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Entry: 1HL5
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HEADER    OXIDOREDUCTASE                          13-MAR-03   1HL5              
TITLE     THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE                    
TITLE    2 DISMUTASE                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE;                                      
COMPND   3 CHAIN: A, H, B, I, C, J, D, K, E, L, F, M, G, N, O, Q, P, S;         
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: EG118;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: YEP351                                    
KEYWDS    OXIDOREDUCTASE, HUMAN CU, ZN SUPEROXIDE DISMUTASE, ANTIOXIDANT,       
KEYWDS   2 METAL-BINDING, AMYOTROPHIC LATERAL SCLEROSIS, DISEASE MUTATION       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.W.STRANGE,S.ANTONYUK,M.A.HOUGH,P.DOUCETTE,J.RODRIGUEZ,P.J.HART,     
AUTHOR   2 L.J.HAYWARD,J.S.VALENTINE,S.S.HASNAIN                                
REVDAT   3   13-JUL-11 1HL5    1       VERSN                                    
REVDAT   2   24-FEB-09 1HL5    1       VERSN                                    
REVDAT   1   08-MAY-03 1HL5    0                                                
JRNL        AUTH   R.W.STRANGE,S.ANTONYUK,M.A.HOUGH,P.DOUCETTE,J.RODRIGUEZ,     
JRNL        AUTH 2 P.J.HART,L.J.HAYWARD,J.S.VALENTINE,S.S.HASNAIN               
JRNL        TITL   THE STRUCTURE OF HOLO AND METAL-DEFICIENT WILD-TYPE HUMAN    
JRNL        TITL 2 CU, ZN SUPEROXIDE DISMUTASE AND ITS RELEVANCE TO FAMILIAL    
JRNL        TITL 3 AMYOTROPHIC LATERAL SCLEROSIS                                
JRNL        REF    J.MOL.BIOL.                   V. 328   877 2003              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   12729761                                                     
JRNL        DOI    10.1016/S0022-2836(03)00355-3                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.8  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 252571                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 13373                           
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.84                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 17869                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2480                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 969                          
REMARK   3   BIN FREE R VALUE                    : 0.2880                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 19783                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 39                                      
REMARK   3   SOLVENT ATOMS            : 1763                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.08                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.30000                                              
REMARK   3    B22 (A**2) : -0.20000                                             
REMARK   3    B33 (A**2) : -0.13000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.30000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.125         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.120         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.086         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.732         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 20321 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 27413 ; 1.604 ; 1.945       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2736 ; 4.679 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3480 ;18.312 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3024 ; 0.128 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 15516 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  9366 ; 0.221 ; 0.300       
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):  2918 ; 0.164 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    65 ; 0.086 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   121 ; 0.410 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    62 ; 0.282 ; 0.500       
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): 13410 ; 0.835 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 21294 ; 1.537 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6911 ; 2.558 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6119 ; 4.276 ; 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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 18                                         
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   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.9990  92.7450  77.5010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2738 T22:   0.3268                                     
REMARK   3      T33:   0.2285 T12:  -0.0297                                     
REMARK   3      T13:   0.0231 T23:   0.0235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3939 L22:   1.7203                                     
REMARK   3      L33:   2.4501 L12:   0.3695                                     
REMARK   3      L13:  -0.3914 L23:  -0.6319                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0155 S12:   0.0176 S13:   0.0329                       
REMARK   3      S21:   0.0771 S22:  -0.0672 S23:  -0.0479                       
REMARK   3      S31:   0.1542 S32:  -0.0681 S33:   0.0517                       
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 :   B     1        B   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.8230  80.8690  18.2360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2560 T22:   0.3025                                     
REMARK   3      T33:   0.2784 T12:   0.0048                                     
REMARK   3      T13:   0.0016 T23:   0.0244                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4364 L22:   1.0334                                     
REMARK   3      L33:   1.9486 L12:   0.2720                                     
REMARK   3      L13:   0.4686 L23:   0.7495                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0165 S12:   0.0149 S13:  -0.0093                       
REMARK   3      S21:  -0.0539 S22:   0.0235 S23:   0.0374                       
REMARK   3      S31:  -0.0721 S32:  -0.1209 S33:  -0.0400                       
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 :   C     1        C   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.2020  79.9080  21.0390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2572 T22:   0.3237                                     
REMARK   3      T33:   0.2667 T12:   0.0115                                     
REMARK   3      T13:   0.0036 T23:  -0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3464 L22:   0.8679                                     
REMARK   3      L33:   1.7061 L12:   0.1293                                     
REMARK   3      L13:   0.1464 L23:   0.3582                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0020 S12:   0.0380 S13:  -0.0468                       
REMARK   3      S21:  -0.0301 S22:   0.0157 S23:  -0.0558                       
REMARK   3      S31:   0.0473 S32:   0.1287 S33:  -0.0138                       
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 :   D     1        D   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.0630  93.6740  74.8370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2818 T22:   0.3293                                     
REMARK   3      T33:   0.2494 T12:  -0.0206                                     
REMARK   3      T13:   0.0451 T23:   0.0321                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4916 L22:   0.8767                                     
REMARK   3      L33:   2.6184 L12:  -0.0501                                     
REMARK   3      L13:  -0.5955 L23:  -0.4587                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0509 S12:   0.0662 S13:   0.1022                       
REMARK   3      S21:  -0.1570 S22:   0.0401 S23:  -0.1000                       
REMARK   3      S31:   0.0299 S32:  -0.1038 S33:  -0.0910                       
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 :   E     1        E   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.9430 120.4050  62.0100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2553 T22:   0.2944                                     
REMARK   3      T33:   0.2748 T12:  -0.0007                                     
REMARK   3      T13:  -0.0046 T23:  -0.0229                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4642 L22:   2.8620                                     
REMARK   3      L33:   0.8262 L12:   0.2942                                     
REMARK   3      L13:   0.2706 L23:   0.5787                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0397 S12:  -0.0420 S13:  -0.0332                       
REMARK   3      S21:  -0.1147 S22:   0.0608 S23:  -0.1131                       
REMARK   3      S31:   0.0056 S32:   0.0490 S33:  -0.0212                       
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 :   F     3        F   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.4560 111.6250 110.1710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3467 T22:   0.2167                                     
REMARK   3      T33:   0.3269 T12:   0.0330                                     
REMARK   3      T13:  -0.0607 T23:  -0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4729 L22:   3.1975                                     
REMARK   3      L33:   0.6928 L12:  -0.8700                                     
REMARK   3      L13:  -0.2605 L23:   0.6916                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0166 S12:  -0.0216 S13:  -0.0197                       
REMARK   3      S21:   0.3467 S22:   0.1034 S23:  -0.1312                       
REMARK   3      S31:   0.1893 S32:   0.0453 S33:  -0.0867                       
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 :   G     1        G   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.3640 148.3970  61.3980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2854 T22:   0.2483                                     
REMARK   3      T33:   0.6222 T12:   0.0851                                     
REMARK   3      T13:  -0.1576 T23:  -0.2325                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1128 L22:   4.4067                                     
REMARK   3      L33:   1.2002 L12:   1.7735                                     
REMARK   3      L13:   0.8128 L23:   0.8956                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2732 S12:  -0.3441 S13:   0.6269                       
REMARK   3      S21:  -0.3784 S22:  -0.2746 S23:   0.9741                       
REMARK   3      S31:  -0.3241 S32:  -0.1849 S33:   0.5478                       
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 :   O     1        O   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.1180 111.6310 105.0200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2499 T22:   0.2039                                     
REMARK   3      T33:   0.4878 T12:  -0.0187                                     
REMARK   3      T13:  -0.0778 T23:   0.0295                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0761 L22:   6.0838                                     
REMARK   3      L33:   0.8752 L12:  -1.0256                                     
REMARK   3      L13:  -0.1423 L23:  -0.3385                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0746 S12:   0.0198 S13:  -0.2476                       
REMARK   3      S21:  -0.2759 S22:   0.1527 S23:   0.8359                       
REMARK   3      S31:   0.1165 S32:  -0.0899 S33:  -0.2273                       
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 :   S     1        S   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.9290 121.2110  22.9610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4754 T22:   0.3928                                     
REMARK   3      T33:   0.1742 T12:   0.0564                                     
REMARK   3      T13:   0.0342 T23:   0.0722                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2152 L22:   1.8234                                     
REMARK   3      L33:   4.1287 L12:  -0.9906                                     
REMARK   3      L13:   0.0157 L23:  -1.5566                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2512 S12:  -0.7339 S13:  -0.1908                       
REMARK   3      S21:   0.2698 S22:   0.2220 S23:  -0.0985                       
REMARK   3      S31:  -0.7130 S32:  -0.2469 S33:   0.0291                       
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 :   P     1        P   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.4320 139.6630  30.5920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7806 T22:   1.2086                                     
REMARK   3      T33:   0.0690 T12:   0.8109                                     
REMARK   3      T13:  -0.1603 T23:  -0.2814                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0487 L22:   6.4738                                     
REMARK   3      L33:  11.4578 L12:  -1.6345                                     
REMARK   3      L13:  -0.9648 L23:   2.9661                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3925 S12:  -1.3673 S13:   0.5828                       
REMARK   3      S21:  -0.4773 S22:  -0.1079 S23:   0.4313                       
REMARK   3      S31:  -1.2460 S32:  -1.7686 S33:   0.5005                       
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 :   Q     1        Q   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.5020 138.8560 106.5970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2163 T22:   0.2577                                     
REMARK   3      T33:   0.3483 T12:   0.0142                                     
REMARK   3      T13:   0.0220 T23:   0.0237                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3408 L22:   6.2236                                     
