLN E   420                                                      
REMARK 465     ILE E   421                                                      
REMARK 465     LYS E   422                                                      
REMARK 465     GLU E   423                                                      
REMARK 465     LEU E   424                                                      
REMARK 465     VAL E   425                                                      
REMARK 465     LYS E   426                                                      
REMARK 465     LYS E   427                                                      
REMARK 465     ILE E   428                                                      
REMARK 465     PHE E   429                                                      
REMARK 465     GLU E   430                                                      
REMARK 465     LYS E   431                                                      
REMARK 465     HIS E   432                                                      
REMARK 465     PRO E   433                                                      
REMARK 465     LYS E   434                                                      
REMARK 465     GLU E   435                                                      
REMARK 465     VAL E   436                                                      
REMARK 465     GLU E   437                                                      
REMARK 465     ARG E   438                                                      
REMARK 465     LEU E   439                                                      
REMARK 465     LYS E   440                                                      
REMARK 465     GLN E   441                                                      
REMARK 465     GLY E   442                                                      
REMARK 465     GLU E   443                                                      
REMARK 465     GLU E   444                                                      
REMARK 465     LYS E   445                                                      
REMARK 465     LEU E   446                                                      
REMARK 465     ILE E   447                                                      
REMARK 465     GLY E   448                                                      
REMARK 465     PHE E   449                                                      
REMARK 465     PHE E   450                                                      
REMARK 465     VAL E   451                                                      
REMARK 465     GLY E   452                                                      
REMARK 465     GLN E   453                                                      
REMARK 465     VAL E   454                                                      
REMARK 465     MET E   455                                                      
REMARK 465     ARG E   456                                                      
REMARK 465     GLU E   457                                                      
REMARK 465     THR E   458                                                      
REMARK 465     ARG E   459                                                      
REMARK 465     GLY E   460                                                      
REMARK 465     LYS E   461                                                      
REMARK 465     ALA E   462                                                      
REMARK 465     ASN E   463                                                      
REMARK 465     PRO E   464                                                      
REMARK 465     GLN E   465                                                      
REMARK 465     VAL E   466                                                      
REMARK 465     VAL E   467                                                      
REMARK 465     ASN E   468                                                      
REMARK 465     LYS E   469                                                      
REMARK 465     VAL E   470                                                      
REMARK 465     ILE E   471                                                      
REMARK 465     ARG E   472                                                      
REMARK 465     GLU E   473                                                      
REMARK 465     LEU E   474                                                      
REMARK 465     VAL E   475                                                      
REMARK 465     LYS E   476                                                      
REMARK 465     GLU E   477                                                      
REMARK 465     VAL E   478                                                      
REMARK 465     MET F     1                                                      
REMARK 465     GLU F    93                                                      
REMARK 465     VAL F    94                                                      
REMARK 465     MET H     1                                                      
REMARK 465     ASN H     2                                                      
REMARK 465     LYS H   413                                                      
REMARK 465     GLN H   414                                                      
REMARK 465     ILE H   415                                                      
REMARK 465     THR H   416                                                      
REMARK 465     ASP H   417                                                      
REMARK 465     GLU H   418                                                      
REMARK 465     ASN H   419                                                      
REMARK 465     GLN H   420                                                      
REMARK 465     ILE H   421                                                      
REMARK 465     LYS H   422                                                      
REMARK 465     GLU H   423                                                      
REMARK 465     LEU H   424                                                      
REMARK 465     VAL H   425                                                      
REMARK 465     LYS H   426                                                      
REMARK 465     LYS H   427                                                      
REMARK 465     ILE H   428                                                      
REMARK 465     PHE H   429                                                      
REMARK 465     GLU H   430                                                      
REMARK 465     LYS H   431                                                      
REMARK 465     HIS H   432                                                      
REMARK 465     PRO H   433                                                      
REMARK 465     LYS H   434                                                      
REMARK 465     GLU H   435                                                      
REMARK 465     VAL H   436                                                      
REMARK 465     GLU H   437                                                      
REMARK 465     ARG H   438                                                      
REMARK 465     LEU H   439                                                      
REMARK 465     LYS H   440                                                      
REMARK 465     GLN H   441                                                      
REMARK 465     GLY H   442                                                      
REMARK 465     GLU H   443                                                      
REMARK 465     GLU H   444                                                      
REMARK 465     LYS H   445                                                      
REMARK 465     LEU H   446                                                      
REMARK 465     ILE H   447                                                      
REMARK 465     GLY H   448                                                      
REMARK 465     PHE H   449                                                      
REMARK 465     PHE H   450                                                      
REMARK 465     VAL H   451                                                      
REMARK 465     GLY H   452                                                      
REMARK 465     GLN H   453                                                      
REMARK 465     VAL H   454                                                      
REMARK 465     MET H   455                                                      
REMARK 465     ARG H   456                                                      
REMARK 465     GLU H   457                                                      
REMARK 465     THR H   458                                                      
REMARK 465     ARG H   459                                                      
REMARK 465     GLY H   460                                                      
REMARK 465     LYS H   461                                                      
REMARK 465     ALA H   462                                                      
REMARK 465     ASN H   463                                                      
REMARK 465     PRO H   464                                                      
REMARK 465     GLN H   465                                                      
REMARK 465     VAL H   466                                                      
REMARK 465     VAL H   467                                                      
REMARK 465     ASN H   468                                                      
REMARK 465     LYS H   469                                                      
REMARK 465     VAL H   470                                                      
REMARK 465     ILE H   471                                                      
REMARK 465     ARG H   472                                                      
REMARK 465     GLU H   473                                                      
REMARK 465     LEU H   474                                                      
REMARK 465     VAL H   475                                                      
REMARK 465     LYS H   476                                                      
REMARK 465     GLU H   477                                                      
REMARK 465     VAL H   478                                                      
REMARK 465     MET I     1                                                      
REMARK 465     GLU I    93                                                      
REMARK 465     VAL I    94                                                      
REMARK 465     MET K     1                                                      
REMARK 465     ASN K     2                                                      
REMARK 465     LYS K   413                                                      
REMARK 465     GLN K   414                                                      
REMARK 465     ILE K   415                                                      
REMARK 465     THR K   416                                                      
REMARK 465     ASP K   417                                                      
REMARK 465     GLU K   418                                                      
REMARK 465     ASN K   419                                                      
REMARK 465     GLN K   420                                                      
REMARK 465     ILE K   421                                                      
REMARK 465     LYS K   422                                                      
REMARK 465     GLU K   423                                                      
REMARK 465     LEU K   424                                                      
REMARK 465     VAL K   425                                                      
REMARK 465     LYS K   426                                                      
REMARK 465     LYS K   427                                                      
REMARK 465     ILE K   428                                                      
REMARK 465     PHE K   429                                                      
REMARK 465     GLU K   430                                                      
REMARK 465     LYS K   431                                                      
REMARK 465     HIS K   432                                                      
REMARK 465     PRO K   433                                                      
REMARK 465     LYS K   434                                                      
REMARK 465     GLU K   435                                                      
REMARK 465     VAL K   436                                                      
REMARK 465     GLU K   437                                                      
REMARK 465     ARG K   438                                                      
REMARK 465     LEU K   439                                                      
REMARK 465     LYS K   440                                                      
REMARK 465     GLN K   441                                                      
REMARK 465     GLY K   442                                                      
REMARK 465     GLU K   443                                                      
REMARK 465     GLU K   444                                                      
REMARK 465     LYS K   445                                                      
REMARK 465     LEU K   446                                                      
REMARK 465     ILE K   447                                                      
REMARK 465     GLY K   448                                                      
REMARK 465     PHE K   449                                                      
REMARK 465     PHE K   450                                                      
REMARK 465     VAL K   451                                                      
REMARK 465     GLY K   452                                                      
REMARK 465     GLN K   453                                                      
REMARK 465     VAL K   454                                                      
REMARK 465     MET K   455                                                      
REMARK 465     ARG K   456                                                      
REMARK 465     GLU K   457                                                      
REMARK 465     THR K   458                                                      
REMARK 465     ARG K   459                                                      
REMARK 465     GLY K   460                                                      
REMARK 465     LYS K   461                                                      
REMARK 465     ALA K   462                                                      
REMARK 465     ASN K   463                                                      
REMARK 465     PRO K   464                                                      
REMARK 465     GLN K   465                                                      
REMARK 465     VAL K   466                                                      
REMARK 465     VAL K   467                                                      
REMARK 465     ASN K   468                                                      
REMARK 465     LYS K   469                                                      
REMARK 465     VAL K   470                                                      
REMARK 465     ILE K   471                                                      
REMARK 465     ARG K   472                                                      
REMARK 465     GLU K   473                                                      
REMARK 465     LEU K   474                                                      
REMARK 465     VAL K   475                                                      
REMARK 465     LYS K   476                                                      
REMARK 465     GLU K   477                                                      
REMARK 465     VAL K   478                                                      
REMARK 465     MET L     1                                                      
REMARK 465     GLU L    93                                                      
REMARK 465     VAL L    94                                                      
REMARK 465     MET N     1                                                      
REMARK 465     ASN N     2                                                      
REMARK 465     LYS N   413                                                      
REMARK 465     GLN N   414                                                      
REMARK 465     ILE N   415                                                      
REMARK 465     THR N   416                                                      
REMARK 465     ASP N   417                                                      
REMARK 465     GLU N   418                                                      
REMARK 465     ASN N   419                                                      
REMARK 465     GLN N   420                                                      
REMARK 465     ILE N   421                                                      
REMARK 465     LYS N   422                                                      
REMARK 465     GLU N   423                                                      
REMARK 465     LEU N   424                                                      
REMARK 465     VAL N   425                                                      
REMARK 465     LYS N   426                                                      
REMARK 465     LYS N   427                                                      
REMARK 465     ILE N   428                                                      
REMARK 465     PHE N   429                                                      
REMARK 465     GLU N   430                                                      
REMARK 465     LYS N   431                                                      
REMARK 465     HIS N   432                                                      
REMARK 465     PRO N   433                                                      
REMARK 465     LYS N   434                                                      
REMARK 465     GLU N   435                                                      
REMARK 465     VAL N   436                                                      
REMARK 465     GLU N   437                                                      
REMARK 465     ARG N   438                                                      
REMARK 465     LEU N   439                                                      
REMARK 465     LYS N   440                                                      
REMARK 465     GLN N   441                                                      
REMARK 465     GLY N   442                                                      
REMARK 465     GLU N   443                                                      
REMARK 465     GLU N   444                                                      
REMARK 465     LYS N   445                                                      
REMARK 465     LEU N   446                                                      
REMARK 465     ILE N   447                                                      
REMARK 465     GLY N   448                                                      
REMARK 465     PHE N   449                                                      
REMARK 465     PHE N   450                                                      
REMARK 465     VAL N   451                                                      
REMARK 465     GLY N   452                                                      
REMARK 465     GLN N   453                                                      
REMARK 465     VAL N   454                                                      
REMARK 465     MET N   455                                                      
REMARK 465     ARG N   456                                                      
REMARK 465     GLU N   457                                                      
REMARK 465     THR N   458                                                      
REMARK 465     ARG N   459                                                      
REMARK 465     GLY N   460                                                      
REMARK 465     LYS N   461                                                      
REMARK 465     ALA N   462                                                      
REMARK 465     ASN N   463                                                      
REMARK 465     PRO N   464                                                      
REMARK 465     GLN N   465                                                      
REMARK 465     VAL N   466                                                      
REMARK 465     VAL N   467                                                      
REMARK 465     ASN N   468                                                      
REMARK 465     LYS N   469                                                      
REMARK 465     VAL N   470                                                      
REMARK 465     ILE N   471                                                      
REMARK 465     ARG N   472                                                      
REMARK 465     GLU N   473                                                      
REMARK 465     LEU N   474                                                      
REMARK 465     VAL N   475                                                      
REMARK 465     LYS N   476                                                      
REMARK 465     GLU N   477                                                      
REMARK 465     VAL N   478                                                      
REMARK 465     MET O     1                                                      
REMARK 465     GLU O    93                                                      
REMARK 465     VAL O    94                                                      
REMARK 465     MET Q     1                                                      
