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Database: PDB
Entry: 1UXM
LinkDB: 1UXM
Original site: 1UXM 
HEADER    OXIDOREDUCTASE                          26-FEB-04   1UXM              
TITLE     A4V 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, K, L;                           
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 1UXM    1       VERSN                                    
REVDAT   3   24-FEB-09 1UXM    1       VERSN                                    
REVDAT   2   05-JAN-05 1UXM    1       JRNL                                     
REVDAT   1   19-MAR-04 1UXM    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.    1.9  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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 225403                         
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) : 0.229                           
REMARK   3   R VALUE            (WORKING SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 11944                           
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 13965                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2920                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 734                          
REMARK   3   BIN FREE R VALUE                    : 0.3080                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13344                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 1096                                    
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) : 18.92                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.40000                                             
REMARK   3    B22 (A**2) : 3.24000                                              
REMARK   3    B33 (A**2) : -2.19000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.35000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.132         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.124         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.100         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.366         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13572 ; 0.016 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18312 ; 1.786 ; 1.945       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1824 ; 4.792 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2331 ;20.379 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2028 ; 0.129 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10344 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  7656 ; 0.319 ; 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):  2194 ; 0.242 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    42 ; 0.130 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   129 ; 0.402 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    44 ; 0.355 ; 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):  8940 ; 0.902 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14220 ; 1.556 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4632 ; 2.637 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4092 ; 4.200 ; 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  : 12                                         
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):   0.0420 -29.1190  -1.8830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1352 T22:   0.0571                                     
REMARK   3      T33:   0.1357 T12:   0.0089                                     
REMARK   3      T13:  -0.0208 T23:   0.0093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6422 L22:   0.8793                                     
REMARK   3      L33:   1.2272 L12:  -0.1822                                     
REMARK   3      L13:   0.4856 L23:  -0.1071                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0486 S12:   0.1913 S13:   0.0020                       
REMARK   3      S21:  -0.0367 S22:  -0.0173 S23:   0.0139                       
REMARK   3      S31:  -0.0323 S32:  -0.0286 S33:  -0.0313                       
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):  23.9950 -29.3360  12.3570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1540 T22:   0.0484                                     
REMARK   3      T33:   0.1429 T12:   0.0006                                     
REMARK   3      T13:  -0.0275 T23:   0.0112                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2851 L22:   0.6703                                     
REMARK   3      L33:   1.6410 L12:   0.1182                                     
REMARK   3      L13:   0.9340 L23:  -0.0840                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0469 S12:   0.1456 S13:   0.0559                       
REMARK   3      S21:   0.0832 S22:  -0.0072 S23:   0.0002                       
REMARK   3      S31:  -0.0972 S32:   0.1248 S33:   0.0541                       
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):   3.9560 -67.4660   4.1650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1523 T22:   0.0268                                     
REMARK   3      T33:   0.1345 T12:  -0.0207                                     
REMARK   3      T13:  -0.0187 T23:   0.0030                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9315 L22:   0.7242                                     
REMARK   3      L33:   1.4761 L12:   0.1384                                     
REMARK   3      L13:   0.8463 L23:   0.0849                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0433 S12:   0.0414 S13:  -0.0082                       
REMARK   3      S21:   0.0183 S22:   0.0245 S23:   0.0547                       
