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Database: PDB
Entry: 1UXL
LinkDB: 1UXL
Original site: 1UXL 
HEADER    OXIDOREDUCTASE                          25-FEB-04   1UXL              
TITLE     I113T MUTANT OF HUMAN SOD1                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J;                                 
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: 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    HUMAN CU, ZN SUPEROXIDE DISMUTASE, ANTIOXIDANT, METAL- BINDING,       
KEYWDS   2 AMYOTROPHIC LATERAL SCLEROSIS, DISEASE MUTATION, OXIDOREDUCTASE      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.HOUGH,J.G.GROSSMANN,S.V.ANTONYUK,R.W.STRANGE,P.A.DOUCETTE,        
AUTHOR   2 J.A.RODRIGUEZ,L.J.WHITSON,P.J.HART,L.J.HAYWARD,J.S.VALENTINE,        
AUTHOR   3 S.S.HASNAIN                                                          
REVDAT   4   13-JUL-11 1UXL    1       VERSN                                    
REVDAT   3   24-FEB-09 1UXL    1       VERSN                                    
REVDAT   2   05-JAN-05 1UXL    1       JRNL                                     
REVDAT   1   19-MAR-04 1UXL    0                                                
JRNL        AUTH   M.A.HOUGH,J.G.GROSSMANN,S.V.ANTONYUK,R.W.STRANGE,            
JRNL        AUTH 2 P.A.DOUCETTE,J.A.RODRIGUEZ,L.J.WHITSON,P.J.HART,L.J.HAYWARD, 
JRNL        AUTH 3 J.S.VALENTINE,S.S.HASNAIN                                    
JRNL        TITL   DIMER DESTABILIZATION IN SUPEROXIDE DISMUTASE MAY RESULT IN  
JRNL        TITL 2 DISEASE-CAUSING PROPERTIES: STRUCTURES OF MOTOR NEURON       
JRNL        TITL 3 DISEASE MUTANTS                                              
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 101  5976 2004              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   15056757                                                     
JRNL        DOI    10.1073/PNAS.0305143101                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.6  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) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 300383                         
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) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 15958                           
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) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 21935                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2430                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 1243                         
REMARK   3   BIN FREE R VALUE                    : 0.2660                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11323                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 61                                      
REMARK   3   SOLVENT ATOMS            : 2447                                    
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) : 21.43                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.68000                                              
REMARK   3    B22 (A**2) : -0.35000                                             
REMARK   3    B33 (A**2) : -0.33000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.066         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.068         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.049         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.400         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.959                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11388 ; 0.011 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15401 ; 1.580 ; 1.941       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1525 ; 4.791 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1877 ;18.540 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1728 ; 0.107 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8677 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  5829 ; 0.275 ; 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):  2749 ; 0.226 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    55 ; 0.122 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   114 ; 0.221 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):   116 ; 0.321 ; 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):  7531 ; 0.764 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11983 ; 1.389 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3855 ; 2.266 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3413 ; 3.779 ; 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  : 10                                         
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): 122.5850  57.7570  53.0520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0337 T22:   0.0762                                     
REMARK   3      T33:   0.0292 T12:  -0.0472                                     
REMARK   3      T13:   0.0168 T23:  -0.0090                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8176 L22:   0.7546                                     
REMARK   3      L33:   0.8731 L12:   0.3333                                     
REMARK   3      L13:  -0.1246 L23:  -0.0468                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0036 S12:   0.0251 S13:   0.0186                       
REMARK   3      S21:   0.0066 S22:   0.0072 S23:   0.0760                       
REMARK   3      S31:   0.0734 S32:  -0.1046 S33:  -0.0036                       
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): 173.8340 118.4530  53.0550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2173 T22:   0.0606                                     
REMARK   3      T33:   0.0633 T12:  -0.0317                                     
REMARK   3      T13:  -0.0732 T23:   0.0128                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6497 L22:   1.0071                                     
REMARK   3      L33:   0.3529 L12:  -0.2850                                     
REMARK   3      L13:   0.1394 L23:   0.2416                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1062 S12:   0.0321 S13:   0.1197                       
REMARK   3      S21:  -0.0880 S22:   0.0174 S23:  -0.0167                       
REMARK   3      S31:  -0.2214 S32:   0.0410 S33:   0.0888                       
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): 201.9200  43.4620  52.7630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0343 T22:   0.0631                                     
REMARK   3      T33:   0.0298 T12:   0.0274                                     
REMARK   3      T13:   0.0012 T23:   0.0135                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9703 L22:   0.9900                                     
REMARK   3      L33:   0.4787 L12:  -0.4860                                     
REMARK   3      L13:  -0.0951 L23:   0.0657                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0005 S12:   0.0022 S13:  -0.0807                       
REMARK   3      S21:  -0.0004 S22:  -0.0002 S23:  -0.0023                       
REMARK   3      S31:   0.0264 S32:   0.0305 S33:   0.0007                       
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): 176.3820 149.7930  52.6980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0672 T22:   0.1862                                     
REMARK   3      T33:   0.0886 T12:  -0.0848                                     
REMARK   3      T13:  -0.0411 T23:   0.0848                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9987 L22:   1.1732                                     
REMARK   3      L33:   0.2170 L12:   0.2352                                     
REMARK   3      L13:   0.0704 L23:   0.4650                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0181 S12:   0.2161 S13:   0.0905                       
REMARK   3      S21:  -0.0195 S22:  -0.0772 S23:  -0.1797                       
REMARK   3      S31:  -0.0960 S32:   0.0214 S33:   0.0953                       
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): 125.2350  88.0070  46.9420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1002 T22:   0.0692                                     
REMARK   3      T33:   0.1373 T12:   0.0039                                     