REMARK 465     ASN Q     2                                                      
REMARK 465     LYS Q   413                                                      
REMARK 465     GLN Q   414                                                      
REMARK 465     ILE Q   415                                                      
REMARK 465     THR Q   416                                                      
REMARK 465     ASP Q   417                                                      
REMARK 465     GLU Q   418                                                      
REMARK 465     ASN Q   419                                                      
REMARK 465     GLN Q   420                                                      
REMARK 465     ILE Q   421                                                      
REMARK 465     LYS Q   422                                                      
REMARK 465     GLU Q   423                                                      
REMARK 465     LEU Q   424                                                      
REMARK 465     VAL Q   425                                                      
REMARK 465     LYS Q   426                                                      
REMARK 465     LYS Q   427                                                      
REMARK 465     ILE Q   428                                                      
REMARK 465     PHE Q   429                                                      
REMARK 465     GLU Q   430                                                      
REMARK 465     LYS Q   431                                                      
REMARK 465     HIS Q   432                                                      
REMARK 465     PRO Q   433                                                      
REMARK 465     LYS Q   434                                                      
REMARK 465     GLU Q   435                                                      
REMARK 465     VAL Q   436                                                      
REMARK 465     GLU Q   437                                                      
REMARK 465     ARG Q   438                                                      
REMARK 465     LEU Q   439                                                      
REMARK 465     LYS Q   440                                                      
REMARK 465     GLN Q   441                                                      
REMARK 465     GLY Q   442                                                      
REMARK 465     GLU Q   443                                                      
REMARK 465     GLU Q   444                                                      
REMARK 465     LYS Q   445                                                      
REMARK 465     LEU Q   446                                                      
REMARK 465     ILE Q   447                                                      
REMARK 465     GLY Q   448                                                      
REMARK 465     PHE Q   449                                                      
REMARK 465     PHE Q   450                                                      
REMARK 465     VAL Q   451                                                      
REMARK 465     GLY Q   452                                                      
REMARK 465     GLN Q   453                                                      
REMARK 465     VAL Q   454                                                      
REMARK 465     MET Q   455                                                      
REMARK 465     ARG Q   456                                                      
REMARK 465     GLU Q   457                                                      
REMARK 465     THR Q   458                                                      
REMARK 465     ARG Q   459                                                      
REMARK 465     GLY Q   460                                                      
REMARK 465     LYS Q   461                                                      
REMARK 465     ALA Q   462                                                      
REMARK 465     ASN Q   463                                                      
REMARK 465     PRO Q   464                                                      
REMARK 465     GLN Q   465                                                      
REMARK 465     VAL Q   466                                                      
REMARK 465     VAL Q   467                                                      
REMARK 465     ASN Q   468                                                      
REMARK 465     LYS Q   469                                                      
REMARK 465     VAL Q   470                                                      
REMARK 465     ILE Q   471                                                      
REMARK 465     ARG Q   472                                                      
REMARK 465     GLU Q   473                                                      
REMARK 465     LEU Q   474                                                      
REMARK 465     VAL Q   475                                                      
REMARK 465     LYS Q   476                                                      
REMARK 465     GLU Q   477                                                      
REMARK 465     VAL Q   478                                                      
REMARK 465     MET R     1                                                      
REMARK 465     GLU R    93                                                      
REMARK 465     VAL R    94                                                      
REMARK 465     MET T     1                                                      
REMARK 465     ASN T     2                                                      
REMARK 465     LYS T   413                                                      
REMARK 465     GLN T   414                                                      
REMARK 465     ILE T   415                                                      
REMARK 465     THR T   416                                                      
REMARK 465     ASP T   417                                                      
REMARK 465     GLU T   418                                                      
REMARK 465     ASN T   419                                                      
REMARK 465     GLN T   420                                                      
REMARK 465     ILE T   421                                                      
REMARK 465     LYS T   422                                                      
REMARK 465     GLU T   423                                                      
REMARK 465     LEU T   424                                                      
REMARK 465     VAL T   425                                                      
REMARK 465     LYS T   426                                                      
REMARK 465     LYS T   427                                                      
REMARK 465     ILE T   428                                                      
REMARK 465     PHE T   429                                                      
REMARK 465     GLU T   430                                                      
REMARK 465     LYS T   431                                                      
REMARK 465     HIS T   432                                                      
REMARK 465     PRO T   433                                                      
REMARK 465     LYS T   434                                                      
REMARK 465     GLU T   435                                                      
REMARK 465     VAL T   436                                                      
REMARK 465     GLU T   437                                                      
REMARK 465     ARG T   438                                                      
REMARK 465     LEU T   439                                                      
REMARK 465     LYS T   440                                                      
REMARK 465     GLN T   441                                                      
REMARK 465     GLY T   442                                                      
REMARK 465     GLU T   443                                                      
REMARK 465     GLU T   444                                                      
REMARK 465     LYS T   445                                                      
REMARK 465     LEU T   446                                                      
REMARK 465     ILE T   447                                                      
REMARK 465     GLY T   448                                                      
REMARK 465     PHE T   449                                                      
REMARK 465     PHE T   450                                                      
REMARK 465     VAL T   451                                                      
REMARK 465     GLY T   452                                                      
REMARK 465     GLN T   453                                                      
REMARK 465     VAL T   454                                                      
REMARK 465     MET T   455                                                      
REMARK 465     ARG T   456                                                      
REMARK 465     GLU T   457                                                      
REMARK 465     THR T   458                                                      
REMARK 465     ARG T   459                                                      
REMARK 465     GLY T   460                                                      
REMARK 465     LYS T   461                                                      
REMARK 465     ALA T   462                                                      
REMARK 465     ASN T   463                                                      
REMARK 465     PRO T   464                                                      
REMARK 465     GLN T   465                                                      
REMARK 465     VAL T   466                                                      
REMARK 465     VAL T   467                                                      
REMARK 465     ASN T   468                                                      
REMARK 465     LYS T   469                                                      
REMARK 465     VAL T   470                                                      
REMARK 465     ILE T   471                                                      
REMARK 465     ARG T   472                                                      
REMARK 465     GLU T   473                                                      
REMARK 465     LEU T   474                                                      
REMARK 465     VAL T   475                                                      
REMARK 465     LYS T   476                                                      
REMARK 465     GLU T   477                                                      
REMARK 465     VAL T   478                                                      
REMARK 465     MET U     1                                                      
REMARK 465     GLU U    93                                                      
REMARK 465     VAL U    94                                                      
REMARK 465     MET W     1                                                      
REMARK 465     ASN W     2                                                      
REMARK 465     LYS W   413                                                      
REMARK 465     GLN W   414                                                      
REMARK 465     ILE W   415                                                      
REMARK 465     THR W   416                                                      
REMARK 465     ASP W   417                                                      
REMARK 465     GLU W   418                                                      
REMARK 465     ASN W   419                                                      
REMARK 465     GLN W   420                                                      
REMARK 465     ILE W   421                                                      
REMARK 465     LYS W   422                                                      
REMARK 465     GLU W   423                                                      
REMARK 465     LEU W   424                                                      
REMARK 465     VAL W   425                                                      
REMARK 465     LYS W   426                                                      
REMARK 465     LYS W   427                                                      
REMARK 465     ILE W   428                                                      
REMARK 465     PHE W   429                                                      
REMARK 465     GLU W   430                                                      
REMARK 465     LYS W   431                                                      
REMARK 465     HIS W   432                                                      
REMARK 465     PRO W   433                                                      
REMARK 465     LYS W   434                                                      
REMARK 465     GLU W   435                                                      
REMARK 465     VAL W   436                                                      
REMARK 465     GLU W   437                                                      
REMARK 465     ARG W   438                                                      
REMARK 465     LEU W   439                                                      
REMARK 465     LYS W   440                                                      
REMARK 465     GLN W   441                                                      
REMARK 465     GLY W   442                                                      
REMARK 465     GLU W   443                                                      
REMARK 465     GLU W   444                                                      
REMARK 465     LYS W   445                                                      
REMARK 465     LEU W   446                                                      
REMARK 465     ILE W   447                                                      
REMARK 465     GLY W   448                                                      
REMARK 465     PHE W   449                                                      
REMARK 465     PHE W   450                                                      
REMARK 465     VAL W   451                                                      
REMARK 465     GLY W   452                                                      
REMARK 465     GLN W   453                                                      
REMARK 465     VAL W   454                                                      
REMARK 465     MET W   455                                                      
REMARK 465     ARG W   456                                                      
REMARK 465     GLU W   457                                                      
REMARK 465     THR W   458                                                      
REMARK 465     ARG W   459                                                      
REMARK 465     GLY W   460                                                      
REMARK 465     LYS W   461                                                      
REMARK 465     ALA W   462                                                      
REMARK 465     ASN W   463                                                      
REMARK 465     PRO W   464                                                      
REMARK 465     GLN W   465                                                      
REMARK 465     VAL W   466                                                      
REMARK 465     VAL W   467                                                      
REMARK 465     ASN W   468                                                      
REMARK 465     LYS W   469                                                      
REMARK 465     VAL W   470                                                      
REMARK 465     ILE W   471                                                      
REMARK 465     ARG W   472                                                      
REMARK 465     GLU W   473                                                      
REMARK 465     LEU W   474                                                      
REMARK 465     VAL W   475                                                      
REMARK 465     LYS W   476                                                      
REMARK 465     GLU W   477                                                      
REMARK 465     VAL W   478                                                      
REMARK 465     MET X     1                                                      
REMARK 465     GLU X    93                                                      
REMARK 465     VAL X    94                                                      
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    LEU A   2      -62.12     86.66                                   
REMARK 500    PHE A  65      -70.73    -26.32                                   
REMARK 500    CYS A  84       26.90     47.18                                   
REMARK 500    ASN A  91        0.36     80.97                                   
REMARK 500    SER A 125      -12.34   -153.85                                   
REMARK 500    THR A 126       -8.10     78.11                                   
REMARK 500    PHE A 132      149.06   -175.31                                   
REMARK 500    ASP A 139      103.55   -169.52                                   
REMARK 500    SER A 148       46.85    -72.01                                   
REMARK 500    PHE A 199      -77.34   -106.33                                   
REMARK 500    ASP A 318       -1.64   -146.80                                   
REMARK 500    TYR A 367      -91.52   -102.51                                   
REMARK 500    GLU A 409      -71.89    -59.34                                   
REMARK 500    ASP A 454       52.63   -102.17                                   
REMARK 500    SER B  95     -152.23   -141.57                                   
REMARK 500    TYR B  97     -114.50   -126.78                                   
REMARK 500    LYS B  99       62.36     70.70                                   
REMARK 500    ASN B 113       -4.99    -56.95                                   
REMARK 500    LYS B 264       43.56    -85.87                                   
REMARK 500    ASP B 350      -66.73   -121.48                                   
REMARK 500    THR B 399      -67.54   -108.79                                   
REMARK 500    LEU D   2      -62.87     88.99                                   
REMARK 500    PHE D  65      -70.79    -29.61                                   
REMARK 500    ASP D  73       24.44    -77.51                                   
REMARK 500    CYS D  84       28.30     46.29                                   
REMARK 500    SER D 125      -13.93   -154.58                                   
REMARK 500    THR D 126       -6.34     75.80                                   
REMARK 500    ASP D 139      104.39   -170.12                                   
REMARK 500    SER D 148       45.76    -71.75                                   
REMARK 500    PHE D 199      -72.56   -107.53                                   
REMARK 500    TYR D 367      -93.74   -101.84                                   
REMARK 500    GLU D 409      -73.30    -56.94                                   
REMARK 500    ASP D 454       50.16   -101.37                                   
REMARK 500    SER E  95     -152.88   -143.63                                   
REMARK 500    TYR E  97     -108.56   -131.18                                   
REMARK 500    ASN E 113       -5.50    -58.31                                   
REMARK 500    LYS E 264       43.97    -83.73                                   
REMARK 500    ASP E 269      126.23    -39.17                                   
REMARK 500    ASP E 350      -65.54   -121.01                                   
REMARK 500    THR E 399      -63.49   -107.83                                   
REMARK 500    ASP F   3      156.45    -47.40                                   
REMARK 500    MET F  76      -38.87    -39.70                                   
REMARK 500    LEU G   2      -61.89     87.30                                   
REMARK 500    PHE G  65      -70.59    -25.32                                   
REMARK 500    ASP G  73       23.95    -79.76                                   
REMARK 500    CYS G  84       27.69     49.04                                   
REMARK 500    ASN G  91       -4.39     83.35                                   
REMARK 500    SER G 125      -10.75   -152.89                                   
REMARK 500    THR G 126       -9.38     77.06                                   
REMARK 500    ASP G 139      101.12   -168.78                                   
REMARK 500    SER G 148       47.53    -74.64                                   
REMARK 500    PHE G 199      -71.69   -104.56                                   
REMARK 500    TYR G 367      -90.61   -106.95                                   
REMARK 500    PRO G 401      122.26    -38.79                                   
REMARK 500    GLU G 409      -72.68    -59.02                                   
REMARK 500    ASP G 454       50.51   -101.99                                   
REMARK 500    SER H  95     -151.19   -136.87                                   
REMARK 500    TYR H  97     -107.75   -132.41                                   
REMARK 500    ASN H 113       -9.05    -52.50                                   
REMARK 500    LYS H 264       40.19    -80.22                                   
REMARK 500    LYS H 308      -71.46    -79.23                                   
REMARK 500    ASP H 350      -69.34   -121.94                                   