REMARK   3      S31:   0.0119 S32:  -0.0101 S33:   0.0188                       
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):  28.2270 -67.0530  17.8000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1394 T22:   0.0314                                     
REMARK   3      T33:   0.1471 T12:   0.0022                                     
REMARK   3      T13:  -0.0134 T23:   0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6553 L22:   0.6276                                     
REMARK   3      L33:   1.4533 L12:  -0.0933                                     
REMARK   3      L13:   0.6461 L23:   0.0209                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0354 S12:  -0.0810 S13:  -0.1196                       
REMARK   3      S21:  -0.0238 S22:   0.0123 S23:  -0.0718                       
REMARK   3      S31:   0.0203 S32:   0.0274 S33:   0.0232                       
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):  11.9530   4.9340  51.6450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1563 T22:   0.1779                                     
REMARK   3      T33:   0.1118 T12:  -0.0096                                     
REMARK   3      T13:  -0.0159 T23:   0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4518 L22:   0.6762                                     
REMARK   3      L33:   6.4102 L12:  -0.1045                                     
REMARK   3      L13:   0.2928 L23:  -0.1270                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0619 S12:  -0.1033 S13:  -0.0946                       
REMARK   3      S21:   0.0118 S22:   0.0238 S23:  -0.0477                       
REMARK   3      S31:  -0.0218 S32:  -0.1830 S33:  -0.0857                       
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):  11.6280   4.6980  23.7830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1590 T22:   0.1240                                     
REMARK   3      T33:   0.1123 T12:   0.0235                                     
REMARK   3      T13:  -0.0250 T23:  -0.0174                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5595 L22:   0.3623                                     
REMARK   3      L33:  10.7670 L12:  -0.2433                                     
REMARK   3      L13:   1.3867 L23:  -0.2241                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1365 S12:   0.0930 S13:  -0.0444                       
REMARK   3      S21:  -0.0130 S22:  -0.0199 S23:   0.0792                       
REMARK   3      S31:   0.0595 S32:   0.3076 S33:  -0.1166                       
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):  28.1950   5.0700  -3.8850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1689 T22:   0.2797                                     
REMARK   3      T33:   0.1624 T12:   0.0347                                     
REMARK   3      T13:   0.0197 T23:   0.0265                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8687 L22:   0.9088                                     
REMARK   3      L33:   1.8924 L12:   0.3960                                     
REMARK   3      L13:  -1.0954 L23:  -0.3765                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1190 S12:  -0.3729 S13:   0.0238                       
REMARK   3      S21:  -0.0051 S22:   0.0136 S23:  -0.0836                       
REMARK   3      S31:   0.1409 S32:   0.3979 S33:   0.1054                       
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):  52.2150   5.7530 -18.1260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1721 T22:   0.3176                                     
REMARK   3      T33:   0.2275 T12:  -0.0194                                     
REMARK   3      T13:   0.0215 T23:   0.0224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0243 L22:  -0.2740                                     
REMARK   3      L33:   1.3593 L12:   0.5342                                     
REMARK   3      L13:  -0.7296 L23:   0.0810                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0699 S12:   0.4753 S13:  -0.1156                       
REMARK   3      S21:   0.0270 S22:   0.0512 S23:  -0.0854                       
REMARK   3      S31:   0.0249 S32:  -0.1289 S33:   0.0187                       
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 :   I     1        I   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  56.3230  44.4450 -12.2030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0910 T22:   0.3930                                     
REMARK   3      T33:   0.1674 T12:  -0.0054                                     
REMARK   3      T13:   0.0082 T23:  -0.0224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4516 L22:   0.6680                                     
REMARK   3      L33:   2.4921 L12:   0.4821                                     
REMARK   3      L13:  -0.9662 L23:  -0.1770                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1469 S12:   0.8672 S13:   0.0212                       
REMARK   3      S21:   0.0482 S22:   0.1092 S23:  -0.0436                       
REMARK   3      S31:  -0.0167 S32:  -0.0035 S33:   0.0377                       
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 :   J     1        J   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.0080  44.2900   1.5150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0953 T22:   0.2355                                     
REMARK   3      T33:   0.1634 T12:   0.0138                                     
REMARK   3      T13:  -0.0068 T23:  -0.0421                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.4031 L22:   0.3809                                     