REMARK   3      T13:  -0.0251 T23:  -0.0078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2632 L22:   1.6745                                     
REMARK   3      L33:   0.3604 L12:  -0.0940                                     
REMARK   3      L13:   0.1627 L23:  -0.2410                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0196 S12:   0.0035 S13:   0.0694                       
REMARK   3      S21:  -0.2377 S22:  -0.0112 S23:   0.1963                       
REMARK   3      S31:   0.0574 S32:  -0.0091 S33:  -0.0084                       
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     1        F   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): 148.8680  66.8900  54.0130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0251 T22:   0.0406                                     
REMARK   3      T33:   0.0054 T12:  -0.0047                                     
REMARK   3      T13:   0.0051 T23:  -0.0065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3240 L22:   0.7338                                     
REMARK   3      L33:   0.5349 L12:   0.0775                                     
REMARK   3      L13:  -0.0899 L23:   0.0705                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0012 S12:   0.0032 S13:  -0.0451                       
REMARK   3      S21:  -0.0023 S22:  -0.0037 S23:  -0.0211                       
REMARK   3      S31:   0.0409 S32:  -0.0030 S33:   0.0049                       
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): 169.5520  91.0320  54.0060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0372 T22:   0.0305                                     
REMARK   3      T33:   0.0182 T12:   0.0053                                     
REMARK   3      T13:  -0.0138 T23:  -0.0092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7259 L22:   1.4873                                     
REMARK   3      L33:   1.0032 L12:   0.3812                                     
REMARK   3      L13:   0.0718 L23:  -0.0624                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0308 S12:   0.0277 S13:   0.0308                       
REMARK   3      S21:  -0.0141 S22:  -0.0247 S23:   0.0540                       
REMARK   3      S31:  -0.0681 S32:   0.0444 S33:   0.0554                       
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 :   H     1        H   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): 180.3520  60.9100  54.0250              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0220 T22:   0.0543                                     
REMARK   3      T33:   0.0242 T12:   0.0159                                     
REMARK   3      T13:   0.0098 T23:   0.0073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0882 L22:   1.1021                                     
REMARK   3      L33:   0.5288 L12:  -0.5913                                     
REMARK   3      L13:   0.0770 L23:   0.0516                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0346 S12:   0.0064 S13:   0.0385                       
REMARK   3      S21:  -0.0016 S22:   0.0003 S23:   0.0350                       
REMARK   3      S31:  -0.0026 S32:  -0.0206 S33:   0.0343                       
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 :   J     1        J   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): 130.1040 115.3020  49.3300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0551 T22:   0.0692                                     
REMARK   3      T33:   0.0935 T12:   0.0135                                     
REMARK   3      T13:  -0.0085 T23:   0.0055                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7409 L22:   1.6369                                     
REMARK   3      L33:   0.2800 L12:   0.2867                                     
REMARK   3      L13:  -0.0172 L23:  -0.0378                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0260 S12:   0.0075 S13:  -0.0719                       
REMARK   3      S21:  -0.0407 S22:  -0.0040 S23:   0.0763                       
REMARK   3      S31:   0.0032 S32:   0.0147 S33:  -0.0221                       
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 :   I     1        I   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): 150.4810 139.8950  52.1910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0450 T22:   0.1179                                     
REMARK   3      T33:   0.0477 T12:  -0.0181                                     
REMARK   3      T13:  -0.0092 T23:  -0.0134                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8422 L22:   0.7384                                     
REMARK   3      L33:   0.6590 L12:   0.0358                                     
REMARK   3      L13:   0.1582 L23:   0.0843                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0600 S12:   0.0572 S13:   0.0513                       
REMARK   3      S21:  -0.0150 S22:   0.0476 S23:  -0.0082                       
REMARK   3      S31:  -0.1087 S32:   0.0821 S33:   0.0124                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS. THIS ENTRY CONTAINS ATOMS THAT HAVE BEEN          
REMARK   3  REFINED WITH AN OCCUPANCY OF 0.00.                                  
REMARK   4                                                                      
REMARK   4 1UXL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-FEB-04.                  
REMARK 100 THE PDBE ID CODE IS EBI-14592.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-NOV-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
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) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
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          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 317774                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
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     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 10.000                             
REMARK 200  R MERGE                    (I) : 0.05100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
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 1HL5                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 60                                         
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NACL, 2.4M AMMONIUM               
REMARK 280  SULPHATE PH 7.5                                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       72.01050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       72.01050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       83.02100            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      101.77300            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       83.02100            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      101.77300            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       72.01050            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       83.02100            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      101.77300            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       72.01050            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       83.02100            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      101.77300            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
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, F                                  
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, G                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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, 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:  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, 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:  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, 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375      HOH D2029  LIES ON A SPECIAL POSITION.                          
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  DESTROYS RADICALS WHICH ARE NORMALLY PRODUCED WITHIN THE            
REMARK 400  CELLS AND WHICH ARE TOXIC TO BIOLOGICAL SYSTEMS.                    