REMARK   3      L33:   1.1933 L12:  -2.4308                                     
REMARK   3      L13:   0.3864 L23:  -1.4006                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0852 S12:   0.0309 S13:  -0.3318                       
REMARK   3      S21:   0.1640 S22:   0.2546 S23:   0.5813                       
REMARK   3      S31:  -0.0673 S32:  -0.0760 S33:  -0.1694                       
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 :   H     1        H   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.3140  79.5130 101.4640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3363 T22:   0.3116                                     
REMARK   3      T33:   0.2280 T12:  -0.0757                                     
REMARK   3      T13:   0.0272 T23:   0.0103                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7127 L22:   1.3878                                     
REMARK   3      L33:   2.1333 L12:   0.5072                                     
REMARK   3      L13:  -0.7318 L23:  -0.9628                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1679 S12:   0.0920 S13:   0.0556                       
REMARK   3      S21:  -0.2056 S22:   0.1427 S23:  -0.0094                       
REMARK   3      S31:   0.3755 S32:  -0.1983 S33:   0.0253                       
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 :   I     1        I   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.3570  93.9820  42.8170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2748 T22:   0.2988                                     
REMARK   3      T33:   0.2817 T12:  -0.0076                                     
REMARK   3      T13:   0.0376 T23:   0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5541 L22:   1.1616                                     
REMARK   3      L33:   1.1983 L12:   0.3217                                     
REMARK   3      L13:   0.1261 L23:   0.5121                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0836 S12:  -0.0690 S13:   0.0100                       
REMARK   3      S21:   0.0553 S22:  -0.0486 S23:   0.0149                       
REMARK   3      S31:  -0.1109 S32:  -0.0794 S33:  -0.0350                       
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 :   J     1        J   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.0100  93.5360  45.2220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2429 T22:   0.3125                                     
REMARK   3      T33:   0.2646 T12:   0.0004                                     
REMARK   3      T13:   0.0045 T23:  -0.0052                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6400 L22:   1.1254                                     
REMARK   3      L33:   2.0804 L12:   0.2251                                     
REMARK   3      L13:   0.3216 L23:   0.6816                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0013 S12:  -0.0196 S13:   0.0683                       
REMARK   3      S21:   0.0852 S22:  -0.0039 S23:   0.0047                       
REMARK   3      S31:   0.0269 S32:   0.0291 S33:   0.0026                       
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 :   K     1        K   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.3960  80.0770  98.5420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2647 T22:   0.2987                                     
REMARK   3      T33:   0.2771 T12:  -0.0088                                     
REMARK   3      T13:  -0.0144 T23:   0.0271                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4975 L22:   1.2445                                     
REMARK   3      L33:   1.5452 L12:   0.2732                                     
REMARK   3      L13:  -0.3589 L23:  -0.4334                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0106 S12:   0.0381 S13:  -0.0258                       
REMARK   3      S21:  -0.0029 S22:   0.1030 S23:   0.0164                       
REMARK   3      S31:   0.0964 S32:  -0.1063 S33:  -0.0925                       
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 :   L     2        L   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.9600 148.0460  62.4030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2947 T22:   0.2789                                     
REMARK   3      T33:   0.2908 T12:  -0.0273                                     
REMARK   3      T13:  -0.0225 T23:  -0.0200                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7298 L22:   2.5633                                     
REMARK   3      L33:   0.6707 L12:   0.8405                                     
REMARK   3      L13:   0.0257 L23:   0.6937                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0812 S12:   0.0371 S13:   0.0803                       
REMARK   3      S21:  -0.2901 S22:   0.0942 S23:  -0.0203                       
REMARK   3      S31:  -0.0679 S32:   0.0490 S33:  -0.0130                       
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 :   M     2        M   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.2370 139.6470 110.6090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2764 T22:   0.2448                                     
REMARK   3      T33:   0.3060 T12:   0.0229                                     
REMARK   3      T13:  -0.0236 T23:  -0.0213                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5893 L22:   3.2359                                     
REMARK   3      L33:   0.7857 L12:  -0.2782                                     
REMARK   3      L13:  -0.1541 L23:   0.3645                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0038 S12:   0.0075 S13:  -0.0058                       
REMARK   3      S21:   0.2012 S22:  -0.0117 S23:  -0.1268                       
REMARK   3      S31:   0.0239 S32:   0.0224 S33:   0.0079                       
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 :   N     1        N   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.3360 120.9760  59.7200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2026 T22:   0.3138                                     
REMARK   3      T33:   0.2948 T12:  -0.0036                                     
REMARK   3      T13:   0.0290 T23:  -0.0780                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9343 L22:   3.5719                                     
REMARK   3      L33:   1.6670 L12:   1.5771                                     
REMARK   3      L13:   0.5156 L23:   0.3822                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0159 S12:  -0.3621 S13:   0.2038                       
REMARK   3      S21:  -0.1528 S22:  -0.1964 S23:   0.2927                       
REMARK   3      S31:   0.0223 S32:  -0.1673 S33:   0.2122                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: DISORDERED REGIONS IN MONOMERS O AND      
REMARK   3  G WERE MODELED STEREOCHEMICALLY                                     
REMARK   4                                                                      
REMARK   4 1HL5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-MAR-03.                  
REMARK 100 THE PDBE ID CODE IS EBI-12308.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JAN-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 265996                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1SOS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 52.2                                       
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.6                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CA ACETATE, 15% PEG 3350,          
REMARK 280  0.1 M TRIS PH 8.0                                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       86.19000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9                               
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 BIOMOLECULE:  2                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, I                                  
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 BIOMOLECULE:  3                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, J                                  
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 BIOMOLECULE:  4                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, K                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 BIOMOLECULE:  5                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, L                                  
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 BIOMOLECULE:  6                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, M                                  
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 BIOMOLECULE:  7                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, N                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 BIOMOLECULE:  8                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: O, Q                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 BIOMOLECULE:  9                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, S                                  
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     GLY E   108                                                      
REMARK 465     ASP E   109                                                      
REMARK 465     ALA F     1                                                      
REMARK 465     THR F     2                                                      
REMARK 465     GLN F    22                                                      
REMARK 465     LYS F    23                                                      
REMARK 465     GLU F    24                                                      
REMARK 465     SER F    25                                                      
REMARK 465     ASN F    26                                                      
REMARK 465     GLY F    27                                                      
REMARK 465     ALA L     1                                                      
REMARK 465     ALA M     1                                                      
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 C  30    NZ                                                  
REMARK 470     ASP D  11    CG   OD1  OD2                                       
REMARK 470     GLN D  15    OE1                                                 
REMARK 470     GLU D  24    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  30    NZ                                                  
REMARK 470     LYS D  70    CD   CE   NZ                                        
REMARK 470     LYS D 122    CE   NZ                                             
REMARK 470     LYS D 136    CE   NZ                                             
REMARK 470     LYS E   3    CE   NZ                                             
REMARK 470     GLN E  15    OE1  NE2                                            
REMARK 470     LYS E  23    CE   NZ                                             
REMARK 470     LYS E  70    NZ                                                  
REMARK 470     LYS E  75    CE   NZ                                             
REMARK 470     GLU E  77    OE1  OE2                                            
REMARK 470     LYS E  91    NZ                                                  
REMARK 470     SER E 107    OG                                                  
REMARK 470     GLU E 132    CD   OE1  OE2                                       
REMARK 470     LYS F   3    N    CA   CB   CG   CD   CE   NZ                    
REMARK 470     GLN F  15    CD   OE1  NE2                                       
REMARK 470     GLU F  21    C    O    CD   OE1  OE2                             
REMARK 470     LYS F  36    CG   CD   CE   NZ                                   
REMARK 470     LYS F  70    CD   CE   NZ                                        
REMARK 470     LYS J  23    CD   CE   NZ                                        
REMARK 470     LYS J  30    CE   NZ                                             
REMARK 470     LYS J 128    NZ                                                  
REMARK 470     LYS J 136    CE   NZ                                             
REMARK 470     GLN K  15    CD   OE1  NE2                                       
REMARK 470     LYS K 136    NZ                                                  
REMARK 470     LYS L   3    CD   CE   NZ                                        
REMARK 470     LYS L   9    NZ                                                  
REMARK 470     GLN L  15    CD   OE1  NE2                                       
REMARK 470     LYS L  91    CE   NZ                                             
REMARK 470     THR M   2    N    CA   CB   OG1  CG2                             
REMARK 470     GLN M  15    OE1  NE2                                            
REMARK 470     GLU M  24    CA   CB   CG   CD   OE1  OE2                        
REMARK 470     SER M  25    CB   OG                                             
REMARK 470     ASN M  26    CB   CG   OD1  ND2                                  
REMARK 470     LYS M  30    CE   NZ                                             
REMARK 470     LYS M  36    CE   NZ                                             
REMARK 470     LYS M  70    CD   CE   NZ                                        
REMARK 470     LYS M  75    CD   CE   NZ                                        
REMARK 470     LYS M 136    NZ                                                  
REMARK 470     LYS P  75    CE   NZ                                             
REMARK 470     LYS P 122    NZ                                                  
REMARK 470     GLU P 132    CA   CB   CG   CD   OE1  OE2                        
REMARK 470     LYS S  70    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   OD1  ASN B    53     O    HOH B  2071              1.76            