REMARK   3      L33:   2.1133 L12:   0.2749                                     
REMARK   3      L13:  -0.3944 L23:  -0.0468                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0055 S12:  -0.2589 S13:   0.2263                       
REMARK   3      S21:  -0.0684 S22:  -0.0234 S23:   0.0215                       
REMARK   3      S31:   0.0397 S32:  -0.1138 S33:   0.0289                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K     1        K   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.8990  43.0440  57.4740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1922 T22:   0.4020                                     
REMARK   3      T33:   0.1407 T12:   0.0125                                     
REMARK   3      T13:  -0.0264 T23:   0.0211                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0991 L22:   0.5256                                     
REMARK   3      L33:  13.3599 L12:  -0.3720                                     
REMARK   3      L13:   1.9363 L23:  -1.1642                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0522 S12:  -0.1596 S13:   0.0204                       
REMARK   3      S21:   0.0534 S22:   0.1924 S23:   0.0043                       
REMARK   3      S31:  -0.1363 S32:  -1.6750 S33:  -0.1402                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     1        L   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.3350  43.6770  29.6130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1646 T22:   0.3025                                     
REMARK   3      T33:   0.1354 T12:  -0.0295                                     
REMARK   3      T13:  -0.0203 T23:  -0.0117                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6275 L22:   0.5399                                     
REMARK   3      L33:   6.5942 L12:  -0.2185                                     
REMARK   3      L13:   2.6414 L23:  -0.6139                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0699 S12:  -0.0880 S13:  -0.0309                       
REMARK   3      S21:   0.0794 S22:   0.0065 S23:  -0.0874                       
REMARK   3      S31:  -0.0135 S32:  -0.4014 S33:  -0.0765                       
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 SOME ATOMS THAT HAVE          
REMARK   3  BEEN REFINED WITH AN OCCUPANCY OF 0.00                              
REMARK   4                                                                      
REMARK   4 1UXM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-FEB-04.                  
REMARK 100 THE PDBE ID CODE IS EBI-14650.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 246133                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
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     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
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  (%): 70                                         
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.2                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CA ACET,                           
REMARK 280  15% PEG 2000, 0.1 M TRIS PH 8.0                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       72.79100            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 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: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 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: E, 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:  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: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 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: I, J                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 BIOMOLECULE:  6                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 ALA 4 TO VAL 4 IN CHAINS A TO L                  
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY)             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES;                                   
REMARK 475 C=CHAIN IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE)         
REMARK 475   M RES C SSEQI                                                      
REMARK 475     LEU K   38                                                       
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     ALA A   1     N   CA   CB                                        
REMARK 480     ASN A  26   ND2                                                  
REMARK 480     LYS A  30    CD   CE   NZ                                        
REMARK 480     LYS A 128    NZ                                                  
REMARK 480     LYS B 122    NZ                                                  
REMARK 480     LYS C  75    CE   NZ                                             
REMARK 480     LYS C 122    CE   NZ                                             
REMARK 480     ALA E   1     N   CA   CB                                        
REMARK 480     LYS E  23    CE   NZ                                             
REMARK 480     LYS E  70    CG   CD   CE   NZ                                   
REMARK 480     ALA F   1    CA   CB                                             
REMARK 480     LYS F   9    CD   CE   NZ                                        
REMARK 480     LYS F  23    CE   NZ                                             
REMARK 480     LYS F  70    CE   NZ                                             
REMARK 480     LYS F  91    CD   CE   NZ                                        
REMARK 480     GLU F 132    CD  OE1  OE2                                        