REMARK 500    THR H 399      -64.67   -109.20                                   
REMARK 500    LEU J   2      -61.99     87.81                                   
REMARK 500    LYS J  58      -41.18   -130.07                                   
REMARK 500    PHE J  65      -69.20    -26.09                                   
REMARK 500    CYS J  84       26.08     48.32                                   
REMARK 500    ASN J  91       -4.65     83.96                                   
REMARK 500    SER J 125       -8.34   -148.62                                   
REMARK 500    THR J 126       -8.50     74.30                                   
REMARK 500    ASP J 139      106.35   -168.97                                   
REMARK 500    SER J 148       45.28    -74.41                                   
REMARK 500    PHE J 199      -75.32   -104.05                                   
REMARK 500    ASP J 318        4.46   -151.11                                   
REMARK 500    VAL J 320      -60.01    -92.99                                   
REMARK 500    TYR J 367      -90.75   -104.77                                   
REMARK 500    GLU J 409      -71.66    -58.35                                   
REMARK 500    ASP J 454       51.85   -100.80                                   
REMARK 500    SER K  95     -149.02   -141.21                                   
REMARK 500    TYR K  97     -108.37   -133.68                                   
REMARK 500    ASN K 113       -9.28    -50.72                                   
REMARK 500    LYS K 264       42.73    -82.77                                   
REMARK 500    LYS K 308      -71.87    -80.26                                   
REMARK 500    LYS K 338       49.14    -75.25                                   
REMARK 500    ASP K 350      -65.67   -120.51                                   
REMARK 500    THR K 399      -64.27   -109.10                                   
REMARK 500    ARG L  90      139.64    -39.37                                   
REMARK 500    LEU M   2      -60.42     87.91                                   
REMARK 500    PHE M  65      -71.02    -26.18                                   
REMARK 500    ASP M  73       23.72    -79.88                                   
REMARK 500    CYS M  84       27.85     48.25                                   
REMARK 500    ASN M  91       -7.27     82.62                                   
REMARK 500    SER M 125      -11.15   -149.65                                   
REMARK 500    THR M 126       -7.58     76.63                                   
REMARK 500    ASP M 139      101.54   -168.21                                   
REMARK 500    SER M 148       47.04    -73.69                                   
REMARK 500    PHE M 199      -80.13   -100.89                                   
REMARK 500    TYR M 367      -89.53   -106.86                                   
REMARK 500    PRO M 401      122.68    -39.98                                   
REMARK 500    GLU M 409      -70.81    -62.25                                   
REMARK 500    ASP M 454       50.48   -102.40                                   
REMARK 500    SER N  95     -151.37   -136.95                                   
REMARK 500    TYR N  97     -108.59   -130.34                                   
REMARK 500    LYS N 264       41.29    -83.17                                   
REMARK 500    LYS N 308      -71.56    -78.56                                   
REMARK 500    ASP N 350      -70.54   -122.23                                   
REMARK 500    THR N 399      -65.32   -108.32                                   
REMARK 500    LEU P   2      -61.54     87.02                                   
REMARK 500    PHE P  65      -69.44    -27.37                                   
REMARK 500    ASP P  73       20.68    -78.11                                   
REMARK 500    CYS P  84       26.86     48.33                                   
REMARK 500    ASN P  91       -5.29     82.23                                   
REMARK 500    SER P 125       -9.40   -151.85                                   
REMARK 500    THR P 126       -6.19     72.24                                   
REMARK 500    ASP P 139       99.96   -173.15                                   
REMARK 500    SER P 148       45.30    -71.66                                   
REMARK 500    PHE P 199      -74.59   -103.99                                   
REMARK 500    ASP P 318       10.56   -148.70                                   
REMARK 500    TYR P 367      -90.80   -103.54                                   
REMARK 500    GLU P 409      -70.03    -61.08                                   
REMARK 500    ASP P 454       49.91   -101.53                                   
REMARK 500    SER Q  95     -147.86   -140.05                                   
REMARK 500    TYR Q  97     -107.44   -132.44                                   
REMARK 500    ASN Q 113        2.77    -63.37                                   
REMARK 500    LYS Q 264       42.10    -83.21                                   
REMARK 500    LYS Q 308      -72.56    -79.26                                   
REMARK 500    ASP Q 350      -66.92   -124.43                                   
REMARK 500    THR Q 399      -64.76   -107.98                                   
REMARK 500    LEU S   2      -63.54     88.46                                   
REMARK 500    PHE S  65      -70.43    -31.37                                   
REMARK 500    CYS S  84       28.06     47.14                                   
REMARK 500    SER S 125      -16.19   -156.27                                   
REMARK 500    THR S 126       -8.48     75.86                                   
REMARK 500    ASP S 139      102.11   -169.33                                   
REMARK 500    SER S 148       48.58    -73.45                                   
REMARK 500    PHE S 199      -70.77   -107.54                                   
REMARK 500    ASP S 318       10.87   -148.37                                   
REMARK 500    TYR S 367      -91.54   -107.13                                   
REMARK 500    GLU S 409      -76.62    -52.56                                   
REMARK 500    TRP S 453       -1.30     80.03                                   
REMARK 500    ASP S 454       50.51    -97.86                                   
REMARK 500    SER T  95     -153.02   -142.48                                   
REMARK 500    TYR T  97     -107.97   -132.80                                   
REMARK 500    ASN T 113       -2.31    -59.37                                   
REMARK 500    LYS T 264       44.93    -82.65                                   
REMARK 500    ASP T 350      -66.50   -122.20                                   
REMARK 500    THR T 399      -64.82   -107.41                                   
REMARK 500    ASN U  47       18.87     81.29                                   
REMARK 500    LEU V   2      -63.16     87.86                                   
REMARK 500    LYS V  58      -38.97   -130.24                                   
REMARK 500    PHE V  65      -69.44    -27.30                                   
REMARK 500    CYS V  84       25.13     48.55                                   
REMARK 500    ASN V  91       -0.20     80.75                                   
REMARK 500    SER V 125      -18.07   -154.84                                   
REMARK 500    THR V 126       -8.95     81.00                                   
REMARK 500    PHE V 132      148.04   -175.89                                   
REMARK 500    ASP V 139      103.79   -167.14                                   
REMARK 500    SER V 148       47.09    -69.34                                   
REMARK 500    PHE V 199      -75.37   -103.91                                   
REMARK 500    ASP V 318       -3.59   -149.21                                   
REMARK 500    TYR V 367      -90.06   -101.58                                   
REMARK 500    GLU V 409      -71.68    -59.09                                   
REMARK 500    TRP V 453        0.43     81.35                                   
REMARK 500    ASP V 454       48.20   -102.37                                   
REMARK 500    SER W  95     -151.53   -139.89                                   
REMARK 500    TYR W  97     -106.24   -133.37                                   
REMARK 500    ASN W 113       -6.31    -55.10                                   
REMARK 500    LYS W 264       42.83    -84.81                                   
REMARK 500    ASP W 350      -65.12   -124.03                                   
REMARK 500    THR W 399      -65.34   -108.81                                   
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 VAL B   39     CYS B   40                 -144.81                    
REMARK 500 TYR B   97     GLU B   98                  145.10                    
REMARK 500 THR I   45     GLU I   46                  145.50                    
REMARK 500 THR O   45     GLU O   46                  149.80                    
REMARK 500 THR U   45     GLU U   46                  144.11                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     ASN A  901                                                       
REMARK 610     ASN D  902                                                       
REMARK 610     ASN G  903                                                       
REMARK 610     ASN J  904                                                       
REMARK 610     ASN M  905                                                       
REMARK 610     ASN P  906                                                       
REMARK 610     ASN S  907                                                       
REMARK 610     ASN V  908                                                       
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 B 801  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  14   NE2                                                    
REMARK 620 2 GLU B 127   OE2  83.5                                              
REMARK 620 3 GLU B 153   OE1  94.8  94.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 901  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  25   SG                                                     
REMARK 620 2 CYS B  27   SG  107.8                                              
REMARK 620 3 CYS B  40   SG  110.0  90.4                                        
REMARK 620 4 CYS B  43   SG  113.6 114.6 117.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 802  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  14   NE2                                                    
REMARK 620 2 GLU E 127   OE2  85.5                                              
REMARK 620 3 GLU E 153   OE1  86.6  93.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 902  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E  25   SG                                                     
REMARK 620 2 CYS E  27   SG  117.8                                              
REMARK 620 3 CYS E  40   SG  116.6 110.3                                        
REMARK 620 4 CYS E  43   SG  103.6 102.7 103.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H 803  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H  14   NE2                                                    
REMARK 620 2 GLU H 153   OE1  83.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H 903  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS H  25   SG                                                     
REMARK 620 2 CYS H  27   SG  114.9                                              
REMARK 620 3 CYS H  40   SG  110.8 102.6                                        
REMARK 620 4 CYS H  43   SG  109.4 109.3 109.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG K 804  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS K  14   NE2                                                    
REMARK 620 2 GLU K 127   OE2  85.0                                              
REMARK 620 3 GLU K 153   OE1  94.9  90.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN K 904  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS K  25   SG                                                     
REMARK 620 2 CYS K  27   SG  119.9                                              
REMARK 620 3 CYS K  40   SG  115.0 109.6                                        
REMARK 620 4 CYS K  43   SG  106.0 100.6 103.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG N 805  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS N  14   NE2                                                    
REMARK 620 2 GLU N 127   OE2  75.0                                              
REMARK 620 3 GLU N 153   OE1  84.2  86.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN N 905  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS N  25   SG                                                     
REMARK 620 2 CYS N  27   SG  115.2                                              
REMARK 620 3 CYS N  40   SG  114.6 102.3                                        
REMARK 620 4 CYS N  43   SG  111.6 100.6 111.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG Q 806  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS Q  14   NE2                                                    
REMARK 620 2 GLU Q 127   OE2  82.9                                              
REMARK 620 3 GLU Q 153   OE1  93.9  80.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN Q 906  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS Q  25   SG                                                     
REMARK 620 2 CYS Q  27   SG  117.0                                              
REMARK 620 3 CYS Q  40   SG  111.4 104.8                                        
REMARK 620 4 CYS Q  43   SG  109.6 107.6 105.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG T 807  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS T  14   NE2                                                    
REMARK 620 2 GLU T 127   OE2  86.4                                              
REMARK 620 3 GLU T 153   OE1  85.7  95.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN T 907  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS T  25   SG                                                     
REMARK 620 2 CYS T  27   SG  114.6                                              
REMARK 620 3 CYS T  40   SG  113.0 110.4                                        
REMARK 620 4 CYS T  43   SG  105.8 110.0 102.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG W 808  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS W  14   NE2                                                    
REMARK 620 2 GLU W 127   OE2  84.5                                              
REMARK 620 3 GLU W 153   OE1  95.3  91.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN W 908  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS W  25   SG                                                     
REMARK 620 2 CYS W  27   SG  117.9                                              
REMARK 620 3 CYS W  40   SG  115.0 107.8                                        
REMARK 620 4 CYS W  43   SG  110.7 100.6 102.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 701                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 801                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 901                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 702                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 802                  
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 902                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP H 703                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 803                  
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 903                  
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP K 704                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG K 804                  
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN K 904                  
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP N 705                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG N 805                  
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN N 905                  
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP Q 706                 
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Q 806                  
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN Q 906                  
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP T 707                 
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG T 807                  
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN T 907                  
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP W 708                 
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG W 808                  
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN W 908                  
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASN A 901                 
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASN D 902                 
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASN G 903                 
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASN J 904                 
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASN M 905                 
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASN P 906                 
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASN S 907                 
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASN V 908                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2G5I   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF TRNA-DEPENDENT AMIDOTRANSFERASE GATCAB FROM             
REMARK 900 STAPHYLOCOCCUS AUREUS WITH ADP                                       
REMARK 900 RELATED ID: 2G5H   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF TRNA-DEPENDENT AMIDOTRANSFERASE GATCAB FROM             
REMARK 900 STAPHYLOCOCCUS AUREUS WITH MG2+                                      
REMARK 900 RELATED ID: 2F2A   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF TRNA-DEPENDENT AMIDOTRANSFERASE GATCAB FROM             
REMARK 900 STAPHYLOCOCCUS AUREUS WITH MG2+ AND GLN                              
REMARK 900 RELATED ID: 2DF4   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF TRNA-DEPENDENT AMIDOTRANSFERASE GATCAB FROM             
REMARK 900 STAPHYLOCOCCUS AUREUS WITH MN2+                                      
REMARK 900 RELATED ID: 2GI3   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE             
REMARK 900 SUBUNIT A (TM1272) FROM THERMOTOGA MARITIMA AT 1.80 A                
REMARK 900 RESOLUTION                                                           
REMARK 900 RELATED ID: 3H0M   RELATED DB: PDB                                   
DBREF  3H0L A    1   478  UNP    O66610   GATA_AQUAE       1    478             
DBREF  3H0L B    1   478  UNP    O66766   GATB_AQUAE       1    478             
DBREF  3H0L C    1    94  UNP    O67904   GATC_AQUAE       1     94             
DBREF  3H0L D    1   478  UNP    O66610   GATA_AQUAE       1    478             
DBREF  3H0L E    1   478  UNP    O66766   GATB_AQUAE       1    478             
DBREF  3H0L F    1    94  UNP    O67904   GATC_AQUAE       1     94             
DBREF  3H0L G    1   478  UNP    O66610   GATA_AQUAE       1    478             
DBREF  3H0L H    1   478  UNP    O66766   GATB_AQUAE       1    478             
DBREF  3H0L I    1    94  UNP    O67904   GATC_AQUAE       1     94             
DBREF  3H0L J    1   478  UNP    O66610   GATA_AQUAE       1    478             
DBREF  3H0L K    1   478  UNP    O66766   GATB_AQUAE       1    478             
DBREF  3H0L L    1    94  UNP    O67904   GATC_AQUAE       1     94             
DBREF  3H0L M    1   478  UNP    O66610   GATA_AQUAE       1    478             
DBREF  3H0L N    1   478  UNP    O66766   GATB_AQUAE       1    478             
DBREF  3H0L O    1    94  UNP    O67904   GATC_AQUAE       1     94             
DBREF  3H0L P    1   478  UNP    O66610   GATA_AQUAE       1    478             
DBREF  3H0L Q    1   478  UNP    O66766   GATB_AQUAE       1    478             
DBREF  3H0L R    1    94  UNP    O67904   GATC_AQUAE       1     94             
DBREF  3H0L S    1   478  UNP    O66610   GATA_AQUAE       1    478             
DBREF  3H0L T    1   478  UNP    O66766   GATB_AQUAE       1    478             
DBREF  3H0L U    1    94  UNP    O67904   GATC_AQUAE       1     94             
DBREF  3H0L V    1   478  UNP    O66610   GATA_AQUAE       1    478             
DBREF  3H0L W    1   478  UNP    O66766   GATB_AQUAE       1    478             
DBREF  3H0L X    1    94  UNP    O67904   GATC_AQUAE       1     94             
SEQRES   1 A  478  MET LEU TRP LYS LYS SER LEU SER GLU LEU ARG GLU LEU          
SEQRES   2 A  478  LEU LYS ARG GLY GLU VAL SER PRO LYS GLU VAL VAL GLU          
SEQRES   3 A  478  SER PHE TYR ASP ARG TYR ASN GLN THR GLU GLU LYS VAL          
SEQRES   4 A  478  LYS ALA TYR ILE THR PRO LEU TYR GLY LYS ALA LEU LYS          
SEQRES   5 A  478  GLN ALA GLU SER LEU LYS GLU ARG GLU LEU PRO LEU PHE          
SEQRES   6 A  478  GLY ILE PRO ILE ALA VAL LYS ASP ASN ILE LEU VAL GLU          
SEQRES   7 A  478  GLY GLU LYS THR THR CYS ALA SER LYS ILE LEU GLU ASN          
SEQRES   8 A  478  PHE VAL ALA PRO TYR ASP ALA THR VAL ILE GLU ARG LEU          
SEQRES   9 A  478  LYS LYS ALA GLY ALA LEU ILE VAL GLY LYS THR ASN LEU          
SEQRES  10 A  478  ASP GLU PHE ALA MET GLY SER SER THR GLU TYR SER ALA          
SEQRES  11 A  478  PHE PHE PRO THR LYS ASN PRO TRP ASP LEU GLU ARG VAL          
SEQRES  12 A  478  PRO GLY GLY SER SER GLY GLY SER ALA ALA SER VAL ALA          
SEQRES  13 A  478  VAL LEU SER ALA PRO VAL SER LEU GLY SER ASP THR GLY          
SEQRES  14 A  478  GLY SER ILE ARG GLN PRO ALA SER PHE CYS GLY VAL ILE          
SEQRES  15 A  478  GLY ILE LYS PRO THR TYR GLY ARG VAL SER ARG TYR GLY          
SEQRES  16 A  478  LEU VAL ALA PHE ALA SER SER LEU ASP GLN ILE GLY VAL          
SEQRES  17 A  478  PHE GLY ARG ARG THR GLU ASP VAL ALA LEU VAL LEU GLU          