REMARK 500   NH1  ARG B    69     OE1  GLU B    78              2.06            
REMARK 500   NH2  ARG B    69     OE2  GLU B    77              2.07            
REMARK 500   NZ   LYS J     3     OD2  ASP S    92              1.97            
REMARK 500   O    GLN J   153     OD1  ASP S    92              1.68            
REMARK 500   OE1  GLU K   100     O    HOH K  2100              2.19            
REMARK 500   OE2  GLU N   133     O    HOH N  2076              2.08            
REMARK 500   O    GLU O    24     N    ASN O    26              2.18            
REMARK 500   NH2  ARG O    79     OD1  ASP O   101              2.17            
REMARK 500   O    HOH A  2080     O    HOH A  2081              2.12            
REMARK 500   O    HOH J  2046     O    HOH J  2109              2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS B   122     OE2  GLU M    40     1546     1.92            
REMARK 500   O    THR M    54     OE2  GLU S   132     1456     1.86            
REMARK 500   O    HOH H  2064     O    HOH C  2120     1556     2.06            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  96   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A 109   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    VAL B  31   CG1 -  CB  -  CG2 ANGL. DEV. =  10.7 DEGREES          
REMARK 500    ASP B 109   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP C 101   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    VAL D  31   CG1 -  CB  -  CG2 ANGL. DEV. =  11.2 DEGREES          
REMARK 500    ARG D  79   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG D  79   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG F  79   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG F  79   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ASP F 101   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP G  83   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP I  96   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP I 101   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP I 109   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP L  76   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP L  92   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP M 109   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP M 124   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG N  79   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ASP O  83   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG Q  79   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG Q  79   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    ASP Q 101   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 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    ASN A  65       65.58   -154.33                                   
REMARK 500    ASN C  26       -4.95     67.09                                   
REMARK 500    ASN D  26        4.68     58.69                                   
REMARK 500    ASN D  65       65.73   -151.65                                   
REMARK 500    ASN E  26       -0.19     70.71                                   
REMARK 500    ASN E  65       67.36   -151.64                                   
REMARK 500    ASN G  65       73.36   -160.29                                   
REMARK 500    ASN G 131      155.03      1.84                                   
REMARK 500    SER G 142      156.12    -49.95                                   
REMARK 500    ASN H  65       60.76   -150.80                                   
REMARK 500    ASN K  26        5.04     59.47                                   
REMARK 500    SER O  25       35.77    -49.53                                   
REMARK 500    ASN O  26       -5.59    169.07                                   
REMARK 500    ASN O  65       77.53   -153.18                                   
REMARK 500    ASP P  90     -169.18    -79.64                                   
REMARK 500    THR Q   2      129.50    -23.76                                   
REMARK 500    GLU Q  24     -122.30   -116.15                                   
REMARK 500    ASN S  65       55.60   -150.09                                   
REMARK 500    ARG S 115     -167.74   -101.87                                   
REMARK 500    SER S 142      153.02    -44.88                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR G   2        23.5      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 120   NE2                                                    
REMARK 620 2 HIS A  46   ND1  95.8                                              
REMARK 620 3 HIS A  48   NE2 111.6 132.5                                        
REMARK 620 4 HIS A  63   NE2 141.3  78.0  99.7                                  
REMARK 620 5 HOH A2047   O    83.1 124.2  97.8  70.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  46   ND1                                                    
REMARK 620 2 HIS B  63   NE2  76.3                                              
REMARK 620 3 HOH B2083   O   117.6  65.9                                        
REMARK 620 4 HIS B  48   NE2 131.2 100.0 103.8                                  
REMARK 620 5 HIS B 120   NE2  93.8 141.8  87.8 113.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  46   ND1                                                    
REMARK 620 2 HIS C  48   NE2 133.8                                              
REMARK 620 3 HIS C 120   NE2  96.9 112.4                                        
REMARK 620 4 HOH C2074   O   118.2  99.2  86.5                                  
REMARK 620 5 HIS C  63   NE2  78.0  97.2 141.3  64.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU D 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  63   NE2                                                    
REMARK 620 2 HOH D2049   O    64.1                                              
REMARK 620 3 HIS D  46   ND1  77.2 120.0                                        
REMARK 620 4 HIS D  48   NE2  96.4  95.6 134.3                                  
REMARK 620 5 HIS D 120   NE2 138.9  82.9 101.3 111.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU E 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH E2052   O                                                      
REMARK 620 2 HIS E  46   ND1 120.3                                              
REMARK 620 3 HIS E 120   NE2  85.9  94.0                                        
REMARK 620 4 HIS E  63   NE2  66.6  79.6 142.4                                  
REMARK 620 5 HIS E  48   NE2  98.5 134.0 113.7  96.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU F 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH F2040   O                                                      
REMARK 620 2 HIS F  46   ND1 121.4                                              
REMARK 620 3 HIS F  63   NE2  66.2  77.9                                        
REMARK 620 4 HIS F 120   NE2  86.8  96.0 142.0                                  
REMARK 620 5 HIS F  48   NE2  94.5 136.3  97.6 111.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU G 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G  63   NE2                                                    
REMARK 620 2 HIS G  48   NE2  93.1                                              
REMARK 620 3 HOH G2022   O    56.6  96.2                                        
REMARK 620 4 HIS G  46   ND1  75.7 132.7 113.3                                  
REMARK 620 5 HIS G 120   NE2 146.2 116.6 101.7  93.4                            
REMARK 620 6 HOH G2010   O   127.8  66.3 161.2  84.7  81.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU H 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H  46   ND1                                                    
REMARK 620 2 HIS H 120   NE2  94.3                                              
REMARK 620 3 HOH H2050   O   127.2  88.0                                        
REMARK 620 4 HIS H  48   NE2 138.5 110.9  87.4                                  
REMARK 620 5 HIS H  63   NE2  82.7 141.5  65.0  95.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU I 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I  46   ND1                                                    
REMARK 620 2 HIS I  48   NE2 137.8                                              
REMARK 620 3 HIS I  63   NE2  76.6  97.9                                        
REMARK 620 4 HIS I 120   NE2  95.9 112.1 140.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU J 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS J 120   NE2                                                    
REMARK 620 2 HOH J2064   O    84.1                                              
REMARK 620 3 HIS J  48   NE2 112.8  99.1                                        
REMARK 620 4 HIS J  46   ND1  96.3 119.3 134.1                                  
REMARK 620 5 HIS J  63   NE2 142.7  68.7  96.9  76.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU K 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS K  48   NE2                                                    
REMARK 620 2 HIS K  46   ND1 133.0                                              
REMARK 620 3 HIS K  63   NE2  97.4  79.3                                        
REMARK 620 4 HIS K 120   NE2 111.2  95.6 144.0                                  
REMARK 620 5 HOH K2063   O    98.0 122.8  68.5  85.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU L 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS L 120   NE2                                                    
REMARK 620 2 HIS L  46   ND1 100.0                                              
REMARK 620 3 HIS L  48   NE2 115.9 134.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU M 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS M 120   NE2                                                    
REMARK 620 2 HOH M2041   O    86.0                                              
REMARK 620 3 HIS M  48   NE2 110.5  96.4                                        
REMARK 620 4 HIS M  46   ND1  95.7 120.3 136.5                                  
REMARK 620 5 HIS M  63   NE2 142.6  66.4  97.7  78.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU N 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS N  46   ND1                                                    
REMARK 620 2 HIS N  48   NE2 137.0                                              
REMARK 620 3 HIS N  63   NE2  77.4  94.4                                        
REMARK 620 4 HIS N 120   NE2  95.9 114.9 140.2                                  
REMARK 620 5 HOH N2038   O   116.3  96.3  63.9  85.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU O 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS O  63   NE2                                                    
REMARK 620 2 HIS O  46   ND1  77.5                                              
REMARK 620 3 HIS O 120   NE2 136.6  98.7                                        
REMARK 620 4 HIS O  48   NE2  99.0 144.3 106.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU P 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS P  48   NE2                                                    
REMARK 620 2 HIS P  46   ND1 155.5                                              
REMARK 620 3 HIS P 120   NE2  92.3  96.5                                        
REMARK 620 4 HIS P  63   NE2 105.4  87.7 126.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU Q 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS Q  48   NE2                                                    
REMARK 620 2 HIS Q  46   ND1 132.7                                              
REMARK 620 3 HIS Q  63   NE2  98.7  78.5                                        
REMARK 620 4 HOH Q2040   O    98.2 121.5  65.4                                  
REMARK 620 5 HIS Q 120   NE2 112.3  99.0 137.4  81.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU S 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS S 120   NE2                                                    
REMARK 620 2 HIS S  48   NE2 116.0                                              
REMARK 620 3 HIS S  46   ND1  97.6 130.3                                        
REMARK 620 4 HIS S  63   NE2 137.4  93.6  83.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  63   ND1                                                    
REMARK 620 2 ASP A  83   OD1 104.7                                              
REMARK 620 3 HIS A  71   ND1 106.6  95.7                                        
REMARK 620 4 HIS A  80   ND1 112.5 114.1 121.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  71   ND1                                                    
REMARK 620 2 HIS B  80   ND1 120.6                                              
REMARK 620 3 ASP B  83   OD1  96.0 114.4                                        
REMARK 620 4 HIS B  63   ND1 106.5 111.8 105.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  71   ND1                                                    
REMARK 620 2 HIS C  63   ND1 107.7                                              
REMARK 620 3 ASP C  83   OD1  95.7 104.5                                        
REMARK 620 4 HIS C  80   ND1 120.6 111.5 114.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  71   ND1                                                    
REMARK 620 2 HIS D  80   ND1 123.1                                              
REMARK 620 3 HIS D  63   ND1 103.4 111.7                                        
REMARK 620 4 ASP D  83   OD1  96.1 115.3 104.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  71   ND1                                                    
REMARK 620 2 HIS E  80   ND1 120.4                                              
REMARK 620 3 ASP E  83   OD1  98.0 114.3                                        
REMARK 620 4 HIS E  63   ND1 106.0 113.5 102.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  63   ND1                                                    
REMARK 620 2 HIS F  71   ND1 107.1                                              
REMARK 620 3 HIS F  80   ND1 108.5 121.4                                        