REMARK 480     GLN G  15    CD  OE1  NE2                                        
REMARK 480     LYS G  23    CE   NZ                                             
REMARK 480     ASN G  26    CG  OD1  ND2                                        
REMARK 480     LYS G  30    CD   CE   NZ                                        
REMARK 480     LYS G  75    CD   CE   NZ                                        
REMARK 480     LYS G  91    CD   CE   NZ                                        
REMARK 480     GLN G 153    CG   CD  OE1  NE2                                   
REMARK 480     ALA H   1     N   CA   CB                                        
REMARK 480     LYS H   3    CE   NZ                                             
REMARK 480     LYS H   9    CE   NZ                                             
REMARK 480     VAL H  14   CG1  CG2                                             
REMARK 480     GLN H  22    CB   CG   CD  OE1  NE2                              
REMARK 480     LYS H  23     O   CE   NZ                                        
REMARK 480     GLU H  24    CD  OE1  OE2                                        
REMARK 480     SER H  25     O                                                  
REMARK 480     LYS H  30    CG   CD   CE   NZ                                   
REMARK 480     LYS H  36    CG   CD   CE   NZ                                   
REMARK 480     LYS H  70    CG   CD   CE   NZ                                   
REMARK 480     LYS H  75    CD   CE   NZ                                        
REMARK 480     GLU H  77    CB   CG   CD  OE1  OE2                              
REMARK 480     LYS H  91    CB   CG   CD   CE   NZ                              
REMARK 480     VAL H  94   CG2                                                  
REMARK 480     GLU H 100    CG   CD  OE1  OE2                                   
REMARK 480     SER H 107    CB   OG                                             
REMARK 480     HIS H 110    CB   CG  ND1  CD2  CE1  NE2                         
REMARK 480     THR H 135   CG2                                                  
REMARK 480     ALA I   1     N   CA   CB                                        
REMARK 480     LYS I   3    CE   NZ                                             
REMARK 480     LYS I  23    CE   NZ                                             
REMARK 480     GLU I  24    CG   CD  OE1  OE2                                   
REMARK 480     SER I  25     O                                                  
REMARK 480     ASN I  26   OD1  ND2                                             
REMARK 480     LYS I  70    CD   CE   NZ                                        
REMARK 480     LYS I  75    CD   CE   NZ                                        
REMARK 480     LYS I  91    CE   NZ                                             
REMARK 480     LYS I 122    CE   NZ                                             
REMARK 480     GLU I 132    CB   CG   CD  OE1  OE2                              
REMARK 480     ALA J   1     N   CA   CB                                        
REMARK 480     LYS J   3    CG   CD   CE   NZ                                   
REMARK 480     LYS J  23    CD   CE   NZ                                        
REMARK 480     ASN J  26   OD1  ND2                                             
REMARK 480     LYS J  36    CD   CE   NZ                                        
REMARK 480     LYS J  70    CD   CE   NZ                                        
REMARK 480     LYS J  91    CG   CD   CE   NZ                                   
REMARK 480     ALA K   1     N   CA   CB                                        
REMARK 480     THR K   2    CB  OG1  CG2                                        
REMARK 480     LYS K   3    CE   NZ                                             
REMARK 480     LYS K   9    CG   CD   CE   NZ                                   
REMARK 480     GLN K  15    CG   CD  OE1  NE2                                   
REMARK 480     GLU K  24    CG   CD  OE1  OE2                                   
REMARK 480     SER K  25     O                                                  
REMARK 480     ASN K  26    CG  OD1  ND2                                        
REMARK 480     LYS K  30    CD   CE   NZ                                        
REMARK 480     LYS K  36    CB   CG   CD   CE   NZ                              
REMARK 480     THR K  39     N                                                  
REMARK 480     GLU K  40    CG   CD  OE1  OE2                                   
REMARK 480     LYS K  75    CE   NZ                                             
REMARK 480     GLU K  77    CG   CD  OE1  OE2                                   
REMARK 480     LYS K  91    CB   CG   CD   CE   NZ                              
REMARK 480     ASP K  92     O   CG  OD1  OD2                                   
REMARK 480     VAL K  94   CG1  CG2                                             
REMARK 480     SER K  98    CB   OG                                             
REMARK 480     SER K 102    OG                                                  
REMARK 480     LYS K 122    CE   NZ                                             
REMARK 480     ALA L   1     N   CA   CB                                        
REMARK 480     LYS L   3    CD   CE   NZ                                        
REMARK 480     ASP L  11   OD1  OD2                                             
REMARK 480     LYS L  23    CD   CE   NZ                                        
REMARK 480     SER L  25    OG                                                  
