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Database: PDB
Entry: 3ODM
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Original site: 3ODM 
HEADER    LYASE                                   11-AUG-10   3ODM              
TITLE     ARCHAEAL-TYPE PHOSPHOENOLPYRUVATE CARBOXYLASE                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHOENOLPYRUVATE CARBOXYLASE;                           
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 SYNONYM: PEPCASE, PEPC;                                              
COMPND   5 EC: 4.1.1.31;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM PERFRINGENS;                        
SOURCE   3 ORGANISM_TAXID: 1502;                                                
SOURCE   4 GENE: CPE1094, PPCA;                                                 
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)(PRIL);                           
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PJLK15-19B                                
KEYWDS    BETA-BARREL, LYASE                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.W.DUNTEN                                                            
REVDAT   4   25-MAY-11 3ODM    1       JRNL                                     
REVDAT   3   11-MAY-11 3ODM    1       REMARK                                   
REVDAT   2   27-APR-11 3ODM    1       JRNL                                     
REVDAT   1   02-FEB-11 3ODM    0                                                
JRNL        AUTH   L.DHARMARAJAN,J.L.KRASZEWSKI,B.MUKHOPADHYAY,P.W.DUNTEN       
JRNL        TITL   STRUCTURE OF AN ARCHAEAL-TYPE PHOSPHOENOLPYRUVATE            
JRNL        TITL 2 CARBOXYLASE SENSITIVE TO INHIBITION BY ASPARTATE.            
JRNL        REF    PROTEINS                      V.  79  1820 2011              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   21491491                                                     
JRNL        DOI    10.1002/PROT.23006                                           
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   L.DHARMARAHAN,J.L.KRASZEWSKI,B.MUKHOPADHYAY,P.W.DUNTEN       
REMARK   1  TITL   EXPRESSION, PURIFICATION AND CRYSTALLIZATION OF AN           
REMARK   1  TITL 2 ARCHAEAL-TYPE PHOSPHOENOLPYRUVATE CARBOXYLASE                
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.F      V.  65  1193 2009              
REMARK   1  REFN                   ESSN 1744-3091                               
REMARK   1  PMID   19923749                                                     
REMARK   1  DOI    10.1107/S1744309109042663                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
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) : 2.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 56.84                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 116208                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : THIN SHELLS                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1135                            
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) : 2.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.03                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8334                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2970                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 0                            
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 33256                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 107                                     
REMARK   3   SOLVENT ATOMS            : 200                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 66.52                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.45000                                              
REMARK   3    B22 (A**2) : -1.66000                                             
REMARK   3    B33 (A**2) : -0.78000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.357         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.294         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.934        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.903                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 33866 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 45628 ; 1.337 ; 1.982       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4200 ; 5.794 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1491 ;39.894 ;25.111       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  6474 ;19.247 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   176 ;19.795 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  5186 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 24912 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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): 20953 ; 0.346 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 33988 ; 0.710 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 12913 ; 1.203 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 11640 ; 2.162 ; 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 : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D E F G H                 
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1976 ;  0.33 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):   1976 ;  0.47 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    C    (A):   1976 ;  0.31 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    D    (A):   1976 ;  0.23 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    E    (A):   1976 ;  0.27 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    F    (A):   1976 ;  0.33 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    G    (A):   1976 ;  0.28 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    H    (A):   1976 ;  0.22 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1909 ;  0.58 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1909 ;  0.66 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   1909 ;  0.53 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   1909 ;  0.52 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    E    (A):   1909 ;  0.52 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    F    (A):   1909 ;  0.58 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    G    (A):   1909 ;  0.54 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    H    (A):   1909 ;  0.50 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1976 ;  1.72 ;  5.00           
REMARK   3   TIGHT THERMAL      1    B (A**2):   1976 ;  1.38 ;  5.00           
REMARK   3   TIGHT THERMAL      1    C (A**2):   1976 ;  1.24 ;  5.00           
REMARK   3   TIGHT THERMAL      1    D (A**2):   1976 ;  1.48 ;  5.00           
REMARK   3   TIGHT THERMAL      1    E (A**2):   1976 ;  1.55 ;  5.00           
REMARK   3   TIGHT THERMAL      1    F (A**2):   1976 ;  1.23 ;  5.00           
REMARK   3   TIGHT THERMAL      1    G (A**2):   1976 ;  1.96 ;  5.00           
REMARK   3   TIGHT THERMAL      1    H (A**2):   1976 ;  1.51 ;  5.00           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1909 ;  2.17 ;  5.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1909 ;  1.72 ;  5.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   1909 ;  1.64 ;  5.00           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   1909 ;  1.81 ;  5.00           
REMARK   3   MEDIUM THERMAL     1    E (A**2):   1909 ;  1.86 ;  5.00           
REMARK   3   MEDIUM THERMAL     1    F (A**2):   1909 ;  1.52 ;  5.00           
REMARK   3   MEDIUM THERMAL     1    G (A**2):   1909 ;  2.17 ;  5.00           
REMARK   3   MEDIUM THERMAL     1    H (A**2):   1909 ;  1.89 ;  5.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B C D E F G H                 
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   2    A    (A):    185 ;  0.59 ;  5.00           
REMARK   3   LOOSE POSITIONAL   2    B    (A):    185 ;  0.67 ;  5.00           
REMARK   3   LOOSE POSITIONAL   2    C    (A):    185 ;  0.78 ;  5.00           
REMARK   3   LOOSE POSITIONAL   2    D    (A):    185 ;  0.87 ;  5.00           
REMARK   3   LOOSE POSITIONAL   2    E    (A):    185 ;  0.85 ;  5.00           
REMARK   3   LOOSE POSITIONAL   2    F    (A):    185 ;  0.78 ;  5.00           
REMARK   3   LOOSE POSITIONAL   2    G    (A):    185 ;  0.70 ;  5.00           
REMARK   3   LOOSE POSITIONAL   2    H    (A):    185 ;  0.68 ;  5.00           
REMARK   3   LOOSE THERMAL      2    A (A**2):    185 ;  3.09 ; 14.00           
REMARK   3   LOOSE THERMAL      2    B (A**2):    185 ;  2.80 ; 14.00           
REMARK   3   LOOSE THERMAL      2    C (A**2):    185 ;  3.69 ; 14.00           
REMARK   3   LOOSE THERMAL      2    D (A**2):    185 ;  1.91 ; 14.00           
REMARK   3   LOOSE THERMAL      2    E (A**2):    185 ;  1.40 ; 14.00           
REMARK   3   LOOSE THERMAL      2    F (A**2):    185 ;  3.70 ; 14.00           
REMARK   3   LOOSE THERMAL      2    G (A**2):    185 ;  1.82 ; 14.00           
REMARK   3   LOOSE THERMAL      2    H (A**2):    185 ;  7.37 ; 14.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 58                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   102                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.9189  33.5284  73.4101              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0367 T22:   0.0244                                     
REMARK   3      T33:   0.0583 T12:   0.0126                                     
REMARK   3      T13:   0.0070 T23:  -0.0195                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0641 L22:   2.2870                                     
REMARK   3      L33:   2.2316 L12:   1.1203                                     
REMARK   3      L13:  -1.4385 L23:   0.2275                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0119 S12:   0.0115 S13:   0.2723                       
REMARK   3      S21:  -0.0951 S22:  -0.0485 S23:  -0.0765                       
REMARK   3      S31:  -0.1532 S32:  -0.2045 S33:   0.0366                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   103        A   202                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.9916  19.1143  68.3066              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0688 T22:   0.0737                                     
REMARK   3      T33:   0.0468 T12:  -0.0511                                     
REMARK   3      T13:  -0.0178 T23:  -0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5457 L22:   2.6366                                     
REMARK   3      L33:   2.0214 L12:   0.0279                                     
REMARK   3      L13:  -0.5704 L23:   0.5085                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0501 S12:  -0.0007 S13:  -0.2084                       
REMARK   3      S21:  -0.1292 S22:  -0.1190 S23:   0.2749                       
REMARK   3      S31:   0.0470 S32:  -0.2619 S33:   0.0689                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   203        A   280                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.2686  24.1737  61.3523              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0737 T22:   0.1263                                     
REMARK   3      T33:   0.0683 T12:   0.0055                                     
REMARK   3      T13:   0.0606 T23:   0.0176                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2129 L22:   1.8611                                     
REMARK   3      L33:   1.9113 L12:   0.1325                                     
REMARK   3      L13:   0.3401 L23:  -0.0940                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1174 S12:   0.4886 S13:   0.1845                       
REMARK   3      S21:  -0.2480 S22:   0.0088 S23:  -0.0864                       
REMARK   3      S31:  -0.0280 S32:   0.0690 S33:  -0.1262                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   281        A   346                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.3793  20.5419  66.6219              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0833 T22:   0.0373                                     
REMARK   3      T33:   0.0394 T12:  -0.0296                                     
REMARK   3      T13:   0.0469 T23:  -0.0350                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7384 L22:   2.4187                                     
REMARK   3      L33:   1.4452 L12:  -0.9740                                     
REMARK   3      L13:   0.1059 L23:   0.8615                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0237 S12:   0.1513 S13:  -0.1010                       
REMARK   3      S21:  -0.0773 S22:   0.0402 S23:  -0.0238                       
REMARK   3      S31:   0.0644 S32:   0.1339 S33:  -0.0639                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   359        A   388                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.8198   1.7179  71.7164              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3838 T22:   0.2326                                     
REMARK   3      T33:   0.3299 T12:   0.0047                                     
REMARK   3      T13:   0.0593 T23:   0.0146                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8293 L22:   7.4671                                     
REMARK   3      L33:   3.6124 L12:   0.3451                                     
REMARK   3      L13:   0.7838 L23:   4.5938                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1216 S12:  -0.4024 S13:  -0.3825                       
REMARK   3      S21:   0.6837 S22:   0.1412 S23:  -0.2510                       
REMARK   3      S31:   0.6358 S32:   0.2155 S33:  -0.2628                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   389        A   393                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.0209  22.7392  78.6705              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1562 T22:   0.0430                                     
REMARK   3      T33:   0.0992 T12:   0.0014                                     
REMARK   3      T13:  -0.0180 T23:  -0.0475                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  28.5858 L22:  68.1060                                     
REMARK   3      L33:  11.8389 L12: -43.8966                                     
REMARK   3      L13:  -2.2599 L23:   6.3227                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6642 S12:   0.5844 S13:  -1.6135                       
REMARK   3      S21:  -1.0362 S22:  -1.0319 S23:   2.5357                       
REMARK   3      S31:  -0.1933 S32:  -0.6222 S33:   0.3676                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   394        A   490                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.6768  19.7195  66.7048              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0865 T22:   0.1398                                     
REMARK   3      T33:   0.1509 T12:   0.0284                                     
REMARK   3      T13:   0.0768 T23:  -0.0707                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2419 L22:   2.3629                                     
REMARK   3      L33:   2.4678 L12:   0.8380                                     
REMARK   3      L13:   0.5837 L23:   1.8438                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1704 S12:   0.2299 S13:  -0.0733                       
REMARK   3      S21:  -0.0979 S22:   0.1806 S23:  -0.3812                       
REMARK   3      S31:   0.0343 S32:   0.4101 S33:  -0.3510                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   491        A   537                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.1011  30.8044  87.1368              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2326 T22:   0.0870                                     
REMARK   3      T33:   0.2216 T12:  -0.0195                                     
REMARK   3      T13:   0.0366 T23:  -0.0679                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5812 L22:   2.0453                                     
REMARK   3      L33:  10.8920 L12:   0.1699                                     
REMARK   3      L13:   1.9845 L23:   0.3048                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0896 S12:  -0.3220 S13:   0.0226                       
REMARK   3      S21:   0.5440 S22:  -0.0558 S23:  -0.1584                       
REMARK   3      S31:  -0.6456 S32:  -0.3551 S33:   0.1455                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   106                          
REMARK   3    ORIGIN FOR THE GROUP (A):  86.3372  75.5700 165.7676              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1287 T22:   0.0653                                     
REMARK   3      T33:   0.0926 T12:  -0.0164                                     
REMARK   3      T13:  -0.0443 T23:   0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7512 L22:   1.1476                                     
REMARK   3      L33:   3.7914 L12:  -0.2331                                     
REMARK   3      L13:   1.1347 L23:   0.6449                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1298 S12:   0.1913 S13:   0.0836                       
REMARK   3      S21:   0.0122 S22:   0.1697 S23:  -0.1528                       
REMARK   3      S31:  -0.1152 S32:   0.1799 S33:  -0.0398                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   107        B   191                          
REMARK   3    ORIGIN FOR THE GROUP (A): 102.6684  72.3204 171.3763              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2290 T22:   0.1182                                     
REMARK   3      T33:   0.2839 T12:  -0.0226                                     
REMARK   3      T13:  -0.1125 T23:   0.0267                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7834 L22:   1.7791                                     
REMARK   3      L33:   2.7641 L12:  -0.0320                                     
REMARK   3      L13:  -0.3145 L23:  -0.0292                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0378 S12:   0.0085 S13:   0.0047                       
REMARK   3      S21:  -0.0864 S22:  -0.0683 S23:  -0.4537                       
REMARK   3      S31:  -0.2753 S32:   0.5361 S33:   0.0306                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   192        B   286                          
REMARK   3    ORIGIN FOR THE GROUP (A):  96.4572  70.6122 150.3909              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2244 T22:   0.2242                                     
REMARK   3      T33:   0.1470 T12:  -0.0531                                     
REMARK   3      T13:   0.0061 T23:  -0.0487                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4437 L22:   2.0688                                     
REMARK   3      L33:   2.0123 L12:  -0.1702                                     
REMARK   3      L13:  -0.1749 L23:  -1.0025                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0587 S12:   0.2348 S13:  -0.1016                       
REMARK   3      S21:  -0.1021 S22:  -0.0829 S23:  -0.3489                       
REMARK   3      S31:   0.1192 S32:   0.4198 S33:   0.1416                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   287        B   346                          
REMARK   3    ORIGIN FOR THE GROUP (A): 100.1016  79.1996 145.4727              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2741 T22:   0.4296                                     
REMARK   3      T33:   0.1567 T12:  -0.0896                                     
REMARK   3      T13:  -0.0810 T23:  -0.0919                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3935 L22:   0.9732                                     
REMARK   3      L33:   1.6793 L12:   0.0286                                     
REMARK   3      L13:  -0.4768 L23:  -1.1507                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1512 S12:   0.0943 S13:   0.0443                       
REMARK   3      S21:   0.0202 S22:  -0.0703 S23:  -0.2930                       
REMARK   3      S31:   0.0429 S32:   0.3561 S33:   0.2215                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   355        B   390                          
REMARK   3    ORIGIN FOR THE GROUP (A): 112.1263  90.3726 145.7011              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4947 T22:   0.6514                                     
REMARK   3      T33:   0.5855 T12:  -0.0641                                     
REMARK   3      T13:  -0.0250 T23:   0.0099                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7877 L22:   0.4663                                     
REMARK   3      L33:   2.1435 L12:  -0.9932                                     
REMARK   3      L13:  -1.2739 L23:   0.2431                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0053 S12:  -0.0064 S13:   0.4081                       