REMARK 620 4 ASP F  83   OD1 107.1  94.8 116.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G  63   ND1                                                    
REMARK 620 2 HIS G  80   ND1 108.3                                              
REMARK 620 3 HIS G  71   ND1 107.2 121.2                                        
REMARK 620 4 ASP G  83   OD1 105.7 118.8  94.0                                  
REMARK 620 5 ASP G  83   OD2 156.9  91.7  70.0  52.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H  63   ND1                                                    
REMARK 620 2 HIS H  80   ND1 110.2                                              
REMARK 620 3 ASP H  83   OD1 107.0 112.6                                        
REMARK 620 4 HIS H  71   ND1 105.1 123.3  97.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN I 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I  80   ND1                                                    
REMARK 620 2 ASP I  83   OD1 114.7                                              
REMARK 620 3 HIS I  63   ND1 108.5 103.4                                        
REMARK 620 4 HIS I  71   ND1 123.3  98.2 106.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN J 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS J  63   ND1                                                    
REMARK 620 2 HIS J  71   ND1 109.0                                              
REMARK 620 3 HIS J  80   ND1 110.7 118.0                                        
REMARK 620 4 ASP J  83   OD1 108.1  98.2 111.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN K 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS K  63   ND1                                                    
REMARK 620 2 HIS K  71   ND1 107.6                                              
REMARK 620 3 HIS K  80   ND1 110.8 121.1                                        
REMARK 620 4 ASP K  83   OD1 105.3  98.0 112.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN L 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS L  63   ND1                                                    
REMARK 620 2 HIS L  71   ND1 105.9                                              
REMARK 620 3 ASP L  83   OD1 105.0  97.9                                        
REMARK 620 4 HIS L  80   ND1 112.7 119.1 114.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN M 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS M  63   ND1                                                    
REMARK 620 2 HIS M  71   ND1 106.5                                              
REMARK 620 3 HIS M  80   ND1 112.8 122.2                                        
REMARK 620 4 ASP M  83   OD1 104.5  96.0 112.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN N 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS N  71   ND1                                                    
REMARK 620 2 ASP N  83   OD1  98.3                                              
REMARK 620 3 HIS N  63   ND1 109.9 102.5                                        
REMARK 620 4 HIS N  80   ND1 120.9 114.2 109.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN O 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS O  71   ND1                                                    
REMARK 620 2 ASP O  83   OD1  98.4                                              
REMARK 620 3 HIS O  63   ND1 106.4 105.9                                        
REMARK 620 4 HIS O  80   ND1 121.0 109.4 113.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN P 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS P  63   ND1                                                    
REMARK 620 2 HIS P  80   ND1 103.2                                              
REMARK 620 3 HIS P  71   ND1 104.6 118.9                                        
REMARK 620 4 ASP P  83   OD1 106.6 123.4  98.4                                  
REMARK 620 5 ASP P  83   OD2 158.6  89.2  83.7  52.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN Q 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS Q  71   ND1                                                    
REMARK 620 2 HIS Q  80   ND1 118.7                                              
REMARK 620 3 ASP Q  83   OD1  99.3 112.2                                        
REMARK 620 4 HIS Q  63   ND1 110.2 111.0 103.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN S 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS S  63   ND1                                                    
REMARK 620 2 HIS S  71   ND1 102.8                                              
REMARK 620 3 ASP S  83   OD1 105.8  90.8                                        
REMARK 620 4 HIS S  80   ND1 108.8 125.2 120.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 156  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C  26   O                                                      
REMARK 620 2 ASN C  26   OD1  64.4                                              
REMARK 620 3 SER C 102   O   132.5 160.6                                        
REMARK 620 4 HOH C2035   O    63.4 117.2  72.7                                  
REMARK 620 5 HOH C2038   O    75.7 113.1  83.5  84.9                            
REMARK 620 6 HOH C2106   O   139.6  91.0  69.7 107.5 144.6                      
REMARK 620 7 HOH C2037   O   131.6  83.4  87.9 159.4  86.0  70.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 156  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D2072   O                                                      
REMARK 620 2 ASN D  26   O   138.0                                              
REMARK 620 3 ASN D  26   OD1  79.2  73.6                                        
REMARK 620 4 SER D 102   O    87.4 123.1 163.2                                  
REMARK 620 5 HOH A2063   O    82.1 128.6  90.3  77.6                            
REMARK 620 6 HOH D2024   O    81.8  76.6 107.3  80.6 153.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA O 156  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER H 102   O                                                      
REMARK 620 2 HOH H2084   O    85.7                                              
REMARK 620 3 HOH H2085   O    84.3  80.7                                        
REMARK 620 4 ASN H  26   OD1 160.5  77.3 102.0                                  
REMARK 620 5 HOH H2081   O    73.9  79.8 151.6  93.5                            
REMARK 620 6 ASN H  26   O   130.5 133.6  76.6  68.9 131.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "FA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700                                                                      
REMARK 700 THE SHEETS PRESENTED AS "PA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU A 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU B 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU C 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN C 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU D 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN D 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA D 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU E 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN E 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU F 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN F 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU G 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN G 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU H 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN H 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU I 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN I 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU J 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN J 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU K 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN K 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU L 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN L 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU M 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN M 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU N 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN N 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU O 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN O 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA O 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU P 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN P 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU Q 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN Q 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU S 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN S 155                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AZV   RELATED DB: PDB                                   
REMARK 900  FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)                            
REMARK 900 RELATED ID: 1BA9   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF REDUCED MONOMERIC                         
REMARK 900  SUPEROXIDE DISMUTASE, NMR, 36 STRUCTURES                            
REMARK 900 RELATED ID: 1DSW   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF A MONOMERIC,                              
REMARK 900  REDUCED FORM OFHUMAN COPPER, ZINC SUPEROXIDE                        
REMARK 900  DISMUTASE BEARING THE SAMECHARGE AS THE                             
REMARK 900  NATIVE PROTEIN                                                      
REMARK 900 RELATED ID: 1FUN   RELATED DB: PDB                                   
REMARK 900  SUPEROXIDE DISMUTASE MUTANT WITH LYS 136                            
REMARK 900  REPLACED BY GLU, CYS 6 REPLACED BY ALA                              
REMARK 900  AND CYS 111 REPLACED BY SER (K136E, C6A,                            
REMARK 900  C111S)                                                              
REMARK 900 RELATED ID: 1HL4   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF APO TYPE HUMAN CU, ZN                              
REMARK 900  SUPEROXIDE DISMUTASE                                                
REMARK 900 RELATED ID: 1KMG   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF MONOMERIC COPPER-                         
REMARK 900  FREE SUPEROXIDEDISMUTASE                                            
REMARK 900 RELATED ID: 1L3N   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF REDUCED DIMERIC                           
REMARK 900  COPPER ZINC SOD:THE STRUCTURAL EFFECTS OF                           
REMARK 900  DIMERIZATION                                                        
REMARK 900 RELATED ID: 1MFM   RELATED DB: PDB                                   
REMARK 900  MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q                          
REMARK 900  AT ATOMIC RESOLUTION                                                
REMARK 900 RELATED ID: 1N18   RELATED DB: PDB                                   
REMARK 900  THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE                             
REMARK 900  DISMUTASE, C6A,C111S                                                
REMARK 900 RELATED ID: 1N19   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE HSOD A4V MUTANT                                    
REMARK 900 RELATED ID: 1SOS   RELATED DB: PDB                                   
REMARK 900  SUPEROXIDE DISMUTASE MUTANT WITH CYS 6                              
REMARK 900  REPLACED BY ALA AND CYS 111 REPLACED BY                             
REMARK 900  SER (C6A, C111S)                                                    
REMARK 900 RELATED ID: 1SPD   RELATED DB: PDB                                   
REMARK 900  SUPEROXIDE DISMUTASE                                                
REMARK 900 RELATED ID: 4SOD   RELATED DB: PDB                                   
REMARK 900  CU,ZN SUPEROXIDE DISMUTASE MUTANT WITH CYS                          
REMARK 900  6 REPLACED BY ALA AND CYS 111 REPLACED                              
REMARK 900  BY SER (C6A,C111S) WITH AN 18-RESIDUE                               
REMARK 900  HEPARIN-BINDING PEPTIDE FUSED TO THE C-                             
REMARK 900  TERMINUS (THEORETICAL MODEL)                                        
DBREF  1HL5 A    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  1HL5 B    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  1HL5 C    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  1HL5 D    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  1HL5 E    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  1HL5 F    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  1HL5 G    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  1HL5 H    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  1HL5 I    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  1HL5 J    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  1HL5 K    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  1HL5 L    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  1HL5 M    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  1HL5 N    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  1HL5 O    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  1HL5 P    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  1HL5 Q    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  1HL5 S    1   153  UNP    P00441   SODC_HUMAN       2    154             