REMARK 480     LYS L  91    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  ASP A    96     O    HOH A  2083              2.16            
REMARK 500   O    GLN A   153     O    HOH A  2135              2.19            
REMARK 500   OD1  ASP B    96     O    HOH B  2089              2.01            
REMARK 500   O    GLU F   132     OG1  THR F   135              2.19            
REMARK 500   SG   CYS G     6     O    HOH G  2076              2.10            
REMARK 500   O    ASN G    86     O    HOH G  2039              2.13            
REMARK 500   OG   SER G   105     O    SER G   107              2.15            
REMARK 500   O    CYS G   111     O    HOH G  2054              2.14            
REMARK 500   NE2  HIS I   120     O    HOH I  2031              2.11            
REMARK 500   O    GLU I   132     CG2  THR I   135              2.06            
REMARK 500   N    ASP J    11     O    HOH J  2003              2.19            
REMARK 500   NE   ARG K    69     O    HOH K  2026              2.11            
REMARK 500   OD1  ASP K    90     N    ASP K    92              2.07            
REMARK 500   N    GLN K   153     O    HOH K  2072              2.15            
REMARK 500   O    GLU L   100     O    HOH L  2038              2.19            
REMARK 500   O    HOH A  2064     O    HOH A  2072              2.15            
REMARK 500   O    HOH B  2023     O    HOH F  2048              2.04            
REMARK 500   O    HOH C  2026     O    HOH C  2032              2.20            
REMARK 500   O    HOH G  2015     O    HOH G  2035              2.17            
REMARK 500   O    HOH I  2020     O    HOH I  2021              2.15            
REMARK 500   O    HOH J  2014     O    HOH J  2036              1.77            
REMARK 500   O    HOH K  2063     O    HOH K  2064              2.19            
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   OE2  GLU A    77     N    ASP C   109     1555     2.04            
REMARK 500   CG   ASN D    26     NE   ARG J    69     1545     2.03            
REMARK 500   ND2  ASN D    26     NH2  ARG J    69     1545     1.95            
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    ASN J  53   CB    ASN J  53   CG      0.141                       
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    THR A   2   N   -  CA  -  C   ANGL. DEV. = -17.2 DEGREES          
REMARK 500    GLY A  27   C   -  N   -  CA  ANGL. DEV. =  13.2 DEGREES          
REMARK 500    ARG A  79   CD  -  NE  -  CZ  ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ARG A  79   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG A  79   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500    ASP A 101   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP B  11   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG B  79   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG B  79   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ASP B 101   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG C  79   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG C  79   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    ASP D  96   CB  -  CG  -  OD2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ARG D 143   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG E  79   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG E  79   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    CYS F  57   CA  -  CB  -  SG  ANGL. DEV. =  -7.1 DEGREES          
REMARK 500    ARG F  79   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG F  79   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    ASP G 101   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    VAL H  87   N   -  CA  -  C   ANGL. DEV. = -17.8 DEGREES          
REMARK 500    ASP I 101   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP I 124   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP J  83   CB  -  CG  -  OD1 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ASP K  90   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP L  11   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP L 101   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 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    THR A   2      -51.97   -127.00                                   
REMARK 500    ASN A  26     -102.80     -3.48                                   
REMARK 500    ASN A  65       63.95   -150.79                                   
REMARK 500    THR B   2      -53.78   -125.57                                   
REMARK 500    ASN B  26      -46.23    177.05                                   
REMARK 500    ASN C  26       19.01     50.96                                   
REMARK 500    ASN D  26      -23.03     82.24                                   
REMARK 500    ARG D 115     -167.07   -103.04                                   
REMARK 500    SER E  25       90.63    -65.68                                   
REMARK 500    ASN E  26      -34.74    135.11                                   
REMARK 500    THR F   2      -53.66   -137.95                                   
REMARK 500    ASN F  26       -1.35     69.38                                   
REMARK 500    ALA F  55       51.08   -117.45                                   
REMARK 500    SER F  68       72.10     46.02                                   
REMARK 500    ASP F  90     -176.14    -68.22                                   
REMARK 500    ARG F 115     -168.74   -102.61                                   
REMARK 500    PRO G  13      -71.51    -42.14                                   
REMARK 500    SER G  68       76.77     43.63                                   
REMARK 500    GLU G  77      -70.22    -60.90                                   