REMARK 400                                                                      
REMARK 400 ENGINEERED MUTATION ILE 113 TO THR 113 IN CHAINS A TO J              
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER;                                
REMARK 480 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 480 I=INSERTION CODE):                                                   
REMARK 480   M RES CSSEQI  ATOMS                                                
REMARK 480     LYS A   9    CD   CE   NZ                                        
REMARK 480     LYS A  23    CG   CD   CE   NZ                                   
REMARK 480     GLU A  24    CD  OE1  OE2                                        
REMARK 480     LYS A  30    NZ                                                  
REMARK 480     LYS A  70    CD   CE   NZ                                        
REMARK 480     GLU A 132    CG   CD  OE1  OE2                                   
REMARK 480     LYS A 136    CG   CD   CE   NZ                                   
REMARK 480     GLU B 132    CG   CD  OE1  OE2                                   
REMARK 480     LYS B 136    CD   CE   NZ                                        
REMARK 480     LYS C   3    CE   NZ                                             
REMARK 480     LYS C  23    CE   NZ                                             
REMARK 480     LYS C  70    CD   CE   NZ                                        
REMARK 480     GLU C  77    CD  OE1  OE2                                        
REMARK 480     LYS C  91    CD   CE   NZ                                        
REMARK 480     LYS D  23    CG   CD   CE   NZ                                   
REMARK 480     GLU D  24    CB   CG   CD  OE1  OE2                              
REMARK 480     LYS D  30    CD   CE   NZ                                        
REMARK 480     LYS D  70    CD   CE   NZ                                        
REMARK 480     GLU D  77    CB   CG   CD  OE1  OE2                              
REMARK 480     LYS D 136    CD   CE   NZ                                        
REMARK 480     LYS E   3    CE   NZ                                             
REMARK 480     GLU E  24    CG   CD  OE1  OE2                                   
REMARK 480     LYS E  70    CG   CD   CE   NZ                                   
REMARK 480     GLU E  77    CG   CD  OE1  OE2                                   
REMARK 480     LYS E  91    CD   CE   NZ                                        
REMARK 480     GLU E 133    CB   CG   CD  OE1  OE2                              
REMARK 480     LYS F  30    CD   CE   NZ                                        
REMARK 480     GLU G  24    CD  OE1  OE2                                        
REMARK 480     LYS G  30    CD   CE   NZ                                        
REMARK 480     LYS G  36    CE   NZ                                             
REMARK 480     LYS G  70    CE   NZ                                             
REMARK 480     LYS G  91    CE   NZ                                             
REMARK 480     LYS H  23    CD   CE   NZ                                        
REMARK 480     LYS H  30    CD   CE   NZ                                        
REMARK 480     LYS H  70    CD   CE   NZ                                        
REMARK 480     ASP H  90    CG  OD1  OD2                                        
REMARK 480     LYS H 136    NZ                                                  
REMARK 480     LYS I  70    CE   NZ                                             
REMARK 480     LYS I  91    CE   NZ                                             
REMARK 480     ASP I 109    CB   CG  OD1  OD2                                   
REMARK 480     HIS I 110    CB   CG  ND1  CD2  CE1  NE2                         
REMARK 480     LYS I 136    CD   CE   NZ                                        
REMARK 480     LYS J   3    CD   CE   NZ                                        
REMARK 480     LYS J   9    CE   NZ                                             
REMARK 480     LYS J  23    CG   CD   CE   NZ                                   
REMARK 480     GLU J  24    CD  OE1  OE2                                        
REMARK 480     ASN J  26    CG  OD1  ND2                                        
REMARK 480     LYS J  70    CE   NZ                                             
REMARK 480     LYS J  75    CD   CE   NZ                                        
REMARK 480     ASP J 109    CG  OD1  OD2                                        
REMARK 480     LYS J 136    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 D    65     O    HOH D  2087              2.10            
REMARK 500   CB   ASP H    90     O    HOH H  2207              2.19            
REMARK 500   CB   ALA I     1     O    HOH I  2004              2.17            
REMARK 500   O    HOH C  2038     O    HOH C  2096              2.16            
REMARK 500   O    HOH F  2075     O    HOH F  2076              2.18            
REMARK 500   O    HOH G  2077     O    HOH G  2176              2.14            
REMARK 500   O    HOH G  2157     O    HOH G  2170              2.01            
REMARK 500   O    HOH H  2123     O    HOH C  2210              2.16            
REMARK 500   O    HOH H  2205     O    HOH H  2207              1.79            
REMARK 500   O    HOH H  2256     O    HOH H  2257              2.05            
REMARK 500   O    HOH H  2268     O    HOH H  2269              2.02            
REMARK 500   O    HOH I  2033     O    HOH I  2081              2.17            
REMARK 500   O    HOH I  2233     O    HOH I  2236              2.14            
REMARK 500   O    HOH J  2020     O    HOH J  2234              2.15            
REMARK 500   O    HOH J  2129     O    HOH J  2131              2.16            
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   O    HOH A  2075     O    HOH D  2152     5445     2.18            
REMARK 500   O    HOH G  2100     O    HOH G  2100     3755     0.36            
REMARK 500   O    HOH J  2141     O    HOH C  2229     5455     2.15            
REMARK 500   O    HOH J  2215     O    HOH C  2231     5455     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ILE A  99   C  A  GLU A 100   N       0.179                       
REMARK 500    SER B 107   C     GLY B 108   N  A    0.398                       
REMARK 500    GLU E  77   CB    GLU E  77   CG      0.120                       
REMARK 500    LYS G  70   CD    LYS G  70   CE      0.243                       