SEQRES   1 A  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 A  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 A  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 A  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 A  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 A  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 A  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 A  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 A  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 A  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 A  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 A  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 B  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 B  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 B  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 B  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 B  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 B  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 B  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 B  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 B  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 B  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 B  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 B  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 C  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 C  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 C  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 C  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 C  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 C  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 C  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 C  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 C  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 C  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 C  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 C  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 D  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 D  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 D  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 D  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 D  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 D  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 D  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 D  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 D  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 D  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 D  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 D  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 E  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 E  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 E  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 E  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 E  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 E  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 E  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 E  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 E  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 E  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 E  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 E  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 F  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 F  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 F  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 F  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 F  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 F  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 F  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 F  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 F  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 F  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 F  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 F  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 G  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 G  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 G  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 G  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 G  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 G  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 G  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 G  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 G  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 G  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 G  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 G  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 H  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 H  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 H  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 H  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 H  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 H  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 H  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 H  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 H  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 H  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 H  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 H  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 I  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 I  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 I  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 I  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 I  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 I  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 I  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 I  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 I  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 I  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 I  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 I  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 J  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 J  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 J  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 J  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 J  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 J  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 J  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 J  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 J  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 J  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 J  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 J  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 K  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 K  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 K  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 K  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 K  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 K  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 K  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 K  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 K  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 K  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 K  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 K  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 L  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 L  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 L  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 L  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 L  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 L  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 L  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 L  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 L  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 L  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 L  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 L  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 M  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 M  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 M  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 M  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 M  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 M  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 M  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 M  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 M  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 M  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 M  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 M  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 N  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 N  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 N  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 N  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 N  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 N  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 N  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 N  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 N  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 N  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 N  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 N  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 O  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 O  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 O  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 O  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 O  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 O  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 O  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 O  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 O  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 O  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 O  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 O  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 P  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 P  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 P  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 P  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 P  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 P  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 P  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 P  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 P  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 P  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 P  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 P  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 Q  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 Q  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 Q  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 Q  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 Q  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 Q  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 Q  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 Q  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 Q  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 Q  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 Q  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 Q  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 S  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 S  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 S  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 S  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 S  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 S  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 S  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 S  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 S  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 S  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 S  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 S  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
HET     CU  A 154       1                                                       
HET     ZN  A 155       1                                                       
HET     CU  B 154       1                                                       
HET     ZN  B 155       1                                                       
HET     CU  C 154       1                                                       
HET     ZN  C 155       1                                                       
HET     CA  C 156       1                                                       
HET     CU  D 154       1                                                       
HET     ZN  D 155       1                                                       
HET     CA  D 156       1                                                       
HET     CU  E 154       1                                                       
HET     ZN  E 155       1                                                       
HET     CU  F 154       1                                                       
HET     ZN  F 155       1                                                       
HET     CU  G 154       1                                                       
HET     ZN  G 155       1                                                       
HET     CU  H 154       1                                                       
HET     ZN  H 155       1                                                       
HET     CU  I 154       1                                                       
HET     ZN  I 155       1                                                       
HET     CU  J 154       1                                                       
HET     ZN  J 155       1                                                       
HET     CU  K 154       1                                                       
HET     ZN  K 155       1                                                       
HET     CU  L 154       1                                                       
HET     ZN  L 155       1                                                       
HET     CU  M 154       1                                                       
HET     ZN  M 155       1                                                       
HET     CU  N 154       1                                                       
HET     ZN  N 155       1                                                       
HET     CU  O 154       1                                                       
HET     ZN  O 155       1                                                       