REMARK 500    GLU G  78       89.09    -67.66                                   
REMARK 500    SER G  98      114.71   -164.85                                   
REMARK 500    ARG G 115     -161.49   -106.75                                   
REMARK 500    THR H   2      -67.77   -107.34                                   
REMARK 500    LYS H  23      -23.56    -32.80                                   
REMARK 500    SER H  25      177.34    -51.89                                   
REMARK 500    ASN H  26      -22.20     44.34                                   
REMARK 500    ASP H  90     -166.27    -79.83                                   
REMARK 500    CYS H 111      131.74    -36.71                                   
REMARK 500    ASN I  26       43.22    -86.11                                   
REMARK 500    SER I  98      106.99   -160.33                                   
REMARK 500    LEU I 126       19.67     54.33                                   
REMARK 500    THR J   2      -48.46   -142.09                                   
REMARK 500    SER J  98      104.46   -162.62                                   
REMARK 500    ASN K  26       41.06   -104.69                                   
REMARK 500    PHE K  64      108.63    -59.73                                   
REMARK 500    ASP L  11       11.03    -68.93                                   
REMARK 500    SER L  98      106.41   -164.45                                   
REMARK 500    HIS L 110       33.30    -94.98                                   
REMARK 500    ARG L 115     -161.06   -101.72                                   
REMARK 500    SER L 142      151.83    -41.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL B  31        23.6      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  48   NE2 129.1                                              
REMARK 620 3 HIS A 120   NE2  95.5 106.8                                        
REMARK 620 4 HOH A2060   O   117.7 107.6  90.0                                  
REMARK 620 5 HIS A  63   NE2  81.6  99.7 147.4  63.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  48   NE2                                                    
REMARK 620 2 HOH B2062   O   104.0                                              
REMARK 620 3 HIS B  46   ND1 131.4 122.6                                        
REMARK 620 4 HIS B 120   NE2 106.6  79.4  95.7                                  
REMARK 620 5 HIS B  63   NE2  98.7  76.7  80.6 148.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  46   ND1                                                    
REMARK 620 2 HIS C  48   NE2 132.7                                              
REMARK 620 3 HIS C  63   NE2  83.4  96.5                                        
REMARK 620 4 HIS C 120   NE2  95.9 105.5 150.0                                  
REMARK 620 5 HOH C2063   O   129.6  94.7  73.6  84.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU D 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  63   NE2                                                    
REMARK 620 2 HIS D  48   NE2  97.8                                              
REMARK 620 3 HIS D 120   NE2 150.2 107.6                                        
REMARK 620 4 HOH D2063   O    75.8 102.1  83.8                                  
REMARK 620 5 HIS D  46   ND1  80.4 130.5  94.0 124.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU E 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH E2032   O                                                      
REMARK 620 2 HIS E  46   ND1 126.8                                              
REMARK 620 3 HIS E  48   NE2  98.0 132.7                                        
REMARK 620 4 HIS E  63   NE2  74.9  81.4  99.1                                  
REMARK 620 5 HIS E 120   NE2  90.6  90.8 104.3 154.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU F 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  63   NE2                                                    
REMARK 620 2 HIS F  46   ND1  82.0                                              
REMARK 620 3 HIS F  48   NE2  94.7 127.4                                        
REMARK 620 4 HIS F 120   NE2 150.7  89.9 112.3                                  
REMARK 620 5 HOH F2018   O    72.8 126.6 101.4  90.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU G 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH G2030   O                                                      
REMARK 620 2 HIS G  46   ND1 126.6                                              
REMARK 620 3 HIS G  48   NE2  99.8 131.1                                        
REMARK 620 4 HIS G  63   NE2  73.9  81.3 100.0                                  
REMARK 620 5 HIS G 120   NE2  88.5  92.5 104.7 151.8                            
REMARK 620 N                    1     2     3     4                             
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 130.4                                              
REMARK 620 3 HIS H  63   NE2  85.4  93.3                                        
REMARK 620 4 HIS H 120   NE2 100.5 101.5 154.0                                  
REMARK 620 5 HOH H2065   O   137.2  90.5  79.1  79.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU I 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I 120   NE2                                                    
REMARK 620 2 HOH I2031   O    56.7                                              
REMARK 620 3 HIS I  46   ND1  88.4 127.4                                        
REMARK 620 4 HIS I  48   NE2 100.4  93.1 134.4                                  