SEQRES  18 A  478  VAL ILE SER GLY TRP ASP GLU LYS ASP SER THR SER ALA          
SEQRES  19 A  478  LYS VAL PRO VAL PRO GLU TRP SER GLU GLU VAL LYS LYS          
SEQRES  20 A  478  GLU VAL LYS GLY LEU LYS ILE GLY LEU PRO LYS GLU PHE          
SEQRES  21 A  478  PHE GLU TYR GLU LEU GLN PRO GLN VAL LYS GLU ALA PHE          
SEQRES  22 A  478  GLU ASN PHE ILE LYS GLU LEU GLU LYS GLU GLY PHE GLU          
SEQRES  23 A  478  ILE LYS GLU VAL SER LEU PRO HIS VAL LYS TYR SER ILE          
SEQRES  24 A  478  PRO THR TYR TYR ILE ILE ALA PRO SER GLU ALA SER SER          
SEQRES  25 A  478  ASN LEU ALA ARG TYR ASP GLY VAL ARG TYR GLY TYR ARG          
SEQRES  26 A  478  ALA LYS GLU TYR LYS ASP ILE PHE GLU MET TYR ALA ARG          
SEQRES  27 A  478  THR ARG ASP GLU GLY PHE GLY PRO GLU VAL LYS ARG ARG          
SEQRES  28 A  478  ILE MET LEU GLY THR PHE ALA LEU SER ALA GLY TYR TYR          
SEQRES  29 A  478  ASP ALA TYR TYR LEU LYS ALA GLN LYS VAL ARG ARG LEU          
SEQRES  30 A  478  ILE THR ASN ASP PHE LEU LYS ALA PHE GLU GLU VAL ASP          
SEQRES  31 A  478  VAL ILE ALA SER PRO THR THR PRO THR LEU PRO PHE LYS          
SEQRES  32 A  478  PHE GLY GLU ARG LEU GLU ASN PRO ILE GLU MET TYR LEU          
SEQRES  33 A  478  SER ASP ILE LEU THR VAL PRO ALA ASN LEU ALA GLY LEU          
SEQRES  34 A  478  PRO ALA ILE SER ILE PRO ILE ALA TRP LYS ASP GLY LEU          
SEQRES  35 A  478  PRO VAL GLY GLY GLN LEU ILE GLY LYS HIS TRP ASP GLU          
SEQRES  36 A  478  THR THR LEU LEU GLN ILE SER TYR LEU TRP GLU GLN LYS          
SEQRES  37 A  478  PHE LYS HIS TYR GLU LYS ILE PRO LEU THR                      
SEQRES   1 B  478  MET ASN GLU LYS TYR GLU ALA VAL ILE GLY LEU GLU ILE          
SEQRES   2 B  478  HIS VAL GLN MET ASP THR LYS THR LYS MET PHE CYS GLY          
SEQRES   3 B  478  CYS LYS VAL GLU PHE GLY ALA GLU PRO ASN THR ASN VAL          
SEQRES   4 B  478  CYS PRO VAL CYS LEU GLY MET PRO GLY ALA LEU PRO ILE          
SEQRES   5 B  478  VAL ASN LYS ARG ALA VAL GLU TYR ALA ILE ARG ALA SER          
SEQRES   6 B  478  LEU ALA LEU ASN CYS GLU VAL HIS GLU GLU SER VAL PHE          
SEQRES   7 B  478  ALA ARG LYS HIS TYR PHE TYR PRO ASP LEU PRO LYS GLY          
SEQRES   8 B  478  TYR GLN ILE SER GLN TYR GLU LYS PRO LEU ALA THR ASN          
SEQRES   9 B  478  GLY TRP VAL GLU LEU ASN LEU PRO ASN GLY GLU LYS LYS          
SEQRES  10 B  478  LYS VAL ARG ILE ARG ARG LEU HIS ILE GLU GLU ASP ALA          
SEQRES  11 B  478  GLY LYS ASN ILE HIS GLU GLY ASP LYS THR LEU VAL ASP          
SEQRES  12 B  478  LEU ASN ARG ALA GLY THR PRO LEU MET GLU ILE VAL THR          
SEQRES  13 B  478  GLU PRO ASP ILE ARG THR PRO GLU GLU ALA ARG LEU PHE          
SEQRES  14 B  478  LEU GLU LYS LEU ARG ASN ILE MET ARG TYR ALA GLY VAL          
SEQRES  15 B  478  SER LYS ALA ASP MET GLU LYS GLY GLN LEU ARG CYS ASP          
SEQRES  16 B  478  ILE ASN VAL SER ILE ARG PRO LYS GLY SER LYS GLU PHE          
SEQRES  17 B  478  GLY THR ARG VAL GLU ILE LYS ASN VAL ASN SER PHE ARG          
SEQRES  18 B  478  PHE VAL GLN LYS ALA LEU GLU TYR GLU ILE GLU ARG GLN          
SEQRES  19 B  478  ILE ASN VAL VAL GLU GLU GLY GLY GLU VAL VAL GLN GLU          
SEQRES  20 B  478  THR ARG THR PHE ASP PRO GLN THR GLY LYS THR TYR PRO          
SEQRES  21 B  478  MET ARG THR LYS GLU GLU ALA GLU ASP TYR ARG TYR PHE          
SEQRES  22 B  478  PRO ASP PRO ASP LEU VAL PRO LEU LYS VAL LYS LYS GLU          
SEQRES  23 B  478  TRP ILE GLU GLU ILE LYS LYS ASN MET PRO GLU LEU PRO          
SEQRES  24 B  478  ASP GLN ARG PHE GLU ARG LEU ILE LYS GLU TYR GLY LEU          
SEQRES  25 B  478  SER GLU TYR GLU ALA GLY ILE LEU VAL ASN HIS LYS GLU          
SEQRES  26 B  478  VAL GLY ASP PHE PHE GLU GLU ALA VAL ARG HIS PHE LYS          
SEQRES  27 B  478  GLU PRO LYS GLY ILE VAL ASN TRP LEU ILE ASN ASP LEU          
SEQRES  28 B  478  LEU GLY LEU LEU ARG ASP LYS GLY ILE SER ILE GLU GLU          
SEQRES  29 B  478  SER PRO VAL LYS PRO GLU HIS LEU ALA GLU LEU VAL LYS          
SEQRES  30 B  478  LEU ILE LYS GLU LYS VAL ILE SER THR LYS ILE GLY LYS          
SEQRES  31 B  478  GLU VAL ILE LYS GLU MET VAL GLU THR GLY LYS THR PRO          
SEQRES  32 B  478  SER GLN ILE VAL GLU GLU LYS GLY LEU LYS GLN ILE THR          
SEQRES  33 B  478  ASP GLU ASN GLN ILE LYS GLU LEU VAL LYS LYS ILE PHE          
SEQRES  34 B  478  GLU LYS HIS PRO LYS GLU VAL GLU ARG LEU LYS GLN GLY          
SEQRES  35 B  478  GLU GLU LYS LEU ILE GLY PHE PHE VAL GLY GLN VAL MET          
SEQRES  36 B  478  ARG GLU THR ARG GLY LYS ALA ASN PRO GLN VAL VAL ASN          
SEQRES  37 B  478  LYS VAL ILE ARG GLU LEU VAL LYS GLU VAL                      
SEQRES   1 C   94  MET VAL ASP ARG GLU TRP VAL LEU LYS ILE ALA LYS LEU          
SEQRES   2 C   94  ALA ARG LEU GLU LEU LYS GLU GLU GLU ILE GLU VAL PHE          
SEQRES   3 C   94  GLN LYS GLN LEU SER ASP ILE LEU ASP PHE ILE ASP GLN          
SEQRES   4 C   94  LEU LYS GLU LEU ASP THR GLU ASN VAL GLU PRO TYR ILE          
SEQRES   5 C   94  GLN GLU PHE GLU GLU THR PRO MET ARG GLU ASP GLU PRO          
SEQRES   6 C   94  HIS PRO SER LEU ASP ARG GLU LYS ALA LEU MET ASN ALA          
SEQRES   7 C   94  PRO GLU ARG LYS ASP GLY PHE PHE VAL VAL PRO ARG VAL          
SEQRES   8 C   94  VAL GLU VAL                                                  
SEQRES   1 D  478  MET LEU TRP LYS LYS SER LEU SER GLU LEU ARG GLU LEU          
SEQRES   2 D  478  LEU LYS ARG GLY GLU VAL SER PRO LYS GLU VAL VAL GLU          
SEQRES   3 D  478  SER PHE TYR ASP ARG TYR ASN GLN THR GLU GLU LYS VAL          
SEQRES   4 D  478  LYS ALA TYR ILE THR PRO LEU TYR GLY LYS ALA LEU LYS          
SEQRES   5 D  478  GLN ALA GLU SER LEU LYS GLU ARG GLU LEU PRO LEU PHE          
SEQRES   6 D  478  GLY ILE PRO ILE ALA VAL LYS ASP ASN ILE LEU VAL GLU          
SEQRES   7 D  478  GLY GLU LYS THR THR CYS ALA SER LYS ILE LEU GLU ASN          
SEQRES   8 D  478  PHE VAL ALA PRO TYR ASP ALA THR VAL ILE GLU ARG LEU          
SEQRES   9 D  478  LYS LYS ALA GLY ALA LEU ILE VAL GLY LYS THR ASN LEU          
SEQRES  10 D  478  ASP GLU PHE ALA MET GLY SER SER THR GLU TYR SER ALA          
SEQRES  11 D  478  PHE PHE PRO THR LYS ASN PRO TRP ASP LEU GLU ARG VAL          
SEQRES  12 D  478  PRO GLY GLY SER SER GLY GLY SER ALA ALA SER VAL ALA          
SEQRES  13 D  478  VAL LEU SER ALA PRO VAL SER LEU GLY SER ASP THR GLY          
SEQRES  14 D  478  GLY SER ILE ARG GLN PRO ALA SER PHE CYS GLY VAL ILE          
SEQRES  15 D  478  GLY ILE LYS PRO THR TYR GLY ARG VAL SER ARG TYR GLY          
SEQRES  16 D  478  LEU VAL ALA PHE ALA SER SER LEU ASP GLN ILE GLY VAL          
SEQRES  17 D  478  PHE GLY ARG ARG THR GLU ASP VAL ALA LEU VAL LEU GLU          
SEQRES  18 D  478  VAL ILE SER GLY TRP ASP GLU LYS ASP SER THR SER ALA          
SEQRES  19 D  478  LYS VAL PRO VAL PRO GLU TRP SER GLU GLU VAL LYS LYS          
SEQRES  20 D  478  GLU VAL LYS GLY LEU LYS ILE GLY LEU PRO LYS GLU PHE          
SEQRES  21 D  478  PHE GLU TYR GLU LEU GLN PRO GLN VAL LYS GLU ALA PHE          
SEQRES  22 D  478  GLU ASN PHE ILE LYS GLU LEU GLU LYS GLU GLY PHE GLU          
SEQRES  23 D  478  ILE LYS GLU VAL SER LEU PRO HIS VAL LYS TYR SER ILE          
SEQRES  24 D  478  PRO THR TYR TYR ILE ILE ALA PRO SER GLU ALA SER SER          
SEQRES  25 D  478  ASN LEU ALA ARG TYR ASP GLY VAL ARG TYR GLY TYR ARG          
SEQRES  26 D  478  ALA LYS GLU TYR LYS ASP ILE PHE GLU MET TYR ALA ARG          
SEQRES  27 D  478  THR ARG ASP GLU GLY PHE GLY PRO GLU VAL LYS ARG ARG          
SEQRES  28 D  478  ILE MET LEU GLY THR PHE ALA LEU SER ALA GLY TYR TYR          
SEQRES  29 D  478  ASP ALA TYR TYR LEU LYS ALA GLN LYS VAL ARG ARG LEU          
SEQRES  30 D  478  ILE THR ASN ASP PHE LEU LYS ALA PHE GLU GLU VAL ASP          
SEQRES  31 D  478  VAL ILE ALA SER PRO THR THR PRO THR LEU PRO PHE LYS          
SEQRES  32 D  478  PHE GLY GLU ARG LEU GLU ASN PRO ILE GLU MET TYR LEU          
SEQRES  33 D  478  SER ASP ILE LEU THR VAL PRO ALA ASN LEU ALA GLY LEU          
SEQRES  34 D  478  PRO ALA ILE SER ILE PRO ILE ALA TRP LYS ASP GLY LEU          
SEQRES  35 D  478  PRO VAL GLY GLY GLN LEU ILE GLY LYS HIS TRP ASP GLU          
SEQRES  36 D  478  THR THR LEU LEU GLN ILE SER TYR LEU TRP GLU GLN LYS          
SEQRES  37 D  478  PHE LYS HIS TYR GLU LYS ILE PRO LEU THR                      
SEQRES   1 E  478  MET ASN GLU LYS TYR GLU ALA VAL ILE GLY LEU GLU ILE          
SEQRES   2 E  478  HIS VAL GLN MET ASP THR LYS THR LYS MET PHE CYS GLY          
SEQRES   3 E  478  CYS LYS VAL GLU PHE GLY ALA GLU PRO ASN THR ASN VAL          
SEQRES   4 E  478  CYS PRO VAL CYS LEU GLY MET PRO GLY ALA LEU PRO ILE          
SEQRES   5 E  478  VAL ASN LYS ARG ALA VAL GLU TYR ALA ILE ARG ALA SER          
SEQRES   6 E  478  LEU ALA LEU ASN CYS GLU VAL HIS GLU GLU SER VAL PHE          
SEQRES   7 E  478  ALA ARG LYS HIS TYR PHE TYR PRO ASP LEU PRO LYS GLY          
SEQRES   8 E  478  TYR GLN ILE SER GLN TYR GLU LYS PRO LEU ALA THR ASN          
SEQRES   9 E  478  GLY TRP VAL GLU LEU ASN LEU PRO ASN GLY GLU LYS LYS          
SEQRES  10 E  478  LYS VAL ARG ILE ARG ARG LEU HIS ILE GLU GLU ASP ALA          
SEQRES  11 E  478  GLY LYS ASN ILE HIS GLU GLY ASP LYS THR LEU VAL ASP          
SEQRES  12 E  478  LEU ASN ARG ALA GLY THR PRO LEU MET GLU ILE VAL THR          
SEQRES  13 E  478  GLU PRO ASP ILE ARG THR PRO GLU GLU ALA ARG LEU PHE          
SEQRES  14 E  478  LEU GLU LYS LEU ARG ASN ILE MET ARG TYR ALA GLY VAL          
SEQRES  15 E  478  SER LYS ALA ASP MET GLU LYS GLY GLN LEU ARG CYS ASP          
SEQRES  16 E  478  ILE ASN VAL SER ILE ARG PRO LYS GLY SER LYS GLU PHE          
SEQRES  17 E  478  GLY THR ARG VAL GLU ILE LYS ASN VAL ASN SER PHE ARG          
SEQRES  18 E  478  PHE VAL GLN LYS ALA LEU GLU TYR GLU ILE GLU ARG GLN          
SEQRES  19 E  478  ILE ASN VAL VAL GLU GLU GLY GLY GLU VAL VAL GLN GLU          
SEQRES  20 E  478  THR ARG THR PHE ASP PRO GLN THR GLY LYS THR TYR PRO          
SEQRES  21 E  478  MET ARG THR LYS GLU GLU ALA GLU ASP TYR ARG TYR PHE          
SEQRES  22 E  478  PRO ASP PRO ASP LEU VAL PRO LEU LYS VAL LYS LYS GLU          
SEQRES  23 E  478  TRP ILE GLU GLU ILE LYS LYS ASN MET PRO GLU LEU PRO          
SEQRES  24 E  478  ASP GLN ARG PHE GLU ARG LEU ILE LYS GLU TYR GLY LEU          
SEQRES  25 E  478  SER GLU TYR GLU ALA GLY ILE LEU VAL ASN HIS LYS GLU          
SEQRES  26 E  478  VAL GLY ASP PHE PHE GLU GLU ALA VAL ARG HIS PHE LYS          
SEQRES  27 E  478  GLU PRO LYS GLY ILE VAL ASN TRP LEU ILE ASN ASP LEU          
SEQRES  28 E  478  LEU GLY LEU LEU ARG ASP LYS GLY ILE SER ILE GLU GLU          
SEQRES  29 E  478  SER PRO VAL LYS PRO GLU HIS LEU ALA GLU LEU VAL LYS          
SEQRES  30 E  478  LEU ILE LYS GLU LYS VAL ILE SER THR LYS ILE GLY LYS          
SEQRES  31 E  478  GLU VAL ILE LYS GLU MET VAL GLU THR GLY LYS THR PRO          
SEQRES  32 E  478  SER GLN ILE VAL GLU GLU LYS GLY LEU LYS GLN ILE THR          
SEQRES  33 E  478  ASP GLU ASN GLN ILE LYS GLU LEU VAL LYS LYS ILE PHE          
SEQRES  34 E  478  GLU LYS HIS PRO LYS GLU VAL GLU ARG LEU LYS GLN GLY          
SEQRES  35 E  478  GLU GLU LYS LEU ILE GLY PHE PHE VAL GLY GLN VAL MET          
SEQRES  36 E  478  ARG GLU THR ARG GLY LYS ALA ASN PRO GLN VAL VAL ASN          
SEQRES  37 E  478  LYS VAL ILE ARG GLU LEU VAL LYS GLU VAL                      
SEQRES   1 F   94  MET VAL ASP ARG GLU TRP VAL LEU LYS ILE ALA LYS LEU          
SEQRES   2 F   94  ALA ARG LEU GLU LEU LYS GLU GLU GLU ILE GLU VAL PHE          
SEQRES   3 F   94  GLN LYS GLN LEU SER ASP ILE LEU ASP PHE ILE ASP GLN          
SEQRES   4 F   94  LEU LYS GLU LEU ASP THR GLU ASN VAL GLU PRO TYR ILE          
SEQRES   5 F   94  GLN GLU PHE GLU GLU THR PRO MET ARG GLU ASP GLU PRO          
SEQRES   6 F   94  HIS PRO SER LEU ASP ARG GLU LYS ALA LEU MET ASN ALA          
SEQRES   7 F   94  PRO GLU ARG LYS ASP GLY PHE PHE VAL VAL PRO ARG VAL          
SEQRES   8 F   94  VAL GLU VAL                                                  
SEQRES   1 G  478  MET LEU TRP LYS LYS SER LEU SER GLU LEU ARG GLU LEU          
SEQRES   2 G  478  LEU LYS ARG GLY GLU VAL SER PRO LYS GLU VAL VAL GLU          
SEQRES   3 G  478  SER PHE TYR ASP ARG TYR ASN GLN THR GLU GLU LYS VAL          
SEQRES   4 G  478  LYS ALA TYR ILE THR PRO LEU TYR GLY LYS ALA LEU LYS          
SEQRES   5 G  478  GLN ALA GLU SER LEU LYS GLU ARG GLU LEU PRO LEU PHE          
SEQRES   6 G  478  GLY ILE PRO ILE ALA VAL LYS ASP ASN ILE LEU VAL GLU          
SEQRES   7 G  478  GLY GLU LYS THR THR CYS ALA SER LYS ILE LEU GLU ASN          
SEQRES   8 G  478  PHE VAL ALA PRO TYR ASP ALA THR VAL ILE GLU ARG LEU          
SEQRES   9 G  478  LYS LYS ALA GLY ALA LEU ILE VAL GLY LYS THR ASN LEU          
SEQRES  10 G  478  ASP GLU PHE ALA MET GLY SER SER THR GLU TYR SER ALA          
SEQRES  11 G  478  PHE PHE PRO THR LYS ASN PRO TRP ASP LEU GLU ARG VAL          
SEQRES  12 G  478  PRO GLY GLY SER SER GLY GLY SER ALA ALA SER VAL ALA          
SEQRES  13 G  478  VAL LEU SER ALA PRO VAL SER LEU GLY SER ASP THR GLY          
SEQRES  14 G  478  GLY SER ILE ARG GLN PRO ALA SER PHE CYS GLY VAL ILE          
SEQRES  15 G  478  GLY ILE LYS PRO THR TYR GLY ARG VAL SER ARG TYR GLY          
SEQRES  16 G  478  LEU VAL ALA PHE ALA SER SER LEU ASP GLN ILE GLY VAL          
SEQRES  17 G  478  PHE GLY ARG ARG THR GLU ASP VAL ALA LEU VAL LEU GLU          
SEQRES  18 G  478  VAL ILE SER GLY TRP ASP GLU LYS ASP SER THR SER ALA          
SEQRES  19 G  478  LYS VAL PRO VAL PRO GLU TRP SER GLU GLU VAL LYS LYS          
SEQRES  20 G  478  GLU VAL LYS GLY LEU LYS ILE GLY LEU PRO LYS GLU PHE          
SEQRES  21 G  478  PHE GLU TYR GLU LEU GLN PRO GLN VAL LYS GLU ALA PHE          
SEQRES  22 G  478  GLU ASN PHE ILE LYS GLU LEU GLU LYS GLU GLY PHE GLU          
SEQRES  23 G  478  ILE LYS GLU VAL SER LEU PRO HIS VAL LYS TYR SER ILE          
SEQRES  24 G  478  PRO THR TYR TYR ILE ILE ALA PRO SER GLU ALA SER SER          
SEQRES  25 G  478  ASN LEU ALA ARG TYR ASP GLY VAL ARG TYR GLY TYR ARG          
SEQRES  26 G  478  ALA LYS GLU TYR LYS ASP ILE PHE GLU MET TYR ALA ARG          
SEQRES  27 G  478  THR ARG ASP GLU GLY PHE GLY PRO GLU VAL LYS ARG ARG          
SEQRES  28 G  478  ILE MET LEU GLY THR PHE ALA LEU SER ALA GLY TYR TYR          
SEQRES  29 G  478  ASP ALA TYR TYR LEU LYS ALA GLN LYS VAL ARG ARG LEU          
SEQRES  30 G  478  ILE THR ASN ASP PHE LEU LYS ALA PHE GLU GLU VAL ASP          
SEQRES  31 G  478  VAL ILE ALA SER PRO THR THR PRO THR LEU PRO PHE LYS          
SEQRES  32 G  478  PHE GLY GLU ARG LEU GLU ASN PRO ILE GLU MET TYR LEU          
SEQRES  33 G  478  SER ASP ILE LEU THR VAL PRO ALA ASN LEU ALA GLY LEU          
SEQRES  34 G  478  PRO ALA ILE SER ILE PRO ILE ALA TRP LYS ASP GLY LEU          
SEQRES  35 G  478  PRO VAL GLY GLY GLN LEU ILE GLY LYS HIS TRP ASP GLU          
SEQRES  36 G  478  THR THR LEU LEU GLN ILE SER TYR LEU TRP GLU GLN LYS          
SEQRES  37 G  478  PHE LYS HIS TYR GLU LYS ILE PRO LEU THR                      
SEQRES   1 H  478  MET ASN GLU LYS TYR GLU ALA VAL ILE GLY LEU GLU ILE          
SEQRES   2 H  478  HIS VAL GLN MET ASP THR LYS THR LYS MET PHE CYS GLY          
SEQRES   3 H  478  CYS LYS VAL GLU PHE GLY ALA GLU PRO ASN THR ASN VAL          
SEQRES   4 H  478  CYS PRO VAL CYS LEU GLY MET PRO GLY ALA LEU PRO ILE          
SEQRES   5 H  478  VAL ASN LYS ARG ALA VAL GLU TYR ALA ILE ARG ALA SER          
SEQRES   6 H  478  LEU ALA LEU ASN CYS GLU VAL HIS GLU GLU SER VAL PHE          
SEQRES   7 H  478  ALA ARG LYS HIS TYR PHE TYR PRO ASP LEU PRO LYS GLY          
SEQRES   8 H  478  TYR GLN ILE SER GLN TYR GLU LYS PRO LEU ALA THR ASN          
SEQRES   9 H  478  GLY TRP VAL GLU LEU ASN LEU PRO ASN GLY GLU LYS LYS          
SEQRES  10 H  478  LYS VAL ARG ILE ARG ARG LEU HIS ILE GLU GLU ASP ALA          
SEQRES  11 H  478  GLY LYS ASN ILE HIS GLU GLY ASP LYS THR LEU VAL ASP          
SEQRES  12 H  478  LEU ASN ARG ALA GLY THR PRO LEU MET GLU ILE VAL THR          
SEQRES  13 H  478  GLU PRO ASP ILE ARG THR PRO GLU GLU ALA ARG LEU PHE          
SEQRES  14 H  478  LEU GLU LYS LEU ARG ASN ILE MET ARG TYR ALA GLY VAL          
SEQRES  15 H  478  SER LYS ALA ASP MET GLU LYS GLY GLN LEU ARG CYS ASP          
SEQRES  16 H  478  ILE ASN VAL SER ILE ARG PRO LYS GLY SER LYS GLU PHE          
SEQRES  17 H  478  GLY THR ARG VAL GLU ILE LYS ASN VAL ASN SER PHE ARG          
SEQRES  18 H  478  PHE VAL GLN LYS ALA LEU GLU TYR GLU ILE GLU ARG GLN          
SEQRES  19 H  478  ILE ASN VAL VAL GLU GLU GLY GLY GLU VAL VAL GLN GLU          
SEQRES  20 H  478  THR ARG THR PHE ASP PRO GLN THR GLY LYS THR TYR PRO          
SEQRES  21 H  478  MET ARG THR LYS GLU GLU ALA GLU ASP TYR ARG TYR PHE          
SEQRES  22 H  478  PRO ASP PRO ASP LEU VAL PRO LEU LYS VAL LYS LYS GLU          
SEQRES  23 H  478  TRP ILE GLU GLU ILE LYS LYS ASN MET PRO GLU LEU PRO          
SEQRES  24 H  478  ASP GLN ARG PHE GLU ARG LEU ILE LYS GLU TYR GLY LEU          
SEQRES  25 H  478  SER GLU TYR GLU ALA GLY ILE LEU VAL ASN HIS LYS GLU          
SEQRES  26 H  478  VAL GLY ASP PHE PHE GLU GLU ALA VAL ARG HIS PHE LYS          
SEQRES  27 H  478  GLU PRO LYS GLY ILE VAL ASN TRP LEU ILE ASN ASP LEU          
SEQRES  28 H  478  LEU GLY LEU LEU ARG ASP LYS GLY ILE SER ILE GLU GLU          
SEQRES  29 H  478  SER PRO VAL LYS PRO GLU HIS LEU ALA GLU LEU VAL LYS          
SEQRES  30 H  478  LEU ILE LYS GLU LYS VAL ILE SER THR LYS ILE GLY LYS          
SEQRES  31 H  478  GLU VAL ILE LYS GLU MET VAL GLU THR GLY LYS THR PRO          
SEQRES  32 H  478  SER GLN ILE VAL GLU GLU LYS GLY LEU LYS GLN ILE THR          
SEQRES  33 H  478  ASP GLU ASN GLN ILE LYS GLU LEU VAL LYS LYS ILE PHE          
SEQRES  34 H  478  GLU LYS HIS PRO LYS GLU VAL GLU ARG LEU LYS GLN GLY          
SEQRES  35 H  478  GLU GLU LYS LEU ILE GLY PHE PHE VAL GLY GLN VAL MET          
SEQRES  36 H  478  ARG GLU THR ARG GLY LYS ALA ASN PRO GLN VAL VAL ASN          
SEQRES  37 H  478  LYS VAL ILE ARG GLU LEU VAL LYS GLU VAL                      
SEQRES   1 I   94  MET VAL ASP ARG GLU TRP VAL LEU LYS ILE ALA LYS LEU          
SEQRES   2 I   94  ALA ARG LEU GLU LEU LYS GLU GLU GLU ILE GLU VAL PHE          
SEQRES   3 I   94  GLN LYS GLN LEU SER ASP ILE LEU ASP PHE ILE ASP GLN          
SEQRES   4 I   94  LEU LYS GLU LEU ASP THR GLU ASN VAL GLU PRO TYR ILE          
SEQRES   5 I   94  GLN GLU PHE GLU GLU THR PRO MET ARG GLU ASP GLU PRO          
SEQRES   6 I   94  HIS PRO SER LEU ASP ARG GLU LYS ALA LEU MET ASN ALA          
SEQRES   7 I   94  PRO GLU ARG LYS ASP GLY PHE PHE VAL VAL PRO ARG VAL          
SEQRES   8 I   94  VAL GLU VAL                                                  
SEQRES   1 J  478  MET LEU TRP LYS LYS SER LEU SER GLU LEU ARG GLU LEU          
SEQRES   2 J  478  LEU LYS ARG GLY GLU VAL SER PRO LYS GLU VAL VAL GLU          
SEQRES   3 J  478  SER PHE TYR ASP ARG TYR ASN GLN THR GLU GLU LYS VAL          
SEQRES   4 J  478  LYS ALA TYR ILE THR PRO LEU TYR GLY LYS ALA LEU LYS          
SEQRES   5 J  478  GLN ALA GLU SER LEU LYS GLU ARG GLU LEU PRO LEU PHE          
SEQRES   6 J  478  GLY ILE PRO ILE ALA VAL LYS ASP ASN ILE LEU VAL GLU          
SEQRES   7 J  478  GLY GLU LYS THR THR CYS ALA SER LYS ILE LEU GLU ASN          
SEQRES   8 J  478  PHE VAL ALA PRO TYR ASP ALA THR VAL ILE GLU ARG LEU          
SEQRES   9 J  478  LYS LYS ALA GLY ALA LEU ILE VAL GLY LYS THR ASN LEU          
SEQRES  10 J  478  ASP GLU PHE ALA MET GLY SER SER THR GLU TYR SER ALA          
SEQRES  11 J  478  PHE PHE PRO THR LYS ASN PRO TRP ASP LEU GLU ARG VAL          
SEQRES  12 J  478  PRO GLY GLY SER SER GLY GLY SER ALA ALA SER VAL ALA          
SEQRES  13 J  478  VAL LEU SER ALA PRO VAL SER LEU GLY SER ASP THR GLY          
SEQRES  14 J  478  GLY SER ILE ARG GLN PRO ALA SER PHE CYS GLY VAL ILE          
SEQRES  15 J  478  GLY ILE LYS PRO THR TYR GLY ARG VAL SER ARG TYR GLY          
SEQRES  16 J  478  LEU VAL ALA PHE ALA SER SER LEU ASP GLN ILE GLY VAL          
SEQRES  17 J  478  PHE GLY ARG ARG THR GLU ASP VAL ALA LEU VAL LEU GLU          
SEQRES  18 J  478  VAL ILE SER GLY TRP ASP GLU LYS ASP SER THR SER ALA          
SEQRES  19 J  478  LYS VAL PRO VAL PRO GLU TRP SER GLU GLU VAL LYS LYS          
SEQRES  20 J  478  GLU VAL LYS GLY LEU LYS ILE GLY LEU PRO LYS GLU PHE          
SEQRES  21 J  478  PHE GLU TYR GLU LEU GLN PRO GLN VAL LYS GLU ALA PHE          
SEQRES  22 J  478  GLU ASN PHE ILE LYS GLU LEU GLU LYS GLU GLY PHE GLU          
SEQRES  23 J  478  ILE LYS GLU VAL SER LEU PRO HIS VAL LYS TYR SER ILE          
SEQRES  24 J  478  PRO THR TYR TYR ILE ILE ALA PRO SER GLU ALA SER SER          
SEQRES  25 J  478  ASN LEU ALA ARG TYR ASP GLY VAL ARG TYR GLY TYR ARG          
SEQRES  26 J  478  ALA LYS GLU TYR LYS ASP ILE PHE GLU MET TYR ALA ARG          
SEQRES  27 J  478  THR ARG ASP GLU GLY PHE GLY PRO GLU VAL LYS ARG ARG          
SEQRES  28 J  478  ILE MET LEU GLY THR PHE ALA LEU SER ALA GLY TYR TYR          
SEQRES  29 J  478  ASP ALA TYR TYR LEU LYS ALA GLN LYS VAL ARG ARG LEU          
SEQRES  30 J  478  ILE THR ASN ASP PHE LEU LYS ALA PHE GLU GLU VAL ASP          
SEQRES  31 J  478  VAL ILE ALA SER PRO THR THR PRO THR LEU PRO PHE LYS          
SEQRES  32 J  478  PHE GLY GLU ARG LEU GLU ASN PRO ILE GLU MET TYR LEU          
SEQRES  33 J  478  SER ASP ILE LEU THR VAL PRO ALA ASN LEU ALA GLY LEU          
SEQRES  34 J  478  PRO ALA ILE SER ILE PRO ILE ALA TRP LYS ASP GLY LEU          
SEQRES  35 J  478  PRO VAL GLY GLY GLN LEU ILE GLY LYS HIS TRP ASP GLU          
SEQRES  36 J  478  THR THR LEU LEU GLN ILE SER TYR LEU TRP GLU GLN LYS          
SEQRES  37 J  478  PHE LYS HIS TYR GLU LYS ILE PRO LEU THR                      
SEQRES   1 K  478  MET ASN GLU LYS TYR GLU ALA VAL ILE GLY LEU GLU ILE          
SEQRES   2 K  478  HIS VAL GLN MET ASP THR LYS THR LYS MET PHE CYS GLY          
SEQRES   3 K  478  CYS LYS VAL GLU PHE GLY ALA GLU PRO ASN THR ASN VAL          
SEQRES   4 K  478  CYS PRO VAL CYS LEU GLY MET PRO GLY ALA LEU PRO ILE          
SEQRES   5 K  478  VAL ASN LYS ARG ALA VAL GLU TYR ALA ILE ARG ALA SER          
SEQRES   6 K  478  LEU ALA LEU ASN CYS GLU VAL HIS GLU GLU SER VAL PHE          
SEQRES   7 K  478  ALA ARG LYS HIS TYR PHE TYR PRO ASP LEU PRO LYS GLY          
SEQRES   8 K  478  TYR GLN ILE SER GLN TYR GLU LYS PRO LEU ALA THR ASN          
SEQRES   9 K  478  GLY TRP VAL GLU LEU ASN LEU PRO ASN GLY GLU LYS LYS          