REMARK   3      S21:   0.2884 S22:   0.0228 S23:  -0.2257                       
REMARK   3      S31:   0.0942 S32:   0.0750 S33:  -0.0281                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   391        B   490                          
REMARK   3    ORIGIN FOR THE GROUP (A):  97.2289  82.7455 131.6736              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2991 T22:   0.3797                                     
REMARK   3      T33:   0.1510 T12:  -0.1333                                     
REMARK   3      T13:   0.0152 T23:   0.0317                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5221 L22:   2.0106                                     
REMARK   3      L33:   2.0599 L12:  -0.9729                                     
REMARK   3      L13:   0.6599 L23:   0.1512                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0303 S12:   0.5725 S13:   0.0323                       
REMARK   3      S21:  -0.4239 S22:  -0.0464 S23:  -0.1674                       
REMARK   3      S31:   0.0408 S32:   0.3498 S33:   0.0767                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   491        B   537                          
REMARK   3    ORIGIN FOR THE GROUP (A):  82.4054  97.9535 141.0876              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3769 T22:   0.2838                                     
REMARK   3      T33:   0.3209 T12:  -0.1146                                     
REMARK   3      T13:  -0.1361 T23:  -0.0066                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6548 L22:   5.3767                                     
REMARK   3      L33:   1.0511 L12:  -1.8813                                     
REMARK   3      L13:  -0.3278 L23:  -1.0395                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1696 S12:  -0.2689 S13:   0.5469                       
REMARK   3      S21:   0.3816 S22:   0.2755 S23:   0.3556                       
REMARK   3      S31:  -0.4358 S32:  -0.0382 S33:  -0.1059                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   102                          
REMARK   3    ORIGIN FOR THE GROUP (A):  55.1247  66.8861 106.1168              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0693 T22:   0.0208                                     
REMARK   3      T33:   0.0977 T12:  -0.0254                                     
REMARK   3      T13:  -0.0511 T23:   0.0224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7376 L22:   4.6775                                     
REMARK   3      L33:   2.0065 L12:   0.2660                                     
REMARK   3      L13:   0.0758 L23:  -0.6995                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1704 S12:   0.1769 S13:  -0.0928                       
REMARK   3      S21:   0.2838 S22:  -0.0634 S23:  -0.2094                       
REMARK   3      S31:  -0.0020 S32:   0.1089 S33:   0.2338                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   103        C   193                          
REMARK   3    ORIGIN FOR THE GROUP (A):  70.8902  73.9110 109.0188              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1236 T22:   0.1480                                     
REMARK   3      T33:   0.1888 T12:  -0.0643                                     
REMARK   3      T13:  -0.1189 T23:   0.0217                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2762 L22:   3.4083                                     
REMARK   3      L33:   2.5735 L12:  -0.4715                                     
REMARK   3      L13:  -0.0357 L23:  -0.6130                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0440 S12:   0.1356 S13:   0.1461                       
REMARK   3      S21:   0.0849 S22:  -0.0200 S23:  -0.5223                       
REMARK   3      S31:  -0.0769 S32:   0.4282 S33:   0.0640                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   194        C   280                          
REMARK   3    ORIGIN FOR THE GROUP (A):  66.5788  52.4369 111.7933              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1716 T22:   0.0766                                     
REMARK   3      T33:   0.2174 T12:   0.0341                                     
REMARK   3      T13:  -0.1206 T23:   0.0270                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7659 L22:   3.3079                                     
REMARK   3      L33:   2.3399 L12:   0.9591                                     
REMARK   3      L13:   0.4856 L23:   1.4393                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1279 S12:  -0.0416 S13:  -0.4102                       
REMARK   3      S21:   0.3832 S22:   0.1895 S23:  -0.4368                       
REMARK   3      S31:   0.1191 S32:   0.3145 S33:  -0.0617                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   281        C   348                          
REMARK   3    ORIGIN FOR THE GROUP (A):  67.7790  48.0226 104.8011              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0786 T22:   0.0976                                     
REMARK   3      T33:   0.3672 T12:  -0.0390                                     
REMARK   3      T13:  -0.0500 T23:   0.0776                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3530 L22:   2.1828                                     
REMARK   3      L33:   2.4555 L12:  -1.2863                                     
REMARK   3      L13:   0.4960 L23:   1.0340                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2108 S12:   0.1530 S13:  -0.1141                       
REMARK   3      S21:   0.2276 S22:   0.0479 S23:  -0.4719                       
REMARK   3      S31:   0.0625 S32:   0.3968 S33:   0.1629                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   356        C   389                          
REMARK   3    ORIGIN FOR THE GROUP (A):  83.3316  46.0725  94.0544              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6840 T22:   0.8602                                     
REMARK   3      T33:   0.8573 T12:  -0.0529                                     
REMARK   3      T13:  -0.0363 T23:   0.0222                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8962 L22:   0.5558                                     
REMARK   3      L33:   0.4438 L12:  -1.0441                                     
REMARK   3      L13:  -1.0245 L23:   0.4840                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2069 S12:   0.5263 S13:  -0.0748                       
REMARK   3      S21:   0.0258 S22:   0.2983 S23:  -0.1417                       
REMARK   3      S31:  -0.0723 S32:   0.2748 S33:  -0.0914                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   390        C   490                          
REMARK   3    ORIGIN FOR THE GROUP (A):  66.9177  33.5574 101.2971              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1808 T22:   0.0824                                     
REMARK   3      T33:   0.4342 T12:   0.0814                                     
REMARK   3      T13:  -0.0262 T23:  -0.0387                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6448 L22:   2.0877                                     
REMARK   3      L33:   2.9234 L12:   0.0930                                     
REMARK   3      L13:   1.2652 L23:  -0.8938                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0132 S12:   0.1388 S13:  -0.5391                       
REMARK   3      S21:   0.2408 S22:  -0.0005 S23:  -0.4459                       
REMARK   3      S31:   0.4357 S32:   0.3657 S33:  -0.0127                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   491        C   537                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.3538  42.1594  85.5897              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0899 T22:   0.1934                                     
REMARK   3      T33:   0.2581 T12:  -0.0457                                     
REMARK   3      T13:   0.0123 T23:  -0.0836                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3655 L22:   1.4063                                     
REMARK   3      L33:   7.1811 L12:   0.1175                                     
REMARK   3      L13:   0.2703 L23:   2.0620                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3244 S12:   0.4909 S13:   0.1517                       
REMARK   3      S21:  -0.2063 S22:   0.0358 S23:  -0.2155                       
REMARK   3      S31:  -0.5272 S32:  -0.5230 S33:   0.2886                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D   102                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.7685  76.9494  82.2803              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0671 T22:   0.2077                                     
REMARK   3      T33:   0.0561 T12:  -0.0299                                     
REMARK   3      T13:  -0.0217 T23:   0.0623                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5303 L22:   1.8953                                     
REMARK   3      L33:   1.0925 L12:  -0.0136                                     
REMARK   3      L13:   1.3245 L23:   0.0902                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0738 S12:   0.4023 S13:   0.0037                       
REMARK   3      S21:  -0.1698 S22:  -0.1870 S23:   0.0225                       
REMARK   3      S31:   0.0278 S32:   0.1117 S33:   0.1132                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   103        D   177                          
REMARK   3    ORIGIN FOR THE GROUP (A):  58.3407  89.3780  84.3674              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0812 T22:   0.2013                                     
REMARK   3      T33:   0.2101 T12:  -0.0755                                     
REMARK   3      T13:  -0.0200 T23:   0.1461                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5820 L22:   3.1407                                     
REMARK   3      L33:   2.9601 L12:  -1.1044                                     
REMARK   3      L13:   0.5251 L23:  -0.2420                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1263 S12:   0.1130 S13:   0.6771                       
REMARK   3      S21:  -0.0567 S22:  -0.0498 S23:  -0.2740                       
REMARK   3      S31:  -0.2481 S32:   0.2610 S33:   0.1761                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   178        D   280                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.5890  92.8686  77.3741              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1273 T22:   0.2379                                     
REMARK   3      T33:   0.2140 T12:  -0.0222                                     
REMARK   3      T13:  -0.0275 T23:   0.1742                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8469 L22:   0.7946                                     
REMARK   3      L33:   1.2716 L12:  -0.0334                                     
REMARK   3      L13:   0.0283 L23:   0.1648                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0709 S12:   0.5842 S13:   0.4469                       
REMARK   3      S21:  -0.1885 S22:  -0.0193 S23:  -0.1596                       
REMARK   3      S31:  -0.1824 S32:   0.0739 S33:  -0.0516                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   281        D   346                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.3072  91.7386  82.8803              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0940 T22:   0.1329                                     
REMARK   3      T33:   0.1149 T12:  -0.1057                                     
REMARK   3      T13:  -0.0844 T23:   0.1129                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4389 L22:   2.8248                                     
REMARK   3      L33:   1.1964 L12:  -1.4574                                     
REMARK   3      L13:  -0.2403 L23:   0.1024                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0469 S12:   0.2356 S13:   0.2962                       
REMARK   3      S21:   0.0307 S22:  -0.1419 S23:  -0.2740                       
REMARK   3      S31:  -0.1512 S32:   0.1341 S33:   0.1888                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   358        D   390                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.7417 104.8873  95.8538              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6454 T22:   0.6398                                     
REMARK   3      T33:   0.5204 T12:  -0.0861                                     
REMARK   3      T13:  -0.1527 T23:  -0.0810                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5109 L22:  12.7086                                     
REMARK   3      L33:   0.9787 L12:  -1.2207                                     
REMARK   3      L13:   0.4373 L23:  -3.2972                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3339 S12:  -0.5848 S13:   0.5506                       
REMARK   3      S21:   0.8675 S22:   0.3040 S23:  -0.1263                       
REMARK   3      S31:  -0.4234 S32:   0.0249 S33:   0.0299                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   391        D   506                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.2006  90.0100  86.0619              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0639 T22:   0.1211                                     
REMARK   3      T33:   0.0985 T12:   0.0357                                     
REMARK   3      T13:  -0.0326 T23:  -0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0808 L22:   2.8295                                     
REMARK   3      L33:   2.3247 L12:   0.7936                                     
REMARK   3      L13:   0.2692 L23:  -1.6595                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1038 S12:   0.2708 S13:   0.1737                       
REMARK   3      S21:   0.1428 S22:  -0.0787 S23:   0.3247                       
REMARK   3      S31:  -0.2548 S32:  -0.0865 S33:  -0.0250                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   507        D   537                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.5029  72.1587  97.6297              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1744 T22:   0.0171                                     
REMARK   3      T33:   0.1957 T12:  -0.0065                                     
REMARK   3      T13:  -0.0451 T23:   0.0325                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4533 L22:   2.4336                                     
REMARK   3      L33:  17.6806 L12:   0.7481                                     
REMARK   3      L13:  -2.3959 L23:  -3.2825                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1811 S12:  -0.1986 S13:  -0.2526                       
REMARK   3      S21:   0.3411 S22:  -0.0162 S23:  -0.1758                       
REMARK   3      S31:   0.7703 S32:  -0.1077 S33:   0.1973                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     1        E   106                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.7876  31.9120  99.3419              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0257 T22:   0.0072                                     
REMARK   3      T33:   0.0407 T12:  -0.0105                                     
REMARK   3      T13:   0.0219 T23:  -0.0147                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3129 L22:   4.1879                                     
REMARK   3      L33:   3.4354 L12:   1.3669                                     
REMARK   3      L13:   0.4203 L23:   1.3116                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0978 S12:  -0.0016 S13:   0.0869                       
REMARK   3      S21:   0.0693 S22:   0.0028 S23:   0.0846                       
REMARK   3      S31:   0.1161 S32:  -0.0900 S33:   0.0951                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   107        E   191                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.4417  25.3043  99.5454              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0701 T22:   0.1037                                     
REMARK   3      T33:   0.1710 T12:  -0.0630                                     
REMARK   3      T13:   0.0182 T23:  -0.0153                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1805 L22:   3.7771                                     
REMARK   3      L33:   3.1037 L12:   0.0222                                     
REMARK   3      L13:  -0.0476 L23:   1.1131                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0361 S12:   0.0807 S13:  -0.1091                       
REMARK   3      S21:  -0.0846 S22:  -0.0354 S23:   0.7180                       
REMARK   3      S31:   0.0824 S32:  -0.4455 S33:   0.0715                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 32                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   192        E   280                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.3385  42.4617 111.3873              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1182 T22:   0.1198                                     
REMARK   3      T33:   0.0951 T12:  -0.0051                                     
REMARK   3      T13:   0.0825 T23:  -0.0474                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2788 L22:   3.8115                                     
REMARK   3      L33:   1.1235 L12:   0.5613                                     
REMARK   3      L13:  -0.4790 L23:  -0.8208                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0260 S12:  -0.0888 S13:   0.1162                       
REMARK   3      S21:   0.4351 S22:   0.0366 S23:   0.4551                       
REMARK   3      S31:   0.0196 S32:  -0.1546 S33:  -0.0626                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 33                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   281        E   346                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.8224  49.7951 107.4847              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0367 T22:   0.1170                                     
REMARK   3      T33:   0.0820 T12:  -0.0251                                     
REMARK   3      T13:   0.0443 T23:  -0.0332                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9714 L22:   2.9246                                     
REMARK   3      L33:   1.3899 L12:  -0.0364                                     
REMARK   3      L13:  -0.5461 L23:  -0.2855                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0684 S12:   0.0128 S13:   0.2023                       
REMARK   3      S21:   0.2527 S22:   0.0698 S23:   0.3559                       
REMARK   3      S31:   0.0364 S32:  -0.3409 S33:  -0.0014                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 34                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   360        E   389                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.3571  55.6734  99.5710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4836 T22:   0.7049                                     
REMARK   3      T33:   0.7924 T12:   0.0820                                     
REMARK   3      T13:  -0.0730 T23:   0.0085                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.5239 L22:   0.5563                                     
REMARK   3      L33:   4.6540 L12:  -0.1826                                     
REMARK   3      L13:  -7.6148 L23:   0.2188                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0205 S12:   0.5372 S13:   0.4613                       
REMARK   3      S21:  -0.2059 S22:   0.1272 S23:   0.5938                       
REMARK   3      S31:  -0.0179 S32:  -0.2973 S33:  -0.1477                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 35                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   390        E   393                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6367  49.7420  96.7083              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.5765 T22:   0.9592                                     
REMARK   3      T33:   0.3736 T12:  -0.6537                                     
REMARK   3      T13:  -0.2449 T23:   0.3982                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  65.0958 L22: 105.3162                                     
REMARK   3      L33:   5.4307 L12: -82.7882                                     
REMARK   3      L13:  18.7968 L23: -23.9137                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -2.9171 S12:  -3.2938 S13:  -4.3700                       
REMARK   3      S21:   3.3940 S22:   4.2491 S23:   5.6038                       
REMARK   3      S31:  -0.7418 S32:  -0.9725 S33:  -1.3320                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 36                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   394        E   490                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.1778  64.8243 110.4589              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2652 T22:   0.0677                                     