REMARK 500    GLU J  24   CG    GLU J  24   CD      0.145                       
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    ILE A  99   CA  -  C   -  N   ANGL. DEV. = -16.9 DEGREES          
REMARK 500    ILE A  99   O   -  C   -  N   ANGL. DEV. =  10.9 DEGREES          
REMARK 500    ASP B  83   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    GLY B 108   C   -  N   -  CA  ANGL. DEV. = -20.8 DEGREES          
REMARK 500    CYS B 111   N   -  CA  -  CB  ANGL. DEV. = -14.4 DEGREES          
REMARK 500    GLU B 132   N   -  CA  -  CB  ANGL. DEV. = -12.5 DEGREES          
REMARK 500    ASP D  83   CB  -  CG  -  OD1 ANGL. DEV. =   7.7 DEGREES          
REMARK 500    ASP H  90   CB  -  CG  -  OD2 ANGL. DEV. =   7.4 DEGREES          
REMARK 500    CYS I 111   N   -  CA  -  CB  ANGL. DEV. =  -9.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
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 F  26        1.36     59.77                                   
REMARK 500    ASN G  65       63.07   -150.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ILE A  99         10.13                                           
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    CYS B 111        22.5      L          L   OUTSIDE RANGE           
REMARK 500    THR C   2        23.9      L          L   OUTSIDE RANGE           
REMARK 500    ASP H 109        22.9      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  46   ND1                                                    
REMARK 620 2 HIS A 120   NE2 102.8                                              
REMARK 620 3 HIS A  48   NE2 135.5 115.5                                        
REMARK 620 N                    1     2                                         
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  46   ND1                                                    
REMARK 620 2 HIS A 120   NE2  90.8                                              
REMARK 620 3 HIS A  48   NE2 112.4 121.0                                        
REMARK 620 N                    1     2                                         
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  48   NE2 121.9                                              
REMARK 620 3 HIS B 120   NE2  97.8 124.1                                        
REMARK 620 4 SO4 B 156   O1  103.3 111.9  92.5                                  
REMARK 620 N                    1     2     3                                   
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 132.8                                              
REMARK 620 3 HIS C 120   NE2  99.8 122.4                                        
REMARK 620 N                    1     2                                         
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  48   NE2                                                    
REMARK 620 2 HIS D 120   NE2 125.2                                              
REMARK 620 3 SO4 D 156   O1   81.4  91.8                                        
REMARK 620 4 HIS D  46   ND1 132.6 100.7 111.3                                  
REMARK 620 N                    1     2     3                                   
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 HIS E  48   NE2                                                    
REMARK 620 2 HIS E 120   NE2 123.4                                              
REMARK 620 3 HIS E  46   ND1 134.0  98.0                                        
REMARK 620 N                    1     2                                         
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 HIS F  48   NE2                                                    
REMARK 620 2 HIS F  46   ND1 130.6                                              
REMARK 620 3 HIS F 120   NE2 123.9 100.8                                        
REMARK 620 N                    1     2                                         
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  46   ND1                                                    
REMARK 620 2 HIS G 120   NE2  98.8                                              
REMARK 620 3 HIS G  48   NE2 141.1 117.8                                        
REMARK 620 N                    1     2                                         
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  48   NE2 135.5                                              
REMARK 620 3 HIS H 120   NE2 102.0 120.5                                        
REMARK 620 N                    1     2                                         
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 134.6                                              
REMARK 620 3 HIS I 120   NE2  99.0 123.0                                        
REMARK 620 N                    1     2                                         
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  48   NE2                                                    
REMARK 620 2 HIS J 120   NE2 117.9                                              
REMARK 620 3 HIS J  46   ND1 144.2  97.7                                        
REMARK 620 N                    1     2                                         
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 ASP A  83   OD1                                                    
REMARK 620 2 HIS A  63   ND1 107.2                                              
REMARK 620 3 HIS A  71   ND1 100.3 104.1                                        
REMARK 620 4 HIS A  80   ND1 114.3 110.1 119.7                                  
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  63   ND1                                                    
REMARK 620 2 HIS B  80   ND1 102.0                                              
REMARK 620 3 HIS B  71   ND1 104.3 125.5                                        
REMARK 620 4 ASP B  83   OD1 109.9 115.6  98.7                                  
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  63   ND1                                                    
REMARK 620 2 HIS C  71   ND1 104.7                                              
REMARK 620 3 HIS C  80   ND1 111.7 121.1                                        
REMARK 620 4 ASP C  83   OD1 105.7  98.5 113.4                                  
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  80   ND1                                                    
REMARK 620 2 HIS D  63   ND1 110.0                                              
REMARK 620 3 HIS D  71   ND1 122.4 107.1                                        