SEQRES  10 K  478  LYS VAL ARG ILE ARG ARG LEU HIS ILE GLU GLU ASP ALA          
SEQRES  11 K  478  GLY LYS ASN ILE HIS GLU GLY ASP LYS THR LEU VAL ASP          
SEQRES  12 K  478  LEU ASN ARG ALA GLY THR PRO LEU MET GLU ILE VAL THR          
SEQRES  13 K  478  GLU PRO ASP ILE ARG THR PRO GLU GLU ALA ARG LEU PHE          
SEQRES  14 K  478  LEU GLU LYS LEU ARG ASN ILE MET ARG TYR ALA GLY VAL          
SEQRES  15 K  478  SER LYS ALA ASP MET GLU LYS GLY GLN LEU ARG CYS ASP          
SEQRES  16 K  478  ILE ASN VAL SER ILE ARG PRO LYS GLY SER LYS GLU PHE          
SEQRES  17 K  478  GLY THR ARG VAL GLU ILE LYS ASN VAL ASN SER PHE ARG          
SEQRES  18 K  478  PHE VAL GLN LYS ALA LEU GLU TYR GLU ILE GLU ARG GLN          
SEQRES  19 K  478  ILE ASN VAL VAL GLU GLU GLY GLY GLU VAL VAL GLN GLU          
SEQRES  20 K  478  THR ARG THR PHE ASP PRO GLN THR GLY LYS THR TYR PRO          
SEQRES  21 K  478  MET ARG THR LYS GLU GLU ALA GLU ASP TYR ARG TYR PHE          
SEQRES  22 K  478  PRO ASP PRO ASP LEU VAL PRO LEU LYS VAL LYS LYS GLU          
SEQRES  23 K  478  TRP ILE GLU GLU ILE LYS LYS ASN MET PRO GLU LEU PRO          
SEQRES  24 K  478  ASP GLN ARG PHE GLU ARG LEU ILE LYS GLU TYR GLY LEU          
SEQRES  25 K  478  SER GLU TYR GLU ALA GLY ILE LEU VAL ASN HIS LYS GLU          
SEQRES  26 K  478  VAL GLY ASP PHE PHE GLU GLU ALA VAL ARG HIS PHE LYS          
SEQRES  27 K  478  GLU PRO LYS GLY ILE VAL ASN TRP LEU ILE ASN ASP LEU          
SEQRES  28 K  478  LEU GLY LEU LEU ARG ASP LYS GLY ILE SER ILE GLU GLU          
SEQRES  29 K  478  SER PRO VAL LYS PRO GLU HIS LEU ALA GLU LEU VAL LYS          
SEQRES  30 K  478  LEU ILE LYS GLU LYS VAL ILE SER THR LYS ILE GLY LYS          
SEQRES  31 K  478  GLU VAL ILE LYS GLU MET VAL GLU THR GLY LYS THR PRO          
SEQRES  32 K  478  SER GLN ILE VAL GLU GLU LYS GLY LEU LYS GLN ILE THR          
SEQRES  33 K  478  ASP GLU ASN GLN ILE LYS GLU LEU VAL LYS LYS ILE PHE          
SEQRES  34 K  478  GLU LYS HIS PRO LYS GLU VAL GLU ARG LEU LYS GLN GLY          
SEQRES  35 K  478  GLU GLU LYS LEU ILE GLY PHE PHE VAL GLY GLN VAL MET          
SEQRES  36 K  478  ARG GLU THR ARG GLY LYS ALA ASN PRO GLN VAL VAL ASN          
SEQRES  37 K  478  LYS VAL ILE ARG GLU LEU VAL LYS GLU VAL                      
SEQRES   1 L   94  MET VAL ASP ARG GLU TRP VAL LEU LYS ILE ALA LYS LEU          
SEQRES   2 L   94  ALA ARG LEU GLU LEU LYS GLU GLU GLU ILE GLU VAL PHE          
SEQRES   3 L   94  GLN LYS GLN LEU SER ASP ILE LEU ASP PHE ILE ASP GLN          
SEQRES   4 L   94  LEU LYS GLU LEU ASP THR GLU ASN VAL GLU PRO TYR ILE          
SEQRES   5 L   94  GLN GLU PHE GLU GLU THR PRO MET ARG GLU ASP GLU PRO          
SEQRES   6 L   94  HIS PRO SER LEU ASP ARG GLU LYS ALA LEU MET ASN ALA          
SEQRES   7 L   94  PRO GLU ARG LYS ASP GLY PHE PHE VAL VAL PRO ARG VAL          
SEQRES   8 L   94  VAL GLU VAL                                                  
SEQRES   1 M  478  MET LEU TRP LYS LYS SER LEU SER GLU LEU ARG GLU LEU          
SEQRES   2 M  478  LEU LYS ARG GLY GLU VAL SER PRO LYS GLU VAL VAL GLU          
SEQRES   3 M  478  SER PHE TYR ASP ARG TYR ASN GLN THR GLU GLU LYS VAL          
SEQRES   4 M  478  LYS ALA TYR ILE THR PRO LEU TYR GLY LYS ALA LEU LYS          
SEQRES   5 M  478  GLN ALA GLU SER LEU LYS GLU ARG GLU LEU PRO LEU PHE          
SEQRES   6 M  478  GLY ILE PRO ILE ALA VAL LYS ASP ASN ILE LEU VAL GLU          
SEQRES   7 M  478  GLY GLU LYS THR THR CYS ALA SER LYS ILE LEU GLU ASN          
SEQRES   8 M  478  PHE VAL ALA PRO TYR ASP ALA THR VAL ILE GLU ARG LEU          
SEQRES   9 M  478  LYS LYS ALA GLY ALA LEU ILE VAL GLY LYS THR ASN LEU          
SEQRES  10 M  478  ASP GLU PHE ALA MET GLY SER SER THR GLU TYR SER ALA          
SEQRES  11 M  478  PHE PHE PRO THR LYS ASN PRO TRP ASP LEU GLU ARG VAL          
SEQRES  12 M  478  PRO GLY GLY SER SER GLY GLY SER ALA ALA SER VAL ALA          
SEQRES  13 M  478  VAL LEU SER ALA PRO VAL SER LEU GLY SER ASP THR GLY          
SEQRES  14 M  478  GLY SER ILE ARG GLN PRO ALA SER PHE CYS GLY VAL ILE          
SEQRES  15 M  478  GLY ILE LYS PRO THR TYR GLY ARG VAL SER ARG TYR GLY          
SEQRES  16 M  478  LEU VAL ALA PHE ALA SER SER LEU ASP GLN ILE GLY VAL          
SEQRES  17 M  478  PHE GLY ARG ARG THR GLU ASP VAL ALA LEU VAL LEU GLU          
SEQRES  18 M  478  VAL ILE SER GLY TRP ASP GLU LYS ASP SER THR SER ALA          
SEQRES  19 M  478  LYS VAL PRO VAL PRO GLU TRP SER GLU GLU VAL LYS LYS          
SEQRES  20 M  478  GLU VAL LYS GLY LEU LYS ILE GLY LEU PRO LYS GLU PHE          
SEQRES  21 M  478  PHE GLU TYR GLU LEU GLN PRO GLN VAL LYS GLU ALA PHE          
SEQRES  22 M  478  GLU ASN PHE ILE LYS GLU LEU GLU LYS GLU GLY PHE GLU          
SEQRES  23 M  478  ILE LYS GLU VAL SER LEU PRO HIS VAL LYS TYR SER ILE          
SEQRES  24 M  478  PRO THR TYR TYR ILE ILE ALA PRO SER GLU ALA SER SER          
SEQRES  25 M  478  ASN LEU ALA ARG TYR ASP GLY VAL ARG TYR GLY TYR ARG          
SEQRES  26 M  478  ALA LYS GLU TYR LYS ASP ILE PHE GLU MET TYR ALA ARG          
SEQRES  27 M  478  THR ARG ASP GLU GLY PHE GLY PRO GLU VAL LYS ARG ARG          
SEQRES  28 M  478  ILE MET LEU GLY THR PHE ALA LEU SER ALA GLY TYR TYR          
SEQRES  29 M  478  ASP ALA TYR TYR LEU LYS ALA GLN LYS VAL ARG ARG LEU          
SEQRES  30 M  478  ILE THR ASN ASP PHE LEU LYS ALA PHE GLU GLU VAL ASP          
SEQRES  31 M  478  VAL ILE ALA SER PRO THR THR PRO THR LEU PRO PHE LYS          
SEQRES  32 M  478  PHE GLY GLU ARG LEU GLU ASN PRO ILE GLU MET TYR LEU          
SEQRES  33 M  478  SER ASP ILE LEU THR VAL PRO ALA ASN LEU ALA GLY LEU          
SEQRES  34 M  478  PRO ALA ILE SER ILE PRO ILE ALA TRP LYS ASP GLY LEU          
SEQRES  35 M  478  PRO VAL GLY GLY GLN LEU ILE GLY LYS HIS TRP ASP GLU          
SEQRES  36 M  478  THR THR LEU LEU GLN ILE SER TYR LEU TRP GLU GLN LYS          
SEQRES  37 M  478  PHE LYS HIS TYR GLU LYS ILE PRO LEU THR                      
SEQRES   1 N  478  MET ASN GLU LYS TYR GLU ALA VAL ILE GLY LEU GLU ILE          
SEQRES   2 N  478  HIS VAL GLN MET ASP THR LYS THR LYS MET PHE CYS GLY          
SEQRES   3 N  478  CYS LYS VAL GLU PHE GLY ALA GLU PRO ASN THR ASN VAL          
SEQRES   4 N  478  CYS PRO VAL CYS LEU GLY MET PRO GLY ALA LEU PRO ILE          
SEQRES   5 N  478  VAL ASN LYS ARG ALA VAL GLU TYR ALA ILE ARG ALA SER          
SEQRES   6 N  478  LEU ALA LEU ASN CYS GLU VAL HIS GLU GLU SER VAL PHE          
SEQRES   7 N  478  ALA ARG LYS HIS TYR PHE TYR PRO ASP LEU PRO LYS GLY          
SEQRES   8 N  478  TYR GLN ILE SER GLN TYR GLU LYS PRO LEU ALA THR ASN          
SEQRES   9 N  478  GLY TRP VAL GLU LEU ASN LEU PRO ASN GLY GLU LYS LYS          
SEQRES  10 N  478  LYS VAL ARG ILE ARG ARG LEU HIS ILE GLU GLU ASP ALA          
SEQRES  11 N  478  GLY LYS ASN ILE HIS GLU GLY ASP LYS THR LEU VAL ASP          
SEQRES  12 N  478  LEU ASN ARG ALA GLY THR PRO LEU MET GLU ILE VAL THR          
SEQRES  13 N  478  GLU PRO ASP ILE ARG THR PRO GLU GLU ALA ARG LEU PHE          
SEQRES  14 N  478  LEU GLU LYS LEU ARG ASN ILE MET ARG TYR ALA GLY VAL          
SEQRES  15 N  478  SER LYS ALA ASP MET GLU LYS GLY GLN LEU ARG CYS ASP          
SEQRES  16 N  478  ILE ASN VAL SER ILE ARG PRO LYS GLY SER LYS GLU PHE          
SEQRES  17 N  478  GLY THR ARG VAL GLU ILE LYS ASN VAL ASN SER PHE ARG          
SEQRES  18 N  478  PHE VAL GLN LYS ALA LEU GLU TYR GLU ILE GLU ARG GLN          
SEQRES  19 N  478  ILE ASN VAL VAL GLU GLU GLY GLY GLU VAL VAL GLN GLU          
SEQRES  20 N  478  THR ARG THR PHE ASP PRO GLN THR GLY LYS THR TYR PRO          
SEQRES  21 N  478  MET ARG THR LYS GLU GLU ALA GLU ASP TYR ARG TYR PHE          
SEQRES  22 N  478  PRO ASP PRO ASP LEU VAL PRO LEU LYS VAL LYS LYS GLU          
SEQRES  23 N  478  TRP ILE GLU GLU ILE LYS LYS ASN MET PRO GLU LEU PRO          
SEQRES  24 N  478  ASP GLN ARG PHE GLU ARG LEU ILE LYS GLU TYR GLY LEU          
SEQRES  25 N  478  SER GLU TYR GLU ALA GLY ILE LEU VAL ASN HIS LYS GLU          
SEQRES  26 N  478  VAL GLY ASP PHE PHE GLU GLU ALA VAL ARG HIS PHE LYS          
SEQRES  27 N  478  GLU PRO LYS GLY ILE VAL ASN TRP LEU ILE ASN ASP LEU          
SEQRES  28 N  478  LEU GLY LEU LEU ARG ASP LYS GLY ILE SER ILE GLU GLU          
SEQRES  29 N  478  SER PRO VAL LYS PRO GLU HIS LEU ALA GLU LEU VAL LYS          
SEQRES  30 N  478  LEU ILE LYS GLU LYS VAL ILE SER THR LYS ILE GLY LYS          
SEQRES  31 N  478  GLU VAL ILE LYS GLU MET VAL GLU THR GLY LYS THR PRO          
SEQRES  32 N  478  SER GLN ILE VAL GLU GLU LYS GLY LEU LYS GLN ILE THR          
SEQRES  33 N  478  ASP GLU ASN GLN ILE LYS GLU LEU VAL LYS LYS ILE PHE          
SEQRES  34 N  478  GLU LYS HIS PRO LYS GLU VAL GLU ARG LEU LYS GLN GLY          
SEQRES  35 N  478  GLU GLU LYS LEU ILE GLY PHE PHE VAL GLY GLN VAL MET          
SEQRES  36 N  478  ARG GLU THR ARG GLY LYS ALA ASN PRO GLN VAL VAL ASN          
SEQRES  37 N  478  LYS VAL ILE ARG GLU LEU VAL LYS GLU VAL                      
SEQRES   1 O   94  MET VAL ASP ARG GLU TRP VAL LEU LYS ILE ALA LYS LEU          
SEQRES   2 O   94  ALA ARG LEU GLU LEU LYS GLU GLU GLU ILE GLU VAL PHE          
SEQRES   3 O   94  GLN LYS GLN LEU SER ASP ILE LEU ASP PHE ILE ASP GLN          
SEQRES   4 O   94  LEU LYS GLU LEU ASP THR GLU ASN VAL GLU PRO TYR ILE          
SEQRES   5 O   94  GLN GLU PHE GLU GLU THR PRO MET ARG GLU ASP GLU PRO          
SEQRES   6 O   94  HIS PRO SER LEU ASP ARG GLU LYS ALA LEU MET ASN ALA          
SEQRES   7 O   94  PRO GLU ARG LYS ASP GLY PHE PHE VAL VAL PRO ARG VAL          
SEQRES   8 O   94  VAL GLU VAL                                                  
SEQRES   1 P  478  MET LEU TRP LYS LYS SER LEU SER GLU LEU ARG GLU LEU          
SEQRES   2 P  478  LEU LYS ARG GLY GLU VAL SER PRO LYS GLU VAL VAL GLU          
SEQRES   3 P  478  SER PHE TYR ASP ARG TYR ASN GLN THR GLU GLU LYS VAL          
SEQRES   4 P  478  LYS ALA TYR ILE THR PRO LEU TYR GLY LYS ALA LEU LYS          
SEQRES   5 P  478  GLN ALA GLU SER LEU LYS GLU ARG GLU LEU PRO LEU PHE          
SEQRES   6 P  478  GLY ILE PRO ILE ALA VAL LYS ASP ASN ILE LEU VAL GLU          
SEQRES   7 P  478  GLY GLU LYS THR THR CYS ALA SER LYS ILE LEU GLU ASN          
SEQRES   8 P  478  PHE VAL ALA PRO TYR ASP ALA THR VAL ILE GLU ARG LEU          
SEQRES   9 P  478  LYS LYS ALA GLY ALA LEU ILE VAL GLY LYS THR ASN LEU          
SEQRES  10 P  478  ASP GLU PHE ALA MET GLY SER SER THR GLU TYR SER ALA          
SEQRES  11 P  478  PHE PHE PRO THR LYS ASN PRO TRP ASP LEU GLU ARG VAL          
SEQRES  12 P  478  PRO GLY GLY SER SER GLY GLY SER ALA ALA SER VAL ALA          
SEQRES  13 P  478  VAL LEU SER ALA PRO VAL SER LEU GLY SER ASP THR GLY          
SEQRES  14 P  478  GLY SER ILE ARG GLN PRO ALA SER PHE CYS GLY VAL ILE          
SEQRES  15 P  478  GLY ILE LYS PRO THR TYR GLY ARG VAL SER ARG TYR GLY          
SEQRES  16 P  478  LEU VAL ALA PHE ALA SER SER LEU ASP GLN ILE GLY VAL          
SEQRES  17 P  478  PHE GLY ARG ARG THR GLU ASP VAL ALA LEU VAL LEU GLU          
SEQRES  18 P  478  VAL ILE SER GLY TRP ASP GLU LYS ASP SER THR SER ALA          
SEQRES  19 P  478  LYS VAL PRO VAL PRO GLU TRP SER GLU GLU VAL LYS LYS          
SEQRES  20 P  478  GLU VAL LYS GLY LEU LYS ILE GLY LEU PRO LYS GLU PHE          
SEQRES  21 P  478  PHE GLU TYR GLU LEU GLN PRO GLN VAL LYS GLU ALA PHE          
SEQRES  22 P  478  GLU ASN PHE ILE LYS GLU LEU GLU LYS GLU GLY PHE GLU          
SEQRES  23 P  478  ILE LYS GLU VAL SER LEU PRO HIS VAL LYS TYR SER ILE          
SEQRES  24 P  478  PRO THR TYR TYR ILE ILE ALA PRO SER GLU ALA SER SER          
SEQRES  25 P  478  ASN LEU ALA ARG TYR ASP GLY VAL ARG TYR GLY TYR ARG          
SEQRES  26 P  478  ALA LYS GLU TYR LYS ASP ILE PHE GLU MET TYR ALA ARG          
SEQRES  27 P  478  THR ARG ASP GLU GLY PHE GLY PRO GLU VAL LYS ARG ARG          
SEQRES  28 P  478  ILE MET LEU GLY THR PHE ALA LEU SER ALA GLY TYR TYR          
SEQRES  29 P  478  ASP ALA TYR TYR LEU LYS ALA GLN LYS VAL ARG ARG LEU          
SEQRES  30 P  478  ILE THR ASN ASP PHE LEU LYS ALA PHE GLU GLU VAL ASP          
SEQRES  31 P  478  VAL ILE ALA SER PRO THR THR PRO THR LEU PRO PHE LYS          
SEQRES  32 P  478  PHE GLY GLU ARG LEU GLU ASN PRO ILE GLU MET TYR LEU          
SEQRES  33 P  478  SER ASP ILE LEU THR VAL PRO ALA ASN LEU ALA GLY LEU          
SEQRES  34 P  478  PRO ALA ILE SER ILE PRO ILE ALA TRP LYS ASP GLY LEU          
SEQRES  35 P  478  PRO VAL GLY GLY GLN LEU ILE GLY LYS HIS TRP ASP GLU          
SEQRES  36 P  478  THR THR LEU LEU GLN ILE SER TYR LEU TRP GLU GLN LYS          
SEQRES  37 P  478  PHE LYS HIS TYR GLU LYS ILE PRO LEU THR                      
SEQRES   1 Q  478  MET ASN GLU LYS TYR GLU ALA VAL ILE GLY LEU GLU ILE          
SEQRES   2 Q  478  HIS VAL GLN MET ASP THR LYS THR LYS MET PHE CYS GLY          
SEQRES   3 Q  478  CYS LYS VAL GLU PHE GLY ALA GLU PRO ASN THR ASN VAL          
SEQRES   4 Q  478  CYS PRO VAL CYS LEU GLY MET PRO GLY ALA LEU PRO ILE          
SEQRES   5 Q  478  VAL ASN LYS ARG ALA VAL GLU TYR ALA ILE ARG ALA SER          
SEQRES   6 Q  478  LEU ALA LEU ASN CYS GLU VAL HIS GLU GLU SER VAL PHE          
SEQRES   7 Q  478  ALA ARG LYS HIS TYR PHE TYR PRO ASP LEU PRO LYS GLY          
SEQRES   8 Q  478  TYR GLN ILE SER GLN TYR GLU LYS PRO LEU ALA THR ASN          
SEQRES   9 Q  478  GLY TRP VAL GLU LEU ASN LEU PRO ASN GLY GLU LYS LYS          
SEQRES  10 Q  478  LYS VAL ARG ILE ARG ARG LEU HIS ILE GLU GLU ASP ALA          
SEQRES  11 Q  478  GLY LYS ASN ILE HIS GLU GLY ASP LYS THR LEU VAL ASP          
SEQRES  12 Q  478  LEU ASN ARG ALA GLY THR PRO LEU MET GLU ILE VAL THR          
SEQRES  13 Q  478  GLU PRO ASP ILE ARG THR PRO GLU GLU ALA ARG LEU PHE          
SEQRES  14 Q  478  LEU GLU LYS LEU ARG ASN ILE MET ARG TYR ALA GLY VAL          
SEQRES  15 Q  478  SER LYS ALA ASP MET GLU LYS GLY GLN LEU ARG CYS ASP          
SEQRES  16 Q  478  ILE ASN VAL SER ILE ARG PRO LYS GLY SER LYS GLU PHE          
SEQRES  17 Q  478  GLY THR ARG VAL GLU ILE LYS ASN VAL ASN SER PHE ARG          
SEQRES  18 Q  478  PHE VAL GLN LYS ALA LEU GLU TYR GLU ILE GLU ARG GLN          
SEQRES  19 Q  478  ILE ASN VAL VAL GLU GLU GLY GLY GLU VAL VAL GLN GLU          
SEQRES  20 Q  478  THR ARG THR PHE ASP PRO GLN THR GLY LYS THR TYR PRO          
SEQRES  21 Q  478  MET ARG THR LYS GLU GLU ALA GLU ASP TYR ARG TYR PHE          
SEQRES  22 Q  478  PRO ASP PRO ASP LEU VAL PRO LEU LYS VAL LYS LYS GLU          
SEQRES  23 Q  478  TRP ILE GLU GLU ILE LYS LYS ASN MET PRO GLU LEU PRO          
SEQRES  24 Q  478  ASP GLN ARG PHE GLU ARG LEU ILE LYS GLU TYR GLY LEU          
SEQRES  25 Q  478  SER GLU TYR GLU ALA GLY ILE LEU VAL ASN HIS LYS GLU          
SEQRES  26 Q  478  VAL GLY ASP PHE PHE GLU GLU ALA VAL ARG HIS PHE LYS          
SEQRES  27 Q  478  GLU PRO LYS GLY ILE VAL ASN TRP LEU ILE ASN ASP LEU          
SEQRES  28 Q  478  LEU GLY LEU LEU ARG ASP LYS GLY ILE SER ILE GLU GLU          
SEQRES  29 Q  478  SER PRO VAL LYS PRO GLU HIS LEU ALA GLU LEU VAL LYS          
SEQRES  30 Q  478  LEU ILE LYS GLU LYS VAL ILE SER THR LYS ILE GLY LYS          
SEQRES  31 Q  478  GLU VAL ILE LYS GLU MET VAL GLU THR GLY LYS THR PRO          
SEQRES  32 Q  478  SER GLN ILE VAL GLU GLU LYS GLY LEU LYS GLN ILE THR          
SEQRES  33 Q  478  ASP GLU ASN GLN ILE LYS GLU LEU VAL LYS LYS ILE PHE          
SEQRES  34 Q  478  GLU LYS HIS PRO LYS GLU VAL GLU ARG LEU LYS GLN GLY          
SEQRES  35 Q  478  GLU GLU LYS LEU ILE GLY PHE PHE VAL GLY GLN VAL MET          
SEQRES  36 Q  478  ARG GLU THR ARG GLY LYS ALA ASN PRO GLN VAL VAL ASN          
SEQRES  37 Q  478  LYS VAL ILE ARG GLU LEU VAL LYS GLU VAL                      
SEQRES   1 R   94  MET VAL ASP ARG GLU TRP VAL LEU LYS ILE ALA LYS LEU          
SEQRES   2 R   94  ALA ARG LEU GLU LEU LYS GLU GLU GLU ILE GLU VAL PHE          
SEQRES   3 R   94  GLN LYS GLN LEU SER ASP ILE LEU ASP PHE ILE ASP GLN          
SEQRES   4 R   94  LEU LYS GLU LEU ASP THR GLU ASN VAL GLU PRO TYR ILE          
SEQRES   5 R   94  GLN GLU PHE GLU GLU THR PRO MET ARG GLU ASP GLU PRO          
SEQRES   6 R   94  HIS PRO SER LEU ASP ARG GLU LYS ALA LEU MET ASN ALA          
SEQRES   7 R   94  PRO GLU ARG LYS ASP GLY PHE PHE VAL VAL PRO ARG VAL          
SEQRES   8 R   94  VAL GLU VAL                                                  
SEQRES   1 S  478  MET LEU TRP LYS LYS SER LEU SER GLU LEU ARG GLU LEU          
SEQRES   2 S  478  LEU LYS ARG GLY GLU VAL SER PRO LYS GLU VAL VAL GLU          
SEQRES   3 S  478  SER PHE TYR ASP ARG TYR ASN GLN THR GLU GLU LYS VAL          
SEQRES   4 S  478  LYS ALA TYR ILE THR PRO LEU TYR GLY LYS ALA LEU LYS          
SEQRES   5 S  478  GLN ALA GLU SER LEU LYS GLU ARG GLU LEU PRO LEU PHE          
SEQRES   6 S  478  GLY ILE PRO ILE ALA VAL LYS ASP ASN ILE LEU VAL GLU          
SEQRES   7 S  478  GLY GLU LYS THR THR CYS ALA SER LYS ILE LEU GLU ASN          
SEQRES   8 S  478  PHE VAL ALA PRO TYR ASP ALA THR VAL ILE GLU ARG LEU          
SEQRES   9 S  478  LYS LYS ALA GLY ALA LEU ILE VAL GLY LYS THR ASN LEU          
SEQRES  10 S  478  ASP GLU PHE ALA MET GLY SER SER THR GLU TYR SER ALA          
SEQRES  11 S  478  PHE PHE PRO THR LYS ASN PRO TRP ASP LEU GLU ARG VAL          
SEQRES  12 S  478  PRO GLY GLY SER SER GLY GLY SER ALA ALA SER VAL ALA          
SEQRES  13 S  478  VAL LEU SER ALA PRO VAL SER LEU GLY SER ASP THR GLY          
SEQRES  14 S  478  GLY SER ILE ARG GLN PRO ALA SER PHE CYS GLY VAL ILE          
SEQRES  15 S  478  GLY ILE LYS PRO THR TYR GLY ARG VAL SER ARG TYR GLY          
SEQRES  16 S  478  LEU VAL ALA PHE ALA SER SER LEU ASP GLN ILE GLY VAL          
SEQRES  17 S  478  PHE GLY ARG ARG THR GLU ASP VAL ALA LEU VAL LEU GLU          
SEQRES  18 S  478  VAL ILE SER GLY TRP ASP GLU LYS ASP SER THR SER ALA          
SEQRES  19 S  478  LYS VAL PRO VAL PRO GLU TRP SER GLU GLU VAL LYS LYS          
SEQRES  20 S  478  GLU VAL LYS GLY LEU LYS ILE GLY LEU PRO LYS GLU PHE          
SEQRES  21 S  478  PHE GLU TYR GLU LEU GLN PRO GLN VAL LYS GLU ALA PHE          
SEQRES  22 S  478  GLU ASN PHE ILE LYS GLU LEU GLU LYS GLU GLY PHE GLU          
SEQRES  23 S  478  ILE LYS GLU VAL SER LEU PRO HIS VAL LYS TYR SER ILE          
SEQRES  24 S  478  PRO THR TYR TYR ILE ILE ALA PRO SER GLU ALA SER SER          
SEQRES  25 S  478  ASN LEU ALA ARG TYR ASP GLY VAL ARG TYR GLY TYR ARG          
SEQRES  26 S  478  ALA LYS GLU TYR LYS ASP ILE PHE GLU MET TYR ALA ARG          
SEQRES  27 S  478  THR ARG ASP GLU GLY PHE GLY PRO GLU VAL LYS ARG ARG          
SEQRES  28 S  478  ILE MET LEU GLY THR PHE ALA LEU SER ALA GLY TYR TYR          
SEQRES  29 S  478  ASP ALA TYR TYR LEU LYS ALA GLN LYS VAL ARG ARG LEU          
SEQRES  30 S  478  ILE THR ASN ASP PHE LEU LYS ALA PHE GLU GLU VAL ASP          
SEQRES  31 S  478  VAL ILE ALA SER PRO THR THR PRO THR LEU PRO PHE LYS          
SEQRES  32 S  478  PHE GLY GLU ARG LEU GLU ASN PRO ILE GLU MET TYR LEU          
SEQRES  33 S  478  SER ASP ILE LEU THR VAL PRO ALA ASN LEU ALA GLY LEU          
SEQRES  34 S  478  PRO ALA ILE SER ILE PRO ILE ALA TRP LYS ASP GLY LEU          
SEQRES  35 S  478  PRO VAL GLY GLY GLN LEU ILE GLY LYS HIS TRP ASP GLU          
SEQRES  36 S  478  THR THR LEU LEU GLN ILE SER TYR LEU TRP GLU GLN LYS          
SEQRES  37 S  478  PHE LYS HIS TYR GLU LYS ILE PRO LEU THR                      
SEQRES   1 T  478  MET ASN GLU LYS TYR GLU ALA VAL ILE GLY LEU GLU ILE          
SEQRES   2 T  478  HIS VAL GLN MET ASP THR LYS THR LYS MET PHE CYS GLY          
SEQRES   3 T  478  CYS LYS VAL GLU PHE GLY ALA GLU PRO ASN THR ASN VAL          
SEQRES   4 T  478  CYS PRO VAL CYS LEU GLY MET PRO GLY ALA LEU PRO ILE          
SEQRES   5 T  478  VAL ASN LYS ARG ALA VAL GLU TYR ALA ILE ARG ALA SER          
SEQRES   6 T  478  LEU ALA LEU ASN CYS GLU VAL HIS GLU GLU SER VAL PHE          
SEQRES   7 T  478  ALA ARG LYS HIS TYR PHE TYR PRO ASP LEU PRO LYS GLY          
SEQRES   8 T  478  TYR GLN ILE SER GLN TYR GLU LYS PRO LEU ALA THR ASN          
SEQRES   9 T  478  GLY TRP VAL GLU LEU ASN LEU PRO ASN GLY GLU LYS LYS          
SEQRES  10 T  478  LYS VAL ARG ILE ARG ARG LEU HIS ILE GLU GLU ASP ALA          
SEQRES  11 T  478  GLY LYS ASN ILE HIS GLU GLY ASP LYS THR LEU VAL ASP          
SEQRES  12 T  478  LEU ASN ARG ALA GLY THR PRO LEU MET GLU ILE VAL THR          
SEQRES  13 T  478  GLU PRO ASP ILE ARG THR PRO GLU GLU ALA ARG LEU PHE          
SEQRES  14 T  478  LEU GLU LYS LEU ARG ASN ILE MET ARG TYR ALA GLY VAL          
SEQRES  15 T  478  SER LYS ALA ASP MET GLU LYS GLY GLN LEU ARG CYS ASP          
SEQRES  16 T  478  ILE ASN VAL SER ILE ARG PRO LYS GLY SER LYS GLU PHE          
SEQRES  17 T  478  GLY THR ARG VAL GLU ILE LYS ASN VAL ASN SER PHE ARG          
SEQRES  18 T  478  PHE VAL GLN LYS ALA LEU GLU TYR GLU ILE GLU ARG GLN          
SEQRES  19 T  478  ILE ASN VAL VAL GLU GLU GLY GLY GLU VAL VAL GLN GLU          
SEQRES  20 T  478  THR ARG THR PHE ASP PRO GLN THR GLY LYS THR TYR PRO          
SEQRES  21 T  478  MET ARG THR LYS GLU GLU ALA GLU ASP TYR ARG TYR PHE          
SEQRES  22 T  478  PRO ASP PRO ASP LEU VAL PRO LEU LYS VAL LYS LYS GLU          
SEQRES  23 T  478  TRP ILE GLU GLU ILE LYS LYS ASN MET PRO GLU LEU PRO          
SEQRES  24 T  478  ASP GLN ARG PHE GLU ARG LEU ILE LYS GLU TYR GLY LEU          
SEQRES  25 T  478  SER GLU TYR GLU ALA GLY ILE LEU VAL ASN HIS LYS GLU          
SEQRES  26 T  478  VAL GLY ASP PHE PHE GLU GLU ALA VAL ARG HIS PHE LYS          
SEQRES  27 T  478  GLU PRO LYS GLY ILE VAL ASN TRP LEU ILE ASN ASP LEU          
SEQRES  28 T  478  LEU GLY LEU LEU ARG ASP LYS GLY ILE SER ILE GLU GLU          
SEQRES  29 T  478  SER PRO VAL LYS PRO GLU HIS LEU ALA GLU LEU VAL LYS          
SEQRES  30 T  478  LEU ILE LYS GLU LYS VAL ILE SER THR LYS ILE GLY LYS          
SEQRES  31 T  478  GLU VAL ILE LYS GLU MET VAL GLU THR GLY LYS THR PRO          
SEQRES  32 T  478  SER GLN ILE VAL GLU GLU LYS GLY LEU LYS GLN ILE THR          
SEQRES  33 T  478  ASP GLU ASN GLN ILE LYS GLU LEU VAL LYS LYS ILE PHE          
SEQRES  34 T  478  GLU LYS HIS PRO LYS GLU VAL GLU ARG LEU LYS GLN GLY          
SEQRES  35 T  478  GLU GLU LYS LEU ILE GLY PHE PHE VAL GLY GLN VAL MET          
SEQRES  36 T  478  ARG GLU THR ARG GLY LYS ALA ASN PRO GLN VAL VAL ASN          
SEQRES  37 T  478  LYS VAL ILE ARG GLU LEU VAL LYS GLU VAL                      
SEQRES   1 U   94  MET VAL ASP ARG GLU TRP VAL LEU LYS ILE ALA LYS LEU          
SEQRES   2 U   94  ALA ARG LEU GLU LEU LYS GLU GLU GLU ILE GLU VAL PHE          