REMARK   3      T33:   0.2340 T12:   0.0709                                     
REMARK   3      T13:   0.0465 T23:  -0.0791                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7908 L22:   3.1442                                     
REMARK   3      L33:   3.6745 L12:   1.3026                                     
REMARK   3      L13:  -1.6029 L23:  -1.1225                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0611 S12:  -0.2961 S13:   0.7372                       
REMARK   3      S21:   0.7089 S22:   0.0059 S23:   0.3109                       
REMARK   3      S31:  -0.5390 S32:  -0.2355 S33:  -0.0670                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 37                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   491        E   537                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.1597  63.5941  91.9954              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0443 T22:   0.1934                                     
REMARK   3      T33:   0.1882 T12:  -0.0522                                     
REMARK   3      T13:  -0.0458 T23:   0.1237                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7241 L22:   3.8333                                     
REMARK   3      L33:   7.7609 L12:   2.0310                                     
REMARK   3      L13:  -0.0369 L23:  -2.3141                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3407 S12:   0.4910 S13:   0.4534                       
REMARK   3      S21:  -0.3028 S22:  -0.0956 S23:  -0.0070                       
REMARK   3      S31:   0.1141 S32:   0.4958 S33:   0.4363                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 38                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     1        F    56                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.6380  81.2537 136.3248              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2580 T22:   0.1398                                     
REMARK   3      T33:   0.0966 T12:   0.0825                                     
REMARK   3      T13:  -0.1464 T23:  -0.0102                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8578 L22:   2.8859                                     
REMARK   3      L33:   2.5404 L12:  -0.3035                                     
REMARK   3      L13:   0.0682 L23:  -1.2801                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0407 S12:  -0.0446 S13:  -0.0009                       
REMARK   3      S21:  -0.1186 S22:  -0.0027 S23:   0.1396                       
REMARK   3      S31:  -0.0793 S32:  -0.0222 S33:   0.0434                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 39                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F    57        F   188                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.2801  84.9394 126.3531              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3043 T22:   0.2089                                     
REMARK   3      T33:   0.1768 T12:   0.0901                                     
REMARK   3      T13:  -0.1560 T23:  -0.0441                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4709 L22:   1.7979                                     
REMARK   3      L33:   1.9094 L12:   0.3714                                     
REMARK   3      L13:  -0.0389 L23:  -0.2797                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0348 S12:  -0.0919 S13:   0.1662                       
REMARK   3      S21:   0.0105 S22:  -0.0323 S23:   0.3997                       
REMARK   3      S31:  -0.0883 S32:  -0.3993 S33:  -0.0025                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 40                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   189        F   292                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.9622  71.2704 141.9802              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2911 T22:   0.2198                                     
REMARK   3      T33:   0.2564 T12:  -0.0253                                     
REMARK   3      T13:  -0.1640 T23:   0.0146                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7883 L22:   0.8253                                     
REMARK   3      L33:   2.9805 L12:   0.4505                                     
REMARK   3      L13:   0.4492 L23:   0.2459                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0092 S12:  -0.1111 S13:  -0.3061                       
REMARK   3      S21:  -0.1370 S22:  -0.0481 S23:   0.2563                       
REMARK   3      S31:   0.2197 S32:  -0.5609 S33:   0.0388                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 41                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   293        F   346                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.2786  78.8267 152.9023              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3048 T22:   0.3939                                     
REMARK   3      T33:   0.4044 T12:   0.1280                                     
REMARK   3      T13:  -0.1735 T23:   0.1267                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7795 L22:   0.7919                                     
REMARK   3      L33:   2.7011 L12:   0.4350                                     
REMARK   3      L13:  -0.6055 L23:   0.9244                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0827 S12:   0.0348 S13:   0.1183                       
REMARK   3      S21:  -0.0566 S22:  -0.0523 S23:   0.3792                       
REMARK   3      S31:   0.0396 S32:  -0.5958 S33:   0.1349                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 42                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   355        F   390                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.0522  85.7358 156.4400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6232 T22:   0.7432                                     
REMARK   3      T33:   0.7806 T12:  -0.0036                                     
REMARK   3      T13:  -0.0753 T23:   0.0400                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.7062 L22:   2.2239                                     
REMARK   3      L33:   0.0623 L12:   3.7104                                     
REMARK   3      L13:  -0.4680 L23:  -0.1584                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0905 S12:   0.0510 S13:   0.4650                       
REMARK   3      S21:  -0.4463 S22:   0.0247 S23:   0.5859                       
REMARK   3      S31:   0.0054 S32:  -0.0694 S33:   0.0659                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 43                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   391        F   490                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.8450  73.3922 165.1436              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2554 T22:   0.3769                                     
REMARK   3      T33:   0.2341 T12:   0.0062                                     
REMARK   3      T13:  -0.0315 T23:   0.0272                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0678 L22:   1.8749                                     
REMARK   3      L33:   2.3430 L12:   0.6745                                     
REMARK   3      L13:   1.5263 L23:   0.0144                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0974 S12:  -0.3736 S13:  -0.3047                       
REMARK   3      S21:   0.2046 S22:  -0.0679 S23:   0.3425                       
REMARK   3      S31:   0.2649 S32:  -0.5768 S33:  -0.0294                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 44                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   491        F   537                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.3109  91.5607 164.0846              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3781 T22:   0.2282                                     
REMARK   3      T33:   0.2182 T12:   0.0414                                     
REMARK   3      T13:  -0.1340 T23:   0.0321                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0531 L22:   5.8528                                     
REMARK   3      L33:   3.3153 L12:   1.5643                                     
REMARK   3      L13:  -0.7420 L23:   2.8088                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0847 S12:  -0.0016 S13:   0.4025                       
REMARK   3      S21:  -0.6080 S22:   0.2208 S23:  -0.0389                       
REMARK   3      S31:  -0.6882 S32:   0.3225 S33:  -0.1361                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 45                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G     1        G   106                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.0225 109.7173 133.0392              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4683 T22:   0.1407                                     
REMARK   3      T33:   0.1195 T12:   0.1026                                     
REMARK   3      T13:  -0.0559 T23:   0.0288                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3969 L22:   1.7847                                     
REMARK   3      L33:   2.2710 L12:   1.0453                                     
REMARK   3      L13:   1.7274 L23:   0.0921                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0865 S12:  -0.1359 S13:   0.1939                       
REMARK   3      S21:   0.0107 S22:  -0.0123 S23:   0.1859                       
REMARK   3      S31:  -0.2395 S32:   0.0190 S33:  -0.0742                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 46                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G   107        G   175                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.0519 112.4976 120.4744              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4449 T22:   0.1470                                     
REMARK   3      T33:   0.2311 T12:   0.1903                                     
REMARK   3      T13:  -0.1260 T23:   0.0025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5122 L22:   2.0145                                     
REMARK   3      L33:   4.7780 L12:   0.6642                                     
REMARK   3      L13:   0.1663 L23:  -0.0905                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0227 S12:   0.2193 S13:   0.1576                       
REMARK   3      S21:  -0.0076 S22:   0.0234 S23:   0.3334                       
REMARK   3      S31:  -0.1309 S32:  -0.4094 S33:  -0.0006                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 47                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G   176        G   286                          
REMARK   3    ORIGIN FOR THE GROUP (A):  48.2248 121.1553 121.1770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5771 T22:   0.1324                                     
REMARK   3      T33:   0.2491 T12:   0.0616                                     
REMARK   3      T13:  -0.0837 T23:   0.0204                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3112 L22:   1.1127                                     
REMARK   3      L33:   0.9179 L12:   0.4132                                     
REMARK   3      L13:  -0.0301 L23:  -0.6381                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0423 S12:   0.1683 S13:   0.3438                       
REMARK   3      S21:   0.0941 S22:  -0.0745 S23:   0.0575                       
REMARK   3      S31:  -0.3582 S32:   0.0338 S33:   0.0322                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 48                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G   287        G   346                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.9498 115.6595 117.4706              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3982 T22:   0.2541                                     
REMARK   3      T33:   0.2670 T12:  -0.0515                                     
REMARK   3      T13:  -0.1530 T23:   0.0319                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8770 L22:   2.3064                                     
REMARK   3      L33:   1.9324 L12:  -0.6423                                     
REMARK   3      L13:  -0.4592 L23:  -0.6601                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1060 S12:   0.2184 S13:   0.3144                       
REMARK   3      S21:  -0.2219 S22:  -0.0425 S23:  -0.2434                       
REMARK   3      S31:  -0.0494 S32:   0.0123 S33:  -0.0634                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 49                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G   357        G   393                          
REMARK   3    ORIGIN FOR THE GROUP (A):  58.8343 109.3758 103.7220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7661 T22:   0.8362                                     
REMARK   3      T33:   0.5196 T12:  -0.0885                                     
REMARK   3      T13:  -0.0639 T23:   0.0030                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1710 L22:   1.6981                                     
REMARK   3      L33:   6.5133 L12:  -0.3756                                     
REMARK   3      L13:   0.6890 L23:  -2.9760                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0001 S12:   0.2133 S13:  -0.0336                       
REMARK   3      S21:  -0.4482 S22:  -0.1651 S23:  -0.1919                       
REMARK   3      S31:   0.7519 S32:  -0.4018 S33:   0.1653                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 50                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G   394        G   491                          
REMARK   3    ORIGIN FOR THE GROUP (A):  72.9647 116.2141 118.2041              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5387 T22:   0.3628                                     
REMARK   3      T33:   0.3168 T12:  -0.0647                                     
REMARK   3      T13:  -0.0214 T23:   0.1154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2605 L22:   3.2469                                     
REMARK   3      L33:   0.8807 L12:   0.1645                                     
REMARK   3      L13:   0.2610 L23:  -0.6367                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0749 S12:   0.2478 S13:   0.3831                       
REMARK   3      S21:  -0.1015 S22:  -0.1729 S23:  -0.3611                       
REMARK   3      S31:  -0.1918 S32:   0.5175 S33:   0.0981                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 51                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G   492        G   537                          
REMARK   3    ORIGIN FOR THE GROUP (A):  69.6478  95.8632 129.9209              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3921 T22:   0.2425                                     
REMARK   3      T33:   0.1387 T12:  -0.0445                                     
REMARK   3      T13:  -0.1705 T23:   0.0340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7621 L22:   7.3560                                     
REMARK   3      L33:   2.3672 L12:  -1.9580                                     
REMARK   3      L13:  -0.9004 L23:   1.2198                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0144 S12:   0.0006 S13:  -0.2139                       
REMARK   3      S21:   0.1793 S22:  -0.0810 S23:   0.1283                       
REMARK   3      S31:   0.1090 S32:  -0.1001 S33:   0.0954                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 52                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     1        H   106                          
REMARK   3    ORIGIN FOR THE GROUP (A):  82.4843  98.5096 177.7386              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2912 T22:   0.0383                                     
REMARK   3      T33:   0.0320 T12:  -0.0720                                     
REMARK   3      T13:  -0.0308 T23:   0.0100                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2949 L22:   1.9046                                     
REMARK   3      L33:   1.7084 L12:  -1.2719                                     
REMARK   3      L13:   0.0704 L23:   0.1734                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1403 S12:   0.1900 S13:   0.0871                       
REMARK   3      S21:  -0.0842 S22:   0.0165 S23:  -0.1334                       
REMARK   3      S31:  -0.1803 S32:   0.0542 S33:  -0.1568                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 53                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   107        H   195                          
REMARK   3    ORIGIN FOR THE GROUP (A):  90.1703  95.4430 193.2606              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3515 T22:   0.1693                                     
REMARK   3      T33:   0.1096 T12:  -0.0659                                     
REMARK   3      T13:  -0.1204 T23:   0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9236 L22:   2.2202                                     
REMARK   3      L33:   3.1309 L12:  -0.6546                                     
REMARK   3      L13:  -0.0641 L23:  -0.0646                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0310 S12:  -0.4709 S13:  -0.0453                       
REMARK   3      S21:   0.2195 S22:   0.0774 S23:  -0.3047                       
REMARK   3      S31:   0.1027 S32:   0.4350 S33:  -0.0464                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 54                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   196        H   285                          
REMARK   3    ORIGIN FOR THE GROUP (A):  69.6346 103.6016 191.4634              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3671 T22:   0.0070                                     
REMARK   3      T33:   0.0731 T12:  -0.0100                                     
REMARK   3      T13:  -0.0100 T23:  -0.0135                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8717 L22:   0.9913                                     
REMARK   3      L33:   1.0788 L12:   0.8316                                     
REMARK   3      L13:  -1.1008 L23:   0.3811                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2207 S12:  -0.1176 S13:   0.1749                       
REMARK   3      S21:  -0.0795 S22:  -0.0420 S23:  -0.0819                       
REMARK   3      S31:  -0.2469 S32:   0.0357 S33:  -0.1787                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 55                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   286        H   346                          
REMARK   3    ORIGIN FOR THE GROUP (A):  64.0784  96.0236 193.5728              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1654 T22:   0.0260                                     
REMARK   3      T33:   0.0625 T12:   0.0374                                     
REMARK   3      T13:  -0.0901 T23:  -0.0254                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0304 L22:   2.5633                                     
REMARK   3      L33:   3.5694 L12:   0.9108                                     
REMARK   3      L13:  -1.5402 L23:   0.3380                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0097 S12:  -0.1343 S13:   0.0979                       
REMARK   3      S21:   0.1334 S22:  -0.0074 S23:   0.1049                       
REMARK   3      S31:  -0.0091 S32:   0.2369 S33:  -0.0022                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 56                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   354        H   393                          
REMARK   3    ORIGIN FOR THE GROUP (A):  63.7727  83.8783 201.2997              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6704 T22:   0.2376                                     
REMARK   3      T33:   0.3657 T12:   0.1113                                     
REMARK   3      T13:   0.0486 T23:  -0.0051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1687 L22:   0.3568                                     
REMARK   3      L33:   7.1405 L12:  -0.0597                                     
REMARK   3      L13:   0.5162 L23:   1.0933                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0393 S12:   0.0074 S13:  -0.0678                       
REMARK   3      S21:   0.2085 S22:   0.2570 S23:  -0.0919                       
REMARK   3      S31:   0.9817 S32:   1.1125 S33:  -0.2177                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 57                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   394        H   504                          