HET     CA  O 156       1                                                       
HET     CU  P 154       1                                                       
HET     ZN  P 155       1                                                       
HET     CU  Q 154       1                                                       
HET     ZN  Q 155       1                                                       
HET     CU  S 154       1                                                       
HET     ZN  S 155       1                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
HETNAM      CA CALCIUM ION                                                      
FORMUL  19   CU    18(CU 2+)                                                    
FORMUL  20   ZN    18(ZN 2+)                                                    
FORMUL  25   CA    3(CA 2+)                                                     
FORMUL  58  HOH   *1763(H2 O)                                                   
HELIX    1   1 ALA A   55  GLY A   61  5                                   7    
HELIX    2   2 GLU A  133  GLY A  138  1                                   6    
HELIX    3   3 ALA B   55  ALA B   60  5                                   6    
HELIX    4   4 GLU B  133  GLY B  138  1                                   6    
HELIX    5   5 ALA C   55  GLY C   61  5                                   7    
HELIX    6   6 GLU C  133  GLY C  138  1                                   6    
HELIX    7   7 ALA D   55  GLY D   61  5                                   7    
HELIX    8   8 GLU D  133  GLY D  138  1                                   6    
HELIX    9   9 ALA E   55  GLY E   61  5                                   7    
HELIX   10  10 GLU E  133  GLY E  138  1                                   6    
HELIX   11  11 ALA F   55  GLY F   61  5                                   7    
HELIX   12  12 GLU F  133  GLY F  138  1                                   6    
HELIX   13  13 ALA G   55  GLY G   61  5                                   7    
HELIX   14  14 SER G  107  HIS G  110  5                                   4    
HELIX   15  15 ASN G  131  THR G  137  1                                   7    
HELIX   16  16 ALA H   55  GLY H   61  5                                   7    
HELIX   17  17 SER H  107  HIS H  110  5                                   4    
HELIX   18  18 GLU H  133  GLY H  138  1                                   6    
HELIX   19  19 ALA I   55  GLY I   61  5                                   7    
HELIX   20  20 GLU I  133  GLY I  138  1                                   6    
HELIX   21  21 ALA J   55  GLY J   61  5                                   7    
HELIX   22  22 SER J  107  HIS J  110  5                                   4    
HELIX   23  23 GLU J  133  GLY J  138  1                                   6    
HELIX   24  24 ALA K   55  GLY K   61  5                                   7    
HELIX   25  25 GLU K  133  GLY K  138  1                                   6    
HELIX   26  26 ALA L   55  GLY L   61  5                                   7    
HELIX   27  27 GLU L  133  GLY L  138  1                                   6    
HELIX   28  28 GLY M   56  GLY M   61  5                                   6    
HELIX   29  29 GLU M  133  GLY M  138  1                                   6    
HELIX   30  30 ALA N   55  GLY N   61  5                                   7    
HELIX   31  31 GLU N  133  GLY N  138  1                                   6    
HELIX   32  32 ALA O   55  GLY O   61  5                                   7    
HELIX   33  33 GLU O  133  GLY O  138  1                                   6    
HELIX   34  34 ALA P   55  GLY P   61  5                                   7    
HELIX   35  35 GLU P  133  GLY P  138  1                                   6    
HELIX   36  36 ALA Q   55  GLY Q   61  5                                   7    
HELIX   37  37 GLU Q  133  GLY Q  138  1                                   6    
HELIX   38  38 ALA S   55  GLY S   61  5                                   7    
HELIX   39  39 GLU S  133  GLY S  138  1                                   6    
SHEET    1  AA 5 ALA A  95  ASP A 101  0                                        
SHEET    2  AA 5 VAL A  29  LYS A  36 -1  O  VAL A  29   N  ASP A 101           
SHEET    3  AA 5 GLN A  15  GLN A  22 -1  O  GLN A  15   N  LYS A  36           
SHEET    4  AA 5 THR A   2  LYS A   9 -1  O  THR A   2   N  GLN A  22           
SHEET    5  AA 5 GLY A 150  ILE A 151 -1  O  GLY A 150   N  VAL A   5           
SHEET    1  AB 4 ASP A  83  ALA A  89  0                                        
SHEET    2  AB 4 GLY A  41  HIS A  48 -1  O  GLY A  41   N  ALA A  89           
SHEET    3  AB 4 THR A 116  HIS A 120 -1  O  THR A 116   N  HIS A  48           
SHEET    4  AB 4 ARG A 143  VAL A 148 -1  N  LEU A 144   O  VAL A 119           
SHEET    1  BA 5 ALA B  95  ASP B 101  0                                        
SHEET    2  BA 5 VAL B  29  LYS B  36 -1  O  VAL B  29   N  ASP B 101           
SHEET    3  BA 5 GLN B  15  GLN B  22 -1  O  GLN B  15   N  LYS B  36           
SHEET    4  BA 5 THR B   2  LEU B   8 -1  O  THR B   2   N  GLN B  22           
SHEET    5  BA 5 GLY B 150  ILE B 151 -1  O  GLY B 150   N  VAL B   5           
SHEET    1  BB 4 ASP B  83  ALA B  89  0                                        
SHEET    2  BB 4 GLY B  41  HIS B  48 -1  O  GLY B  41   N  ALA B  89           
SHEET    3  BB 4 THR B 116  HIS B 120 -1  O  THR B 116   N  HIS B  48           
SHEET    4  BB 4 ARG B 143  VAL B 148 -1  N  LEU B 144   O  VAL B 119           
SHEET    1  CA 5 ALA C  95  ASP C 101  0                                        
SHEET    2  CA 5 VAL C  29  LYS C  36 -1  O  VAL C  29   N  ASP C 101           
SHEET    3  CA 5 GLN C  15  GLN C  22 -1  O  GLN C  15   N  LYS C  36           
SHEET    4  CA 5 THR C   2  LEU C   8 -1  O  THR C   2   N  GLN C  22           
SHEET    5  CA 5 GLY C 150  ILE C 151 -1  O  GLY C 150   N  VAL C   5           
SHEET    1  CB 4 ASP C  83  ALA C  89  0                                        
SHEET    2  CB 4 GLY C  41  HIS C  48 -1  O  GLY C  41   N  ALA C  89           
SHEET    3  CB 4 THR C 116  HIS C 120 -1  O  THR C 116   N  HIS C  48           
SHEET    4  CB 4 ARG C 143  VAL C 148 -1  N  LEU C 144   O  VAL C 119           
SHEET    1  DA 5 ALA D  95  ASP D 101  0                                        
SHEET    2  DA 5 VAL D  29  LYS D  36 -1  O  VAL D  29   N  ASP D 101           
SHEET    3  DA 5 GLN D  15  GLN D  22 -1  O  GLN D  15   N  LYS D  36           
SHEET    4  DA 5 THR D   2  LEU D   8 -1  O  THR D   2   N  GLN D  22           
SHEET    5  DA 5 GLY D 150  ILE D 151 -1  O  GLY D 150   N  VAL D   5           
SHEET    1  DB 4 ASP D  83  ALA D  89  0                                        
SHEET    2  DB 4 GLY D  41  HIS D  48 -1  O  GLY D  41   N  ALA D  89           
SHEET    3  DB 4 THR D 116  HIS D 120 -1  O  THR D 116   N  HIS D  48           
SHEET    4  DB 4 ARG D 143  VAL D 148 -1  N  LEU D 144   O  VAL D 119           
SHEET    1  EA 5 ALA E  95  ASP E 101  0                                        
SHEET    2  EA 5 VAL E  29  LYS E  36 -1  O  VAL E  29   N  ASP E 101           
SHEET    3  EA 5 GLN E  15  GLN E  22 -1  O  GLN E  15   N  LYS E  36           
SHEET    4  EA 5 THR E   2  LEU E   8 -1  O  THR E   2   N  GLN E  22           
SHEET    5  EA 5 GLY E 150  ILE E 151 -1  O  GLY E 150   N  VAL E   5           
SHEET    1  EB 4 ASP E  83  ALA E  89  0                                        
SHEET    2  EB 4 GLY E  41  HIS E  48 -1  O  GLY E  41   N  ALA E  89           
SHEET    3  EB 4 THR E 116  HIS E 120 -1  O  THR E 116   N  HIS E  48           
SHEET    4  EB 4 ARG E 143  VAL E 148 -1  N  LEU E 144   O  VAL E 119           
SHEET    1  FA 9 LYS F   3  LYS F   9  0                                        
SHEET    2  FA 9 GLN F  15  GLU F  21 -1  O  GLY F  16   N  LEU F   8           
SHEET    3  FA 9 VAL F  29  LYS F  36 -1  O  LYS F  30   N  GLU F  21           
SHEET    4  FA 9 ALA F  95  ASP F 101 -1  O  ALA F  95   N  ILE F  35           
SHEET    5  FA 9 ASP F  83  ALA F  89 -1  O  THR F  88   N  ASP F  96           
SHEET    6  FA 9 GLY F  41  HIS F  48 -1  O  GLY F  41   N  ALA F  89           
SHEET    7  FA 9 THR F 116  HIS F 120 -1  O  THR F 116   N  HIS F  48           
SHEET    8  FA 9 ARG F 143  ILE F 151 -1  N  LEU F 144   O  VAL F 119           
SHEET    9  FA 9 LYS F   3  LYS F   9 -1  O  VAL F   5   N  GLY F 150           
SHEET    1  GA 5 ALA G  95  ASP G 101  0                                        
SHEET    2  GA 5 VAL G  29  LYS G  36 -1  O  VAL G  29   N  ASP G 101           
SHEET    3  GA 5 GLN G  15  GLN G  22 -1  O  GLN G  15   N  LYS G  36           
SHEET    4  GA 5 THR G   2  LEU G   8 -1  O  THR G   2   N  GLN G  22           
SHEET    5  GA 5 GLY G 150  ALA G 152 -1  O  GLY G 150   N  VAL G   5           
SHEET    1  GB 4 ASP G  83  ALA G  89  0                                        
SHEET    2  GB 4 GLY G  41  HIS G  48 -1  O  GLY G  41   N  ALA G  89           
SHEET    3  GB 4 THR G 116  HIS G 120 -1  O  THR G 116   N  HIS G  48           
SHEET    4  GB 4 ARG G 143  VAL G 148 -1  N  LEU G 144   O  VAL G 119           
SHEET    1  HA 5 ALA H  95  ASP H 101  0                                        
SHEET    2  HA 5 VAL H  29  LYS H  36 -1  O  VAL H  29   N  ASP H 101           
SHEET    3  HA 5 GLN H  15  GLN H  22 -1  O  GLN H  15   N  LYS H  36           
SHEET    4  HA 5 THR H   2  LEU H   8 -1  O  THR H   2   N  GLN H  22           
SHEET    5  HA 5 GLY H 150  ILE H 151 -1  O  GLY H 150   N  VAL H   5           
SHEET    1  HB 4 ASP H  83  ALA H  89  0                                        
SHEET    2  HB 4 GLY H  41  HIS H  48 -1  O  GLY H  41   N  ALA H  89           
SHEET    3  HB 4 THR H 116  HIS H 120 -1  O  THR H 116   N  HIS H  48           
SHEET    4  HB 4 ARG H 143  VAL H 148 -1  N  LEU H 144   O  VAL H 119           
SHEET    1  IA 5 ALA I  95  ASP I 101  0                                        
SHEET    2  IA 5 VAL I  29  LYS I  36 -1  O  VAL I  29   N  ASP I 101           
SHEET    3  IA 5 GLN I  15  GLN I  22 -1  O  GLN I  15   N  LYS I  36           
SHEET    4  IA 5 THR I   2  LEU I   8 -1  O  THR I   2   N  GLN I  22           
SHEET    5  IA 5 GLY I 150  ILE I 151 -1  O  GLY I 150   N  VAL I   5           
SHEET    1  IB 4 ASP I  83  ALA I  89  0                                        
SHEET    2  IB 4 GLY I  41  HIS I  48 -1  O  GLY I  41   N  ALA I  89           
SHEET    3  IB 4 THR I 116  HIS I 120 -1  O  THR I 116   N  HIS I  48           
SHEET    4  IB 4 ARG I 143  VAL I 148 -1  N  LEU I 144   O  VAL I 119           
SHEET    1  JA 5 ALA J  95  ASP J 101  0                                        
SHEET    2  JA 5 VAL J  29  LYS J  36 -1  O  VAL J  29   N  ASP J 101           
SHEET    3  JA 5 GLN J  15  GLN J  22 -1  O  GLN J  15   N  LYS J  36           
SHEET    4  JA 5 THR J   2  LEU J   8 -1  O  THR J   2   N  GLN J  22           
SHEET    5  JA 5 GLY J 150  ILE J 151 -1  O  GLY J 150   N  VAL J   5           
SHEET    1  JB 4 ASP J  83  ALA J  89  0                                        
SHEET    2  JB 4 GLY J  41  HIS J  48 -1  O  GLY J  41   N  ALA J  89           
SHEET    3  JB 4 THR J 116  HIS J 120 -1  O  THR J 116   N  HIS J  48           
SHEET    4  JB 4 ARG J 143  VAL J 148 -1  N  LEU J 144   O  VAL J 119           
SHEET    1  KA 5 ALA K  95  ASP K 101  0                                        
SHEET    2  KA 5 VAL K  29  LYS K  36 -1  O  VAL K  29   N  ASP K 101           
SHEET    3  KA 5 GLN K  15  GLN K  22 -1  O  GLN K  15   N  LYS K  36           
SHEET    4  KA 5 THR K   2  LYS K   9 -1  O  THR K   2   N  GLN K  22           
SHEET    5  KA 5 GLY K 150  ILE K 151 -1  O  GLY K 150   N  VAL K   5           
SHEET    1  KB 4 ASP K  83  ALA K  89  0                                        
SHEET    2  KB 4 GLY K  41  HIS K  48 -1  O  GLY K  41   N  ALA K  89           
SHEET    3  KB 4 THR K 116  HIS K 120 -1  O  THR K 116   N  HIS K  48           
SHEET    4  KB 4 ARG K 143  VAL K 148 -1  N  LEU K 144   O  VAL K 119           
SHEET    1  LA 5 ALA L  95  ASP L 101  0                                        
SHEET    2  LA 5 VAL L  29  LYS L  36 -1  O  VAL L  29   N  ASP L 101           
SHEET    3  LA 5 GLN L  15  GLN L  22 -1  O  GLN L  15   N  LYS L  36           
SHEET    4  LA 5 LYS L   3  LEU L   8 -1  O  ALA L   4   N  PHE L  20           
SHEET    5  LA 5 GLY L 150  ILE L 151 -1  O  GLY L 150   N  VAL L   5           
SHEET    1  LB 4 ASP L  83  ALA L  89  0                                        
SHEET    2  LB 4 GLY L  41  HIS L  48 -1  O  GLY L  41   N  ALA L  89           
SHEET    3  LB 4 THR L 116  HIS L 120 -1  O  THR L 116   N  HIS L  48           
SHEET    4  LB 4 ARG L 143  VAL L 148 -1  N  LEU L 144   O  VAL L 119           
SHEET    1  MA 5 ALA M  95  ASP M 101  0                                        
SHEET    2  MA 5 VAL M  29  LYS M  36 -1  O  VAL M  29   N  ASP M 101           
SHEET    3  MA 5 GLN M  15  GLN M  22 -1  O  GLN M  15   N  LYS M  36           
SHEET    4  MA 5 THR M   2  LEU M   8 -1  O  THR M   2   N  GLN M  22           
SHEET    5  MA 5 GLY M 150  ILE M 151 -1  O  GLY M 150   N  VAL M   5           
SHEET    1  MB 4 ASP M  83  ALA M  89  0                                        
SHEET    2  MB 4 GLY M  41  HIS M  48 -1  O  GLY M  41   N  ALA M  89           
SHEET    3  MB 4 THR M 116  HIS M 120 -1  O  THR M 116   N  HIS M  48           
SHEET    4  MB 4 ARG M 143  VAL M 148 -1  N  LEU M 144   O  VAL M 119           
SHEET    1  NA 5 ALA N  95  ASP N 101  0                                        
SHEET    2  NA 5 VAL N  29  LYS N  36 -1  O  VAL N  29   N  ASP N 101           
SHEET    3  NA 5 GLN N  15  GLN N  22 -1  O  GLN N  15   N  LYS N  36           
SHEET    4  NA 5 LYS N   3  LEU N   8 -1  O  ALA N   4   N  PHE N  20           
SHEET    5  NA 5 GLY N 150  ILE N 151 -1  O  GLY N 150   N  VAL N   5           
SHEET    1  NB 4 ASP N  83  ALA N  89  0                                        
SHEET    2  NB 4 GLY N  41  HIS N  48 -1  O  GLY N  41   N  ALA N  89           