SEQRES   3 U   94  GLN LYS GLN LEU SER ASP ILE LEU ASP PHE ILE ASP GLN          
SEQRES   4 U   94  LEU LYS GLU LEU ASP THR GLU ASN VAL GLU PRO TYR ILE          
SEQRES   5 U   94  GLN GLU PHE GLU GLU THR PRO MET ARG GLU ASP GLU PRO          
SEQRES   6 U   94  HIS PRO SER LEU ASP ARG GLU LYS ALA LEU MET ASN ALA          
SEQRES   7 U   94  PRO GLU ARG LYS ASP GLY PHE PHE VAL VAL PRO ARG VAL          
SEQRES   8 U   94  VAL GLU VAL                                                  
SEQRES   1 V  478  MET LEU TRP LYS LYS SER LEU SER GLU LEU ARG GLU LEU          
SEQRES   2 V  478  LEU LYS ARG GLY GLU VAL SER PRO LYS GLU VAL VAL GLU          
SEQRES   3 V  478  SER PHE TYR ASP ARG TYR ASN GLN THR GLU GLU LYS VAL          
SEQRES   4 V  478  LYS ALA TYR ILE THR PRO LEU TYR GLY LYS ALA LEU LYS          
SEQRES   5 V  478  GLN ALA GLU SER LEU LYS GLU ARG GLU LEU PRO LEU PHE          
SEQRES   6 V  478  GLY ILE PRO ILE ALA VAL LYS ASP ASN ILE LEU VAL GLU          
SEQRES   7 V  478  GLY GLU LYS THR THR CYS ALA SER LYS ILE LEU GLU ASN          
SEQRES   8 V  478  PHE VAL ALA PRO TYR ASP ALA THR VAL ILE GLU ARG LEU          
SEQRES   9 V  478  LYS LYS ALA GLY ALA LEU ILE VAL GLY LYS THR ASN LEU          
SEQRES  10 V  478  ASP GLU PHE ALA MET GLY SER SER THR GLU TYR SER ALA          
SEQRES  11 V  478  PHE PHE PRO THR LYS ASN PRO TRP ASP LEU GLU ARG VAL          
SEQRES  12 V  478  PRO GLY GLY SER SER GLY GLY SER ALA ALA SER VAL ALA          
SEQRES  13 V  478  VAL LEU SER ALA PRO VAL SER LEU GLY SER ASP THR GLY          
SEQRES  14 V  478  GLY SER ILE ARG GLN PRO ALA SER PHE CYS GLY VAL ILE          
SEQRES  15 V  478  GLY ILE LYS PRO THR TYR GLY ARG VAL SER ARG TYR GLY          
SEQRES  16 V  478  LEU VAL ALA PHE ALA SER SER LEU ASP GLN ILE GLY VAL          
SEQRES  17 V  478  PHE GLY ARG ARG THR GLU ASP VAL ALA LEU VAL LEU GLU          
SEQRES  18 V  478  VAL ILE SER GLY TRP ASP GLU LYS ASP SER THR SER ALA          
SEQRES  19 V  478  LYS VAL PRO VAL PRO GLU TRP SER GLU GLU VAL LYS LYS          
SEQRES  20 V  478  GLU VAL LYS GLY LEU LYS ILE GLY LEU PRO LYS GLU PHE          
SEQRES  21 V  478  PHE GLU TYR GLU LEU GLN PRO GLN VAL LYS GLU ALA PHE          
SEQRES  22 V  478  GLU ASN PHE ILE LYS GLU LEU GLU LYS GLU GLY PHE GLU          
SEQRES  23 V  478  ILE LYS GLU VAL SER LEU PRO HIS VAL LYS TYR SER ILE          
SEQRES  24 V  478  PRO THR TYR TYR ILE ILE ALA PRO SER GLU ALA SER SER          
SEQRES  25 V  478  ASN LEU ALA ARG TYR ASP GLY VAL ARG TYR GLY TYR ARG          
SEQRES  26 V  478  ALA LYS GLU TYR LYS ASP ILE PHE GLU MET TYR ALA ARG          
SEQRES  27 V  478  THR ARG ASP GLU GLY PHE GLY PRO GLU VAL LYS ARG ARG          
SEQRES  28 V  478  ILE MET LEU GLY THR PHE ALA LEU SER ALA GLY TYR TYR          
SEQRES  29 V  478  ASP ALA TYR TYR LEU LYS ALA GLN LYS VAL ARG ARG LEU          
SEQRES  30 V  478  ILE THR ASN ASP PHE LEU LYS ALA PHE GLU GLU VAL ASP          
SEQRES  31 V  478  VAL ILE ALA SER PRO THR THR PRO THR LEU PRO PHE LYS          
SEQRES  32 V  478  PHE GLY GLU ARG LEU GLU ASN PRO ILE GLU MET TYR LEU          
SEQRES  33 V  478  SER ASP ILE LEU THR VAL PRO ALA ASN LEU ALA GLY LEU          
SEQRES  34 V  478  PRO ALA ILE SER ILE PRO ILE ALA TRP LYS ASP GLY LEU          
SEQRES  35 V  478  PRO VAL GLY GLY GLN LEU ILE GLY LYS HIS TRP ASP GLU          
SEQRES  36 V  478  THR THR LEU LEU GLN ILE SER TYR LEU TRP GLU GLN LYS          
SEQRES  37 V  478  PHE LYS HIS TYR GLU LYS ILE PRO LEU THR                      
SEQRES   1 W  478  MET ASN GLU LYS TYR GLU ALA VAL ILE GLY LEU GLU ILE          
SEQRES   2 W  478  HIS VAL GLN MET ASP THR LYS THR LYS MET PHE CYS GLY          
SEQRES   3 W  478  CYS LYS VAL GLU PHE GLY ALA GLU PRO ASN THR ASN VAL          
SEQRES   4 W  478  CYS PRO VAL CYS LEU GLY MET PRO GLY ALA LEU PRO ILE          
SEQRES   5 W  478  VAL ASN LYS ARG ALA VAL GLU TYR ALA ILE ARG ALA SER          
SEQRES   6 W  478  LEU ALA LEU ASN CYS GLU VAL HIS GLU GLU SER VAL PHE          
SEQRES   7 W  478  ALA ARG LYS HIS TYR PHE TYR PRO ASP LEU PRO LYS GLY          
SEQRES   8 W  478  TYR GLN ILE SER GLN TYR GLU LYS PRO LEU ALA THR ASN          
SEQRES   9 W  478  GLY TRP VAL GLU LEU ASN LEU PRO ASN GLY GLU LYS LYS          
SEQRES  10 W  478  LYS VAL ARG ILE ARG ARG LEU HIS ILE GLU GLU ASP ALA          
SEQRES  11 W  478  GLY LYS ASN ILE HIS GLU GLY ASP LYS THR LEU VAL ASP          
SEQRES  12 W  478  LEU ASN ARG ALA GLY THR PRO LEU MET GLU ILE VAL THR          
SEQRES  13 W  478  GLU PRO ASP ILE ARG THR PRO GLU GLU ALA ARG LEU PHE          
SEQRES  14 W  478  LEU GLU LYS LEU ARG ASN ILE MET ARG TYR ALA GLY VAL          
SEQRES  15 W  478  SER LYS ALA ASP MET GLU LYS GLY GLN LEU ARG CYS ASP          
SEQRES  16 W  478  ILE ASN VAL SER ILE ARG PRO LYS GLY SER LYS GLU PHE          
SEQRES  17 W  478  GLY THR ARG VAL GLU ILE LYS ASN VAL ASN SER PHE ARG          
SEQRES  18 W  478  PHE VAL GLN LYS ALA LEU GLU TYR GLU ILE GLU ARG GLN          
SEQRES  19 W  478  ILE ASN VAL VAL GLU GLU GLY GLY GLU VAL VAL GLN GLU          
SEQRES  20 W  478  THR ARG THR PHE ASP PRO GLN THR GLY LYS THR TYR PRO          
SEQRES  21 W  478  MET ARG THR LYS GLU GLU ALA GLU ASP TYR ARG TYR PHE          
SEQRES  22 W  478  PRO ASP PRO ASP LEU VAL PRO LEU LYS VAL LYS LYS GLU          
SEQRES  23 W  478  TRP ILE GLU GLU ILE LYS LYS ASN MET PRO GLU LEU PRO          
SEQRES  24 W  478  ASP GLN ARG PHE GLU ARG LEU ILE LYS GLU TYR GLY LEU          
SEQRES  25 W  478  SER GLU TYR GLU ALA GLY ILE LEU VAL ASN HIS LYS GLU          
SEQRES  26 W  478  VAL GLY ASP PHE PHE GLU GLU ALA VAL ARG HIS PHE LYS          
SEQRES  27 W  478  GLU PRO LYS GLY ILE VAL ASN TRP LEU ILE ASN ASP LEU          
SEQRES  28 W  478  LEU GLY LEU LEU ARG ASP LYS GLY ILE SER ILE GLU GLU          
SEQRES  29 W  478  SER PRO VAL LYS PRO GLU HIS LEU ALA GLU LEU VAL LYS          
SEQRES  30 W  478  LEU ILE LYS GLU LYS VAL ILE SER THR LYS ILE GLY LYS          
SEQRES  31 W  478  GLU VAL ILE LYS GLU MET VAL GLU THR GLY LYS THR PRO          
SEQRES  32 W  478  SER GLN ILE VAL GLU GLU LYS GLY LEU LYS GLN ILE THR          
SEQRES  33 W  478  ASP GLU ASN GLN ILE LYS GLU LEU VAL LYS LYS ILE PHE          
SEQRES  34 W  478  GLU LYS HIS PRO LYS GLU VAL GLU ARG LEU LYS GLN GLY          
SEQRES  35 W  478  GLU GLU LYS LEU ILE GLY PHE PHE VAL GLY GLN VAL MET          
SEQRES  36 W  478  ARG GLU THR ARG GLY LYS ALA ASN PRO GLN VAL VAL ASN          
SEQRES  37 W  478  LYS VAL ILE ARG GLU LEU VAL LYS GLU VAL                      
SEQRES   1 X   94  MET VAL ASP ARG GLU TRP VAL LEU LYS ILE ALA LYS LEU          
SEQRES   2 X   94  ALA ARG LEU GLU LEU LYS GLU GLU GLU ILE GLU VAL PHE          
SEQRES   3 X   94  GLN LYS GLN LEU SER ASP ILE LEU ASP PHE ILE ASP GLN          
SEQRES   4 X   94  LEU LYS GLU LEU ASP THR GLU ASN VAL GLU PRO TYR ILE          
SEQRES   5 X   94  GLN GLU PHE GLU GLU THR PRO MET ARG GLU ASP GLU PRO          
SEQRES   6 X   94  HIS PRO SER LEU ASP ARG GLU LYS ALA LEU MET ASN ALA          
SEQRES   7 X   94  PRO GLU ARG LYS ASP GLY PHE PHE VAL VAL PRO ARG VAL          
SEQRES   8 X   94  VAL GLU VAL                                                  
HET    ADP  B 701      27                                                       
HET     MG  B 801       1                                                       
HET     ZN  B 901       1                                                       
HET    ADP  E 702      27                                                       
HET     MG  E 802       1                                                       
HET     ZN  E 902       1                                                       
HET    ADP  H 703      27                                                       
HET     MG  H 803       1                                                       
HET     ZN  H 903       1                                                       
HET    ADP  K 704      27                                                       
HET     MG  K 804       1                                                       
HET     ZN  K 904       1                                                       
HET    ADP  N 705      27                                                       
HET     MG  N 805       1                                                       
HET     ZN  N 905       1                                                       
HET    ADP  Q 706      27                                                       
HET     MG  Q 806       1                                                       
HET     ZN  Q 906       1                                                       
HET    ADP  T 707      27                                                       
HET     MG  T 807       1                                                       
HET     ZN  T 907       1                                                       
HET    ADP  W 708      27                                                       
HET     MG  W 808       1                                                       
HET     ZN  W 908       1                                                       
HET    ASN  A 901       8                                                       
HET    ASN  D 902       8                                                       
HET    ASN  G 903       8                                                       
HET    ASN  J 904       8                                                       
HET    ASN  M 905       8                                                       
HET    ASN  P 906       8                                                       
HET    ASN  S 907       8                                                       
HET    ASN  V 908       8                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      ZN ZINC ION                                                         
HETNAM     ASN ASPARAGINE                                                       
FORMUL  25  ADP    8(C10 H15 N5 O10 P2)                                         
FORMUL  26   MG    8(MG 2+)                                                     
FORMUL  27   ZN    8(ZN 2+)                                                     
FORMUL  49  ASN    8(C4 H8 N2 O3)                                               
HELIX    1   1 SER A    6  ARG A   16  1                                  11    
HELIX    2   2 SER A   20  LYS A   40  1                                  21    
HELIX    3   3 LEU A   46  SER A   56  1                                  11    
HELIX    4   4 SER A   86  GLU A   90  5                                   5    
HELIX    5   5 ALA A   98  ALA A  107  1                                  10    
HELIX    6   6 ASP A  118  MET A  122  5                                   5    
HELIX    7   7 SER A  148  VAL A  157  1                                  10    
HELIX    8   8 ILE A  172  GLY A  180  1                                   9    
HELIX    9   9 ARG A  212  SER A  224  1                                  13    
HELIX   10  10 GLU A  240  VAL A  245  1                                   6    
HELIX   11  11 GLU A  259  TYR A  263  5                                   5    
HELIX   12  12 GLN A  266  GLU A  283  1                                  18    
HELIX   13  13 HIS A  294  LYS A  296  5                                   3    
HELIX   14  14 TYR A  297  LEU A  314  1                                  18    
HELIX   15  15 ASP A  331  PHE A  344  1                                  14    
HELIX   16  16 GLY A  345  LEU A  359  1                                  15    
HELIX   17  17 TYR A  367  PHE A  386  1                                  20    
HELIX   18  18 ASN A  410  LEU A  416  1                                   7    
HELIX   19  19 SER A  417  ILE A  419  5                                   3    
HELIX   20  20 THR A  421  GLY A  428  1                                   8    
HELIX   21  21 ASP A  454  PHE A  469  1                                  16    
HELIX   22  22 LYS A  470  LYS A  474  5                                   5    
HELIX   23  23 ASN B   54  LEU B   68  1                                  15    
HELIX   24  24 THR B  162  GLY B  181  1                                  20    
HELIX   25  25 ASP B  186  GLY B  190  5                                   5    
HELIX   26  26 SER B  219  GLU B  240  1                                  22    
HELIX   27  27 LYS B  284  ASN B  294  1                                  11    
HELIX   28  28 LEU B  298  TYR B  310  1                                  13    
HELIX   29  29 SER B  313  HIS B  323  1                                  11    
HELIX   30  30 HIS B  323  PHE B  337  1                                  15    
HELIX   31  31 GLU B  339  ASP B  350  1                                  12    
HELIX   32  32 ASP B  350  GLY B  359  1                                  10    
HELIX   33  33 SER B  361  SER B  365  5                                   5    
HELIX   34  34 LYS B  368  GLU B  381  1                                  14    
HELIX   35  35 SER B  385  GLY B  400  1                                  16    
HELIX   36  36 THR B  402  GLY B  411  1                                  10    
HELIX   37  37 ASP C    3  ALA C   14  1                                  12    
HELIX   38  38 LYS C   19  ILE C   37  1                                  19    
HELIX   39  39 GLN C   39  LEU C   43  5                                   5    
HELIX   40  40 ASP C   70  MET C   76  1                                   7    
HELIX   41  41 SER D    6  ARG D   16  1                                  11    
HELIX   42  42 SER D   20  LYS D   40  1                                  21    
HELIX   43  43 LEU D   46  SER D   56  1                                  11    
HELIX   44  44 SER D   86  GLU D   90  5                                   5    
HELIX   45  45 ALA D   98  ALA D  107  1                                  10    
HELIX   46  46 ASP D  118  MET D  122  5                                   5    
HELIX   47  47 SER D  148  VAL D  157  1                                  10    
HELIX   48  48 ILE D  172  GLY D  180  1                                   9    
HELIX   49  49 ARG D  212  SER D  224  1                                  13    
HELIX   50  50 GLU D  240  VAL D  245  1                                   6    
HELIX   51  51 GLU D  259  TYR D  263  5                                   5    
HELIX   52  52 GLN D  266  GLU D  283  1                                  18    
HELIX   53  53 HIS D  294  LYS D  296  5                                   3    
HELIX   54  54 TYR D  297  LEU D  314  1                                  18    
HELIX   55  55 ASP D  331  PHE D  344  1                                  14    
HELIX   56  56 GLY D  345  LEU D  359  1                                  15    
HELIX   57  57 TYR D  367  VAL D  389  1                                  23    
HELIX   58  58 ASN D  410  LEU D  416  1                                   7    
HELIX   59  59 SER D  417  ILE D  419  5                                   3    
HELIX   60  60 THR D  421  ALA D  427  1                                   7    
HELIX   61  61 ASP D  454  PHE D  469  1                                  16    
HELIX   62  62 LYS D  470  LYS D  474  5                                   5    
HELIX   63  63 LYS E   55  LEU E   68  1                                  14    
HELIX   64  64 THR E  162  GLY E  181  1                                  20    
HELIX   65  65 ASP E  186  GLY E  190  5                                   5    
HELIX   66  66 SER E  219  GLU E  240  1                                  22    
HELIX   67  67 LYS E  284  ASN E  294  1                                  11    
HELIX   68  68 LEU E  298  TYR E  310  1                                  13    
HELIX   69  69 SER E  313  HIS E  323  1                                  11    
HELIX   70  70 HIS E  323  PHE E  337  1                                  15    
HELIX   71  71 GLU E  339  ASP E  350  1                                  12    
HELIX   72  72 ASP E  350  GLY E  359  1                                  10    
HELIX   73  73 SER E  361  SER E  365  5                                   5    
HELIX   74  74 LYS E  368  GLU E  381  1                                  14    
HELIX   75  75 SER E  385  GLY E  400  1                                  16    
HELIX   76  76 THR E  402  GLY E  411  1                                  10    
HELIX   77  77 ASP F    3  ALA F   14  1                                  12    
HELIX   78  78 LYS F   19  ILE F   37  1                                  19    
HELIX   79  79 GLN F   39  LEU F   43  5                                   5    
HELIX   80  80 ASP F   70  MET F   76  1                                   7    
HELIX   81  81 SER G    6  ARG G   16  1                                  11    
HELIX   82  82 SER G   20  LYS G   40  1                                  21    
HELIX   83  83 LEU G   46  SER G   56  1                                  11    
HELIX   84  84 SER G   86  GLU G   90  5                                   5    
HELIX   85  85 ALA G   98  ALA G  107  1                                  10    
HELIX   86  86 ASP G  118  MET G  122  5                                   5    
HELIX   87  87 SER G  148  VAL G  157  1                                  10    
HELIX   88  88 ILE G  172  GLY G  180  1                                   9    
HELIX   89  89 ARG G  212  SER G  224  1                                  13    
HELIX   90  90 GLU G  240  VAL G  245  1                                   6    
HELIX   91  91 GLU G  259  TYR G  263  5                                   5    
HELIX   92  92 GLN G  266  GLU G  283  1                                  18    
HELIX   93  93 HIS G  294  LYS G  296  5                                   3    
HELIX   94  94 TYR G  297  LEU G  314  1                                  18    
HELIX   95  95 ASP G  331  PHE G  344  1                                  14    
HELIX   96  96 GLY G  345  LEU G  359  1                                  15    
HELIX   97  97 TYR G  367  PHE G  386  1                                  20    
HELIX   98  98 ASN G  410  LEU G  416  1                                   7    
HELIX   99  99 SER G  417  ILE G  419  5                                   3    
HELIX  100 100 THR G  421  ALA G  427  1                                   7    
HELIX  101 101 ASP G  454  PHE G  469  1                                  16    
HELIX  102 102 LYS G  470  LYS G  474  5                                   5    
HELIX  103 103 LYS H   55  LEU H   68  1                                  14    
HELIX  104 104 THR H  162  GLY H  181  1                                  20    
HELIX  105 105 ASP H  186  GLY H  190  5                                   5    
HELIX  106 106 SER H  219  GLU H  240  1                                  22    
HELIX  107 107 LYS H  284  ASN H  294  1                                  11    
HELIX  108 108 LEU H  298  TYR H  310  1                                  13    
HELIX  109 109 SER H  313  HIS H  323  1                                  11    
HELIX  110 110 HIS H  323  PHE H  337  1                                  15    
HELIX  111 111 GLU H  339  ASP H  350  1                                  12    
HELIX  112 112 ASP H  350  GLY H  359  1                                  10    
HELIX  113 113 SER H  361  SER H  365  5                                   5    
HELIX  114 114 LYS H  368  GLU H  381  1                                  14    
HELIX  115 115 SER H  385  GLY H  400  1                                  16    
HELIX  116 116 THR H  402  GLY H  411  1                                  10    
HELIX  117 117 ASP I    3  ALA I   14  1                                  12    
HELIX  118 118 LYS I   19  ILE I   37  1                                  19    
HELIX  119 119 GLN I   39  LEU I   43  5                                   5    
HELIX  120 120 ASP I   70  MET I   76  1                                   7    
HELIX  121 121 SER J    6  ARG J   16  1                                  11    
HELIX  122 122 SER J   20  LYS J   40  1                                  21    
HELIX  123 123 LEU J   46  SER J   56  1                                  11    
HELIX  124 124 SER J   86  GLU J   90  5                                   5    
HELIX  125 125 ALA J   98  ALA J  107  1                                  10    
HELIX  126 126 ASP J  118  MET J  122  5                                   5    
HELIX  127 127 SER J  148  VAL J  157  1                                  10    
HELIX  128 128 ILE J  172  GLY J  180  1                                   9    
HELIX  129 129 ARG J  212  SER J  224  1                                  13    
HELIX  130 130 GLU J  240  VAL J  245  1                                   6    
HELIX  131 131 GLU J  259  TYR J  263  5                                   5    
HELIX  132 132 GLN J  266  GLU J  283  1                                  18    
HELIX  133 133 HIS J  294  LYS J  296  5                                   3    
HELIX  134 134 TYR J  297  LEU J  314  1                                  18    
HELIX  135 135 ASP J  331  PHE J  344  1                                  14    
HELIX  136 136 GLY J  345  LEU J  359  1                                  15    
HELIX  137 137 TYR J  367  PHE J  386  1                                  20    
HELIX  138 138 ASN J  410  LEU J  416  1                                   7    
HELIX  139 139 SER J  417  ILE J  419  5                                   3    
HELIX  140 140 THR J  421  ALA J  427  1                                   7    
HELIX  141 141 ASP J  454  PHE J  469  1                                  16    
HELIX  142 142 LYS J  470  LYS J  474  5                                   5    
HELIX  143 143 LYS K   55  LEU K   68  1                                  14    
HELIX  144 144 THR K  162  GLY K  181  1                                  20    
HELIX  145 145 ASP K  186  GLY K  190  5                                   5    
HELIX  146 146 SER K  219  GLU K  240  1                                  22    
HELIX  147 147 LYS K  284  ASN K  294  1                                  11    
HELIX  148 148 LEU K  298  TYR K  310  1                                  13    
HELIX  149 149 SER K  313  HIS K  323  1                                  11    