REMARK   3    ORIGIN FOR THE GROUP (A):  48.7727  95.2389 190.8243              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2557 T22:   0.1013                                     
REMARK   3      T33:   0.1928 T12:   0.0709                                     
REMARK   3      T13:   0.0366 T23:   0.0182                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3935 L22:   1.7334                                     
REMARK   3      L33:   3.4332 L12:  -0.3258                                     
REMARK   3      L13:   0.9391 L23:   1.1344                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1154 S12:  -0.0443 S13:   0.2293                       
REMARK   3      S21:  -0.0285 S22:  -0.2047 S23:   0.2877                       
REMARK   3      S31:  -0.2657 S32:  -0.5545 S33:   0.0893                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 58                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   505        H   537                          
REMARK   3    ORIGIN FOR THE GROUP (A):  55.7289  84.4844 171.7650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2338 T22:   0.2859                                     
REMARK   3      T33:   0.2353 T12:   0.0796                                     
REMARK   3      T13:  -0.0772 T23:  -0.1280                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4098 L22:   9.6574                                     
REMARK   3      L33:   4.2422 L12:   1.2843                                     
REMARK   3      L13:  -0.5035 L23:   1.8043                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0855 S12:   0.1940 S13:  -0.1648                       
REMARK   3      S21:  -1.2057 S22:   0.2192 S23:  -0.4160                       
REMARK   3      S31:  -0.1751 S32:  -0.0486 S33:  -0.1337                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3ODM COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB060982.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JUN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03948                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 116208                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 56.830                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 14.300                             
REMARK 200  R MERGE                    (I) : 0.13300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELX                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.61                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5M SODIUM MALONATE, PH 7.0, VAPOR      
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 295K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       60.71000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      139.99000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       80.79000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      139.99000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       60.71000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       80.79000            
REMARK 290   SMTRY3   4  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                                        
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 72810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 73150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F, G, 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: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G                                  
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 A   -22                                                      
REMARK 465     GLY A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     ILE A    -6                                                      
REMARK 465     ASP A    -5                                                      
REMARK 465     ASP A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     ASP A    -2                                                      
REMARK 465     LYS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     LYS A   347                                                      
REMARK 465     ALA A   348                                                      
REMARK 465     LYS A   349                                                      
REMARK 465     THR A   350                                                      
REMARK 465     GLY A   351                                                      
REMARK 465     LEU A   352                                                      
REMARK 465     GLU A   353                                                      
REMARK 465     TYR A   354                                                      
REMARK 465     ASN A   355                                                      
REMARK 465     ARG A   356                                                      
REMARK 465     GLU A   357                                                      
REMARK 465     VAL A   358                                                      
REMARK 465     MET B   -22                                                      
REMARK 465     GLY B   -21                                                      
REMARK 465     HIS B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     SER B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     GLY B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     ILE B    -6                                                      
REMARK 465     ASP B    -5                                                      
REMARK 465     ASP B    -4                                                      
REMARK 465     ASP B    -3                                                      
REMARK 465     ASP B    -2                                                      
REMARK 465     LYS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     LYS B   347                                                      
REMARK 465     ALA B   348                                                      
REMARK 465     LYS B   349                                                      
REMARK 465     THR B   350                                                      
REMARK 465     GLY B   351                                                      
REMARK 465     LEU B   352                                                      
REMARK 465     GLU B   353                                                      
REMARK 465     TYR B   354                                                      
REMARK 465     MET C   -22                                                      
REMARK 465     GLY C   -21                                                      
REMARK 465     HIS C   -20                                                      
REMARK 465     HIS C   -19                                                      
REMARK 465     HIS C   -18                                                      
REMARK 465     HIS C   -17                                                      
REMARK 465     HIS C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     SER C   -10                                                      
REMARK 465     SER C    -9                                                      
REMARK 465     GLY C    -8                                                      
REMARK 465     HIS C    -7                                                      
REMARK 465     ILE C    -6                                                      
REMARK 465     ASP C    -5                                                      
REMARK 465     ASP C    -4                                                      
REMARK 465     ASP C    -3                                                      
REMARK 465     ASP C    -2                                                      
REMARK 465     LYS C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     LYS C   349                                                      
REMARK 465     THR C   350                                                      
REMARK 465     GLY C   351                                                      
REMARK 465     LEU C   352                                                      
REMARK 465     GLU C   353                                                      
REMARK 465     TYR C   354                                                      
REMARK 465     ASN C   355                                                      
REMARK 465     MET D   -22                                                      
REMARK 465     GLY D   -21                                                      
REMARK 465     HIS D   -20                                                      
REMARK 465     HIS D   -19                                                      
REMARK 465     HIS D   -18                                                      
REMARK 465     HIS D   -17                                                      
REMARK 465     HIS D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     SER D   -10                                                      
REMARK 465     SER D    -9                                                      
REMARK 465     GLY D    -8                                                      
REMARK 465     HIS D    -7                                                      
REMARK 465     ILE D    -6                                                      
REMARK 465     ASP D    -5                                                      
REMARK 465     ASP D    -4                                                      
REMARK 465     ASP D    -3                                                      
REMARK 465     ASP D    -2                                                      
REMARK 465     LYS D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     LYS D   347                                                      
REMARK 465     ALA D   348                                                      
REMARK 465     LYS D   349                                                      
REMARK 465     THR D   350                                                      
REMARK 465     GLY D   351                                                      
REMARK 465     LEU D   352                                                      
REMARK 465     GLU D   353                                                      
REMARK 465     TYR D   354                                                      
REMARK 465     ASN D   355                                                      
REMARK 465     ARG D   356                                                      
REMARK 465     GLU D   357                                                      
REMARK 465     MET E   -22                                                      
REMARK 465     GLY E   -21                                                      
REMARK 465     HIS E   -20                                                      
REMARK 465     HIS E   -19                                                      
REMARK 465     HIS E   -18                                                      
REMARK 465     HIS E   -17                                                      
REMARK 465     HIS E   -16                                                      
REMARK 465     HIS E   -15                                                      
REMARK 465     HIS E   -14                                                      
REMARK 465     HIS E   -13                                                      
REMARK 465     HIS E   -12                                                      
REMARK 465     HIS E   -11                                                      
REMARK 465     SER E   -10                                                      
REMARK 465     SER E    -9                                                      
REMARK 465     GLY E    -8                                                      
REMARK 465     HIS E    -7                                                      
REMARK 465     ILE E    -6                                                      
REMARK 465     ASP E    -5                                                      
REMARK 465     ASP E    -4                                                      
REMARK 465     ASP E    -3                                                      
REMARK 465     ASP E    -2                                                      
REMARK 465     LYS E    -1                                                      
REMARK 465     HIS E     0                                                      
REMARK 465     LYS E   347                                                      
REMARK 465     ALA E   348                                                      
REMARK 465     LYS E   349                                                      
REMARK 465     THR E   350                                                      
REMARK 465     GLY E   351                                                      
REMARK 465     LEU E   352                                                      
REMARK 465     GLU E   353                                                      
REMARK 465     TYR E   354                                                      
REMARK 465     ASN E   355                                                      
REMARK 465     ARG E   356                                                      
REMARK 465     GLU E   357                                                      
REMARK 465     VAL E   358                                                      
REMARK 465     ALA E   359                                                      
REMARK 465     MET F   -22                                                      
REMARK 465     GLY F   -21                                                      
REMARK 465     HIS F   -20                                                      
REMARK 465     HIS F   -19                                                      
REMARK 465     HIS F   -18                                                      
REMARK 465     HIS F   -17                                                      
REMARK 465     HIS F   -16                                                      
REMARK 465     HIS F   -15                                                      
REMARK 465     HIS F   -14                                                      
REMARK 465     HIS F   -13                                                      
REMARK 465     HIS F   -12                                                      
REMARK 465     HIS F   -11                                                      
REMARK 465     SER F   -10                                                      
REMARK 465     SER F    -9                                                      
REMARK 465     GLY F    -8                                                      
REMARK 465     HIS F    -7                                                      
REMARK 465     ILE F    -6                                                      
REMARK 465     ASP F    -5                                                      
REMARK 465     ASP F    -4                                                      
REMARK 465     ASP F    -3                                                      
REMARK 465     ASP F    -2                                                      
REMARK 465     LYS F    -1                                                      
REMARK 465     HIS F     0                                                      
REMARK 465     LYS F   347                                                      
REMARK 465     ALA F   348                                                      
REMARK 465     LYS F   349                                                      
REMARK 465     THR F   350                                                      
REMARK 465     GLY F   351                                                      
REMARK 465     LEU F   352                                                      
REMARK 465     GLU F   353                                                      
REMARK 465     TYR F   354                                                      
REMARK 465     MET G   -22                                                      
REMARK 465     GLY G   -21                                                      
REMARK 465     HIS G   -20                                                      
REMARK 465     HIS G   -19                                                      
REMARK 465     HIS G   -18                                                      
REMARK 465     HIS G   -17                                                      
REMARK 465     HIS G   -16                                                      
REMARK 465     HIS G   -15                                                      
REMARK 465     HIS G   -14                                                      
REMARK 465     HIS G   -13                                                      
REMARK 465     HIS G   -12                                                      
REMARK 465     HIS G   -11                                                      
REMARK 465     SER G   -10                                                      
REMARK 465     SER G    -9                                                      
REMARK 465     GLY G    -8                                                      
REMARK 465     HIS G    -7                                                      
REMARK 465     ILE G    -6                                                      
REMARK 465     ASP G    -5                                                      
REMARK 465     ASP G    -4                                                      
REMARK 465     ASP G    -3                                                      
REMARK 465     ASP G    -2                                                      
REMARK 465     LYS G    -1                                                      
REMARK 465     HIS G     0                                                      
REMARK 465     LYS G   347                                                      
REMARK 465     ALA G   348                                                      
REMARK 465     LYS G   349                                                      
REMARK 465     THR G   350                                                      
REMARK 465     GLY G   351                                                      
REMARK 465     LEU G   352                                                      
REMARK 465     GLU G   353                                                      
REMARK 465     TYR G   354                                                      
REMARK 465     ASN G   355                                                      
REMARK 465     ARG G   356                                                      
REMARK 465     MET H   -22                                                      
REMARK 465     GLY H   -21                                                      
REMARK 465     HIS H   -20                                                      
REMARK 465     HIS H   -19                                                      
REMARK 465     HIS H   -18                                                      
REMARK 465     HIS H   -17                                                      
REMARK 465     HIS H   -16                                                      
REMARK 465     HIS H   -15                                                      
REMARK 465     HIS H   -14                                                      
REMARK 465     HIS H   -13                                                      
REMARK 465     HIS H   -12                                                      
REMARK 465     HIS H   -11                                                      
REMARK 465     SER H   -10                                                      
REMARK 465     SER H    -9                                                      
REMARK 465     GLY H    -8                                                      
REMARK 465     HIS H    -7                                                      
REMARK 465     ILE H    -6                                                      
REMARK 465     ASP H    -5                                                      
REMARK 465     ASP H    -4                                                      
REMARK 465     ASP H    -3                                                      
REMARK 465     ASP H    -2                                                      
REMARK 465     LYS H    -1                                                      
REMARK 465     HIS H     0                                                      
REMARK 465     LYS H   347                                                      
REMARK 465     ALA H   348                                                      
REMARK 465     LYS H   349                                                      
REMARK 465     THR H   350                                                      
REMARK 465     GLY H   351                                                      
REMARK 465     LEU H   352                                                      
REMARK 465     GLU H   353                                                      
REMARK 465     ASP H   381                                                      