REMARK 620 4 ASP D  83   OD1 113.7 103.8  97.9                                  
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  63   ND1 107.7                                              
REMARK 620 3 HIS E  80   ND1 121.6 108.3                                        
REMARK 620 4 ASP E  83   OD1  96.1 105.0 116.6                                  
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 ASP F  83   OD1 105.1                                              
REMARK 620 3 HIS F  80   ND1 111.5 113.1                                        
REMARK 620 4 HIS F  71   ND1 104.9  99.8 120.9                                  
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  80   ND1                                                    
REMARK 620 2 ASP G  83   OD1 113.2                                              
REMARK 620 3 HIS G  63   ND1 110.5 103.0                                        
REMARK 620 4 HIS G  71   ND1 122.9  98.4 106.6                                  
REMARK 620 N                    1     2     3                                   
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  80   ND1                                                    
REMARK 620 2 ASP H  83   OD1 114.8                                              
REMARK 620 3 HIS H  63   ND1 110.5 103.9                                        
REMARK 620 4 HIS H  71   ND1 120.4  99.6 105.9                                  
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  71   ND1                                                    
REMARK 620 2 ASP I  83   OD1  99.0                                              
REMARK 620 3 HIS I  80   ND1 122.0 114.4                                        
REMARK 620 4 HIS I  63   ND1 104.7 106.5 108.8                                  
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 ASP J  83   OD1                                                    
REMARK 620 2 HIS J  80   ND1 114.0                                              
REMARK 620 3 HIS J  63   ND1 107.1 108.8                                        
REMARK 620 4 HIS J  71   ND1  97.7 121.2 106.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  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 SO4 A 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU B 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU C 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN C 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 157                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU D 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN D 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU E 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN E 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU F 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN F 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU G 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN G 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU H 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN H 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU I 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN I 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU J 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN J 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: 1HL5   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF HOLO 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: 1OEZ   RELATED DB: PDB                                   
REMARK 900  ZN HIS46ARG MUTANT OF HUMAN CU, ZN                                  
REMARK 900  SUPEROXIDE DISMUTASE                                                
REMARK 900 RELATED ID: 1OZT   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF APO-H46R FAMILIAL ALS                          
REMARK 900  MUTANT HUMAN CU,ZN SUPEROXIDE DISMUTASE (                           
REMARK 900  CUZNSOD) TO 2.5A RESOLUTION                                         
REMARK 900 RELATED ID: 1OZU   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF FAMILIAL ALS MUTANT                            
REMARK 900  S134N OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (                         
REMARK 900  CUZNSOD) TO 1.3A RESOLUTION                                         
REMARK 900 RELATED ID: 1P1V   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF FALS-ASSOCIATED HUMAN                          
REMARK 900  COPPER-ZINCSUPEROXIDE DISMUTASE (CUZNSOD) MUTANT                    
REMARK 900   D125H TO 1.4A                                                      
REMARK 900 RELATED ID: 1PTZ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN CU, ZN                               
REMARK 900  SUPEROXIDE DISMUTASE,FAMILIAL AMYOTROPHIC                           
REMARK 900  LATERAL SCLEROSIS (FALS) MUTANT H43R                                
REMARK 900 RELATED ID: 1PU0   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN CU,ZN SUPEROXIDE                                 
REMARK 900  DISMUTASE                                                           
REMARK 900 RELATED ID: 1RK7   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF APO CU,ZN SUPEROXIDE                          
REMARK 900  DISMUTASE: ROLEOF METAL IONS IN PROTEIN                             
REMARK 900  FOLDING                                                             
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: 1UXM   RELATED DB: PDB                                   
REMARK 900  A4V MUTANT OF HUMAN SOD1                                            
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  1UXL A    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1UXL B    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1UXL C    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1UXL D    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1UXL E    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1UXL F    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1UXL G    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1UXL H    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1UXL I    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1UXL J    1   153  UNP    P00441   SODC_HUMAN       1    153             
SEQADV 1UXL THR A  113  UNP  P00441    ILE   113 ENGINEERED MUTATION            
SEQADV 1UXL THR B  113  UNP  P00441    ILE   113 ENGINEERED MUTATION            
SEQADV 1UXL THR C  113  UNP  P00441    ILE   113 ENGINEERED MUTATION            