HELIX  150 150 HIS K  323  PHE K  337  1                                  15    
HELIX  151 151 GLU K  339  ASP K  350  1                                  12    
HELIX  152 152 ASP K  350  GLY K  359  1                                  10    
HELIX  153 153 SER K  361  SER K  365  5                                   5    
HELIX  154 154 LYS K  368  GLU K  381  1                                  14    
HELIX  155 155 SER K  385  GLY K  400  1                                  16    
HELIX  156 156 THR K  402  GLY K  411  1                                  10    
HELIX  157 157 ASP L    3  ALA L   14  1                                  12    
HELIX  158 158 LYS L   19  ILE L   37  1                                  19    
HELIX  159 159 GLN L   39  LEU L   43  5                                   5    
HELIX  160 160 ASP L   70  MET L   76  1                                   7    
HELIX  161 161 SER M    6  ARG M   16  1                                  11    
HELIX  162 162 SER M   20  LYS M   40  1                                  21    
HELIX  163 163 LEU M   46  SER M   56  1                                  11    
HELIX  164 164 SER M   86  GLU M   90  5                                   5    
HELIX  165 165 ALA M   98  ALA M  107  1                                  10    
HELIX  166 166 ASP M  118  MET M  122  5                                   5    
HELIX  167 167 SER M  148  VAL M  157  1                                  10    
HELIX  168 168 ILE M  172  GLY M  180  1                                   9    
HELIX  169 169 ARG M  212  SER M  224  1                                  13    
HELIX  170 170 GLU M  240  VAL M  245  1                                   6    
HELIX  171 171 GLU M  259  TYR M  263  5                                   5    
HELIX  172 172 GLN M  266  GLU M  283  1                                  18    
HELIX  173 173 HIS M  294  LYS M  296  5                                   3    
HELIX  174 174 TYR M  297  LEU M  314  1                                  18    
HELIX  175 175 ASP M  331  PHE M  344  1                                  14    
HELIX  176 176 GLY M  345  LEU M  359  1                                  15    
HELIX  177 177 TYR M  367  PHE M  386  1                                  20    
HELIX  178 178 ASN M  410  LEU M  416  1                                   7    
HELIX  179 179 SER M  417  ILE M  419  5                                   3    
HELIX  180 180 THR M  421  ALA M  427  1                                   7    
HELIX  181 181 ASP M  454  PHE M  469  1                                  16    
HELIX  182 182 LYS M  470  LYS M  474  5                                   5    
HELIX  183 183 LYS N   55  LEU N   68  1                                  14    
HELIX  184 184 THR N  162  GLY N  181  1                                  20    
HELIX  185 185 ASP N  186  GLY N  190  5                                   5    
HELIX  186 186 SER N  219  GLU N  240  1                                  22    
HELIX  187 187 LYS N  284  ASN N  294  1                                  11    
HELIX  188 188 LEU N  298  TYR N  310  1                                  13    
HELIX  189 189 SER N  313  HIS N  323  1                                  11    
HELIX  190 190 HIS N  323  PHE N  337  1                                  15    
HELIX  191 191 GLU N  339  ASP N  350  1                                  12    
HELIX  192 192 ASP N  350  GLY N  359  1                                  10    
HELIX  193 193 SER N  361  SER N  365  5                                   5    
HELIX  194 194 LYS N  368  GLU N  381  1                                  14    
HELIX  195 195 SER N  385  THR N  399  1                                  15    
HELIX  196 196 THR N  402  GLY N  411  1                                  10    
HELIX  197 197 ASP O    3  ALA O   14  1                                  12    
HELIX  198 198 LYS O   19  ILE O   37  1                                  19    
HELIX  199 199 GLN O   39  LEU O   43  5                                   5    
HELIX  200 200 ASP O   70  MET O   76  1                                   7    
HELIX  201 201 SER P    6  ARG P   16  1                                  11    
HELIX  202 202 SER P   20  LYS P   40  1                                  21    
HELIX  203 203 LEU P   46  SER P   56  1                                  11    
HELIX  204 204 ALA P   98  ALA P  107  1                                  10    
HELIX  205 205 ASP P  118  MET P  122  5                                   5    
HELIX  206 206 SER P  148  VAL P  157  1                                  10    
HELIX  207 207 ILE P  172  GLY P  180  1                                   9    
HELIX  208 208 ARG P  212  SER P  224  1                                  13    
HELIX  209 209 GLU P  240  VAL P  245  1                                   6    
HELIX  210 210 GLU P  259  TYR P  263  5                                   5    
HELIX  211 211 GLN P  266  GLU P  283  1                                  18    
HELIX  212 212 HIS P  294  LYS P  296  5                                   3    
HELIX  213 213 TYR P  297  LEU P  314  1                                  18    
HELIX  214 214 ASP P  331  PHE P  344  1                                  14    
HELIX  215 215 GLY P  345  LEU P  359  1                                  15    
HELIX  216 216 TYR P  367  PHE P  386  1                                  20    
HELIX  217 217 ASN P  410  LEU P  416  1                                   7    
HELIX  218 218 SER P  417  ILE P  419  5                                   3    
HELIX  219 219 THR P  421  ALA P  427  1                                   7    
HELIX  220 220 ASP P  454  PHE P  469  1                                  16    
HELIX  221 221 LYS P  470  LYS P  474  5                                   5    
HELIX  222 222 ASN Q   54  LEU Q   68  1                                  15    
HELIX  223 223 THR Q  162  ALA Q  180  1                                  19    
HELIX  224 224 ASP Q  186  GLY Q  190  5                                   5    
HELIX  225 225 SER Q  219  GLU Q  240  1                                  22    
HELIX  226 226 LYS Q  284  ASN Q  294  1                                  11    
HELIX  227 227 LEU Q  298  TYR Q  310  1                                  13    
HELIX  228 228 SER Q  313  HIS Q  323  1                                  11    
HELIX  229 229 HIS Q  323  PHE Q  337  1                                  15    
HELIX  230 230 GLU Q  339  ASP Q  350  1                                  12    
HELIX  231 231 ASP Q  350  GLY Q  359  1                                  10    
HELIX  232 232 SER Q  361  SER Q  365  5                                   5    
HELIX  233 233 LYS Q  368  GLU Q  381  1                                  14    
HELIX  234 234 SER Q  385  GLY Q  400  1                                  16    
HELIX  235 235 THR Q  402  GLY Q  411  1                                  10    
HELIX  236 236 ASP R    3  ALA R   14  1                                  12    
HELIX  237 237 LYS R   19  ILE R   37  1                                  19    
HELIX  238 238 GLN R   39  LEU R   43  5                                   5    
HELIX  239 239 ASP R   70  MET R   76  1                                   7    
HELIX  240 240 SER S    6  ARG S   16  1                                  11    
HELIX  241 241 SER S   20  LYS S   40  1                                  21    
HELIX  242 242 LEU S   46  SER S   56  1                                  11    
HELIX  243 243 SER S   86  GLU S   90  5                                   5    
HELIX  244 244 ALA S   98  ALA S  107  1                                  10    
HELIX  245 245 ASP S  118  MET S  122  5                                   5    
HELIX  246 246 SER S  148  VAL S  157  1                                  10    
HELIX  247 247 ILE S  172  GLY S  180  1                                   9    
HELIX  248 248 ARG S  212  SER S  224  1                                  13    
HELIX  249 249 GLU S  240  VAL S  245  1                                   6    
HELIX  250 250 GLU S  259  TYR S  263  5                                   5    
HELIX  251 251 GLN S  266  GLU S  283  1                                  18    
HELIX  252 252 HIS S  294  LYS S  296  5                                   3    
HELIX  253 253 TYR S  297  LEU S  314  1                                  18    
HELIX  254 254 ASP S  331  PHE S  344  1                                  14    
HELIX  255 255 GLY S  345  LEU S  359  1                                  15    
HELIX  256 256 TYR S  367  VAL S  389  1                                  23    
HELIX  257 257 ASN S  410  LEU S  416  1                                   7    
HELIX  258 258 SER S  417  ILE S  419  5                                   3    
HELIX  259 259 THR S  421  ALA S  427  1                                   7    
HELIX  260 260 ASP S  454  PHE S  469  1                                  16    
HELIX  261 261 LYS S  470  LYS S  474  5                                   5    
HELIX  262 262 ASN T   54  LEU T   68  1                                  15    
HELIX  263 263 THR T  162  GLY T  181  1                                  20    
HELIX  264 264 ASP T  186  GLY T  190  5                                   5    
HELIX  265 265 SER T  219  GLU T  240  1                                  22    
HELIX  266 266 LYS T  284  ASN T  294  1                                  11    
HELIX  267 267 LEU T  298  TYR T  310  1                                  13    
HELIX  268 268 SER T  313  HIS T  323  1                                  11    
HELIX  269 269 HIS T  323  PHE T  337  1                                  15    
HELIX  270 270 GLU T  339  ASP T  350  1                                  12    
HELIX  271 271 ASP T  350  GLY T  359  1                                  10    
HELIX  272 272 SER T  361  SER T  365  5                                   5    
HELIX  273 273 LYS T  368  GLU T  381  1                                  14    
HELIX  274 274 SER T  385  GLY T  400  1                                  16    
HELIX  275 275 THR T  402  GLY T  411  1                                  10    
HELIX  276 276 ASP U    3  ALA U   14  1                                  12    
HELIX  277 277 LYS U   19  ILE U   37  1                                  19    
HELIX  278 278 GLN U   39  LEU U   43  5                                   5    
HELIX  279 279 ASP U   70  MET U   76  1                                   7    
HELIX  280 280 SER V    6  ARG V   16  1                                  11    
HELIX  281 281 SER V   20  LYS V   40  1                                  21    
HELIX  282 282 LEU V   46  SER V   56  1                                  11    
HELIX  283 283 SER V   86  GLU V   90  5                                   5    
HELIX  284 284 ALA V   98  ALA V  107  1                                  10    
HELIX  285 285 ASP V  118  MET V  122  5                                   5    
HELIX  286 286 SER V  148  VAL V  157  1                                  10    
HELIX  287 287 ILE V  172  GLY V  180  1                                   9    
HELIX  288 288 ARG V  212  SER V  224  1                                  13    
HELIX  289 289 GLU V  240  VAL V  245  1                                   6    
HELIX  290 290 GLU V  259  TYR V  263  5                                   5    
HELIX  291 291 GLN V  266  GLU V  283  1                                  18    
HELIX  292 292 HIS V  294  LYS V  296  5                                   3    
HELIX  293 293 TYR V  297  LEU V  314  1                                  18    
HELIX  294 294 ASP V  331  PHE V  344  1                                  14    
HELIX  295 295 GLY V  345  LEU V  359  1                                  15    
HELIX  296 296 TYR V  367  PHE V  386  1                                  20    
HELIX  297 297 ASN V  410  LEU V  416  1                                   7    
HELIX  298 298 SER V  417  ILE V  419  5                                   3    
HELIX  299 299 THR V  421  ALA V  427  1                                   7    
HELIX  300 300 ASP V  454  PHE V  469  1                                  16    
HELIX  301 301 LYS V  470  LYS V  474  5                                   5    
HELIX  302 302 ASN W   54  LEU W   68  1                                  15    
HELIX  303 303 THR W  162  GLY W  181  1                                  20    
HELIX  304 304 ASP W  186  GLY W  190  5                                   5    
HELIX  305 305 SER W  219  GLU W  240  1                                  22    
HELIX  306 306 LYS W  284  ASN W  294  1                                  11    
HELIX  307 307 LEU W  298  TYR W  310  1                                  13    
HELIX  308 308 SER W  313  HIS W  323  1                                  11    
HELIX  309 309 HIS W  323  PHE W  337  1                                  15    
HELIX  310 310 GLU W  339  ASP W  350  1                                  12    
HELIX  311 311 ASP W  350  GLY W  359  1                                  10    
HELIX  312 312 SER W  361  SER W  365  5                                   5    
HELIX  313 313 LYS W  368  GLU W  381  1                                  14    
HELIX  314 314 SER W  385  GLY W  400  1                                  16    
HELIX  315 315 THR W  402  GLY W  411  1                                  10    
HELIX  316 316 ASP X    3  ALA X   14  1                                  12    
HELIX  317 317 LYS X   19  ILE X   37  1                                  19    
HELIX  318 318 GLN X   39  LEU X   43  5                                   5    
HELIX  319 319 ASP X   70  MET X   76  1                                   7    
SHEET    1   A11 TYR A  42  PRO A  45  0                                        
SHEET    2   A11 LEU A 110  THR A 115 -1  O  LYS A 114   N  ILE A  43           
SHEET    3   A11 PRO A  68  LYS A  72  1  N  VAL A  71   O  THR A 115           
SHEET    4   A11 SER A 163  SER A 166  1  O  LEU A 164   N  ALA A  70           
SHEET    5   A11 ILE A 206  GLY A 210 -1  O  PHE A 209   N  SER A 163           
SHEET    6   A11 ILE A 182  LYS A 185 -1  N  ILE A 182   O  GLY A 210           
SHEET    7   A11 ALA A 431  LYS A 439 -1  O  SER A 433   N  GLY A 183           
SHEET    8   A11 LEU A 442  GLY A 450 -1  O  GLY A 446   N  ILE A 434           
SHEET    9   A11 VAL A 391  PRO A 395 -1  N  SER A 394   O  GLN A 447           
SHEET   10   A11 LYS A 253  PRO A 257  1  N  GLY A 255   O  ALA A 393           
SHEET   11   A11 GLU A 286  VAL A 290  1  O  LYS A 288   N  ILE A 254           
SHEET    1   B 9 GLU B  71  VAL B  72  0                                        
SHEET    2   B 9 ALA B 102  ASN B 110 -1  O  THR B 103   N  GLU B  71           
SHEET    3   B 9 LYS B 116  GLU B 128 -1  O  LYS B 117   N  LEU B 109           
SHEET    4   B 9 PRO B 150  THR B 156 -1  O  LEU B 151   N  GLU B 127           
SHEET    5   B 9 TYR B   5  GLN B  16 -1  N  ILE B  13   O  ILE B 154           
SHEET    6   B 9 LEU B 192  PRO B 202 -1  O  SER B 199   N  VAL B   8           
SHEET    7   B 9 VAL B 212  LYS B 215 -1  O  ILE B 214   N  ILE B 196           
SHEET    8   B 9 THR B 248  ASP B 252  1  O  ARG B 249   N  GLU B 213           
SHEET    9   B 9 LYS B 257  TYR B 259 -1  O  TYR B 259   N  THR B 250           
SHEET    1   C 2 GLU B  75  SER B  76  0                                        
SHEET    2   C 2 LEU B 281  LYS B 282 -1  O  LEU B 281   N  SER B  76           
SHEET    1   D 3 TYR B  92  GLN B  96  0                                        
SHEET    2   D 3 PHE B  78  HIS B  82 -1  N  ALA B  79   O  SER B  95           
SHEET    3   D 3 PHE B 273  PRO B 274 -1  O  PHE B 273   N  ARG B  80           
SHEET    1   E 4 LYS B 132  GLU B 136  0                                        
SHEET    2   E 4 LYS B 139  ASP B 143 -1  O  LEU B 141   N  ILE B 134           
SHEET    3   E 4 PHE C  85  PRO C  89 -1  O  VAL C  88   N  THR B 140           
SHEET    4   E 4 ARG C  81  LYS C  82 -1  N  LYS C  82   O  PHE C  85           
SHEET    1   F11 TYR D  42  PRO D  45  0                                        
SHEET    2   F11 LEU D 110  THR D 115 -1  O  LYS D 114   N  ILE D  43           
SHEET    3   F11 PRO D  68  LYS D  72  1  N  VAL D  71   O  THR D 115           
SHEET    4   F11 VAL D 162  SER D 166  1  O  LEU D 164   N  ALA D  70           
SHEET    5   F11 ILE D 206  GLY D 210 -1  O  PHE D 209   N  SER D 163           
SHEET    6   F11 ILE D 182  LYS D 185 -1  N  ILE D 182   O  GLY D 210           
SHEET    7   F11 ALA D 431  LYS D 439 -1  O  SER D 433   N  GLY D 183           
SHEET    8   F11 LEU D 442  GLY D 450 -1  O  GLY D 446   N  ILE D 434           
SHEET    9   F11 VAL D 391  PRO D 395 -1  N  SER D 394   O  GLN D 447           
SHEET   10   F11 LYS D 253  PRO D 257  1  N  GLY D 255   O  VAL D 391           
SHEET   11   F11 GLU D 286  VAL D 290  1  O  LYS D 288   N  ILE D 254           
SHEET    1   G 9 GLU E  71  VAL E  72  0                                        
SHEET    2   G 9 ALA E 102  ASN E 110 -1  O  THR E 103   N  GLU E  71           
SHEET    3   G 9 LYS E 116  GLU E 128 -1  O  LYS E 117   N  LEU E 109           
SHEET    4   G 9 PRO E 150  THR E 156 -1  O  LEU E 151   N  GLU E 127           
SHEET    5   G 9 TYR E   5  GLN E  16 -1  N  ILE E  13   O  ILE E 154           
SHEET    6   G 9 LEU E 192  PRO E 202 -1  O  SER E 199   N  VAL E   8           
SHEET    7   G 9 VAL E 212  LYS E 215 -1  O  VAL E 212   N  VAL E 198           
SHEET    8   G 9 THR E 248  ASP E 252  1  O  ARG E 249   N  GLU E 213           
SHEET    9   G 9 LYS E 257  TYR E 259 -1  O  TYR E 259   N  THR E 250           
SHEET    1   H 2 VAL E  53  ASN E  54  0                                        
SHEET    2   H 2 MET F  60  ARG F  61  1  O  ARG F  61   N  VAL E  53           
SHEET    1   I 2 GLU E  75  SER E  76  0                                        
SHEET    2   I 2 LEU E 281  LYS E 282 -1  O  LEU E 281   N  SER E  76           
SHEET    1   J 3 TYR E  92  GLN E  96  0                                        
SHEET    2   J 3 PHE E  78  HIS E  82 -1  N  ALA E  79   O  SER E  95           
SHEET    3   J 3 PHE E 273  PRO E 274 -1  O  PHE E 273   N  ARG E  80           
SHEET    1   K 4 LYS E 132  GLU E 136  0                                        
SHEET    2   K 4 LYS E 139  ASP E 143 -1  O  LEU E 141   N  ILE E 134           
SHEET    3   K 4 PHE F  85  PRO F  89 -1  O  VAL F  88   N  THR E 140           
SHEET    4   K 4 ARG F  81  LYS F  82 -1  N  LYS F  82   O  PHE F  85           
SHEET    1   L11 TYR G  42  PRO G  45  0                                        
SHEET    2   L11 LEU G 110  THR G 115 -1  O  LYS G 114   N  THR G  44           
SHEET    3   L11 PRO G  68  LYS G  72  1  N  VAL G  71   O  THR G 115           
SHEET    4   L11 SER G 163  SER G 166  1  O  LEU G 164   N  ALA G  70           
SHEET    5   L11 ILE G 206  GLY G 210 -1  O  PHE G 209   N  SER G 163           
SHEET    6   L11 ILE G 182  LYS G 185 -1  N  ILE G 184   O  VAL G 208           
SHEET    7   L11 ALA G 431  LYS G 439 -1  O  ALA G 431   N  LYS G 185           
SHEET    8   L11 LEU G 442  ILE G 449 -1  O  GLY G 446   N  ILE G 434           
SHEET    9   L11 VAL G 391  PRO G 395 -1  N  SER G 394   O  GLN G 447           
SHEET   10   L11 LYS G 253  PRO G 257  1  N  GLY G 255   O  VAL G 391           
SHEET   11   L11 GLU G 286  VAL G 290  1  O  LYS G 288   N  ILE G 254           
SHEET    1   M 9 GLU H  71  VAL H  72  0                                        
SHEET    2   M 9 ALA H 102  ASN H 110 -1  O  THR H 103   N  GLU H  71           
SHEET    3   M 9 LYS H 116  GLU H 128 -1  O  VAL H 119   N  VAL H 107           
SHEET    4   M 9 PRO H 150  THR H 156 -1  O  LEU H 151   N  GLU H 127           
SHEET    5   M 9 TYR H   5  GLN H  16 -1  N  ILE H  13   O  ILE H 154           
SHEET    6   M 9 LEU H 192  PRO H 202 -1  O  SER H 199   N  VAL H   8           
SHEET    7   M 9 VAL H 212  LYS H 215 -1  O  VAL H 212   N  VAL H 198           
SHEET    8   M 9 THR H 248  ASP H 252  1  O  ARG H 249   N  GLU H 213           
SHEET    9   M 9 LYS H 257  TYR H 259 -1  O  TYR H 259   N  THR H 250           
SHEET    1   N 2 VAL H  53  ASN H  54  0                                        
SHEET    2   N 2 MET I  60  ARG I  61  1  O  ARG I  61   N  VAL H  53           
SHEET    1   O 2 GLU H  75  SER H  76  0                                        
SHEET    2   O 2 LEU H 281  LYS H 282 -1  O  LEU H 281   N  SER H  76           
SHEET    1   P 3 TYR H  92  GLN H  96  0                                        
SHEET    2   P 3 PHE H  78  HIS H  82 -1  N  LYS H  81   O  GLN H  93           
SHEET    3   P 3 PHE H 273  PRO H 274 -1  O  PHE H 273   N  ARG H  80           
SHEET    1   Q 4 LYS H 132  GLU H 136  0                                        
SHEET    2   Q 4 LYS H 139  ASP H 143 -1  O  LEU H 141   N  ILE H 134           
SHEET    3   Q 4 PHE I  85  PRO I  89 -1  O  VAL I  88   N  THR H 140           
SHEET    4   Q 4 ARG I  81  LYS I  82 -1  N  LYS I  82   O  PHE I  85           
SHEET    1   R11 TYR J  42  PRO J  45  0                                        
SHEET    2   R11 LEU J 110  THR J 115 -1  O  LYS J 114   N  THR J  44           
SHEET    3   R11 PRO J  68  LYS J  72  1  N  VAL J  71   O  THR J 115           
SHEET    4   R11 VAL J 162  SER J 166  1  O  LEU J 164   N  ALA J  70           
SHEET    5   R11 ILE J 206  GLY J 210 -1  O  PHE J 209   N  SER J 163           
SHEET    6   R11 ILE J 182  LYS J 185 -1  N  ILE J 182   O  GLY J 210           
SHEET    7   R11 ALA J 431  LYS J 439 -1  O  ALA J 431   N  LYS J 185           
SHEET    8   R11 LEU J 442  ILE J 449 -1  O  GLY J 446   N  ILE J 434           
SHEET    9   R11 VAL J 391  PRO J 395 -1  N  SER J 394   O  GLN J 447           
SHEET   10   R11 LYS J 253  PRO J 257  1  N  GLY J 255   O  VAL J 391           
SHEET   11   R11 GLU J 286  VAL J 290  1  O  LYS J 288   N  ILE J 254           
SHEET    1   S 9 GLU K  71  VAL K  72  0                                        
SHEET    2   S 9 ALA K 102  ASN K 110 -1  O  THR K 103   N  GLU K  71           
SHEET    3   S 9 LYS K 116  GLU K 128 -1  O  LYS K 117   N  LEU K 109           