REMARK 465     ASN H   382                                                      
REMARK 465     SER H   383                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS B 340    CG   CD   CE   NZ                                   
REMARK 470     ASN B 355    CG   OD1                                            
REMARK 470     VAL B 358    CG1  CG2                                            
REMARK 470     LYS B 369    CD   CE   NZ                                        
REMARK 470     ALA C 348    C    O    CB                                        
REMARK 470     ARG C 356    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL C 358    CG1  CG2                                            
REMARK 470     ARG C 390    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS E 192    CG   CD   CE   NZ                                   
REMARK 470     ARG F 175    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN F 355    CG   OD1                                            
REMARK 470     ARG F 356    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL F 358    CG1  CG2                                            
REMARK 470     LYS F 384    CG   CD   CE   NZ                                   
REMARK 470     GLU G 357    CG   CD   OE1  OE2                                  
REMARK 470     VAL G 358    CG1  CG2                                            
REMARK 470     ASN H 355    CG   OD1                                            
REMARK 470     LYS H 384    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   SG   CYS E     5    AU    AUC E   605              1.32            
REMARK 500   SG   CYS A     5    AU    AUC A   608              1.54            
REMARK 500   SG   CYS B     5    AU    AUC B   609              1.56            
REMARK 500   SG   CYS D     5    AU    AUC D   604              1.64            
REMARK 500   SG   CYS C     5    AU    AUC C   601              1.65            
REMARK 500   OE1  GLU H   279    AU    AUC H   617              1.71            
REMARK 500   OH   TYR C    18     OD2  ASP C   343              2.05            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A   5   CA  -  CB  -  SG  ANGL. DEV. =   7.5 DEGREES          
REMARK 500    CYS G   5   CA  -  CB  -  SG  ANGL. DEV. =   8.6 DEGREES          
REMARK 500    CYS H   5   CA  -  CB  -  SG  ANGL. DEV. =   6.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
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    PRO A  12       47.04    -83.69                                   
REMARK 500    LEU A  53       31.49    -86.99                                   
REMARK 500    GLU A  89     -144.99   -107.34                                   
REMARK 500    ASN A 300       73.35     47.60                                   
REMARK 500    ASN A 341       31.05    -90.78                                   
REMARK 500    ASP A 366       -8.19    -53.58                                   
REMARK 500    SER A 379       61.43   -104.86                                   
REMARK 500    ASP A 381      107.70    -57.82                                   
REMARK 500    SER A 383       38.25    -67.63                                   
REMARK 500    LYS A 454       -6.36     78.98                                   
REMARK 500    ILE A 455      -63.36   -100.97                                   
REMARK 500    ASN A 476       59.66     32.96                                   
REMARK 500    PRO B  12       45.52    -89.50                                   
REMARK 500    LEU B  53       30.52    -74.78                                   
REMARK 500    LYS B  75      -63.56   -124.89                                   
REMARK 500    GLU B  89     -104.09    -81.16                                   
REMARK 500    GLU B 126      -39.86   -133.45                                   
REMARK 500    ALA B 171      -75.64    -83.47                                   
REMARK 500    ASN B 172       55.88    -69.91                                   
REMARK 500    ASN B 300       73.03     31.94                                   
REMARK 500    ASP B 366      -15.58    -49.99                                   
REMARK 500    ASN B 448      113.05   -163.17                                   
REMARK 500    LYS B 454        6.33     90.08                                   
REMARK 500    ASN B 476       70.57     36.69                                   
REMARK 500    LYS C   2      163.18    -44.91                                   
REMARK 500    PRO C  12       40.73    -81.02                                   
REMARK 500    LEU C  53       36.19    -77.65                                   
REMARK 500    GLU C  89     -112.63    -79.83                                   
REMARK 500    GLU C 126      -61.16   -130.67                                   
REMARK 500    GLU C 130      -54.79    -24.65                                   
REMARK 500    ASN C 172       28.49   -140.84                                   
REMARK 500    ALA C 294        0.34    -53.44                                   
REMARK 500    ASN C 300       76.42     65.72                                   
REMARK 500    ASN C 341       42.74   -101.41                                   
REMARK 500    THR C 346       80.86    -15.96                                   
REMARK 500    LYS C 347       49.82    173.59                                   
REMARK 500    GLU C 357      126.16    155.87                                   
REMARK 500    VAL C 372       -1.49    -59.88                                   
REMARK 500    ILE C 377      -74.46    -72.07                                   
REMARK 500    ASN C 382       35.06   -147.52                                   
REMARK 500    GLU C 385       55.33    -60.18                                   
REMARK 500    GLU C 424      -57.61    -20.87                                   
REMARK 500    ASN C 476       52.07     27.78                                   
REMARK 500    GLU C 509      -55.60    -25.65                                   
REMARK 500    PRO D  12       47.03    -88.49                                   
REMARK 500    PRO D  34      154.48    -49.38                                   
REMARK 500    LEU D  53       34.98    -81.94                                   
REMARK 500    GLU D  89     -116.46   -105.72                                   
REMARK 500    ASN D 156       18.88     51.50                                   
REMARK 500    ASN D 172       59.31   -110.68                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     119 RAMACHANDRAN OUTLIERS.                        
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     AUC A  608                                                       
REMARK 610     AUC A  624                                                       
REMARK 610     AUC B  630                                                       
REMARK 610     AUC B  609                                                       
REMARK 610     AUC B  622                                                       
REMARK 610     AUC B  638                                                       
REMARK 610     AUC B  640                                                       
REMARK 610     AUC C  635                                                       
REMARK 610     AUC C  601                                                       
REMARK 610     AUC C  621                                                       
REMARK 610     AUC C  634                                                       
REMARK 610     AUC D  604                                                       
REMARK 610     AUC D  618                                                       
REMARK 610     AUC D  640                                                       
REMARK 610     AUC E  605                                                       
REMARK 610     AUC E  619                                                       
REMARK 610     AUC E  628                                                       
REMARK 610     AUC F  637                                                       
REMARK 610     AUC F  613                                                       
REMARK 610     AUC F  620                                                       
REMARK 610     AUC F  627                                                       
REMARK 610     AUC F  641                                                       
REMARK 610     AUC G  616                                                       
REMARK 610     AUC G  626                                                       
REMARK 610     AUC H  612                                                       
REMARK 610     AUC H  617                                                       
REMARK 610     AUC H  629                                                       
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                             AUC G 615  AU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G  48   OD2                                                    
REMARK 620 2 AUC G 615   C1  101.5                                              
REMARK 620 3 AUC G 615   C2   77.6 177.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             AUC F 637  AU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET F 144   SD                                                     
REMARK 620 2 MET G 144   SD  152.0                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC A 624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC B 630                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC A 631                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC C 635                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC F 637                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI A 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC B 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC B 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC B 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC B 638                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC B 640                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC C 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC C 634                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI C 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC D 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC D 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC D 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC D 640                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI D 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC E 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC E 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC E 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI E 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC F 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC F 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC F 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC F 627                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC F 641                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC G 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC G 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC G 626                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC H 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC H 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC H 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC H 629                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI H 901                 
DBREF  3ODM A    1   537  UNP    Q8XLE8   CAPPA_CLOPE      1    537             
DBREF  3ODM B    1   537  UNP    Q8XLE8   CAPPA_CLOPE      1    537             
DBREF  3ODM C    1   537  UNP    Q8XLE8   CAPPA_CLOPE      1    537             
DBREF  3ODM D    1   537  UNP    Q8XLE8   CAPPA_CLOPE      1    537             
DBREF  3ODM E    1   537  UNP    Q8XLE8   CAPPA_CLOPE      1    537             
DBREF  3ODM F    1   537  UNP    Q8XLE8   CAPPA_CLOPE      1    537             
DBREF  3ODM G    1   537  UNP    Q8XLE8   CAPPA_CLOPE      1    537             
DBREF  3ODM H    1   537  UNP    Q8XLE8   CAPPA_CLOPE      1    537             
SEQADV 3ODM MET A  -22  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM GLY A  -21  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS A  -20  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS A  -19  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS A  -18  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS A  -17  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS A  -16  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS A  -15  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS A  -14  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS A  -13  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS A  -12  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS A  -11  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM SER A  -10  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM SER A   -9  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM GLY A   -8  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS A   -7  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ILE A   -6  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP A   -5  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP A   -4  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP A   -3  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP A   -2  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM LYS A   -1  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS A    0  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM MET B  -22  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM GLY B  -21  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS B  -20  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS B  -19  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS B  -18  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS B  -17  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS B  -16  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS B  -15  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS B  -14  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS B  -13  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS B  -12  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS B  -11  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM SER B  -10  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM SER B   -9  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM GLY B   -8  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS B   -7  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ILE B   -6  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP B   -5  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP B   -4  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP B   -3  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP B   -2  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM LYS B   -1  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS B    0  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM MET C  -22  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM GLY C  -21  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS C  -20  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS C  -19  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS C  -18  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS C  -17  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS C  -16  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS C  -15  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS C  -14  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS C  -13  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS C  -12  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS C  -11  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM SER C  -10  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM SER C   -9  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM GLY C   -8  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS C   -7  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ILE C   -6  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP C   -5  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP C   -4  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP C   -3  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP C   -2  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM LYS C   -1  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS C    0  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM MET D  -22  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM GLY D  -21  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS D  -20  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS D  -19  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS D  -18  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS D  -17  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS D  -16  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS D  -15  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS D  -14  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS D  -13  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS D  -12  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS D  -11  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM SER D  -10  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM SER D   -9  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM GLY D   -8  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS D   -7  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ILE D   -6  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP D   -5  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP D   -4  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP D   -3  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP D   -2  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM LYS D   -1  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS D    0  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM MET E  -22  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM GLY E  -21  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS E  -20  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS E  -19  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS E  -18  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS E  -17  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS E  -16  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS E  -15  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS E  -14  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS E  -13  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS E  -12  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS E  -11  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM SER E  -10  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM SER E   -9  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM GLY E   -8  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS E   -7  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ILE E   -6  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP E   -5  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP E   -4  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP E   -3  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP E   -2  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM LYS E   -1  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS E    0  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM MET F  -22  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM GLY F  -21  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS F  -20  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS F  -19  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS F  -18  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS F  -17  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS F  -16  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS F  -15  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS F  -14  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS F  -13  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS F  -12  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS F  -11  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM SER F  -10  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM SER F   -9  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM GLY F   -8  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS F   -7  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ILE F   -6  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP F   -5  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP F   -4  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP F   -3  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP F   -2  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM LYS F   -1  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS F    0  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM MET G  -22  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM GLY G  -21  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS G  -20  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS G  -19  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS G  -18  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS G  -17  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS G  -16  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS G  -15  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS G  -14  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS G  -13  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS G  -12  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS G  -11  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM SER G  -10  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM SER G   -9  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM GLY G   -8  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS G   -7  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ILE G   -6  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP G   -5  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP G   -4  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP G   -3  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP G   -2  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM LYS G   -1  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS G    0  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM MET H  -22  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM GLY H  -21  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS H  -20  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS H  -19  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS H  -18  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS H  -17  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS H  -16  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS H  -15  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS H  -14  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS H  -13  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS H  -12  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS H  -11  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM SER H  -10  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM SER H   -9  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM GLY H   -8  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS H   -7  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ILE H   -6  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP H   -5  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP H   -4  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP H   -3  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM ASP H   -2  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM LYS H   -1  UNP  Q8XLE8              EXPRESSION TAG                 