SEQADV 1UXL THR D  113  UNP  P00441    ILE   113 ENGINEERED MUTATION            
SEQADV 1UXL THR E  113  UNP  P00441    ILE   113 ENGINEERED MUTATION            
SEQADV 1UXL THR F  113  UNP  P00441    ILE   113 ENGINEERED MUTATION            
SEQADV 1UXL THR G  113  UNP  P00441    ILE   113 ENGINEERED MUTATION            
SEQADV 1UXL THR H  113  UNP  P00441    ILE   113 ENGINEERED MUTATION            
SEQADV 1UXL THR I  113  UNP  P00441    ILE   113 ENGINEERED MUTATION            
SEQADV 1UXL THR J  113  UNP  P00441    ILE   113 ENGINEERED MUTATION            
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 THR 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 THR 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 THR 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 THR 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 THR 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 THR 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 THR 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 THR 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 THR 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 THR 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                      
HET     CU  A 154       2                                                       
HET     ZN  A 155       1                                                       
HET    SO4  A 156       5                                                       
HET     CU  B 154       1                                                       
HET     ZN  B 155       1                                                       
HET    SO4  B 156       5                                                       
HET     CU  C 154       1                                                       
HET     ZN  C 155       1                                                       
HET    SO4  C 157       5                                                       
HET     CU  D 154       1                                                       
HET     ZN  D 155       1                                                       
HET    SO4  D 156       5                                                       
HET     CU  E 154       1                                                       
HET     ZN  E 155       1                                                       
HET    SO4  E 156       5                                                       
HET     CU  F 154       1                                                       
HET     ZN  F 155       1                                                       
HET    SO4  F 156       5                                                       
HET     CU  G 154       1                                                       
HET     ZN  G 155       1                                                       
HET     CU  H 154       1                                                       
HET     ZN  H 155       1                                                       
HET    SO4  H 156       5                                                       
HET     CU  I 154       1                                                       
HET     ZN  I 155       1                                                       
HET    SO4  I 156       5                                                       
HET     CU  J 154       1                                                       
HET     ZN  J 155       1                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL  11   CU    10(CU 2+)                                                    
FORMUL  12   ZN    10(ZN 2+)                                                    
FORMUL  13  SO4    8(O4 S 2-)                                                   
FORMUL  39  HOH   *2447(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  GLY B   61  5                                   7    
HELIX    4   4 ASN B  131  THR B  137  1                                   7    
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 ALA E   55  GLY E   61  5                                   7    
HELIX    9   9 SER E  107  HIS E  110  5                                   4    
HELIX   10  10 GLU E  132  LYS E  136  5                                   5    
HELIX   11  11 ALA F   55  GLY F   61  5                                   7    
HELIX   12  12 SER F  107  HIS F  110  5                                   4    
HELIX   13  13 ALA G   55  GLY G   61  5                                   7    
HELIX   14  14 GLU G  133  GLY G  138  1                                   6    
HELIX   15  15 ALA H   55  GLY H   61  5                                   7    
HELIX   16  16 SER H  107  HIS H  110  5                                   4    
HELIX   17  17 GLU H  133  GLY H  138  1                                   6    
HELIX   18  18 ALA I   55  GLY I   61  5                                   7    
HELIX   19  19 GLU I  132  LYS I  136  5                                   5    
HELIX   20  20 ALA J   55  GLY J   61  5                                   7    
HELIX   21  21 GLU J  133  GLY J  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  LEU A   8 -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  ALA D 152 -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 5 ALA F  95  ASP F 101  0                                        
SHEET    2  FA 5 VAL F  29  LYS F  36 -1  O  VAL F  29   N  ASP F 101           
SHEET    3  FA 5 GLN F  15  GLN F  22 -1  O  GLN F  15   N  LYS F  36           
SHEET    4  FA 5 THR F   2  LEU F   8 -1  O  THR F   2   N  GLN F  22           
SHEET    5  FA 5 GLY F 150  ALA F 152 -1  O  GLY F 150   N  VAL F   5           
SHEET    1  FB 4 ASP F  83  ALA F  89  0                                        
SHEET    2  FB 4 GLY F  41  HIS F  48 -1  O  GLY F  41   N  ALA F  89           
SHEET    3  FB 4 THR F 116  HIS F 120 -1  O  THR F 116   N  HIS F  48           
SHEET    4  FB 4 ARG F 143  VAL F 148 -1  N  LEU F 144   O  VAL F 119           
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  GLU I  21 -1  O  GLN I  15   N  LYS I  36           
SHEET    4  IA 5 LYS I   3  LEU I   8 -1  O  ALA I   4   N  PHE I  20           
SHEET    5  IA 5 GLY I 150  ALA I 152 -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           
SSBOND   1 CYS C   57    CYS C  146                          1555   1555  2.20  
SSBOND   2 CYS D   57    CYS D  146                          1555   1555  2.10  