SHEET    4   S 9 PRO K 150  THR K 156 -1  O  LEU K 151   N  GLU K 127           
SHEET    5   S 9 TYR K   5  GLN K  16 -1  N  ILE K  13   O  ILE K 154           
SHEET    6   S 9 LEU K 192  PRO K 202 -1  O  SER K 199   N  VAL K   8           
SHEET    7   S 9 VAL K 212  LYS K 215 -1  O  ILE K 214   N  ILE K 196           
SHEET    8   S 9 THR K 248  ASP K 252  1  O  ARG K 249   N  GLU K 213           
SHEET    9   S 9 LYS K 257  TYR K 259 -1  O  TYR K 259   N  THR K 250           
SHEET    1   T 2 VAL K  53  ASN K  54  0                                        
SHEET    2   T 2 MET L  60  ARG L  61  1  O  ARG L  61   N  VAL K  53           
SHEET    1   U 2 GLU K  75  SER K  76  0                                        
SHEET    2   U 2 LEU K 281  LYS K 282 -1  O  LEU K 281   N  SER K  76           
SHEET    1   V 2 PHE K  78  HIS K  82  0                                        
SHEET    2   V 2 TYR K  92  GLN K  96 -1  O  SER K  95   N  ALA K  79           
SHEET    1   W 4 LYS K 132  GLU K 136  0                                        
SHEET    2   W 4 LYS K 139  ASP K 143 -1  O  LEU K 141   N  ILE K 134           
SHEET    3   W 4 PHE L  85  PRO L  89 -1  O  VAL L  88   N  THR K 140           
SHEET    4   W 4 ARG L  81  LYS L  82 -1  N  LYS L  82   O  PHE L  85           
SHEET    1   X11 TYR M  42  PRO M  45  0                                        
SHEET    2   X11 LEU M 110  THR M 115 -1  O  LYS M 114   N  THR M  44           
SHEET    3   X11 PRO M  68  LYS M  72  1  N  VAL M  71   O  THR M 115           
SHEET    4   X11 VAL M 162  SER M 166  1  O  LEU M 164   N  ALA M  70           
SHEET    5   X11 ILE M 206  GLY M 210 -1  O  PHE M 209   N  SER M 163           
SHEET    6   X11 ILE M 182  LYS M 185 -1  N  ILE M 184   O  VAL M 208           
SHEET    7   X11 ALA M 431  LYS M 439 -1  O  ALA M 431   N  LYS M 185           
SHEET    8   X11 LEU M 442  ILE M 449 -1  O  GLY M 446   N  ILE M 434           
SHEET    9   X11 VAL M 391  PRO M 395 -1  N  SER M 394   O  GLN M 447           
SHEET   10   X11 LYS M 253  PRO M 257  1  N  GLY M 255   O  VAL M 391           
SHEET   11   X11 GLU M 286  VAL M 290  1  O  LYS M 288   N  ILE M 254           
SHEET    1   Y 9 GLU N  71  VAL N  72  0                                        
SHEET    2   Y 9 ALA N 102  ASN N 110 -1  O  THR N 103   N  GLU N  71           
SHEET    3   Y 9 LYS N 116  GLU N 128 -1  O  VAL N 119   N  VAL N 107           
SHEET    4   Y 9 PRO N 150  THR N 156 -1  O  LEU N 151   N  GLU N 127           
SHEET    5   Y 9 TYR N   5  GLN N  16 -1  N  ILE N  13   O  ILE N 154           
SHEET    6   Y 9 LEU N 192  PRO N 202 -1  O  SER N 199   N  VAL N   8           
SHEET    7   Y 9 VAL N 212  LYS N 215 -1  O  VAL N 212   N  VAL N 198           
SHEET    8   Y 9 THR N 248  ASP N 252  1  O  ARG N 249   N  GLU N 213           
SHEET    9   Y 9 LYS N 257  TYR N 259 -1  O  TYR N 259   N  THR N 250           
SHEET    1   Z 2 VAL N  53  ASN N  54  0                                        
SHEET    2   Z 2 MET O  60  ARG O  61  1  O  ARG O  61   N  VAL N  53           
SHEET    1  AA 2 GLU N  75  SER N  76  0                                        
SHEET    2  AA 2 LEU N 281  LYS N 282 -1  O  LEU N 281   N  SER N  76           
SHEET    1  AB 3 TYR N  92  GLN N  96  0                                        
SHEET    2  AB 3 PHE N  78  HIS N  82 -1  N  LYS N  81   O  GLN N  93           
SHEET    3  AB 3 PHE N 273  PRO N 274 -1  O  PHE N 273   N  ARG N  80           
SHEET    1  AC 4 LYS N 132  GLU N 136  0                                        
SHEET    2  AC 4 LYS N 139  ASP N 143 -1  O  LEU N 141   N  ILE N 134           
SHEET    3  AC 4 PHE O  85  PRO O  89 -1  O  VAL O  88   N  THR N 140           
SHEET    4  AC 4 ARG O  81  LYS O  82 -1  N  LYS O  82   O  PHE O  85           
SHEET    1  AD11 TYR P  42  PRO P  45  0                                        
SHEET    2  AD11 LEU P 110  THR P 115 -1  O  LYS P 114   N  THR P  44           
SHEET    3  AD11 PRO P  68  LYS P  72  1  N  VAL P  71   O  THR P 115           
SHEET    4  AD11 VAL P 162  SER P 166  1  O  LEU P 164   N  ALA P  70           
SHEET    5  AD11 ILE P 206  GLY P 210 -1  O  PHE P 209   N  SER P 163           
SHEET    6  AD11 ILE P 182  LYS P 185 -1  N  ILE P 182   O  GLY P 210           
SHEET    7  AD11 ALA P 431  LYS P 439 -1  O  ALA P 431   N  LYS P 185           
SHEET    8  AD11 LEU P 442  ILE P 449 -1  O  GLY P 446   N  ILE P 434           
SHEET    9  AD11 VAL P 391  PRO P 395 -1  N  SER P 394   O  GLN P 447           
SHEET   10  AD11 LYS P 253  PRO P 257  1  N  GLY P 255   O  VAL P 391           
SHEET   11  AD11 GLU P 286  VAL P 290  1  O  LYS P 288   N  ILE P 254           
SHEET    1  AE 9 GLU Q  71  VAL Q  72  0                                        
SHEET    2  AE 9 ALA Q 102  ASN Q 110 -1  O  THR Q 103   N  GLU Q  71           
SHEET    3  AE 9 LYS Q 116  GLU Q 128 -1  O  LYS Q 117   N  LEU Q 109           
SHEET    4  AE 9 PRO Q 150  THR Q 156 -1  O  LEU Q 151   N  GLU Q 127           
SHEET    5  AE 9 TYR Q   5  GLN Q  16 -1  N  ILE Q  13   O  ILE Q 154           
SHEET    6  AE 9 LEU Q 192  PRO Q 202 -1  O  SER Q 199   N  VAL Q   8           
SHEET    7  AE 9 VAL Q 212  LYS Q 215 -1  O  ILE Q 214   N  ILE Q 196           
SHEET    8  AE 9 THR Q 248  ASP Q 252  1  O  ARG Q 249   N  GLU Q 213           
SHEET    9  AE 9 LYS Q 257  TYR Q 259 -1  O  TYR Q 259   N  THR Q 250           
SHEET    1  AF 2 GLU Q  75  SER Q  76  0                                        
SHEET    2  AF 2 LEU Q 281  LYS Q 282 -1  O  LEU Q 281   N  SER Q  76           
SHEET    1  AG 2 PHE Q  78  HIS Q  82  0                                        
SHEET    2  AG 2 TYR Q  92  GLN Q  96 -1  O  SER Q  95   N  ALA Q  79           
SHEET    1  AH 4 LYS Q 132  GLU Q 136  0                                        
SHEET    2  AH 4 LYS Q 139  ASP Q 143 -1  O  LEU Q 141   N  ILE Q 134           
SHEET    3  AH 4 PHE R  85  PRO R  89 -1  O  VAL R  88   N  THR Q 140           
SHEET    4  AH 4 ARG R  81  LYS R  82 -1  N  LYS R  82   O  PHE R  85           
SHEET    1  AI11 TYR S  42  PRO S  45  0                                        
SHEET    2  AI11 LEU S 110  THR S 115 -1  O  LYS S 114   N  THR S  44           
SHEET    3  AI11 PRO S  68  LYS S  72  1  N  VAL S  71   O  THR S 115           
SHEET    4  AI11 SER S 163  ASP S 167  1  O  LEU S 164   N  ALA S  70           
SHEET    5  AI11 GLN S 205  GLY S 210 -1  O  PHE S 209   N  SER S 163           
SHEET    6  AI11 ILE S 182  LYS S 185 -1  N  ILE S 182   O  GLY S 210           
SHEET    7  AI11 ALA S 431  LYS S 439 -1  O  SER S 433   N  GLY S 183           
SHEET    8  AI11 LEU S 442  GLY S 450 -1  O  GLY S 446   N  ILE S 434           
SHEET    9  AI11 VAL S 391  PRO S 395 -1  N  SER S 394   O  GLN S 447           
SHEET   10  AI11 LYS S 253  PRO S 257  1  N  GLY S 255   O  VAL S 391           
SHEET   11  AI11 GLU S 286  VAL S 290  1  O  LYS S 288   N  ILE S 254           
SHEET    1  AJ 9 GLU T  71  VAL T  72  0                                        
SHEET    2  AJ 9 ALA T 102  ASN T 110 -1  O  THR T 103   N  GLU T  71           
SHEET    3  AJ 9 LYS T 116  GLU T 128 -1  O  LYS T 117   N  LEU T 109           
SHEET    4  AJ 9 PRO T 150  THR T 156 -1  O  LEU T 151   N  GLU T 127           
SHEET    5  AJ 9 TYR T   5  GLN T  16 -1  N  ILE T  13   O  ILE T 154           
SHEET    6  AJ 9 LEU T 192  PRO T 202 -1  O  SER T 199   N  VAL T   8           
SHEET    7  AJ 9 VAL T 212  LYS T 215 -1  O  VAL T 212   N  VAL T 198           
SHEET    8  AJ 9 THR T 248  ASP T 252  1  O  ARG T 249   N  GLU T 213           
SHEET    9  AJ 9 LYS T 257  TYR T 259 -1  O  TYR T 259   N  THR T 250           
SHEET    1  AK 2 GLU T  75  SER T  76  0                                        
SHEET    2  AK 2 LEU T 281  LYS T 282 -1  O  LEU T 281   N  SER T  76           
SHEET    1  AL 3 TYR T  92  GLN T  96  0                                        
SHEET    2  AL 3 PHE T  78  HIS T  82 -1  N  LYS T  81   O  GLN T  93           
SHEET    3  AL 3 PHE T 273  PRO T 274 -1  O  PHE T 273   N  ARG T  80           
SHEET    1  AM 4 LYS T 132  GLU T 136  0                                        
SHEET    2  AM 4 LYS T 139  ASP T 143 -1  O  LEU T 141   N  ILE T 134           
SHEET    3  AM 4 PHE U  85  PRO U  89 -1  O  VAL U  88   N  THR T 140           
SHEET    4  AM 4 ARG U  81  LYS U  82 -1  N  LYS U  82   O  PHE U  85           
SHEET    1  AN11 TYR V  42  PRO V  45  0                                        
SHEET    2  AN11 LEU V 110  THR V 115 -1  O  LYS V 114   N  ILE V  43           
SHEET    3  AN11 PRO V  68  LYS V  72  1  N  VAL V  71   O  THR V 115           
SHEET    4  AN11 VAL V 162  SER V 166  1  O  LEU V 164   N  ALA V  70           
SHEET    5  AN11 ILE V 206  GLY V 210 -1  O  PHE V 209   N  SER V 163           
SHEET    6  AN11 ILE V 182  LYS V 185 -1  N  ILE V 182   O  GLY V 210           
SHEET    7  AN11 ALA V 431  LYS V 439 -1  O  SER V 433   N  GLY V 183           
SHEET    8  AN11 LEU V 442  GLY V 450 -1  O  GLY V 446   N  ILE V 434           
SHEET    9  AN11 VAL V 391  PRO V 395 -1  N  SER V 394   O  GLN V 447           
SHEET   10  AN11 LYS V 253  PRO V 257  1  N  GLY V 255   O  VAL V 391           
SHEET   11  AN11 GLU V 286  VAL V 290  1  O  LYS V 288   N  ILE V 254           
SHEET    1  AO 9 GLU W  71  VAL W  72  0                                        
SHEET    2  AO 9 ALA W 102  ASN W 110 -1  O  THR W 103   N  GLU W  71           
SHEET    3  AO 9 LYS W 116  GLU W 128 -1  O  LYS W 117   N  LEU W 109           
SHEET    4  AO 9 PRO W 150  THR W 156 -1  O  LEU W 151   N  GLU W 127           
SHEET    5  AO 9 TYR W   5  GLN W  16 -1  N  ILE W  13   O  ILE W 154           
SHEET    6  AO 9 LEU W 192  PRO W 202 -1  O  SER W 199   N  VAL W   8           
SHEET    7  AO 9 VAL W 212  LYS W 215 -1  O  ILE W 214   N  ILE W 196           
SHEET    8  AO 9 THR W 248  ASP W 252  1  O  ARG W 249   N  GLU W 213           
SHEET    9  AO 9 LYS W 257  TYR W 259 -1  O  TYR W 259   N  THR W 250           
SHEET    1  AP 2 GLU W  75  SER W  76  0                                        
SHEET    2  AP 2 LEU W 281  LYS W 282 -1  O  LEU W 281   N  SER W  76           
SHEET    1  AQ 3 TYR W  92  GLN W  96  0                                        
SHEET    2  AQ 3 PHE W  78  HIS W  82 -1  N  LYS W  81   O  GLN W  93           
SHEET    3  AQ 3 PHE W 273  PRO W 274 -1  O  PHE W 273   N  ARG W  80           
SHEET    1  AR 4 LYS W 132  GLU W 136  0                                        
SHEET    2  AR 4 LYS W 139  ASP W 143 -1  O  LEU W 141   N  ILE W 134           
SHEET    3  AR 4 PHE X  85  PRO X  89 -1  O  VAL X  88   N  THR W 140           
SHEET    4  AR 4 ARG X  81  LYS X  82 -1  N  LYS X  82   O  PHE X  85           
LINK         NE2 HIS B  14                MG    MG B 801     1555   1555  2.04  
LINK         SG  CYS B  25                ZN    ZN B 901     1555   1555  2.24  
LINK         SG  CYS B  27                ZN    ZN B 901     1555   1555  2.36  
LINK         SG  CYS B  40                ZN    ZN B 901     1555   1555  2.94  
LINK         SG  CYS B  43                ZN    ZN B 901     1555   1555  2.39  
LINK         OE2 GLU B 127                MG    MG B 801     1555   1555  2.50  
LINK         OE1 GLU B 153                MG    MG B 801     1555   1555  1.95  
LINK         NE2 HIS E  14                MG    MG E 802     1555   1555  1.99  
LINK         SG  CYS E  25                ZN    ZN E 902     1555   1555  2.21  
LINK         SG  CYS E  27                ZN    ZN E 902     1555   1555  2.15  
LINK         SG  CYS E  40                ZN    ZN E 902     1555   1555  2.26  
LINK         SG  CYS E  43                ZN    ZN E 902     1555   1555  2.45  
LINK         OE2 GLU E 127                MG    MG E 802     1555   1555  2.33  
LINK         OE1 GLU E 153                MG    MG E 802     1555   1555  2.15  
LINK         NE2 HIS H  14                MG    MG H 803     1555   1555  2.00  
LINK         SG  CYS H  25                ZN    ZN H 903     1555   1555  2.17  
LINK         SG  CYS H  27                ZN    ZN H 903     1555   1555  2.30  
LINK         SG  CYS H  40                ZN    ZN H 903     1555   1555  2.40  
LINK         SG  CYS H  43                ZN    ZN H 903     1555   1555  2.39  
LINK         OE1 GLU H 153                MG    MG H 803     1555   1555  1.87  
LINK         NE2 HIS K  14                MG    MG K 804     1555   1555  2.03  
LINK         SG  CYS K  25                ZN    ZN K 904     1555   1555  2.02  
LINK         SG  CYS K  27                ZN    ZN K 904     1555   1555  2.20  
LINK         SG  CYS K  40                ZN    ZN K 904     1555   1555  2.10  
LINK         SG  CYS K  43                ZN    ZN K 904     1555   1555  2.41  
LINK         OE2 GLU K 127                MG    MG K 804     1555   1555  2.39  
LINK         OE1 GLU K 153                MG    MG K 804     1555   1555  2.00  
LINK         NE2 HIS N  14                MG    MG N 805     1555   1555  2.00  
LINK         SG  CYS N  25                ZN    ZN N 905     1555   1555  2.12  
LINK         SG  CYS N  27                ZN    ZN N 905     1555   1555  2.34  
LINK         SG  CYS N  40                ZN    ZN N 905     1555   1555  2.30  
LINK         SG  CYS N  43                ZN    ZN N 905     1555   1555  2.26  
LINK         OE2 GLU N 127                MG    MG N 805     1555   1555  2.37  
LINK         OE1 GLU N 153                MG    MG N 805     1555   1555  1.92  
LINK         NE2 HIS Q  14                MG    MG Q 806     1555   1555  2.04  
LINK         SG  CYS Q  25                ZN    ZN Q 906     1555   1555  2.07  
LINK         SG  CYS Q  27                ZN    ZN Q 906     1555   1555  2.35  
LINK         SG  CYS Q  40                ZN    ZN Q 906     1555   1555  2.15  
LINK         SG  CYS Q  43                ZN    ZN Q 906     1555   1555  2.33  
LINK         OE2 GLU Q 127                MG    MG Q 806     1555   1555  2.27  
LINK         OE1 GLU Q 153                MG    MG Q 806     1555   1555  2.04  
LINK         NE2 HIS T  14                MG    MG T 807     1555   1555  1.95  
LINK         SG  CYS T  25                ZN    ZN T 907     1555   1555  2.19  
LINK         SG  CYS T  27                ZN    ZN T 907     1555   1555  2.17  
LINK         SG  CYS T  40                ZN    ZN T 907     1555   1555  2.18  
LINK         SG  CYS T  43                ZN    ZN T 907     1555   1555  2.44  
LINK         OE2 GLU T 127                MG    MG T 807     1555   1555  2.33  
LINK         OE1 GLU T 153                MG    MG T 807     1555   1555  1.97  
LINK         NE2 HIS W  14                MG    MG W 808     1555   1555  1.99  
LINK         SG  CYS W  25                ZN    ZN W 908     1555   1555  2.17  
LINK         SG  CYS W  27                ZN    ZN W 908     1555   1555  2.21  
LINK         SG  CYS W  40                ZN    ZN W 908     1555   1555  2.09  
LINK         SG  CYS W  43                ZN    ZN W 908     1555   1555  2.37  
LINK         OE2 GLU W 127                MG    MG W 808     1555   1555  2.35  
LINK         OE1 GLU W 153                MG    MG W 808     1555   1555  1.98  
LINK         OG  SER P 171                 CG  ASN P 906     1555   1555  1.37  
LINK         OG  SER D 171                 CG  ASN D 902     1555   1555  1.39  
LINK         OG  SER V 171                 CG  ASN V 908     1555   1555  1.43  
LINK         OG  SER M 171                 CG  ASN M 905     1555   1555  1.43  
LINK         OG  SER S 171                 CG  ASN S 907     1555   1555  1.45  
LINK         OG  SER A 171                 CG  ASN A 901     1555   1555  1.48  
LINK         OG  SER J 171                 CG  ASN J 904     1555   1555  1.50  
LINK         OG  SER G 171                 CG  ASN G 903     1555   1555  1.52  
CISPEP   1 GLY A  146    SER A  147          0         8.15                     
CISPEP   2 GLY D  146    SER D  147          0         4.61                     
CISPEP   3 GLY G  146    SER G  147          0         9.70                     
CISPEP   4 GLY J  146    SER J  147          0         8.26                     
CISPEP   5 GLY M  146    SER M  147          0         6.67                     
CISPEP   6 GLY P  146    SER P  147          0         8.40                     
CISPEP   7 GLY S  146    SER S  147          0         9.28                     
CISPEP   8 GLY V  146    SER V  147          0        10.04                     
SITE     1 AC1 12 VAL B   8  GLY B  10  LEU B  11  GLU B  12                    
SITE     2 AC1 12 VAL B 155  THR B 156  GLU B 157  PRO B 158                    
SITE     3 AC1 12 ASN B 197  SER B 199  GLY B 209  ARG B 211                    
SITE     1 AC2  3 HIS B  14  GLU B 127  GLU B 153                               
SITE     1 AC3  4 CYS B  25  CYS B  27  CYS B  40  CYS B  43                    
SITE     1 AC4 12 VAL E   8  GLY E  10  LEU E  11  GLU E  12                    
SITE     2 AC4 12 VAL E 155  THR E 156  GLU E 157  PRO E 158                    
SITE     3 AC4 12 ASN E 197  SER E 199  GLY E 209  ARG E 211                    
SITE     1 AC5  3 HIS E  14  GLU E 127  GLU E 153                               
SITE     1 AC6  4 CYS E  25  CYS E  27  CYS E  40  CYS E  43                    
SITE     1 AC7 12 VAL H   8  GLY H  10  LEU H  11  GLU H  12                    
SITE     2 AC7 12 VAL H 155  THR H 156  GLU H 157  PRO H 158                    
SITE     3 AC7 12 ASN H 197  SER H 199  GLY H 209  ARG H 211                    
SITE     1 AC8  3 HIS H  14  GLU H 127  GLU H 153                               
SITE     1 AC9  4 CYS H  25  CYS H  27  CYS H  40  CYS H  43                    
SITE     1 BC1 12 VAL K   8  GLY K  10  LEU K  11  GLU K  12                    
SITE     2 BC1 12 VAL K 155  THR K 156  GLU K 157  PRO K 158                    
SITE     3 BC1 12 ASN K 197  SER K 199  GLY K 209  ARG K 211                    
SITE     1 BC2  3 HIS K  14  GLU K 127  GLU K 153                               
SITE     1 BC3  4 CYS K  25  CYS K  27  CYS K  40  CYS K  43                    
SITE     1 BC4 12 VAL N   8  GLY N  10  LEU N  11  GLU N  12                    
SITE     2 BC4 12 VAL N 155  THR N 156  GLU N 157  PRO N 158                    
SITE     3 BC4 12 ASN N 197  SER N 199  GLY N 209  ARG N 211                    
SITE     1 BC5  3 HIS N  14  GLU N 127  GLU N 153                               
SITE     1 BC6  4 CYS N  25  CYS N  27  CYS N  40  CYS N  43                    
SITE     1 BC7 13 VAL Q   8  GLY Q  10  LEU Q  11  GLU Q  12                    
SITE     2 BC7 13 VAL Q 155  THR Q 156  GLU Q 157  PRO Q 158                    
SITE     3 BC7 13 ASN Q 197  VAL Q 198  SER Q 199  GLY Q 209                    
SITE     4 BC7 13 ARG Q 211                                                     
SITE     1 BC8  3 HIS Q  14  GLU Q 127  GLU Q 153                               
SITE     1 BC9  4 CYS Q  25  CYS Q  27  CYS Q  40  CYS Q  43                    
SITE     1 CC1 12 VAL T   8  GLY T  10  LEU T  11  GLU T  12                    
SITE     2 CC1 12 VAL T 155  THR T 156  GLU T 157  PRO T 158                    
SITE     3 CC1 12 ASN T 197  SER T 199  GLY T 209  ARG T 211                    
SITE     1 CC2  3 HIS T  14  GLU T 127  GLU T 153                               
SITE     1 CC3  4 CYS T  25  CYS T  27  CYS T  40  CYS T  43                    
SITE     1 CC4 12 VAL W   8  GLY W  10  LEU W  11  GLU W  12                    
SITE     2 CC4 12 VAL W 155  THR W 156  GLU W 157  PRO W 158                    
SITE     3 CC4 12 ASN W 197  SER W 199  GLY W 209  ARG W 211                    
SITE     1 CC5  3 HIS W  14  GLU W 127  GLU W 153                               
SITE     1 CC6  4 CYS W  25  CYS W  27  CYS W  40  CYS W  43                    
SITE     1 CC7 11 ALA A 121  GLY A 123  SER A 124  SER A 147                    
SITE     2 CC7 11 GLY A 169  GLY A 170  SER A 171  TYR A 302                    
SITE     3 CC7 11 TYR A 303  ARG A 351  ASP A 418                               
SITE     1 CC8 11 ALA D 121  MET D 122  GLY D 123  SER D 124                    
SITE     2 CC8 11 GLY D 169  GLY D 170  SER D 171  PHE D 199                    
SITE     3 CC8 11 TYR D 302  ARG D 351  ASP D 418                               
SITE     1 CC9 11 ALA G 121  GLY G 123  SER G 124  THR G 168                    
SITE     2 CC9 11 GLY G 169  GLY G 170  SER G 171  PHE G 199                    
SITE     3 CC9 11 TYR G 302  ARG G 351  ASP G 418                               
SITE     1 DC1 12 ALA J 121  MET J 122  GLY J 123  SER J 124                    
SITE     2 DC1 12 THR J 168  GLY J 169  GLY J 170  SER J 171                    
SITE     3 DC1 12 PHE J 199  TYR J 302  ARG J 351  ASP J 418                    
SITE     1 DC2 11 ALA M 121  MET M 122  GLY M 123  SER M 124                    
SITE     2 DC2 11 GLY M 169  GLY M 170  SER M 171  TYR M 302                    
SITE     3 DC2 11 TYR M 303  ARG M 351  ASP M 418                               
SITE     1 DC3 13 ALA P 121  MET P 122  GLY P 123  SER P 124                    
SITE     2 DC3 13 SER P 147  THR P 168  GLY P 169  GLY P 170                    
SITE     3 DC3 13 SER P 171  PHE P 199  TYR P 302  ARG P 351                    
SITE     4 DC3 13 ASP P 418                                                     
SITE     1 DC4 12 ALA S 121  MET S 122  GLY S 123  SER S 124                    
SITE     2 DC4 12 THR S 168  GLY S 169  GLY S 170  SER S 171                    
SITE     3 DC4 12 PHE S 199  TYR S 302  ARG S 351  ASP S 418                    
SITE     1 DC5  9 ALA V 121  GLY V 123  GLY V 169  GLY V 170                    
SITE     2 DC5  9 SER V 171  PHE V 199  TYR V 302  ARG V 351                    
SITE     3 DC5  9 ASP V 418                                                     
CRYST1  127.482  131.012  154.668  90.02  90.00  89.91 P 1           8          
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      0.007844 -0.000012  0.000000        0.00000                         
SCALE2      0.000000  0.007633  0.000002        0.00000                         
SCALE3      0.000000  0.000000  0.006465        0.00000                         
(ATOM LINES ARE NOT SHOWN.)

DBGET integrated database retrieval system