SEQADV 3ODM HIS H    0  UNP  Q8XLE8              EXPRESSION TAG                 
SEQRES   1 A  560  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 A  560  SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET LYS ILE          
SEQRES   3 A  560  PRO CYS SER MET MET THR GLN HIS PRO ASP ASN VAL GLU          
SEQRES   4 A  560  THR TYR ILE SER ILE GLN GLN GLU PRO ALA GLU ALA ILE          
SEQRES   5 A  560  LYS GLY LEU THR PRO GLN ASP LYS GLY GLY LEU GLY ILE          
SEQRES   6 A  560  GLU GLU VAL MET ILE ASP PHE GLU GLY LYS LEU THR PRO          
SEQRES   7 A  560  TYR HIS GLN THR SER GLN ILE ALA LEU GLY LEU ILE SER          
SEQRES   8 A  560  ASN GLY ILE ILE PRO GLY LYS ASP VAL ARG VAL THR PRO          
SEQRES   9 A  560  ARG ILE PRO ASN ALA ASN LYS GLU SER VAL PHE ARG GLN          
SEQRES  10 A  560  LEU MET SER ILE MET SER ILE ILE GLU THR ASN VAL GLN          
SEQRES  11 A  560  SER LYS GLU LEU THR GLY THR PRO ALA ILE SER GLU VAL          
SEQRES  12 A  560  VAL VAL PRO MET ILE GLU THR GLY LYS GLU ILE SER GLU          
SEQRES  13 A  560  PHE GLN ASP ARG VAL ASN SER VAL VAL ASP MET GLY ASN          
SEQRES  14 A  560  LYS ASN TYR LYS THR LYS LEU ASP LEU ASN SER VAL ARG          
SEQRES  15 A  560  ILE ILE PRO LEU VAL GLU ASP VAL PRO ALA LEU ALA ASN          
SEQRES  16 A  560  ILE ASP ARG ILE LEU ASP GLU HIS TYR GLU ILE GLU LYS          
SEQRES  17 A  560  SER LYS GLY HIS ILE LEU LYS ASP LEU ARG ILE MET ILE          
SEQRES  18 A  560  ALA ARG SER ASP THR ALA MET SER TYR GLY LEU ILE SER          
SEQRES  19 A  560  GLY VAL LEU SER VAL LEU MET ALA VAL ASP GLY ALA TYR          
SEQRES  20 A  560  LYS TRP GLY GLU LYS HIS GLY VAL THR ILE SER PRO ILE          
SEQRES  21 A  560  LEU GLY CYS GLY SER LEU PRO PHE ARG GLY HIS PHE SER          
SEQRES  22 A  560  GLU GLU ASN ILE ASP GLU ILE LEU ALA THR TYR SER GLY          
SEQRES  23 A  560  ILE LYS THR PHE THR PHE GLN SER ALA LEU ARG TYR ASP          
SEQRES  24 A  560  HIS GLY GLU GLU ALA THR LYS HIS ALA VAL ARG GLU LEU          
SEQRES  25 A  560  LYS GLU LYS ILE ALA GLN SER LYS PRO ARG ASN PHE SER          
SEQRES  26 A  560  GLU GLU ASP LYS ASP LEU MET LYS GLU PHE ILE GLY ILE          
SEQRES  27 A  560  CYS SER LYS HIS TYR LEU GLN THR PHE LEU LYS VAL ILE          
SEQRES  28 A  560  ASP THR VAL SER PHE VAL SER ASP PHE ILE PRO LYS ASN          
SEQRES  29 A  560  ARG ASP ARG LEU THR LYS ALA LYS THR GLY LEU GLU TYR          
SEQRES  30 A  560  ASN ARG GLU VAL ALA ASN LEU ASP ASN VAL ALA ASP LEU          
SEQRES  31 A  560  VAL LYS ASP GLU VAL LEU LYS GLN GLU ILE LEU SER ILE          
SEQRES  32 A  560  ASP ASN SER LYS GLU TYR ALA VAL PRO ARG ALA ILE SER          
SEQRES  33 A  560  PHE THR GLY ALA MET TYR THR LEU GLY MET PRO PRO GLU          
SEQRES  34 A  560  LEU MET GLY MET GLY ARG ALA LEU ASN GLU ILE LYS THR          
SEQRES  35 A  560  LYS TYR GLY GLN GLU GLY ILE ASP LYS LEU LEU GLU ILE          
SEQRES  36 A  560  TYR PRO ILE LEU ARG LYS ASP LEU ALA PHE ALA ALA ARG          
SEQRES  37 A  560  PHE ALA ASN GLY GLY VAL SER LYS LYS ILE ILE ASP GLU          
SEQRES  38 A  560  GLU ALA ARG GLN GLU TYR LYS GLU ASP MET LYS TYR VAL          
SEQRES  39 A  560  ASN GLU ILE LEU ASN LEU GLY LEU ASP TYR ASP PHE LEU          
SEQRES  40 A  560  ASN GLU ASN GLU PHE TYR HIS THR LEU LEU LYS THR THR          
SEQRES  41 A  560  LYS PRO ILE ILE MET HIS LEU MET GLY LEU GLU GLU ASN          
SEQRES  42 A  560  VAL MET ARG ASN SER THR GLU GLU LEU LYS ILE LEU ASN          
SEQRES  43 A  560  GLU TRP ILE VAL ARG MET GLY LYS VAL ARG GLY SER ILE          
SEQRES  44 A  560  GLY                                                          
SEQRES   1 B  560  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 B  560  SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET LYS ILE          
SEQRES   3 B  560  PRO CYS SER MET MET THR GLN HIS PRO ASP ASN VAL GLU          
SEQRES   4 B  560  THR TYR ILE SER ILE GLN GLN GLU PRO ALA GLU ALA ILE          
SEQRES   5 B  560  LYS GLY LEU THR PRO GLN ASP LYS GLY GLY LEU GLY ILE          
SEQRES   6 B  560  GLU GLU VAL MET ILE ASP PHE GLU GLY LYS LEU THR PRO          
SEQRES   7 B  560  TYR HIS GLN THR SER GLN ILE ALA LEU GLY LEU ILE SER          
SEQRES   8 B  560  ASN GLY ILE ILE PRO GLY LYS ASP VAL ARG VAL THR PRO          
SEQRES   9 B  560  ARG ILE PRO ASN ALA ASN LYS GLU SER VAL PHE ARG GLN          
SEQRES  10 B  560  LEU MET SER ILE MET SER ILE ILE GLU THR ASN VAL GLN          
SEQRES  11 B  560  SER LYS GLU LEU THR GLY THR PRO ALA ILE SER GLU VAL          
SEQRES  12 B  560  VAL VAL PRO MET ILE GLU THR GLY LYS GLU ILE SER GLU          
SEQRES  13 B  560  PHE GLN ASP ARG VAL ASN SER VAL VAL ASP MET GLY ASN          
SEQRES  14 B  560  LYS ASN TYR LYS THR LYS LEU ASP LEU ASN SER VAL ARG          
SEQRES  15 B  560  ILE ILE PRO LEU VAL GLU ASP VAL PRO ALA LEU ALA ASN          
SEQRES  16 B  560  ILE ASP ARG ILE LEU ASP GLU HIS TYR GLU ILE GLU LYS          
SEQRES  17 B  560  SER LYS GLY HIS ILE LEU LYS ASP LEU ARG ILE MET ILE          
SEQRES  18 B  560  ALA ARG SER ASP THR ALA MET SER TYR GLY LEU ILE SER          
SEQRES  19 B  560  GLY VAL LEU SER VAL LEU MET ALA VAL ASP GLY ALA TYR          
SEQRES  20 B  560  LYS TRP GLY GLU LYS HIS GLY VAL THR ILE SER PRO ILE          
SEQRES  21 B  560  LEU GLY CYS GLY SER LEU PRO PHE ARG GLY HIS PHE SER          
SEQRES  22 B  560  GLU GLU ASN ILE ASP GLU ILE LEU ALA THR TYR SER GLY          
SEQRES  23 B  560  ILE LYS THR PHE THR PHE GLN SER ALA LEU ARG TYR ASP          
SEQRES  24 B  560  HIS GLY GLU GLU ALA THR LYS HIS ALA VAL ARG GLU LEU          
SEQRES  25 B  560  LYS GLU LYS ILE ALA GLN SER LYS PRO ARG ASN PHE SER          
SEQRES  26 B  560  GLU GLU ASP LYS ASP LEU MET LYS GLU PHE ILE GLY ILE          
SEQRES  27 B  560  CYS SER LYS HIS TYR LEU GLN THR PHE LEU LYS VAL ILE          
SEQRES  28 B  560  ASP THR VAL SER PHE VAL SER ASP PHE ILE PRO LYS ASN          
SEQRES  29 B  560  ARG ASP ARG LEU THR LYS ALA LYS THR GLY LEU GLU TYR          
SEQRES  30 B  560  ASN ARG GLU VAL ALA ASN LEU ASP ASN VAL ALA ASP LEU          
SEQRES  31 B  560  VAL LYS ASP GLU VAL LEU LYS GLN GLU ILE LEU SER ILE          
SEQRES  32 B  560  ASP ASN SER LYS GLU TYR ALA VAL PRO ARG ALA ILE SER          
SEQRES  33 B  560  PHE THR GLY ALA MET TYR THR LEU GLY MET PRO PRO GLU          
SEQRES  34 B  560  LEU MET GLY MET GLY ARG ALA LEU ASN GLU ILE LYS THR          
SEQRES  35 B  560  LYS TYR GLY GLN GLU GLY ILE ASP LYS LEU LEU GLU ILE          
SEQRES  36 B  560  TYR PRO ILE LEU ARG LYS ASP LEU ALA PHE ALA ALA ARG          
SEQRES  37 B  560  PHE ALA ASN GLY GLY VAL SER LYS LYS ILE ILE ASP GLU          
SEQRES  38 B  560  GLU ALA ARG GLN GLU TYR LYS GLU ASP MET LYS TYR VAL          
SEQRES  39 B  560  ASN GLU ILE LEU ASN LEU GLY LEU ASP TYR ASP PHE LEU          
SEQRES  40 B  560  ASN GLU ASN GLU PHE TYR HIS THR LEU LEU LYS THR THR          
SEQRES  41 B  560  LYS PRO ILE ILE MET HIS LEU MET GLY LEU GLU GLU ASN          
SEQRES  42 B  560  VAL MET ARG ASN SER THR GLU GLU LEU LYS ILE LEU ASN          
SEQRES  43 B  560  GLU TRP ILE VAL ARG MET GLY LYS VAL ARG GLY SER ILE          
SEQRES  44 B  560  GLY                                                          
SEQRES   1 C  560  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 C  560  SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET LYS ILE          
SEQRES   3 C  560  PRO CYS SER MET MET THR GLN HIS PRO ASP ASN VAL GLU          
SEQRES   4 C  560  THR TYR ILE SER ILE GLN GLN GLU PRO ALA GLU ALA ILE          
SEQRES   5 C  560  LYS GLY LEU THR PRO GLN ASP LYS GLY GLY LEU GLY ILE          
SEQRES   6 C  560  GLU GLU VAL MET ILE ASP PHE GLU GLY LYS LEU THR PRO          
SEQRES   7 C  560  TYR HIS GLN THR SER GLN ILE ALA LEU GLY LEU ILE SER          
SEQRES   8 C  560  ASN GLY ILE ILE PRO GLY LYS ASP VAL ARG VAL THR PRO          
SEQRES   9 C  560  ARG ILE PRO ASN ALA ASN LYS GLU SER VAL PHE ARG GLN          
SEQRES  10 C  560  LEU MET SER ILE MET SER ILE ILE GLU THR ASN VAL GLN          
SEQRES  11 C  560  SER LYS GLU LEU THR GLY THR PRO ALA ILE SER GLU VAL          
SEQRES  12 C  560  VAL VAL PRO MET ILE GLU THR GLY LYS GLU ILE SER GLU          
SEQRES  13 C  560  PHE GLN ASP ARG VAL ASN SER VAL VAL ASP MET GLY ASN          
SEQRES  14 C  560  LYS ASN TYR LYS THR LYS LEU ASP LEU ASN SER VAL ARG          
SEQRES  15 C  560  ILE ILE PRO LEU VAL GLU ASP VAL PRO ALA LEU ALA ASN          
SEQRES  16 C  560  ILE ASP ARG ILE LEU ASP GLU HIS TYR GLU ILE GLU LYS          
SEQRES  17 C  560  SER LYS GLY HIS ILE LEU LYS ASP LEU ARG ILE MET ILE          
SEQRES  18 C  560  ALA ARG SER ASP THR ALA MET SER TYR GLY LEU ILE SER          
SEQRES  19 C  560  GLY VAL LEU SER VAL LEU MET ALA VAL ASP GLY ALA TYR          
SEQRES  20 C  560  LYS TRP GLY GLU LYS HIS GLY VAL THR ILE SER PRO ILE          
SEQRES  21 C  560  LEU GLY CYS GLY SER LEU PRO PHE ARG GLY HIS PHE SER          
SEQRES  22 C  560  GLU GLU ASN ILE ASP GLU ILE LEU ALA THR TYR SER GLY          
SEQRES  23 C  560  ILE LYS THR PHE THR PHE GLN SER ALA LEU ARG TYR ASP          
SEQRES  24 C  560  HIS GLY GLU GLU ALA THR LYS HIS ALA VAL ARG GLU LEU          
SEQRES  25 C  560  LYS GLU LYS ILE ALA GLN SER LYS PRO ARG ASN PHE SER          
SEQRES  26 C  560  GLU GLU ASP LYS ASP LEU MET LYS GLU PHE ILE GLY ILE          
SEQRES  27 C  560  CYS SER LYS HIS TYR LEU GLN THR PHE LEU LYS VAL ILE          
SEQRES  28 C  560  ASP THR VAL SER PHE VAL SER ASP PHE ILE PRO LYS ASN          
SEQRES  29 C  560  ARG ASP ARG LEU THR LYS ALA LYS THR GLY LEU GLU TYR          
SEQRES  30 C  560  ASN ARG GLU VAL ALA ASN LEU ASP ASN VAL ALA ASP LEU          
SEQRES  31 C  560  VAL LYS ASP GLU VAL LEU LYS GLN GLU ILE LEU SER ILE          
SEQRES  32 C  560  ASP ASN SER LYS GLU TYR ALA VAL PRO ARG ALA ILE SER          
SEQRES  33 C  560  PHE THR GLY ALA MET TYR THR LEU GLY MET PRO PRO GLU          
SEQRES  34 C  560  LEU MET GLY MET GLY ARG ALA LEU ASN GLU ILE LYS THR          
SEQRES  35 C  560  LYS TYR GLY GLN GLU GLY ILE ASP LYS LEU LEU GLU ILE          
SEQRES  36 C  560  TYR PRO ILE LEU ARG LYS ASP LEU ALA PHE ALA ALA ARG          
SEQRES  37 C  560  PHE ALA ASN GLY GLY VAL SER LYS LYS ILE ILE ASP GLU          
SEQRES  38 C  560  GLU ALA ARG GLN GLU TYR LYS GLU ASP MET LYS TYR VAL          
SEQRES  39 C  560  ASN GLU ILE LEU ASN LEU GLY LEU ASP TYR ASP PHE LEU          
SEQRES  40 C  560  ASN GLU ASN GLU PHE TYR HIS THR LEU LEU LYS THR THR          
SEQRES  41 C  560  LYS PRO ILE ILE MET HIS LEU MET GLY LEU GLU GLU ASN          
SEQRES  42 C  560  VAL MET ARG ASN SER THR GLU GLU LEU LYS ILE LEU ASN          
SEQRES  43 C  560  GLU TRP ILE VAL ARG MET GLY LYS VAL ARG GLY SER ILE          
SEQRES  44 C  560  GLY                                                          
SEQRES   1 D  560  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 D  560  SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET LYS ILE          
SEQRES   3 D  560  PRO CYS SER MET MET THR GLN HIS PRO ASP ASN VAL GLU          
SEQRES   4 D  560  THR TYR ILE SER ILE GLN GLN GLU PRO ALA GLU ALA ILE          
SEQRES   5 D  560  LYS GLY LEU THR PRO GLN ASP LYS GLY GLY LEU GLY ILE          
SEQRES   6 D  560  GLU GLU VAL MET ILE ASP PHE GLU GLY LYS LEU THR PRO          
SEQRES   7 D  560  TYR HIS GLN THR SER GLN ILE ALA LEU GLY LEU ILE SER          
SEQRES   8 D  560  ASN GLY ILE ILE PRO GLY LYS ASP VAL ARG VAL THR PRO          
SEQRES   9 D  560  ARG ILE PRO ASN ALA ASN LYS GLU SER VAL PHE ARG GLN          
SEQRES  10 D  560  LEU MET SER ILE MET SER ILE ILE GLU THR ASN VAL GLN          
SEQRES  11 D  560  SER LYS GLU LEU THR GLY THR PRO ALA ILE SER GLU VAL          
SEQRES  12 D  560  VAL VAL PRO MET ILE GLU THR GLY LYS GLU ILE SER GLU          
SEQRES  13 D  560  PHE GLN ASP ARG VAL ASN SER VAL VAL ASP MET GLY ASN          
SEQRES  14 D  560  LYS ASN TYR LYS THR LYS LEU ASP LEU ASN SER VAL ARG          
SEQRES  15 D  560  ILE ILE PRO LEU VAL GLU ASP VAL PRO ALA LEU ALA ASN          
SEQRES  16 D  560  ILE ASP ARG ILE LEU ASP GLU HIS TYR GLU ILE GLU LYS          
SEQRES  17 D  560  SER LYS GLY HIS ILE LEU LYS ASP LEU ARG ILE MET ILE          
SEQRES  18 D  560  ALA ARG SER ASP THR ALA MET SER TYR GLY LEU ILE SER          
SEQRES  19 D  560  GLY VAL LEU SER VAL LEU MET ALA VAL ASP GLY ALA TYR          
SEQRES  20 D  560  LYS TRP GLY GLU LYS HIS GLY VAL THR ILE SER PRO ILE          
SEQRES  21 D  560  LEU GLY CYS GLY SER LEU PRO PHE ARG GLY HIS PHE SER          
SEQRES  22 D  560  GLU GLU ASN ILE ASP GLU ILE LEU ALA THR TYR SER GLY          
SEQRES  23 D  560  ILE LYS THR PHE THR PHE GLN SER ALA LEU ARG TYR ASP          
SEQRES  24 D  560  HIS GLY GLU GLU ALA THR LYS HIS ALA VAL ARG GLU LEU          
SEQRES  25 D  560  LYS GLU LYS ILE ALA GLN SER LYS PRO ARG ASN PHE SER          
SEQRES  26 D  560  GLU GLU ASP LYS ASP LEU MET LYS GLU PHE ILE GLY ILE          
SEQRES  27 D  560  CYS SER LYS HIS TYR LEU GLN THR PHE LEU LYS VAL ILE          
SEQRES  28 D  560  ASP THR VAL SER PHE VAL SER ASP PHE ILE PRO LYS ASN          
SEQRES  29 D  560  ARG ASP ARG LEU THR LYS ALA LYS THR GLY LEU GLU TYR          
SEQRES  30 D  560  ASN ARG GLU VAL ALA ASN LEU ASP ASN VAL ALA ASP LEU          
SEQRES  31 D  560  VAL LYS ASP GLU VAL LEU LYS GLN GLU ILE LEU SER ILE          
SEQRES  32 D  560  ASP ASN SER LYS GLU TYR ALA VAL PRO ARG ALA ILE SER          
SEQRES  33 D  560  PHE THR GLY ALA MET TYR THR LEU GLY MET PRO PRO GLU          
SEQRES  34 D  560  LEU MET GLY MET GLY ARG ALA LEU ASN GLU ILE LYS THR          
SEQRES  35 D  560  LYS TYR GLY GLN GLU GLY ILE ASP LYS LEU LEU GLU ILE          
SEQRES  36 D  560  TYR PRO ILE LEU ARG LYS ASP LEU ALA PHE ALA ALA ARG          
SEQRES  37 D  560  PHE ALA ASN GLY GLY VAL SER LYS LYS ILE ILE ASP GLU          
SEQRES  38 D  560  GLU ALA ARG GLN GLU TYR LYS GLU ASP MET LYS TYR VAL          
SEQRES  39 D  560  ASN GLU ILE LEU ASN LEU GLY LEU ASP TYR ASP PHE LEU          
SEQRES  40 D  560  ASN GLU ASN GLU PHE TYR HIS THR LEU LEU LYS THR THR          
SEQRES  41 D  560  LYS PRO ILE ILE MET HIS LEU MET GLY LEU GLU GLU ASN          
SEQRES  42 D  560  VAL MET ARG ASN SER THR GLU GLU LEU LYS ILE LEU ASN          
SEQRES  43 D  560  GLU TRP ILE VAL ARG MET GLY LYS VAL ARG GLY SER ILE          
SEQRES  44 D  560  GLY                                                          
SEQRES   1 E  560  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 E  560  SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET LYS ILE          
SEQRES   3 E  560  PRO CYS SER MET MET THR GLN HIS PRO ASP ASN VAL GLU          
SEQRES   4 E  560  THR TYR ILE SER ILE GLN GLN GLU PRO ALA GLU ALA ILE          
SEQRES   5 E  560  LYS GLY LEU THR PRO GLN ASP LYS GLY GLY LEU GLY ILE          
SEQRES   6 E  560  GLU GLU VAL MET ILE ASP PHE GLU GLY LYS LEU THR PRO          
SEQRES   7 E  560  TYR HIS GLN THR SER GLN ILE ALA LEU GLY LEU ILE SER          
SEQRES   8 E  560  ASN GLY ILE ILE PRO GLY LYS ASP VAL ARG VAL THR PRO          
SEQRES   9 E  560  ARG ILE PRO ASN ALA ASN LYS GLU SER VAL PHE ARG GLN          
SEQRES  10 E  560  LEU MET SER ILE MET SER ILE ILE GLU THR ASN VAL GLN          
SEQRES  11 E  560  SER LYS GLU LEU THR GLY THR PRO ALA ILE SER GLU VAL          
SEQRES  12 E  560  VAL VAL PRO MET ILE GLU THR GLY LYS GLU ILE SER GLU          
SEQRES  13 E  560  PHE GLN ASP ARG VAL ASN SER VAL VAL ASP MET GLY ASN          
SEQRES  14 E  560  LYS ASN TYR LYS THR LYS LEU ASP LEU ASN SER VAL ARG          
SEQRES  15 E  560  ILE ILE PRO LEU VAL GLU ASP VAL PRO ALA LEU ALA ASN          
SEQRES  16 E  560  ILE ASP ARG ILE LEU ASP GLU HIS TYR GLU ILE GLU LYS          
SEQRES  17 E  560  SER LYS GLY HIS ILE LEU LYS ASP LEU ARG ILE MET ILE          
SEQRES  18 E  560  ALA ARG SER ASP THR ALA MET SER TYR GLY LEU ILE SER          
SEQRES  19 E  560  GLY VAL LEU SER VAL LEU MET ALA VAL ASP GLY ALA TYR          
SEQRES  20 E  560  LYS TRP GLY GLU LYS HIS GLY VAL THR ILE SER PRO ILE          
SEQRES  21 E  560  LEU GLY CYS GLY SER LEU PRO PHE ARG GLY HIS PHE SER          
SEQRES  22 E  560  GLU GLU ASN ILE ASP GLU ILE LEU ALA THR TYR SER GLY          
SEQRES  23 E  560  ILE LYS THR PHE THR PHE GLN SER ALA LEU ARG TYR ASP          
SEQRES  24 E  560  HIS GLY GLU GLU ALA THR LYS HIS ALA VAL ARG GLU LEU          
SEQRES  25 E  560  LYS GLU LYS ILE ALA GLN SER LYS PRO ARG ASN PHE SER          
SEQRES  26 E  560  GLU GLU ASP LYS ASP LEU MET LYS GLU PHE ILE GLY ILE          
SEQRES  27 E  560  CYS SER LYS HIS TYR LEU GLN THR PHE LEU LYS VAL ILE          
SEQRES  28 E  560  ASP THR VAL SER PHE VAL SER ASP PHE ILE PRO LYS ASN          
SEQRES  29 E  560  ARG ASP ARG LEU THR LYS ALA LYS THR GLY LEU GLU TYR          
SEQRES  30 E  560  ASN ARG GLU VAL ALA ASN LEU ASP ASN VAL ALA ASP LEU          
SEQRES  31 E  560  VAL LYS ASP GLU VAL LEU LYS GLN GLU ILE LEU SER ILE          
SEQRES  32 E  560  ASP ASN SER LYS GLU TYR ALA VAL PRO ARG ALA ILE SER          
SEQRES  33 E  560  PHE THR GLY ALA MET TYR THR LEU GLY MET PRO PRO GLU          
SEQRES  34 E  560  LEU MET GLY MET GLY ARG ALA LEU ASN GLU ILE LYS THR          
SEQRES  35 E  560  LYS TYR GLY GLN GLU GLY ILE ASP LYS LEU LEU GLU ILE          
SEQRES  36 E  560  TYR PRO ILE LEU ARG LYS ASP LEU ALA PHE ALA ALA ARG          
SEQRES  37 E  560  PHE ALA ASN GLY GLY VAL SER LYS LYS ILE ILE ASP GLU          
SEQRES  38 E  560  GLU ALA ARG GLN GLU TYR LYS GLU ASP MET LYS TYR VAL          
SEQRES  39 E  560  ASN GLU ILE LEU ASN LEU GLY LEU ASP TYR ASP PHE LEU          
SEQRES  40 E  560  ASN GLU ASN GLU PHE TYR HIS THR LEU LEU LYS THR THR          
SEQRES  41 E  560  LYS PRO ILE ILE MET HIS LEU MET GLY LEU GLU GLU ASN          
SEQRES  42 E  560  VAL MET ARG ASN SER THR GLU GLU LEU LYS ILE LEU ASN          
SEQRES  43 E  560  GLU TRP ILE VAL ARG MET GLY LYS VAL ARG GLY SER ILE          
SEQRES  44 E  560  GLY                                                          
SEQRES   1 F  560  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 F  560  SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET LYS ILE          
SEQRES   3 F  560  PRO CYS SER MET MET THR GLN HIS PRO ASP ASN VAL GLU          
SEQRES   4 F  560  THR TYR ILE SER ILE GLN GLN GLU PRO ALA GLU ALA ILE          
SEQRES   5 F  560  LYS GLY LEU THR PRO GLN ASP LYS GLY GLY LEU GLY ILE          
SEQRES   6 F  560  GLU GLU VAL MET ILE ASP PHE GLU GLY LYS LEU THR PRO          