SHEET    3  NB 4 THR N 116  HIS N 120 -1  O  THR N 116   N  HIS N  48           
SHEET    4  NB 4 ARG N 143  VAL N 148 -1  N  LEU N 144   O  VAL N 119           
SHEET    1  OA 5 ALA O  95  ASP O 101  0                                        
SHEET    2  OA 5 VAL O  29  LYS O  36 -1  O  VAL O  29   N  ASP O 101           
SHEET    3  OA 5 GLN O  15  GLU O  21 -1  O  GLN O  15   N  LYS O  36           
SHEET    4  OA 5 LYS O   3  LEU O   8 -1  O  ALA O   4   N  PHE O  20           
SHEET    5  OA 5 GLY O 150  ILE O 151 -1  O  GLY O 150   N  VAL O   5           
SHEET    1  OB 4 ASP O  83  ALA O  89  0                                        
SHEET    2  OB 4 GLY O  41  HIS O  48 -1  O  GLY O  41   N  ALA O  89           
SHEET    3  OB 4 THR O 116  HIS O 120 -1  O  THR O 116   N  HIS O  48           
SHEET    4  OB 4 ARG O 143  VAL O 148 -1  N  LEU O 144   O  VAL O 119           
SHEET    1  PA 9 THR P   2  LYS P   9  0                                        
SHEET    2  PA 9 GLN P  15  GLN P  22 -1  O  GLY P  16   N  LEU P   8           
SHEET    3  PA 9 VAL P  29  LYS P  36 -1  O  LYS P  30   N  GLU P  21           
SHEET    4  PA 9 ALA P  95  ASP P 101 -1  O  ALA P  95   N  ILE P  35           
SHEET    5  PA 9 ASP P  83  ALA P  89 -1  O  THR P  88   N  ASP P  96           
SHEET    6  PA 9 GLY P  41  HIS P  48 -1  O  GLY P  41   N  ALA P  89           
SHEET    7  PA 9 THR P 116  HIS P 120 -1  O  THR P 116   N  HIS P  48           
SHEET    8  PA 9 ARG P 143  ILE P 151 -1  N  LEU P 144   O  VAL P 119           
SHEET    9  PA 9 THR P   2  LYS P   9 -1  O  VAL P   5   N  GLY P 150           
SHEET    1  QA 5 ALA Q  95  ASP Q 101  0                                        
SHEET    2  QA 5 VAL Q  29  LYS Q  36 -1  O  VAL Q  29   N  ASP Q 101           
SHEET    3  QA 5 GLN Q  15  GLU Q  21 -1  O  GLN Q  15   N  LYS Q  36           
SHEET    4  QA 5 LYS Q   3  LEU Q   8 -1  O  ALA Q   4   N  PHE Q  20           
SHEET    5  QA 5 GLY Q 150  ILE Q 151 -1  O  GLY Q 150   N  VAL Q   5           
SHEET    1  QB 4 ASP Q  83  ALA Q  89  0                                        
SHEET    2  QB 4 GLY Q  41  HIS Q  48 -1  O  GLY Q  41   N  ALA Q  89           
SHEET    3  QB 4 THR Q 116  HIS Q 120 -1  O  THR Q 116   N  HIS Q  48           
SHEET    4  QB 4 ARG Q 143  VAL Q 148 -1  N  LEU Q 144   O  VAL Q 119           
SHEET    1  SA 5 ALA S  95  ASP S 101  0                                        
SHEET    2  SA 5 VAL S  29  LYS S  36 -1  O  VAL S  29   N  ASP S 101           
SHEET    3  SA 5 GLN S  15  GLN S  22 -1  O  GLN S  15   N  LYS S  36           
SHEET    4  SA 5 THR S   2  LEU S   8 -1  O  THR S   2   N  GLN S  22           
SHEET    5  SA 5 GLY S 150  ALA S 152 -1  O  GLY S 150   N  VAL S   5           
SHEET    1  SB 4 ASP S  83  ALA S  89  0                                        
SHEET    2  SB 4 GLY S  41  HIS S  48 -1  O  GLY S  41   N  ALA S  89           
SHEET    3  SB 4 THR S 116  HIS S 120 -1  O  THR S 116   N  HIS S  48           
SHEET    4  SB 4 ARG S 143  VAL S 148 -1  N  LEU S 144   O  VAL S 119           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.13  
SSBOND   2 CYS B   57    CYS B  146                          1555   1555  2.21  
SSBOND   3 CYS C   57    CYS C  146                          1555   1555  2.21  
SSBOND   4 CYS D   57    CYS D  146                          1555   1555  2.16  
SSBOND   5 CYS E   57    CYS E  146                          1555   1555  2.17  
SSBOND   6 CYS F   57    CYS F  146                          1555   1555  2.16  
SSBOND   7 CYS G   57    CYS G  146                          1555   1555  2.12  
SSBOND   8 CYS H   57    CYS H  146                          1555   1555  2.11  
SSBOND   9 CYS I   57    CYS I  146                          1555   1555  2.17  
SSBOND  10 CYS J   57    CYS J  146                          1555   1555  2.17  
SSBOND  11 CYS K   57    CYS K  146                          1555   1555  2.18  
SSBOND  12 CYS L   57    CYS L  146                          1555   1555  2.14  
SSBOND  13 CYS M   57    CYS M  146                          1555   1555  2.15  
SSBOND  14 CYS N   57    CYS N  146                          1555   1555  2.15  
SSBOND  15 CYS O   57    CYS O  146                          1555   1555  2.11  
SSBOND  16 CYS P   57    CYS P  146                          1555   1555  2.04  
SSBOND  17 CYS Q   57    CYS Q  146                          1555   1555  2.13  
SSBOND  18 CYS S   57    CYS S  146                          1555   1555  2.06  
LINK        CU    CU A 154                 NE2 HIS A 120     1555   1555  2.12  
LINK        CU    CU A 154                 ND1 HIS A  46     1555   1555  2.14  
LINK        CU    CU A 154                 NE2 HIS A  48     1555   1555  2.13  
LINK        CU    CU A 154                 NE2 HIS A  63     1555   1555  2.46  
LINK        CU    CU A 154                 O   HOH A2047     1555   1555  2.65  
LINK        ZN    ZN A 155                 ND1 HIS A  63     1555   1555  2.02  
LINK        ZN    ZN A 155                 OD1 ASP A  83     1555   1555  1.90  
LINK        ZN    ZN A 155                 ND1 HIS A  71     1555   1555  1.99  
LINK        ZN    ZN A 155                 ND1 HIS A  80     1555   1555  2.00  
LINK        CU    CU B 154                 NE2 HIS B 120     1555   1555  2.12  
LINK        CU    CU B 154                 ND1 HIS B  46     1555   1555  2.12  
LINK        CU    CU B 154                 NE2 HIS B  63     1555   1555  2.60  
LINK        CU    CU B 154                 O   HOH B2083     1555   1555  2.47  
LINK        CU    CU B 154                 NE2 HIS B  48     1555   1555  2.11  
LINK        ZN    ZN B 155                 ND1 HIS B  71     1555   1555  2.02  
LINK        ZN    ZN B 155                 ND1 HIS B  80     1555   1555  2.01  
LINK        ZN    ZN B 155                 OD1 ASP B  83     1555   1555  1.94  
LINK        ZN    ZN B 155                 ND1 HIS B  63     1555   1555  1.99  
LINK        CU    CU C 154                 ND1 HIS C  46     1555   1555  2.13  
LINK        CU    CU C 154                 NE2 HIS C  48     1555   1555  2.11  
LINK        CU    CU C 154                 NE2 HIS C 120     1555   1555  2.19  
LINK        CU    CU C 154                 O   HOH C2074     1555   1555  2.52  
LINK        CU    CU C 154                 NE2 HIS C  63     1555   1555  2.72  
LINK        ZN    ZN C 155                 ND1 HIS C  71     1555   1555  2.05  
LINK        ZN    ZN C 155                 ND1 HIS C  63     1555   1555  1.94  
LINK        ZN    ZN C 155                 OD1 ASP C  83     1555   1555  1.97  
LINK        ZN    ZN C 155                 ND1 HIS C  80     1555   1555  2.08  
LINK        CA    CA C 156                 O   HOH C2037     1555   1555  2.20  
LINK        CA    CA C 156                 O   HOH C2106     1555   1555  2.69  
LINK        CA    CA C 156                 O   HOH C2038     1555   1555  2.43  
LINK        CA    CA C 156                 O   HOH C2035     1555   1555  2.35  
LINK        CA    CA C 156                 O   SER C 102     1555   1555  2.49  
LINK        CA    CA C 156                 O   ASN C  26     1555   1555  2.50  
LINK        CA    CA C 156                 OD1 ASN C  26     1555   1555  2.44  
LINK        CU    CU D 154                 NE2 HIS D  48     1555   1555  2.07  
LINK        CU    CU D 154                 NE2 HIS D 120     1555   1555  2.14  
LINK        CU    CU D 154                 NE2 HIS D  63     1555   1555  2.60  
LINK        CU    CU D 154                 O   HOH D2049     1555   1555  2.70  
LINK        CU    CU D 154                 ND1 HIS D  46     1555   1555  2.17  
LINK        ZN    ZN D 155                 ND1 HIS D  71     1555   1555  2.06  
LINK        ZN    ZN D 155                 ND1 HIS D  80     1555   1555  1.99  
LINK        ZN    ZN D 155                 ND1 HIS D  63     1555   1555  2.02  
LINK        ZN    ZN D 155                 OD1 ASP D  83     1555   1555  1.89  
LINK        CA    CA D 156                 O   SER D 102     1555   1555  2.59  
LINK        CA    CA D 156                 O   HOH D2072     1555   1555  2.34  
LINK        CA    CA D 156                 O   ASN D  26     1555   1555  2.73  
LINK        CA    CA D 156                 OD1 ASN D  26     1555   1555  2.45  
LINK        CA    CA D 156                 O   HOH D2024     1555   1555  2.43  
LINK        CA    CA D 156                 O   HOH A2063     1555   1455  2.43  
LINK        CU    CU E 154                 O   HOH E2052     1555   1555  2.66  
LINK        CU    CU E 154                 ND1 HIS E  46     1555   1555  2.15  
LINK        CU    CU E 154                 NE2 HIS E 120     1555   1555  2.16  
LINK        CU    CU E 154                 NE2 HIS E  63     1555   1555  2.52  
LINK        CU    CU E 154                 NE2 HIS E  48     1555   1555  2.10  
LINK        ZN    ZN E 155                 ND1 HIS E  71     1555   1555  2.00  
LINK        ZN    ZN E 155                 ND1 HIS E  80     1555   1555  2.00  
LINK        ZN    ZN E 155                 OD1 ASP E  83     1555   1555  1.95  
LINK        ZN    ZN E 155                 ND1 HIS E  63     1555   1555  2.02  
LINK        CU    CU F 154                 NE2 HIS F  63     1555   1555  2.51  
LINK        CU    CU F 154                 NE2 HIS F 120     1555   1555  2.14  
LINK        CU    CU F 154                 NE2 HIS F  48     1555   1555  2.09  
LINK        CU    CU F 154                 O   HOH F2040     1555   1555  2.72  
LINK        CU    CU F 154                 ND1 HIS F  46     1555   1555  2.04  
LINK        ZN    ZN F 155                 ND1 HIS F  63     1555   1555  2.02  
LINK        ZN    ZN F 155                 ND1 HIS F  71     1555   1555  2.08  
LINK        ZN    ZN F 155                 ND1 HIS F  80     1555   1555  1.95  
LINK        ZN    ZN F 155                 OD1 ASP F  83     1555   1555  1.93  
LINK        CU    CU G 154                 NE2 HIS G  63     1555   1555  2.70  
LINK        CU    CU G 154                 NE2 HIS G  48     1555   1555  2.14  
LINK        CU    CU G 154                 O   HOH G2022     1555   1555  2.01  
LINK        CU    CU G 154                 ND1 HIS G  46     1555   1555  2.05  
LINK        CU    CU G 154                 NE2 HIS G 120     1555   1555  1.96  
LINK        CU    CU G 154                 O   HOH G2010     1555   1555  1.96  
LINK        ZN    ZN G 155                 OD1 ASP G  83     1555   1555  1.86  
LINK        ZN    ZN G 155                 ND1 HIS G  71     1555   1555  2.10  
LINK        ZN    ZN G 155                 ND1 HIS G  80     1555   1555  1.95  
LINK        ZN    ZN G 155                 ND1 HIS G  63     1555   1555  2.10  
LINK        ZN    ZN G 155                 OD2 ASP G  83     1555   1555  2.67  
LINK        CU    CU H 154                 ND1 HIS H  46     1555   1555  2.13  
LINK        CU    CU H 154                 NE2 HIS H 120     1555   1555  2.11  
LINK        CU    CU H 154                 NE2 HIS H  63     1555   1555  2.52  
LINK        CU    CU H 154                 NE2 HIS H  48     1555   1555  2.10  
LINK        CU    CU H 154                 O   HOH H2050     1555   1555  2.74  
LINK        ZN    ZN H 155                 OD1 ASP H  83     1555   1555  1.98  
LINK        ZN    ZN H 155                 ND1 HIS H  71     1555   1555  2.06  
LINK        ZN    ZN H 155                 ND1 HIS H  80     1555   1555  1.86  
LINK        ZN    ZN H 155                 ND1 HIS H  63     1555   1555  2.03  
LINK        CU    CU I 154                 NE2 HIS I  63     1555   1555  2.67  
LINK        CU    CU I 154                 ND1 HIS I  46     1555   1555  2.12  
LINK        CU    CU I 154                 NE2 HIS I 120     1555   1555  2.03  
LINK        CU    CU I 154                 NE2 HIS I  48     1555   1555  2.11  
LINK        ZN    ZN I 155                 ND1 HIS I  80     1555   1555  2.09  
LINK        ZN    ZN I 155                 ND1 HIS I  71     1555   1555  2.06  
LINK        ZN    ZN I 155                 OD1 ASP I  83     1555   1555  2.01  
LINK        ZN    ZN I 155                 ND1 HIS I  63     1555   1555  1.94  
LINK        CU    CU J 154                 NE2 HIS J  63     1555   1555  2.61  
LINK        CU    CU J 154                 ND1 HIS J  46     1555   1555  2.15  
LINK        CU    CU J 154                 NE2 HIS J  48     1555   1555  2.09  
LINK        CU    CU J 154                 O   HOH J2064     1555   1555  2.63  
LINK        CU    CU J 154                 NE2 HIS J 120     1555   1555  2.14  
LINK        ZN    ZN J 155                 OD1 ASP J  83     1555   1555  2.01  
LINK        ZN    ZN J 155                 ND1 HIS J  63     1555   1555  1.95  
LINK        ZN    ZN J 155                 ND1 HIS J  71     1555   1555  2.07  
LINK        ZN    ZN J 155                 ND1 HIS J  80     1555   1555  2.00  
LINK        CU    CU K 154                 O   HOH K2063     1555   1555  2.65  
LINK        CU    CU K 154                 NE2 HIS K 120     1555   1555  2.15  
LINK        CU    CU K 154                 NE2 HIS K  63     1555   1555  2.48  
LINK        CU    CU K 154                 ND1 HIS K  46     1555   1555  2.11  
LINK        CU    CU K 154                 NE2 HIS K  48     1555   1555  2.11  
LINK        ZN    ZN K 155                 ND1 HIS K  63     1555   1555  1.98  
LINK        ZN    ZN K 155                 ND1 HIS K  71     1555   1555  2.12  
LINK        ZN    ZN K 155                 ND1 HIS K  80     1555   1555  2.03  
LINK        ZN    ZN K 155                 OD1 ASP K  83     1555   1555  1.90  
LINK        CU    CU L 154                 NE2 HIS L  48     1555   1555  2.05  
LINK        CU    CU L 154                 ND1 HIS L  46     1555   1555  2.09  
LINK        CU    CU L 154                 NE2 HIS L 120     1555   1555  2.02  
LINK        ZN    ZN L 155                 ND1 HIS L  63     1555   1555  2.00  
LINK        ZN    ZN L 155                 ND1 HIS L  71     1555   1555  2.06  
LINK        ZN    ZN L 155                 OD1 ASP L  83     1555   1555  1.90  