SSBOND   3 CYS E   57    CYS E  146                          1555   1555  2.09  
SSBOND   4 CYS F   57    CYS F  146                          1555   1555  2.16  
SSBOND   5 CYS G   57    CYS G  146                          1555   1555  2.14  
SSBOND   6 CYS J   57    CYS J  146                          1555   1555  2.12  
LINK        CU  A CU A 154                 ND1 HIS A  46     1555   1555  1.86  
LINK        CU  A CU A 154                 NE2 HIS A 120     1555   1555  2.07  
LINK        CU  A CU A 154                 NE2 HIS A  48     1555   1555  2.08  
LINK        CU  B CU A 154                 ND1 HIS A  46     1555   1555  2.33  
LINK        CU  B CU A 154                 NE2 HIS A 120     1555   1555  1.97  
LINK        CU  B CU A 154                 NE2 HIS A  48     1555   1555  2.06  
LINK        ZN    ZN A 155                 OD1 ASP A  83     1555   1555  1.97  
LINK        ZN    ZN A 155                 ND1 HIS A  63     1555   1555  1.98  
LINK        ZN    ZN A 155                 ND1 HIS A  71     1555   1555  2.02  
LINK        ZN    ZN A 155                 ND1 HIS A  80     1555   1555  2.09  
LINK        CU    CU B 154                 ND1 HIS B  46     1555   1555  2.20  
LINK        CU    CU B 154                 NE2 HIS B  48     1555   1555  1.98  
LINK        CU    CU B 154                 NE2 HIS B 120     1555   1555  1.96  
LINK        CU    CU B 154                 O1  SO4 B 156     1555   1555  2.17  
LINK        ZN    ZN B 155                 ND1 HIS B  63     1555   1555  2.09  
LINK        ZN    ZN B 155                 ND1 HIS B  80     1555   1555  1.73  
LINK        ZN    ZN B 155                 ND1 HIS B  71     1555   1555  2.08  
LINK        ZN    ZN B 155                 OD1 ASP B  83     1555   1555  1.91  
LINK        CU    CU C 154                 ND1 HIS C  46     1555   1555  2.16  
LINK        CU    CU C 154                 NE2 HIS C  48     1555   1555  1.96  
LINK        CU    CU C 154                 NE2 HIS C 120     1555   1555  1.94  
LINK        ZN    ZN C 155                 ND1 HIS C  63     1555   1555  1.99  
LINK        ZN    ZN C 155                 ND1 HIS C  71     1555   1555  2.06  
LINK        ZN    ZN C 155                 ND1 HIS C  80     1555   1555  1.99  
LINK        ZN    ZN C 155                 OD1 ASP C  83     1555   1555  1.93  
LINK        CU    CU D 154                 O1  SO4 D 156     1555   1555  1.49  
LINK        CU    CU D 154                 NE2 HIS D  48     1555   1555  1.97  
LINK        CU    CU D 154                 NE2 HIS D 120     1555   1555  1.98  
LINK        CU    CU D 154                 ND1 HIS D  46     1555   1555  2.08  
LINK        ZN    ZN D 155                 OD1 ASP D  83     1555   1555  1.61  
LINK        ZN    ZN D 155                 ND1 HIS D  63     1555   1555  2.02  
LINK        ZN    ZN D 155                 ND1 HIS D  71     1555   1555  2.09  
LINK        ZN    ZN D 155                 ND1 HIS D  80     1555   1555  1.79  
LINK        CU    CU E 154                 NE2 HIS E 120     1555   1555  2.01  
LINK        CU    CU E 154                 ND1 HIS E  46     1555   1555  2.24  
LINK        CU    CU E 154                 NE2 HIS E  48     1555   1555  2.01  
LINK        ZN    ZN E 155                 OD1 ASP E  83     1555   1555  1.95  
LINK        ZN    ZN E 155                 ND1 HIS E  80     1555   1555  1.99  
LINK        ZN    ZN E 155                 ND1 HIS E  71     1555   1555  2.07  
LINK        ZN    ZN E 155                 ND1 HIS E  63     1555   1555  2.06  
LINK        CU    CU F 154                 NE2 HIS F 120     1555   1555  1.95  
LINK        CU    CU F 154                 ND1 HIS F  46     1555   1555  2.06  
LINK        CU    CU F 154                 NE2 HIS F  48     1555   1555  2.01  
LINK        ZN    ZN F 155                 OD1 ASP F  83     1555   1555  1.93  
LINK        ZN    ZN F 155                 ND1 HIS F  80     1555   1555  2.02  
LINK        ZN    ZN F 155                 ND1 HIS F  71     1555   1555  2.04  
LINK        ZN    ZN F 155                 ND1 HIS F  63     1555   1555  1.98  
LINK        CU    CU G 154                 NE2 HIS G 120     1555   1555  1.98  
LINK        CU    CU G 154                 ND1 HIS G  46     1555   1555  2.15  
LINK        CU    CU G 154                 NE2 HIS G  48     1555   1555  1.94  
LINK        ZN    ZN G 155                 ND1 HIS G  80     1555   1555  2.01  
LINK        ZN    ZN G 155                 ND1 HIS G  71     1555   1555  2.07  
LINK        ZN    ZN G 155                 OD1 ASP G  83     1555   1555  2.01  
LINK        ZN    ZN G 155                 ND1 HIS G  63     1555   1555  1.99  
LINK        CU    CU H 154                 NE2 HIS H 120     1555   1555  1.95  
LINK        CU    CU H 154                 NE2 HIS H  48     1555   1555  1.99  
LINK        CU    CU H 154                 ND1 HIS H  46     1555   1555  2.08  
LINK        ZN    ZN H 155                 ND1 HIS H  63     1555   1555  2.02  
LINK        ZN    ZN H 155                 ND1 HIS H  71     1555   1555  2.03  
LINK        ZN    ZN H 155                 ND1 HIS H  80     1555   1555  2.02  
LINK        ZN    ZN H 155                 OD1 ASP H  83     1555   1555  1.99  
LINK        CU    CU I 154                 NE2 HIS I 120     1555   1555  1.95  
LINK        CU    CU I 154                 NE2 HIS I  48     1555   1555  1.99  
LINK        CU    CU I 154                 ND1 HIS I  46     1555   1555  2.13  
LINK        ZN    ZN I 155                 ND1 HIS I  80     1555   1555  2.00  
LINK        ZN    ZN I 155                 ND1 HIS I  71     1555   1555  2.04  
LINK        ZN    ZN I 155                 OD1 ASP I  83     1555   1555  1.95  
LINK        ZN    ZN I 155                 ND1 HIS I  63     1555   1555  2.02  
LINK        CU    CU J 154                 ND1 HIS J  46     1555   1555  2.07  
LINK        CU    CU J 154                 NE2 HIS J 120     1555   1555  2.03  
LINK        CU    CU J 154                 NE2 HIS J  48     1555   1555  1.97  
LINK        ZN    ZN J 155                 ND1 HIS J  63     1555   1555  1.97  
LINK        ZN    ZN J 155                 ND1 HIS J  71     1555   1555  2.06  
LINK        ZN    ZN J 155                 ND1 HIS J  80     1555   1555  2.04  
LINK        ZN    ZN J 155                 OD1 ASP J  83     1555   1555  1.94  
SITE     1 AC1  5 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC1  5 SO4 A 156                                                     