SEQRES   7 F  560  TYR HIS GLN THR SER GLN ILE ALA LEU GLY LEU ILE SER          
SEQRES   8 F  560  ASN GLY ILE ILE PRO GLY LYS ASP VAL ARG VAL THR PRO          
SEQRES   9 F  560  ARG ILE PRO ASN ALA ASN LYS GLU SER VAL PHE ARG GLN          
SEQRES  10 F  560  LEU MET SER ILE MET SER ILE ILE GLU THR ASN VAL GLN          
SEQRES  11 F  560  SER LYS GLU LEU THR GLY THR PRO ALA ILE SER GLU VAL          
SEQRES  12 F  560  VAL VAL PRO MET ILE GLU THR GLY LYS GLU ILE SER GLU          
SEQRES  13 F  560  PHE GLN ASP ARG VAL ASN SER VAL VAL ASP MET GLY ASN          
SEQRES  14 F  560  LYS ASN TYR LYS THR LYS LEU ASP LEU ASN SER VAL ARG          
SEQRES  15 F  560  ILE ILE PRO LEU VAL GLU ASP VAL PRO ALA LEU ALA ASN          
SEQRES  16 F  560  ILE ASP ARG ILE LEU ASP GLU HIS TYR GLU ILE GLU LYS          
SEQRES  17 F  560  SER LYS GLY HIS ILE LEU LYS ASP LEU ARG ILE MET ILE          
SEQRES  18 F  560  ALA ARG SER ASP THR ALA MET SER TYR GLY LEU ILE SER          
SEQRES  19 F  560  GLY VAL LEU SER VAL LEU MET ALA VAL ASP GLY ALA TYR          
SEQRES  20 F  560  LYS TRP GLY GLU LYS HIS GLY VAL THR ILE SER PRO ILE          
SEQRES  21 F  560  LEU GLY CYS GLY SER LEU PRO PHE ARG GLY HIS PHE SER          
SEQRES  22 F  560  GLU GLU ASN ILE ASP GLU ILE LEU ALA THR TYR SER GLY          
SEQRES  23 F  560  ILE LYS THR PHE THR PHE GLN SER ALA LEU ARG TYR ASP          
SEQRES  24 F  560  HIS GLY GLU GLU ALA THR LYS HIS ALA VAL ARG GLU LEU          
SEQRES  25 F  560  LYS GLU LYS ILE ALA GLN SER LYS PRO ARG ASN PHE SER          
SEQRES  26 F  560  GLU GLU ASP LYS ASP LEU MET LYS GLU PHE ILE GLY ILE          
SEQRES  27 F  560  CYS SER LYS HIS TYR LEU GLN THR PHE LEU LYS VAL ILE          
SEQRES  28 F  560  ASP THR VAL SER PHE VAL SER ASP PHE ILE PRO LYS ASN          
SEQRES  29 F  560  ARG ASP ARG LEU THR LYS ALA LYS THR GLY LEU GLU TYR          
SEQRES  30 F  560  ASN ARG GLU VAL ALA ASN LEU ASP ASN VAL ALA ASP LEU          
SEQRES  31 F  560  VAL LYS ASP GLU VAL LEU LYS GLN GLU ILE LEU SER ILE          
SEQRES  32 F  560  ASP ASN SER LYS GLU TYR ALA VAL PRO ARG ALA ILE SER          
SEQRES  33 F  560  PHE THR GLY ALA MET TYR THR LEU GLY MET PRO PRO GLU          
SEQRES  34 F  560  LEU MET GLY MET GLY ARG ALA LEU ASN GLU ILE LYS THR          
SEQRES  35 F  560  LYS TYR GLY GLN GLU GLY ILE ASP LYS LEU LEU GLU ILE          
SEQRES  36 F  560  TYR PRO ILE LEU ARG LYS ASP LEU ALA PHE ALA ALA ARG          
SEQRES  37 F  560  PHE ALA ASN GLY GLY VAL SER LYS LYS ILE ILE ASP GLU          
SEQRES  38 F  560  GLU ALA ARG GLN GLU TYR LYS GLU ASP MET LYS TYR VAL          
SEQRES  39 F  560  ASN GLU ILE LEU ASN LEU GLY LEU ASP TYR ASP PHE LEU          
SEQRES  40 F  560  ASN GLU ASN GLU PHE TYR HIS THR LEU LEU LYS THR THR          
SEQRES  41 F  560  LYS PRO ILE ILE MET HIS LEU MET GLY LEU GLU GLU ASN          
SEQRES  42 F  560  VAL MET ARG ASN SER THR GLU GLU LEU LYS ILE LEU ASN          
SEQRES  43 F  560  GLU TRP ILE VAL ARG MET GLY LYS VAL ARG GLY SER ILE          
SEQRES  44 F  560  GLY                                                          
SEQRES   1 G  560  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 G  560  SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET LYS ILE          
SEQRES   3 G  560  PRO CYS SER MET MET THR GLN HIS PRO ASP ASN VAL GLU          
SEQRES   4 G  560  THR TYR ILE SER ILE GLN GLN GLU PRO ALA GLU ALA ILE          
SEQRES   5 G  560  LYS GLY LEU THR PRO GLN ASP LYS GLY GLY LEU GLY ILE          
SEQRES   6 G  560  GLU GLU VAL MET ILE ASP PHE GLU GLY LYS LEU THR PRO          
SEQRES   7 G  560  TYR HIS GLN THR SER GLN ILE ALA LEU GLY LEU ILE SER          
SEQRES   8 G  560  ASN GLY ILE ILE PRO GLY LYS ASP VAL ARG VAL THR PRO          
SEQRES   9 G  560  ARG ILE PRO ASN ALA ASN LYS GLU SER VAL PHE ARG GLN          
SEQRES  10 G  560  LEU MET SER ILE MET SER ILE ILE GLU THR ASN VAL GLN          
SEQRES  11 G  560  SER LYS GLU LEU THR GLY THR PRO ALA ILE SER GLU VAL          
SEQRES  12 G  560  VAL VAL PRO MET ILE GLU THR GLY LYS GLU ILE SER GLU          
SEQRES  13 G  560  PHE GLN ASP ARG VAL ASN SER VAL VAL ASP MET GLY ASN          
SEQRES  14 G  560  LYS ASN TYR LYS THR LYS LEU ASP LEU ASN SER VAL ARG          
SEQRES  15 G  560  ILE ILE PRO LEU VAL GLU ASP VAL PRO ALA LEU ALA ASN          
SEQRES  16 G  560  ILE ASP ARG ILE LEU ASP GLU HIS TYR GLU ILE GLU LYS          
SEQRES  17 G  560  SER LYS GLY HIS ILE LEU LYS ASP LEU ARG ILE MET ILE          
SEQRES  18 G  560  ALA ARG SER ASP THR ALA MET SER TYR GLY LEU ILE SER          
SEQRES  19 G  560  GLY VAL LEU SER VAL LEU MET ALA VAL ASP GLY ALA TYR          
SEQRES  20 G  560  LYS TRP GLY GLU LYS HIS GLY VAL THR ILE SER PRO ILE          
SEQRES  21 G  560  LEU GLY CYS GLY SER LEU PRO PHE ARG GLY HIS PHE SER          
SEQRES  22 G  560  GLU GLU ASN ILE ASP GLU ILE LEU ALA THR TYR SER GLY          
SEQRES  23 G  560  ILE LYS THR PHE THR PHE GLN SER ALA LEU ARG TYR ASP          
SEQRES  24 G  560  HIS GLY GLU GLU ALA THR LYS HIS ALA VAL ARG GLU LEU          
SEQRES  25 G  560  LYS GLU LYS ILE ALA GLN SER LYS PRO ARG ASN PHE SER          
SEQRES  26 G  560  GLU GLU ASP LYS ASP LEU MET LYS GLU PHE ILE GLY ILE          
SEQRES  27 G  560  CYS SER LYS HIS TYR LEU GLN THR PHE LEU LYS VAL ILE          
SEQRES  28 G  560  ASP THR VAL SER PHE VAL SER ASP PHE ILE PRO LYS ASN          
SEQRES  29 G  560  ARG ASP ARG LEU THR LYS ALA LYS THR GLY LEU GLU TYR          
SEQRES  30 G  560  ASN ARG GLU VAL ALA ASN LEU ASP ASN VAL ALA ASP LEU          
SEQRES  31 G  560  VAL LYS ASP GLU VAL LEU LYS GLN GLU ILE LEU SER ILE          
SEQRES  32 G  560  ASP ASN SER LYS GLU TYR ALA VAL PRO ARG ALA ILE SER          
SEQRES  33 G  560  PHE THR GLY ALA MET TYR THR LEU GLY MET PRO PRO GLU          
SEQRES  34 G  560  LEU MET GLY MET GLY ARG ALA LEU ASN GLU ILE LYS THR          
SEQRES  35 G  560  LYS TYR GLY GLN GLU GLY ILE ASP LYS LEU LEU GLU ILE          
SEQRES  36 G  560  TYR PRO ILE LEU ARG LYS ASP LEU ALA PHE ALA ALA ARG          
SEQRES  37 G  560  PHE ALA ASN GLY GLY VAL SER LYS LYS ILE ILE ASP GLU          
SEQRES  38 G  560  GLU ALA ARG GLN GLU TYR LYS GLU ASP MET LYS TYR VAL          
SEQRES  39 G  560  ASN GLU ILE LEU ASN LEU GLY LEU ASP TYR ASP PHE LEU          
SEQRES  40 G  560  ASN GLU ASN GLU PHE TYR HIS THR LEU LEU LYS THR THR          
SEQRES  41 G  560  LYS PRO ILE ILE MET HIS LEU MET GLY LEU GLU GLU ASN          
SEQRES  42 G  560  VAL MET ARG ASN SER THR GLU GLU LEU LYS ILE LEU ASN          
SEQRES  43 G  560  GLU TRP ILE VAL ARG MET GLY LYS VAL ARG GLY SER ILE          
SEQRES  44 G  560  GLY                                                          
SEQRES   1 H  560  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 H  560  SER GLY HIS ILE ASP ASP ASP ASP LYS HIS MET LYS ILE          
SEQRES   3 H  560  PRO CYS SER MET MET THR GLN HIS PRO ASP ASN VAL GLU          
SEQRES   4 H  560  THR TYR ILE SER ILE GLN GLN GLU PRO ALA GLU ALA ILE          
SEQRES   5 H  560  LYS GLY LEU THR PRO GLN ASP LYS GLY GLY LEU GLY ILE          
SEQRES   6 H  560  GLU GLU VAL MET ILE ASP PHE GLU GLY LYS LEU THR PRO          
SEQRES   7 H  560  TYR HIS GLN THR SER GLN ILE ALA LEU GLY LEU ILE SER          
SEQRES   8 H  560  ASN GLY ILE ILE PRO GLY LYS ASP VAL ARG VAL THR PRO          
SEQRES   9 H  560  ARG ILE PRO ASN ALA ASN LYS GLU SER VAL PHE ARG GLN          
SEQRES  10 H  560  LEU MET SER ILE MET SER ILE ILE GLU THR ASN VAL GLN          
SEQRES  11 H  560  SER LYS GLU LEU THR GLY THR PRO ALA ILE SER GLU VAL          
SEQRES  12 H  560  VAL VAL PRO MET ILE GLU THR GLY LYS GLU ILE SER GLU          
SEQRES  13 H  560  PHE GLN ASP ARG VAL ASN SER VAL VAL ASP MET GLY ASN          
SEQRES  14 H  560  LYS ASN TYR LYS THR LYS LEU ASP LEU ASN SER VAL ARG          
SEQRES  15 H  560  ILE ILE PRO LEU VAL GLU ASP VAL PRO ALA LEU ALA ASN          
SEQRES  16 H  560  ILE ASP ARG ILE LEU ASP GLU HIS TYR GLU ILE GLU LYS          
SEQRES  17 H  560  SER LYS GLY HIS ILE LEU LYS ASP LEU ARG ILE MET ILE          
SEQRES  18 H  560  ALA ARG SER ASP THR ALA MET SER TYR GLY LEU ILE SER          
SEQRES  19 H  560  GLY VAL LEU SER VAL LEU MET ALA VAL ASP GLY ALA TYR          
SEQRES  20 H  560  LYS TRP GLY GLU LYS HIS GLY VAL THR ILE SER PRO ILE          
SEQRES  21 H  560  LEU GLY CYS GLY SER LEU PRO PHE ARG GLY HIS PHE SER          
SEQRES  22 H  560  GLU GLU ASN ILE ASP GLU ILE LEU ALA THR TYR SER GLY          
SEQRES  23 H  560  ILE LYS THR PHE THR PHE GLN SER ALA LEU ARG TYR ASP          
SEQRES  24 H  560  HIS GLY GLU GLU ALA THR LYS HIS ALA VAL ARG GLU LEU          
SEQRES  25 H  560  LYS GLU LYS ILE ALA GLN SER LYS PRO ARG ASN PHE SER          
SEQRES  26 H  560  GLU GLU ASP LYS ASP LEU MET LYS GLU PHE ILE GLY ILE          
SEQRES  27 H  560  CYS SER LYS HIS TYR LEU GLN THR PHE LEU LYS VAL ILE          
SEQRES  28 H  560  ASP THR VAL SER PHE VAL SER ASP PHE ILE PRO LYS ASN          
SEQRES  29 H  560  ARG ASP ARG LEU THR LYS ALA LYS THR GLY LEU GLU TYR          
SEQRES  30 H  560  ASN ARG GLU VAL ALA ASN LEU ASP ASN VAL ALA ASP LEU          
SEQRES  31 H  560  VAL LYS ASP GLU VAL LEU LYS GLN GLU ILE LEU SER ILE          
SEQRES  32 H  560  ASP ASN SER LYS GLU TYR ALA VAL PRO ARG ALA ILE SER          
SEQRES  33 H  560  PHE THR GLY ALA MET TYR THR LEU GLY MET PRO PRO GLU          
SEQRES  34 H  560  LEU MET GLY MET GLY ARG ALA LEU ASN GLU ILE LYS THR          
SEQRES  35 H  560  LYS TYR GLY GLN GLU GLY ILE ASP LYS LEU LEU GLU ILE          
SEQRES  36 H  560  TYR PRO ILE LEU ARG LYS ASP LEU ALA PHE ALA ALA ARG          
SEQRES  37 H  560  PHE ALA ASN GLY GLY VAL SER LYS LYS ILE ILE ASP GLU          
SEQRES  38 H  560  GLU ALA ARG GLN GLU TYR LYS GLU ASP MET LYS TYR VAL          
SEQRES  39 H  560  ASN GLU ILE LEU ASN LEU GLY LEU ASP TYR ASP PHE LEU          
SEQRES  40 H  560  ASN GLU ASN GLU PHE TYR HIS THR LEU LEU LYS THR THR          
SEQRES  41 H  560  LYS PRO ILE ILE MET HIS LEU MET GLY LEU GLU GLU ASN          
SEQRES  42 H  560  VAL MET ARG ASN SER THR GLU GLU LEU LYS ILE LEU ASN          
SEQRES  43 H  560  GLU TRP ILE VAL ARG MET GLY LYS VAL ARG GLY SER ILE          
SEQRES  44 H  560  GLY                                                          
HET    AUC  A 607       5                                                       
HET    AUC  A 608       1                                                       
HET    AUC  A 624       1                                                       
HET    AUC  A 631       5                                                       
HET    MLI  A 901       7                                                       
HET    AUC  B 630       1                                                       
HET    AUC  B 609       1                                                       
HET    AUC  B 610       5                                                       
HET    AUC  B 622       1                                                       
HET    AUC  B 638       1                                                       
HET    AUC  B 640       1                                                       
HET    AUC  C 635       1                                                       
HET    AUC  C 601       1                                                       
HET    AUC  C 602       5                                                       
HET    AUC  C 621       1                                                       
HET    AUC  C 634       1                                                       
HET    MLI  C 901       7                                                       
HET    AUC  D 603       5                                                       
HET    AUC  D 604       1                                                       
HET    AUC  D 618       1                                                       
HET    AUC  D 640       1                                                       
HET    MLI  D 901       7                                                       
HET    AUC  E 605       1                                                       
HET    AUC  E 606       5                                                       
HET    AUC  E 619       1                                                       
HET    AUC  E 628       1                                                       
HET    MLI  E 901       7                                                       
HET    AUC  F 637       1                                                       
HET    AUC  F 613       1                                                       
HET    AUC  F 614       5                                                       
HET    AUC  F 620       1                                                       
HET    AUC  F 627       1                                                       
HET    AUC  F 641       1                                                       
HET    AUC  G 615       5                                                       
HET    AUC  G 616       1                                                       
HET    AUC  G 626       1                                                       
HET    AUC  H 611       5                                                       
HET    AUC  H 612       1                                                       
HET    AUC  H 617       1                                                       
HET    AUC  H 629       1                                                       
HET    MLI  H 901       7                                                       
HETNAM     AUC GOLD (I) CYANIDE ION                                             
HETNAM     MLI MALONATE ION                                                     
FORMUL   9  AUC    36(C2 AU N2)                                                 
FORMUL  13  MLI    5(C3 H2 O4 2-)                                               
FORMUL  50  HOH   *200(H2 O)                                                    
HELIX    1   1 GLN A   23  LEU A   32  1                                  10    
HELIX    2   2 PRO A   34  GLY A   38  5                                   5    
HELIX    3   3 HIS A   57  SER A   68  1                                  12    
HELIX    4   4 SER A   90  GLY A  113  1                                  24    
HELIX    5   5 THR A  127  TYR A  149  1                                  23    
HELIX    6   6 ASP A  166  ASN A  172  1                                   7    
HELIX    7   7 ILE A  173  LYS A  187  1                                  15    
HELIX    8   8 ARG A  200  GLY A  208  1                                   9    
HELIX    9   9 GLY A  208  GLY A  231  1                                  24    
HELIX   10  10 LEU A  243  GLY A  247  5                                   5    
HELIX   11  11 ASN A  253  TYR A  261  1                                   9    
HELIX   12  12 GLN A  270  ASP A  276  1                                   7    
HELIX   13  13 GLY A  278  ILE A  293  1                                  16    
HELIX   14  14 ALA A  294  SER A  296  5                                   3    
HELIX   15  15 SER A  302  ASP A  336  1                                  35    
HELIX   16  16 ASN A  360  ASP A  366  1                                   7    
HELIX   17  17 ASP A  370  SER A  379  1                                  10    
HELIX   18  18 ARG A  390  LEU A  401  1                                  12    
HELIX   19  19 PRO A  404  MET A  408  5                                   5    
HELIX   20  20 GLY A  409  GLY A  422  1                                  14    
HELIX   21  21 GLY A  422  TYR A  433  1                                  12    
HELIX   22  22 ILE A  435  ARG A  445  1                                  11    
HELIX   23  23 ASP A  457  LEU A  475  1                                  19    
HELIX   24  24 ASP A  480  GLU A  488  1                                   9    
HELIX   25  25 GLU A  488  LEU A  507  1                                  20    
HELIX   26  26 GLU A  508  SER A  515  1                                   8    
HELIX   27  27 SER A  515  GLY A  534  1                                  20    
HELIX   28  28 GLN B   23  THR B   33  1                                  11    
HELIX   29  29 PRO B   34  GLY B   38  5                                   5    
HELIX   30  30 HIS B   57  SER B   68  1                                  12    
HELIX   31  31 SER B   90  GLY B  113  1                                  24    
HELIX   32  32 THR B  127  TYR B  149  1                                  23    
HELIX   33  33 ASP B  166  ASN B  172  1                                   7    
HELIX   34  34 ASN B  172  LYS B  187  1                                  16    
HELIX   35  35 ARG B  200  GLY B  208  1                                   9    
HELIX   36  36 GLY B  208  GLY B  231  1                                  24    
HELIX   37  37 LEU B  243  GLY B  247  5                                   5    
HELIX   38  38 SER B  250  GLU B  252  5                                   3    
HELIX   39  39 ASN B  253  TYR B  261  1                                   9    
HELIX   40  40 GLN B  270  ASP B  276  1                                   7    
HELIX   41  41 HIS B  277  ILE B  293  1                                  17    
HELIX   42  42 ALA B  294  SER B  296  5                                   3    
HELIX   43  43 SER B  302  ASP B  336  1                                  35    
HELIX   44  44 LEU B  361  ASP B  366  1                                   6    
HELIX   45  45 ASP B  370  SER B  379  1                                  10    
HELIX   46  46 ARG B  390  LEU B  401  1                                  12    
HELIX   47  47 GLY B  409  TYR B  433  1                                  25    
HELIX   48  48 ILE B  435  ARG B  445  1                                  11    
HELIX   49  49 ASP B  457  LEU B  475  1                                  19    
HELIX   50  50 ASP B  480  GLU B  488  1                                   9    
HELIX   51  51 GLU B  488  GLY B  506  1                                  19    
HELIX   52  52 GLU B  508  SER B  515  1                                   8    
HELIX   53  53 SER B  515  GLY B  534  1                                  20    
HELIX   54  54 GLN C   23  THR C   33  1                                  11    
HELIX   55  55 PRO C   34  GLY C   38  5                                   5    
HELIX   56  56 HIS C   57  ASN C   69  1                                  13    
HELIX   57  57 SER C   90  GLY C  113  1                                  24    
HELIX   58  58 THR C  127  TYR C  149  1                                  23    
HELIX   59  59 ASN C  172  LYS C  187  1                                  16    
HELIX   60  60 ARG C  200  GLY C  208  1                                   9    
HELIX   61  61 GLY C  208  GLY C  231  1                                  24    
HELIX   62  62 LEU C  243  GLY C  247  5                                   5    
HELIX   63  63 ASN C  253  TYR C  261  1                                   9    
HELIX   64  64 GLN C  270  ASP C  276  1                                   7    
HELIX   65  65 GLY C  278  ALA C  294  1                                  17    
HELIX   66  66 SER C  302  ASP C  336  1                                  35    
HELIX   67  67 LEU C  361  ASP C  366  1                                   6    
HELIX   68  68 ASP C  370  ILE C  380  1                                  11    
HELIX   69  69 ARG C  390  LEU C  401  1                                  12    
HELIX   70  70 GLY C  409  TYR C  433  1                                  25    
HELIX   71  71 ILE C  435  ARG C  445  1                                  11    
HELIX   72  72 ASP C  457  LEU C  475  1                                  19    
HELIX   73  73 ASP C  482  GLU C  488  1                                   7    
HELIX   74  74 GLU C  488  GLY C  506  1                                  19    
HELIX   75  75 GLU C  508  SER C  515  1                                   8    
HELIX   76  76 SER C  515  GLY C  534  1                                  20    
HELIX   77  77 SER D   20  GLN D   22  5                                   3    
HELIX   78  78 GLN D   23  THR D   33  1                                  11    
HELIX   79  79 PRO D   34  GLY D   38  5                                   5    
HELIX   80  80 HIS D   57  ASN D   69  1                                  13    
HELIX   81  81 SER D   90  GLY D  113  1                                  24    
HELIX   82  82 THR D  127  TYR D  149  1                                  23    
HELIX   83  83 ASP D  166  ASN D  172  1                                   7    
HELIX   84  84 ASN D  172  SER D  186  1                                  15    
HELIX   85  85 ARG D  200  GLY D  208  1                                   9    
HELIX   86  86 GLY D  208  HIS D  230  1                                  23    
HELIX   87  87 LEU D  243  GLY D  247  5                                   5    
HELIX   88  88 ASN D  253  TYR D  261  1                                   9    
HELIX   89  89 GLN D  270  ASP D  276  1                                   7    
HELIX   90  90 GLY D  278  ILE D  293  1                                  16    
HELIX   91  91 ALA D  294  SER D  296  5                                   3    