LINK        ZN    ZN L 155                 ND1 HIS L  80     1555   1555  1.98  
LINK        CU    CU M 154                 NE2 HIS M  63     1555   1555  2.53  
LINK        CU    CU M 154                 ND1 HIS M  46     1555   1555  2.11  
LINK        CU    CU M 154                 NE2 HIS M  48     1555   1555  2.11  
LINK        CU    CU M 154                 O   HOH M2041     1555   1555  2.62  
LINK        CU    CU M 154                 NE2 HIS M 120     1555   1555  2.10  
LINK        ZN    ZN M 155                 ND1 HIS M  63     1555   1555  1.95  
LINK        ZN    ZN M 155                 ND1 HIS M  71     1555   1555  2.06  
LINK        ZN    ZN M 155                 ND1 HIS M  80     1555   1555  2.05  
LINK        ZN    ZN M 155                 OD1 ASP M  83     1555   1555  1.91  
LINK        CU    CU N 154                 O   HOH N2038     1555   1555  2.65  
LINK        CU    CU N 154                 NE2 HIS N 120     1555   1555  2.04  
LINK        CU    CU N 154                 NE2 HIS N  63     1555   1555  2.72  
LINK        CU    CU N 154                 NE2 HIS N  48     1555   1555  2.07  
LINK        CU    CU N 154                 ND1 HIS N  46     1555   1555  2.12  
LINK        ZN    ZN N 155                 ND1 HIS N  71     1555   1555  1.99  
LINK        ZN    ZN N 155                 OD1 ASP N  83     1555   1555  2.02  
LINK        ZN    ZN N 155                 ND1 HIS N  63     1555   1555  1.96  
LINK        ZN    ZN N 155                 ND1 HIS N  80     1555   1555  2.18  
LINK        CU    CU O 154                 NE2 HIS O  48     1555   1555  2.18  
LINK        CU    CU O 154                 NE2 HIS O 120     1555   1555  2.10  
LINK        CU    CU O 154                 ND1 HIS O  46     1555   1555  2.19  
LINK        CU    CU O 154                 NE2 HIS O  63     1555   1555  2.60  
LINK        ZN    ZN O 155                 OD1 ASP O  83     1555   1555  1.92  
LINK        ZN    ZN O 155                 ND1 HIS O  63     1555   1555  2.03  
LINK        ZN    ZN O 155                 ND1 HIS O  80     1555   1555  2.19  
LINK        ZN    ZN O 155                 ND1 HIS O  71     1555   1555  1.95  
LINK        CA    CA O 156                 O   SER H 102     1555   1555  2.45  
LINK        CA    CA O 156                 O   HOH H2085     1555   1555  2.40  
LINK        CA    CA O 156                 OD1 ASN H  26     1555   1555  2.61  
LINK        CA    CA O 156                 O   HOH H2081     1555   1555  2.44  
LINK        CA    CA O 156                 O   HOH H2084     1555   1555  2.40  
LINK        CA    CA O 156                 O   ASN H  26     1555   1555  2.69  
LINK        CU    CU P 154                 NE2 HIS P  63     1555   1555  2.33  
LINK        CU    CU P 154                 NE2 HIS P 120     1555   1555  2.57  
LINK        CU    CU P 154                 ND1 HIS P  46     1555   1555  2.07  
LINK        CU    CU P 154                 NE2 HIS P  48     1555   1555  2.12  
LINK        ZN    ZN P 155                 OD2 ASP P  83     1555   1555  2.72  
LINK        ZN    ZN P 155                 OD1 ASP P  83     1555   1555  1.81  
LINK        ZN    ZN P 155                 ND1 HIS P  71     1555   1555  2.08  
LINK        ZN    ZN P 155                 ND1 HIS P  80     1555   1555  2.18  
LINK        ZN    ZN P 155                 ND1 HIS P  63     1555   1555  2.15  
LINK        CU    CU Q 154                 NE2 HIS Q 120     1555   1555  2.12  
LINK        CU    CU Q 154                 O   HOH Q2040     1555   1555  2.74  
LINK        CU    CU Q 154                 NE2 HIS Q  63     1555   1555  2.63  
LINK        CU    CU Q 154                 ND1 HIS Q  46     1555   1555  2.08  
LINK        CU    CU Q 154                 NE2 HIS Q  48     1555   1555  2.06  
LINK        ZN    ZN Q 155                 ND1 HIS Q  63     1555   1555  1.92  
LINK        ZN    ZN Q 155                 OD1 ASP Q  83     1555   1555  1.93  
LINK        ZN    ZN Q 155                 ND1 HIS Q  80     1555   1555  2.08  
LINK        ZN    ZN Q 155                 ND1 HIS Q  71     1555   1555  2.03  
LINK        CU    CU S 154                 NE2 HIS S  63     1555   1555  2.52  
LINK        CU    CU S 154                 ND1 HIS S  46     1555   1555  2.18  
LINK        CU    CU S 154                 NE2 HIS S  48     1555   1555  2.02  
LINK        CU    CU S 154                 NE2 HIS S 120     1555   1555  2.20  
LINK        ZN    ZN S 155                 ND1 HIS S  80     1555   1555  2.05  
LINK        ZN    ZN S 155                 OD1 ASP S  83     1555   1555  2.00  
LINK        ZN    ZN S 155                 ND1 HIS S  71     1555   1555  2.11  
LINK        ZN    ZN S 155                 ND1 HIS S  63     1555   1555  2.10  
SITE     1 AC1  5 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC1  5 HOH A2047                                                     
SITE     1 AC2  5 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     2 AC2  5 LYS A 136                                                     
SITE     1 AC3  5 HIS B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     2 AC3  5 HOH B2083                                                     
SITE     1 AC4  4 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     1 AC5  5 HIS C  46  HIS C  48  HIS C  63  HIS C 120                    
SITE     2 AC5  5 HOH C2074                                                     
SITE     1 AC6  4 HIS C  63  HIS C  71  HIS C  80  ASP C  83                    
SITE     1 AC7  6 ASN C  26  SER C 102  HOH C2035  HOH C2037                    
SITE     2 AC7  6 HOH C2038  HOH C2106                                          
SITE     1 AC8  5 HIS D  46  HIS D  48  HIS D  63  HIS D 120                    
SITE     2 AC8  5 HOH D2049                                                     
SITE     1 AC9  4 HIS D  63  HIS D  71  HIS D  80  ASP D  83                    
SITE     1 BC1  5 HOH A2063  ASN D  26  SER D 102  HOH D2024                    
SITE     2 BC1  5 HOH D2072                                                     
SITE     1 BC2  5 HIS E  46  HIS E  48  HIS E  63  HIS E 120                    
SITE     2 BC2  5 HOH E2052                                                     
SITE     1 BC3  4 HIS E  63  HIS E  71  HIS E  80  ASP E  83                    
SITE     1 BC4  5 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     2 BC4  5 HOH F2040                                                     
SITE     1 BC5  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 BC6  6 HIS G  46  HIS G  48  HIS G  63  HIS G 120                    
SITE     2 BC6  6 HOH G2010  HOH G2022                                          
SITE     1 BC7  5 HIS G  63  HIS G  71  HIS G  80  ASP G  83                    
SITE     2 BC7  5 LYS G 136                                                     
SITE     1 BC8  5 HIS H  46  HIS H  48  HIS H  63  HIS H 120                    
SITE     2 BC8  5 HOH H2050                                                     
SITE     1 BC9  4 HIS H  63  HIS H  71  HIS H  80  ASP H  83                    
SITE     1 CC1  5 HIS I  46  HIS I  48  HIS I  63  HIS I 120                    
SITE     2 CC1  5 HOH I2069                                                     
SITE     1 CC2  4 HIS I  63  HIS I  71  HIS I  80  ASP I  83                    
SITE     1 CC3  5 HIS J  46  HIS J  48  HIS J  63  HIS J 120                    
SITE     2 CC3  5 HOH J2064                                                     
SITE     1 CC4  4 HIS J  63  HIS J  71  HIS J  80  ASP J  83                    
SITE     1 CC5  5 HIS K  46  HIS K  48  HIS K  63  HIS K 120                    
SITE     2 CC5  5 HOH K2063                                                     
SITE     1 CC6  5 HIS K  63  HIS K  71  HIS K  80  ASP K  83                    
SITE     2 CC6  5 LYS K 136                                                     
SITE     1 CC7  4 HIS L  46  HIS L  48  HIS L  63  HIS L 120                    
SITE     1 CC8  4 HIS L  63  HIS L  71  HIS L  80  ASP L  83                    
SITE     1 CC9  5 HIS M  46  HIS M  48  HIS M  63  HIS M 120                    
SITE     2 CC9  5 HOH M2041                                                     
SITE     1 DC1  5 HIS M  63  HIS M  71  HIS M  80  ASP M  83                    
SITE     2 DC1  5 LYS M 136                                                     
SITE     1 DC2  5 HIS N  46  HIS N  48  HIS N  63  HIS N 120                    
SITE     2 DC2  5 HOH N2038                                                     
SITE     1 DC3  4 HIS N  63  HIS N  71  HIS N  80  ASP N  83                    
SITE     1 DC4  4 HIS O  46  HIS O  48  HIS O  63  HIS O 120                    
SITE     1 DC5  5 HIS O  63  HIS O  71  HIS O  80  ASP O  83                    
SITE     2 DC5  5 LYS O 136                                                     
SITE     1 DC6  5 ASN H  26  SER H 102  HOH H2081  HOH H2084                    
SITE     2 DC6  5 HOH H2085                                                     
SITE     1 DC7  4 HIS P  46  HIS P  48  HIS P  63  HIS P 120                    
SITE     1 DC8  4 HIS P  63  HIS P  71  HIS P  80  ASP P  83                    
SITE     1 DC9  5 HIS Q  46  HIS Q  48  HIS Q  63  HIS Q 120                    
SITE     2 DC9  5 HOH Q2040                                                     
SITE     1 EC1  4 HIS Q  63  HIS Q  71  HIS Q  80  ASP Q  83                    
SITE     1 EC2  4 HIS S  46  HIS S  48  HIS S  63  HIS S 120                    
SITE     1 EC3  4 HIS S  63  HIS S  71  HIS S  80  ASP S  83                    
CRYST1   76.871  172.380  112.450  90.00  93.45  90.00 P 1 21 1     36          
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      0.013009  0.000000  0.000784        0.00000                         
SCALE2      0.000000  0.005801  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008909        0.00000                         
MTRIX1   1  0.895050 -0.368850  0.250680        3.40235    1                    
MTRIX2   1 -0.372240 -0.927450 -0.035590      183.62323    1                    
MTRIX3   1  0.245620 -0.061460 -0.967420      171.62170    1                    
MTRIX1   2 -0.986350  0.057530 -0.154280       41.97392    1                    
MTRIX2   2 -0.057730 -0.998330 -0.003230      173.66074    1                    
MTRIX3   2 -0.154210  0.005720  0.988020       59.29191    1                    
MTRIX1   3 -0.915130  0.389020  0.105830        4.91064    1                    
MTRIX2   3  0.392310  0.919760  0.011510        4.10431    1                    
MTRIX3   3 -0.092860  0.052050 -0.994320      115.60555    1                    
MTRIX1   4  0.956450 -0.194120 -0.218000       23.65226    1                    
MTRIX2   4 -0.084730  0.530050 -0.843720       71.57378    1                    
MTRIX3   4  0.279340  0.825450  0.490520      -10.01044    1                    
MTRIX1   5  0.957930 -0.190040  0.215050        8.83297    1                    
MTRIX2   5 -0.280800 -0.465950  0.839070      110.49805    1                    
MTRIX3   5 -0.059250 -0.864160 -0.499710      183.51767    1                    
MTRIX1   6 -0.925350  0.224510 -0.305480       46.64627    1                    
MTRIX2   6  0.146330 -0.531820 -0.834120      204.50653    1                    
MTRIX3   6 -0.349720 -0.816560  0.459270      120.70108    1                    
MTRIX1   7 -0.964170  0.227780  0.135960        8.10633    1                    
MTRIX2   7  0.228470  0.452630  0.861930      -27.88937    1                    
MTRIX3   7  0.134790  0.862120 -0.488450       56.90441    1                    
MTRIX1   8  0.911560 -0.356640 -0.204620       53.72966    1                    
MTRIX2   8 -0.350000 -0.411870 -0.841350      211.35992    1                    
MTRIX3   8  0.215780  0.838550 -0.500260       -2.85196    1                    
MTRIX1   9  0.999010  0.029030 -0.033620      -13.08864    1                    
MTRIX2   9  0.015690  0.477480  0.878500      -33.34248    1                    
MTRIX3   9  0.041560 -0.878160  0.476560      175.54706    1                    
MTRIX1  10  0.977310 -0.039520  0.208080       22.31427    1                    
MTRIX2  10  0.163110 -0.486220 -0.858480      242.66022    1                    
MTRIX3  10  0.135100  0.872940 -0.468740       31.64304    1                    
MTRIX1  11  0.862630  0.368500  0.346530      -44.52737    1                    
MTRIX2  11 -0.487130  0.420620  0.765360      -52.29001    1                    
MTRIX3  11  0.136280 -0.829030  0.542350      133.84116    1                    
MTRIX1  12 -0.932870  0.360180  0.005670        1.61367    1                    
MTRIX2  12  0.191420  0.508970 -0.839230       66.00793    1                    
MTRIX3  12 -0.305160 -0.781810 -0.543740      231.29517    1                    
MTRIX1  13 -0.983110 -0.024850  0.181300       43.37927    1                    
MTRIX2  13  0.163560 -0.563660  0.809650      111.04368    1                    
MTRIX3  13  0.082070  0.825630  0.558210      -56.49068    1                    
MTRIX1  14 -0.915630 -0.365090 -0.168290      137.16948    1                    
MTRIX2  14  0.054550 -0.527580  0.847750       60.40010    1                    
MTRIX3  14 -0.398290  0.767050  0.502990      -44.98087    1                    
MTRIX1  15 -0.950280  0.006510 -0.311320      107.06050    1                    
MTRIX2  15  0.257450  0.578810 -0.773760       86.02035    1                    
MTRIX3  15  0.175150 -0.815440 -0.551710      243.48880    1                    
MTRIX1  16  0.539870  0.661280  0.520810      -87.03172    1                    
MTRIX2  16 -0.544850 -0.197090  0.815040      116.28680    1                    
MTRIX3  16  0.641620 -0.723780  0.253890      146.14423    1                    
MTRIX1  17  0.844560  0.480970  0.235360      -70.59261    1                    
MTRIX2  17  0.284100 -0.029920 -0.958330      101.88297    1                    
MTRIX3  17 -0.453880  0.876230 -0.161910        1.33548    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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