SITE     1 AC2  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC3 11 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC3 11 THR A 137  ARG A 143   CU A 154  HOH A2224                    
SITE     3 AC3 11 HOH A2246  HOH A2247  HOH A2248                               
SITE     1 AC4  5 HIS B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     2 AC4  5 SO4 B 156                                                     
SITE     1 AC5  4 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     1 AC6  9 HIS B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     2 AC6  9 THR B 137  ARG B 143   CU B 154  HOH B2177                    
SITE     3 AC6  9 HOH B2197                                                     
SITE     1 AC7  5 HIS C  46  HIS C  48  HIS C  63  HIS C 120                    
SITE     2 AC7  5 SO4 C 157                                                     
SITE     1 AC8  4 HIS C  63  HIS C  71  HIS C  80  ASP C  83                    
SITE     1 AC9 11 HIS C  48  HIS C  63  HIS C 120  THR C 137                    
SITE     2 AC9 11 ARG C 143   CU C 154  HOH C2242  HOH C2259                    
SITE     3 AC9 11 HOH C2261  HOH C2262  HOH C2263                               
SITE     1 BC1  5 HIS D  46  HIS D  48  HIS D  63  HIS D 120                    
SITE     2 BC1  5 SO4 D 156                                                     
SITE     1 BC2  4 HIS D  63  HIS D  71  HIS D  80  ASP D  83                    
SITE     1 BC3 10 HIS D  46  HIS D  48  HIS D  63  HIS D 120                    
SITE     2 BC3 10 THR D 137  ARG D 143   CU D 154  HOH D2176                    
SITE     3 BC3 10 HOH D2177  HOH D2178                                          
SITE     1 BC4  5 HIS E  46  HIS E  48  HIS E  63  HIS E 120                    
SITE     2 BC4  5 SO4 E 156                                                     
SITE     1 BC5  4 HIS E  63  HIS E  71  HIS E  80  ASP E  83                    
SITE     1 BC6 10 HIS E  48  HIS E  63  HIS E 120  THR E 137                    
SITE     2 BC6 10 ARG E 143   CU E 154  HOH E2158  HOH E2177                    
SITE     3 BC6 10 HOH E2178  HOH E2179                                          
SITE     1 BC7  5 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     2 BC7  5 SO4 F 156                                                     
SITE     1 BC8  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 BC9 11 HIS F  48  HIS F  63  HIS F 120  THR F 137                    
SITE     2 BC9 11 ARG F 143   CU F 154  HOH F2281  HOH F2301                    
SITE     3 BC9 11 HOH F2302  HOH F2303  HOH F2304                               
SITE     1 CC1  4 HIS G  46  HIS G  48  HIS G  63  HIS G 120                    
SITE     1 CC2  4 HIS G  63  HIS G  71  HIS G  80  ASP G  83                    
SITE     1 CC3  5 HIS H  46  HIS H  48  HIS H  63  HIS H 120                    
SITE     2 CC3  5 SO4 H 156                                                     
SITE     1 CC4  4 HIS H  63  HIS H  71  HIS H  80  ASP H  83                    
SITE     1 CC5 10 HIS H  48  HIS H  63  HIS H 120  THR H 137                    
SITE     2 CC5 10 ARG H 143   CU H 154  HOH H2291  HOH H2313                    
SITE     3 CC5 10 HOH H2315  HOH H2316                                          
SITE     1 CC6  5 HIS I  46  HIS I  48  HIS I  63  HIS I 120                    
SITE     2 CC6  5 SO4 I 156                                                     
SITE     1 CC7  4 HIS I  63  HIS I  71  HIS I  80  ASP I  83                    
SITE     1 CC8  9 HIS I  48  HIS I  63  HIS I 120  THR I 137                    
SITE     2 CC8  9 ARG I 143   CU I 154  HOH I2244  HOH I2245                    
SITE     3 CC8  9 HOH I2246                                                     
SITE     1 CC9  4 HIS J  46  HIS J  48  HIS J  63  HIS J 120                    
SITE     1 DC1  4 HIS J  63  HIS J  71  HIS J  80  ASP J  83                    
CRYST1  166.042  203.546  144.021  90.00  90.00  90.00 C 2 2 21     80          
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      0.006022  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004913  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006943        0.00000                         
MTRIX1   1 -0.989340 -0.016840 -0.144630      278.68262    1                    
MTRIX2   1 -0.012840 -0.979330  0.201840      114.40730    1                    
MTRIX3   1 -0.145040  0.201550  0.968680        8.76991    1                    
MTRIX1   2 -0.462140  0.886480 -0.024130      180.61057    1                    
MTRIX2   2 -0.886530 -0.462510 -0.012380      254.55972    1                    
MTRIX3   2 -0.022140  0.015670  0.999630        1.88276    1                    
MTRIX1   3 -0.529560 -0.847210  0.042480      313.56665    1                    
MTRIX2   3  0.848200 -0.528190  0.039790      -32.03505    1                    
MTRIX3   3 -0.011270  0.057100  0.998300       -2.08507    1                    
MTRIX1   4 -0.999350  0.031630  0.017320      296.06339    1                    
MTRIX2   4 -0.034330 -0.981480 -0.188480      220.87741    1                    
MTRIX3   4  0.011040 -0.188950  0.981920       10.09263    1                    
MTRIX1   5  0.486460 -0.873600  0.013180      115.38712    1                    
MTRIX2   5  0.873660  0.486230 -0.017430      -46.33193    1                    
MTRIX3   5  0.008820  0.020000  0.999760       -8.33963    1                    
MTRIX1   6  0.463300 -0.856100  0.229000      150.19960    1                    
MTRIX2   6  0.875950  0.481580  0.028180      -45.67095    1                    
MTRIX3   6 -0.134410  0.187540  0.973020        8.04293    1                    
MTRIX1   7  0.529420  0.845820 -0.065620      150.19960    1                    
MTRIX2   7 -0.835950  0.506940 -0.210230      -45.67095    1                    
MTRIX3   7 -0.144550  0.166160  0.975450        8.04293    1                    
MTRIX1   8  0.988090 -0.021530  0.152370       22.51875    1                    
MTRIX2   8  0.076360  0.928240 -0.364050       96.23938    1                    
MTRIX3   8 -0.133600  0.371350  0.918830       -1.63597    1                    
MTRIX1   9 -0.453980  0.859880 -0.233490      148.29253    1                    
MTRIX2   9 -0.865690 -0.487700 -0.112870      255.53433    1                    
MTRIX3   9 -0.210920  0.150890  0.965790       15.07458    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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