HELIX   92  92 SER D  302  ASP D  336  1                                  35    
HELIX   93  93 ASN D  360  ASP D  366  1                                   7    
HELIX   94  94 ASP D  370  SER D  379  1                                  10    
HELIX   95  95 ARG D  390  LEU D  401  1                                  12    
HELIX   96  96 PRO D  404  MET D  408  5                                   5    
HELIX   97  97 GLY D  409  TYR D  433  1                                  25    
HELIX   98  98 ILE D  435  ARG D  445  1                                  11    
HELIX   99  99 ASP D  457  LEU D  475  1                                  19    
HELIX  100 100 ASP D  480  GLU D  488  1                                   9    
HELIX  101 101 GLU D  488  GLY D  506  1                                  19    
HELIX  102 102 GLU D  508  SER D  515  1                                   8    
HELIX  103 103 SER D  515  GLY D  534  1                                  20    
HELIX  104 104 SER E   20  GLN E   22  5                                   3    
HELIX  105 105 GLN E   23  THR E   33  1                                  11    
HELIX  106 106 PRO E   34  GLY E   38  5                                   5    
HELIX  107 107 HIS E   57  SER E   68  1                                  12    
HELIX  108 108 SER E   90  GLY E  113  1                                  24    
HELIX  109 109 THR E  127  TYR E  149  1                                  23    
HELIX  110 110 ASP E  166  ASN E  172  1                                   7    
HELIX  111 111 ASN E  172  LYS E  187  1                                  16    
HELIX  112 112 ARG E  200  GLY E  208  1                                   9    
HELIX  113 113 GLY E  208  GLY E  231  1                                  24    
HELIX  114 114 LEU E  243  GLY E  247  5                                   5    
HELIX  115 115 SER E  250  GLU E  252  5                                   3    
HELIX  116 116 ASN E  253  TYR E  261  1                                   9    
HELIX  117 117 GLN E  270  ASP E  276  1                                   7    
HELIX  118 118 GLY E  278  ILE E  293  1                                  16    
HELIX  119 119 ALA E  294  SER E  296  5                                   3    
HELIX  120 120 SER E  302  ASP E  336  1                                  35    
HELIX  121 121 ASN E  360  ASP E  366  1                                   7    
HELIX  122 122 ASP E  370  SER E  379  1                                  10    
HELIX  123 123 ARG E  390  LEU E  401  1                                  12    
HELIX  124 124 PRO E  404  MET E  408  5                                   5    
HELIX  125 125 GLY E  409  TYR E  433  1                                  25    
HELIX  126 126 ILE E  435  ARG E  445  1                                  11    
HELIX  127 127 ASP E  457  LEU E  475  1                                  19    
HELIX  128 128 ASP E  480  GLU E  488  1                                   9    
HELIX  129 129 GLU E  488  GLY E  506  1                                  19    
HELIX  130 130 GLU E  508  ASN E  514  1                                   7    
HELIX  131 131 SER E  515  GLY E  534  1                                  20    
HELIX  132 132 GLN F   23  LEU F   32  1                                  10    
HELIX  133 133 PRO F   34  GLY F   38  5                                   5    
HELIX  134 134 HIS F   57  ASN F   69  1                                  13    
HELIX  135 135 SER F   90  GLY F  113  1                                  24    
HELIX  136 136 THR F  127  LYS F  147  1                                  21    
HELIX  137 137 ASP F  166  ASN F  172  1                                   7    
HELIX  138 138 ILE F  173  LYS F  187  1                                  15    
HELIX  139 139 ARG F  200  GLY F  208  1                                   9    
HELIX  140 140 GLY F  208  HIS F  230  1                                  23    
HELIX  141 141 LEU F  243  GLY F  247  5                                   5    
HELIX  142 142 ASN F  253  TYR F  261  1                                   9    
HELIX  143 143 GLN F  270  ASP F  276  1                                   7    
HELIX  144 144 GLY F  278  ILE F  293  1                                  16    
HELIX  145 145 ALA F  294  SER F  296  5                                   3    
HELIX  146 146 SER F  302  ASP F  336  1                                  35    
HELIX  147 147 LEU F  361  ASP F  366  1                                   6    
HELIX  148 148 ASP F  370  SER F  379  1                                  10    
HELIX  149 149 ARG F  390  LEU F  401  1                                  12    
HELIX  150 150 PRO F  404  MET F  408  5                                   5    
HELIX  151 151 GLY F  409  TYR F  421  1                                  13    
HELIX  152 152 TYR F  421  TYR F  433  1                                  13    
HELIX  153 153 ILE F  435  ARG F  445  1                                  11    
HELIX  154 154 GLY F  449  LYS F  453  5                                   5    
HELIX  155 155 ASP F  457  LEU F  475  1                                  19    
HELIX  156 156 ASP F  480  GLU F  488  1                                   9    
HELIX  157 157 GLU F  488  GLY F  506  1                                  19    
HELIX  158 158 GLU F  508  SER F  515  1                                   8    
HELIX  159 159 SER F  515  GLY F  534  1                                  20    
HELIX  160 160 GLN G   23  THR G   33  1                                  11    
HELIX  161 161 PRO G   34  GLY G   38  5                                   5    
HELIX  162 162 HIS G   57  ASN G   69  1                                  13    
HELIX  163 163 SER G   90  GLY G  113  1                                  24    
HELIX  164 164 THR G  127  TYR G  149  1                                  23    
HELIX  165 165 ASP G  166  ASN G  172  1                                   7    
HELIX  166 166 ILE G  173  SER G  186  1                                  14    
HELIX  167 167 ARG G  200  GLY G  208  1                                   9    
HELIX  168 168 GLY G  208  HIS G  230  1                                  23    
HELIX  169 169 LEU G  243  GLY G  247  5                                   5    
HELIX  170 170 ASN G  253  TYR G  261  1                                   9    
HELIX  171 171 GLN G  270  ASP G  276  1                                   7    
HELIX  172 172 GLY G  278  ILE G  293  1                                  16    
HELIX  173 173 ALA G  294  SER G  296  5                                   3    
HELIX  174 174 SER G  302  ASP G  336  1                                  35    
HELIX  175 175 LEU G  361  ASP G  366  1                                   6    
HELIX  176 176 ASP G  370  LEU G  378  1                                   9    
HELIX  177 177 ARG G  390  LEU G  401  1                                  12    
HELIX  178 178 GLY G  409  TYR G  433  1                                  25    
HELIX  179 179 ILE G  435  ARG G  445  1                                  11    
HELIX  180 180 ASP G  457  LEU G  475  1                                  19    
HELIX  181 181 ASP G  480  GLU G  488  1                                   9    
HELIX  182 182 GLU G  488  GLY G  506  1                                  19    
HELIX  183 183 GLU G  508  SER G  515  1                                   8    
HELIX  184 184 SER G  515  GLY G  534  1                                  20    
HELIX  185 185 GLN H   23  THR H   33  1                                  11    
HELIX  186 186 PRO H   34  GLY H   38  5                                   5    
HELIX  187 187 HIS H   57  SER H   68  1                                  12    
HELIX  188 188 SER H   90  GLY H  113  1                                  24    
HELIX  189 189 THR H  127  TYR H  149  1                                  23    
HELIX  190 190 ASP H  166  ASN H  172  1                                   7    
HELIX  191 191 ILE H  173  SER H  186  1                                  14    
HELIX  192 192 ARG H  200  GLY H  208  1                                   9    
HELIX  193 193 GLY H  208  GLY H  231  1                                  24    
HELIX  194 194 LEU H  243  GLY H  247  5                                   5    
HELIX  195 195 ASN H  253  TYR H  261  1                                   9    
HELIX  196 196 GLN H  270  ASP H  276  1                                   7    
HELIX  197 197 GLY H  278  ILE H  293  1                                  16    
HELIX  198 198 ALA H  294  SER H  296  5                                   3    
HELIX  199 199 SER H  302  SER H  335  1                                  34    
HELIX  200 200 ASP H  336  ILE H  338  5                                   3    
HELIX  201 201 ASN H  360  ASP H  366  1                                   7    
HELIX  202 202 ASP H  370  LEU H  378  1                                   9    
HELIX  203 203 ARG H  390  LEU H  401  1                                  12    
HELIX  204 204 PRO H  404  MET H  408  5                                   5    
HELIX  205 205 GLY H  409  TYR H  433  1                                  25    
HELIX  206 206 ILE H  435  ARG H  445  1                                  11    
HELIX  207 207 ASP H  457  LEU H  475  1                                  19    
HELIX  208 208 ASP H  480  GLU H  488  1                                   9    
HELIX  209 209 GLU H  488  GLY H  506  1                                  19    
HELIX  210 210 GLU H  508  SER H  515  1                                   8    
HELIX  211 211 SER H  515  GLY H  534  1                                  20    
SHEET    1   A 9 SER A   6  MET A   8  0                                        
SHEET    2   A 9 GLU A  44  ASP A  48  1  O  GLU A  44   N  MET A   8           
SHEET    3   A 9 ARG A  78  ARG A  82  1  O  THR A  80   N  VAL A  45           
SHEET    4   A 9 GLU A 119  VAL A 122  1  O  VAL A 121   N  PRO A  81           
SHEET    5   A 9 ARG A 159  VAL A 164  1  O  ILE A 161   N  VAL A 120           
SHEET    6   A 9 ASP A 193  ALA A 199  1  O  MET A 197   N  PRO A 162           
SHEET    7   A 9 THR A 233  GLY A 239  1  O  ILE A 237   N  ILE A 196           
SHEET    8   A 9 THR A 266  PHE A 269  1  O  THR A 266   N  LEU A 238           
SHEET    9   A 9 SER A   6  MET A   8  1  N  MET A   7   O  PHE A 269           
SHEET    1   B 8 ARG B  78  VAL B  79  0                                        
SHEET    2   B 8 GLU B  44  VAL B  45  1  N  VAL B  45   O  ARG B  78           
SHEET    3   B 8 SER B   6  MET B   8  1  N  MET B   8   O  GLU B  44           
SHEET    4   B 8 THR B 266  PHE B 269  1  O  PHE B 269   N  MET B   7           
SHEET    5   B 8 THR B 233  GLY B 239  1  N  LEU B 238   O  THR B 266           
SHEET    6   B 8 ASP B 193  ALA B 199  1  N  ILE B 198   O  ILE B 237           
SHEET    7   B 8 ARG B 159  VAL B 164  1  N  VAL B 164   O  MET B 197           
SHEET    8   B 8 GLU B 119  VAL B 122  1  N  VAL B 120   O  ILE B 161           
SHEET    1   C 2 ARG B 356  VAL B 358  0                                        
SHEET    2   C 2 GLU B 385  ALA B 387 -1  O  TYR B 386   N  GLU B 357           
SHEET    1   D 9 SER C   6  MET C   8  0                                        
SHEET    2   D 9 GLU C  44  ASP C  48  1  O  GLU C  44   N  MET C   8           
SHEET    3   D 9 ARG C  78  ARG C  82  1  O  THR C  80   N  VAL C  45           
SHEET    4   D 9 GLU C 119  VAL C 122  1  O  VAL C 121   N  PRO C  81           
SHEET    5   D 9 ARG C 159  VAL C 164  1  O  ILE C 161   N  VAL C 120           
SHEET    6   D 9 ASP C 193  ALA C 199  1  O  MET C 197   N  PRO C 162           
SHEET    7   D 9 THR C 233  GLY C 239  1  O  THR C 233   N  LEU C 194           
SHEET    8   D 9 THR C 266  PHE C 269  1  O  THR C 266   N  LEU C 238           
SHEET    9   D 9 SER C   6  MET C   8  1  N  MET C   7   O  PHE C 269           
SHEET    1   E 8 ARG D  78  VAL D  79  0                                        
SHEET    2   E 8 GLU D  44  VAL D  45  1  N  VAL D  45   O  ARG D  78           
SHEET    3   E 8 SER D   6  MET D   8  1  N  MET D   8   O  GLU D  44           
SHEET    4   E 8 THR D 266  PHE D 269  1  O  PHE D 269   N  MET D   7           
SHEET    5   E 8 THR D 233  GLY D 239  1  N  LEU D 238   O  THR D 266           
SHEET    6   E 8 ASP D 193  ALA D 199  1  N  ILE D 198   O  ILE D 237           
SHEET    7   E 8 ARG D 159  VAL D 164  1  N  PRO D 162   O  MET D 197           
SHEET    8   E 8 GLU D 119  VAL D 122  1  N  VAL D 120   O  ILE D 161           
SHEET    1   F 9 SER E   6  MET E   8  0                                        
SHEET    2   F 9 GLU E  44  ASP E  48  1  O  MET E  46   N  MET E   8           
SHEET    3   F 9 ARG E  78  ARG E  82  1  O  THR E  80   N  VAL E  45           
SHEET    4   F 9 GLU E 119  VAL E 122  1  O  VAL E 121   N  PRO E  81           
SHEET    5   F 9 ARG E 159  VAL E 164  1  O  ILE E 161   N  VAL E 120           
SHEET    6   F 9 ASP E 193  ALA E 199  1  O  MET E 197   N  PRO E 162           
SHEET    7   F 9 THR E 233  GLY E 239  1  O  ILE E 237   N  ILE E 196           
SHEET    8   F 9 THR E 266  PHE E 269  1  O  THR E 266   N  LEU E 238           
SHEET    9   F 9 SER E   6  MET E   8  1  N  MET E   7   O  PHE E 269           
SHEET    1   G 6 SER F   6  MET F   8  0                                        
SHEET    2   G 6 THR F 266  PHE F 269  1  O  PHE F 269   N  MET F   7           
SHEET    3   G 6 THR F 233  GLY F 239  1  N  LEU F 238   O  THR F 266           
SHEET    4   G 6 ASP F 193  ALA F 199  1  N  ILE F 196   O  ILE F 237           
SHEET    5   G 6 ARG F 159  VAL F 164  1  N  VAL F 164   O  MET F 197           
SHEET    6   G 6 GLU F 119  VAL F 122  1  N  VAL F 120   O  ILE F 161           
SHEET    1   H 2 GLU F  44  VAL F  45  0                                        
SHEET    2   H 2 ARG F  78  VAL F  79  1  O  ARG F  78   N  VAL F  45           
SHEET    1   I 2 ARG F 356  GLU F 357  0                                        
SHEET    2   I 2 TYR F 386  ALA F 387 -1  O  TYR F 386   N  GLU F 357           
SHEET    1   J 8 ARG G  78  VAL G  79  0                                        
SHEET    2   J 8 GLU G  44  MET G  46  1  N  VAL G  45   O  ARG G  78           
SHEET    3   J 8 SER G   6  THR G   9  1  N  MET G   8   O  GLU G  44           
SHEET    4   J 8 THR G 266  PHE G 269  1  O  PHE G 269   N  MET G   7           
SHEET    5   J 8 THR G 233  GLY G 239  1  N  LEU G 238   O  THR G 266           
SHEET    6   J 8 ASP G 193  ALA G 199  1  N  LEU G 194   O  THR G 233           
SHEET    7   J 8 ARG G 159  VAL G 164  1  N  PRO G 162   O  MET G 197           
SHEET    8   J 8 GLU G 119  VAL G 122  1  N  VAL G 120   O  ILE G 161           
SHEET    1   K 9 SER H   6  MET H   8  0                                        
SHEET    2   K 9 GLU H  44  ASP H  48  1  O  GLU H  44   N  MET H   8           
SHEET    3   K 9 ARG H  78  ARG H  82  1  O  ARG H  82   N  ILE H  47           
SHEET    4   K 9 GLU H 119  VAL H 122  1  O  VAL H 121   N  PRO H  81           
SHEET    5   K 9 ARG H 159  VAL H 164  1  O  ILE H 161   N  VAL H 120           
SHEET    6   K 9 ASP H 193  ALA H 199  1  O  MET H 197   N  PRO H 162           
SHEET    7   K 9 THR H 233  GLY H 239  1  O  THR H 233   N  LEU H 194           
SHEET    8   K 9 THR H 266  PHE H 269  1  O  THR H 266   N  LEU H 238           
SHEET    9   K 9 SER H   6  MET H   8  1  N  MET H   7   O  PHE H 269           
LINK         SG  CYS H   5                AU   AUC H 612     1555   1555  2.03  
LINK         OE2 GLU C 279                AU   AUC C 621     1555   1555  2.12  
LINK         SG  CYS G   5                AU   AUC G 616     1555   1555  2.13  
LINK         OE1 GLU E 279                AU   AUC E 619     1555   1555  2.35  
LINK         OE1 GLU G 279                AU   AUC G 626     1555   1555  2.50  
LINK         OE1 GLU B 279                AU   AUC B 622     1555   1555  2.53  
LINK         SG  CYS F   5                AU   AUC F 613     1555   1555  2.63  
LINK         NH1 ARG B  82                AU   AUC B 640     1555   1555  2.72  
LINK         O   GLY H  38                AU   AUC H 617     1555   1555  2.74  
LINK         OD2 ASP G  48                AU   AUC G 615     1555   1555  2.79  
LINK         SD  MET F 144                AU   AUC F 637     1555   1555  2.96  
LINK         SD  MET G 144                AU   AUC F 637     1555   1555  2.99  
SITE     1 AC1  5 GLN A  10  HIS A  11  MET A  46  ASP A  48                    
SITE     2 AC1  5 ARG A 344                                                     
SITE     1 AC2  1 CYS A   5                                                     
SITE     1 AC3  3 GLY A  38  LEU A  40  GLU A 279                               
SITE     1 AC4  2 MET B 144  MET H 144                                          
SITE     1 AC5  7 ASP A  36  LYS A  37  GLN H 423  LEU H 430                    
SITE     2 AC5  7 ARG H 437  ILE H 474  ASN H 476                               
SITE     1 AC6  2 MET C 144  MET D 144                                          
SITE     1 AC7  2 MET F 144  MET G 144                                          
SITE     1 AC8  7 HIS A  11  ARG A  82  ALA A 199  ARG A 200                    
SITE     2 AC8  7 SER A 201  GLY A 239  GLN A 270                               
SITE     1 AC9  3 CYS B   5  GLU B  43  LYS B 290                               
SITE     1 BC1  5 GLN B  10  HIS B  11  ASP B  48  ARG B  82                    
SITE     2 BC1  5 ARG B 344                                                     
SITE     1 BC2  4 LYS B  30  GLY B  38  LEU B  40  GLU B 279                    
SITE     1 BC3  1 HIS B 284                                                     
SITE     1 BC4  3 HIS B  11  ARG B  82  MET B 197                               
SITE     1 BC5  3 LYS C   2  CYS C   5  LYS C 290                               
SITE     1 BC6  6 THR C   9  GLN C  10  HIS C  11  MET C  46                    
SITE     2 BC6  6 ASP C  48  ARG C 344                                          
SITE     1 BC7  4 LYS C  30  GLY C  38  LEU C  40  GLU C 279                    
SITE     1 BC8  1 HIS C 284                                                     
SITE     1 BC9  5 HIS C  11  ARG C  82  ALA C 199  SER C 201                    
SITE     2 BC9  5 GLY C 239                                                     
SITE     1 CC1  5 THR D   9  GLN D  10  HIS D  11  ASP D  48                    
SITE     2 CC1  5 ARG D 344                                                     
SITE     1 CC2  2 CYS D   5  LYS D 290                                          
SITE     1 CC3  4 LYS D  30  GLY D  38  LEU D  40  GLU D 279                    
SITE     1 CC4  1 HIS D 284                                                     
SITE     1 CC5  7 HIS D  11  ARG D  82  ALA D 199  ARG D 200                    
SITE     2 CC5  7 SER D 201  ASP D 202  GLY D 239                               
SITE     1 CC6  2 CYS E   5  LYS E 290                                          
SITE     1 CC7  6 GLN E  10  HIS E  11  MET E  46  ASP E  48                    
SITE     2 CC7  6 ARG E 344  ARG E 390                                          
SITE     1 CC8  3 GLY E  38  LEU E  40  GLU E 279                               
SITE     1 CC9  8 HIS E  11  ARG E  82  ALA E 199  ARG E 200                    
SITE     2 CC9  8 SER E 201  ASP E 202  GLY E 239  GLN E 270                    
SITE     1 DC1  2 CYS F   5  LYS F 290                                          
SITE     1 DC2  5 GLN F  10  HIS F  11  ASP F  48  ARG F 344                    
SITE     2 DC2  5 ARG F 390                                                     
SITE     1 DC3  4 LYS F  30  GLY F  38  LEU F  40  GLU F 279                    
SITE     1 DC4  1 HIS F 284                                                     
SITE     1 DC5  3 HIS F  11  ARG F  82  MET F 197                               
SITE     1 DC6  5 GLN G  10  HIS G  11  MET G  46  ASP G  48                    
SITE     2 DC6  5 ARG G 344                                                     
SITE     1 DC7  2 CYS G   5  LYS G 290                                          
SITE     1 DC8  3 GLY G  38  LEU G  40  GLU G 279                               
SITE     1 DC9  4 HIS H  11  MET H  46  ASP H  48  ARG H 344                    
SITE     1 EC1  3 CYS H   5  GLU H  43  LYS H 290                               
SITE     1 EC2  4 LYS H  30  GLY H  38  LEU H  40  GLU H 279                    
SITE     1 EC3  1 HIS H 284                                                     
SITE     1 EC4  6 HIS H  11  ARG H  82  ALA H 199  ARG H 200                    
SITE     2 EC4  6 SER H 201  ASP H 202                                          
CRYST1  121.420  161.580  279.980  90.00  90.00  90.00 P 21 21 21   32          
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      0.008236  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006189  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003572        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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