REMARK 620 5 HIS I  63   NE2 137.0  86.1 100.4 102.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU J 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS J 120   NE2                                                    
REMARK 620 2 HIS J  46   ND1  96.4                                              
REMARK 620 3 HIS J  63   NE2 149.4  81.5                                        
REMARK 620 4 HOH J2030   O    81.6 128.8  76.4                                  
REMARK 620 5 HIS J  48   NE2 108.1 129.6  96.1  98.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU K 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS K  46   ND1                                                    
REMARK 620 2 HIS K 120   NE2  92.1                                              
REMARK 620 3 HIS K  48   NE2 131.3 104.6                                        
REMARK 620 4 HOH K2021   O   125.5  83.7 102.0                                  
REMARK 620 5 HIS K  63   NE2  80.3 153.6  99.3  80.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU L 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS L  48   NE2                                                    
REMARK 620 2 HOH L2023   O    94.9                                              
REMARK 620 3 HIS L  63   NE2 101.7  65.0                                        
REMARK 620 4 HIS L 120   NE2 102.2  87.8 145.0                                  
REMARK 620 5 HIS L  46   ND1 137.3 126.2  87.7  91.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  71   ND1                                                    
REMARK 620 2 ASP A  83   OD1  99.6                                              
REMARK 620 3 HIS A  63   ND1 106.7 103.9                                        
REMARK 620 4 HIS A  80   ND1 121.9 107.4 114.8                                  
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  71   ND1 109.5                                              
REMARK 620 3 ASP B  83   OD1 106.0  89.9                                        
REMARK 620 4 HIS B  80   ND1 113.5 124.2 109.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  71   ND1                                                    
REMARK 620 2 ASP C  83   OD1  95.7                                              
REMARK 620 3 HIS C  80   ND1 121.9 111.7                                        
REMARK 620 4 HIS C  63   ND1 109.1 104.1 111.9                                  
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  63   ND1                                                    
REMARK 620 2 HIS D  80   ND1 113.4                                              
REMARK 620 3 ASP D  83   OD1 102.0 110.2                                        
REMARK 620 4 HIS D  71   ND1 108.9 121.7  98.0                                  
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  80   ND1                                                    
REMARK 620 2 HIS E  63   ND1 113.1                                              
REMARK 620 3 HIS E  71   ND1 124.3 103.9                                        
REMARK 620 4 ASP E  83   OD1 108.2 104.7 100.5                                  
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  71   ND1                                                    
REMARK 620 2 ASP F  83   OD1  92.5                                              
REMARK 620 3 HIS F  63   ND1 107.7 115.5                                        
REMARK 620 4 HIS F  80   ND1 127.0 104.4 109.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G  63   ND1                                                    
REMARK 620 2 HIS G  71   ND1 109.8                                              
REMARK 620 3 HIS G  80   ND1 111.0 124.0                                        
REMARK 620 4 ASP G  83   OD1  98.8  96.8 112.8                                  
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  63   ND1                                                    
REMARK 620 2 HIS H  71   ND1 105.7                                              
REMARK 620 3 HIS H  80   ND1 118.4 117.6                                        
REMARK 620 4 ASP H  83   OD1 114.0  96.8 102.3                                  
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  63   ND1                                                    
REMARK 620 2 HIS I  71   ND1  98.6                                              
REMARK 620 3 HIS I  80   ND1 115.1 125.0                                        
REMARK 620 4 ASP I  83   OD1 115.7 107.9  95.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN J 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS J  63   ND1                                                    
REMARK 620 2 HIS J  71   ND1 102.6                                              
REMARK 620 3 HIS J  80   ND1 118.4 130.8                                        
REMARK 620 4 ASP J  83   OD1 111.2 108.7  81.9                                  
REMARK 620 5 ASP J  83   OD2 152.1  72.2  81.9  49.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN K 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP K  83   OD1                                                    
REMARK 620 2 HIS K  63   ND1 109.2                                              
REMARK 620 3 HIS K  71   ND1  94.0 109.1                                        
REMARK 620 4 HIS K  80   ND1 108.0 112.8 121.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN L 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS L  71   ND1                                                    
REMARK 620 2 HIS L  63   ND1 105.3                                              
REMARK 620 3 HIS L  80   ND1 109.1 126.0                                        
REMARK 620 4 ASP L  83   OD1  95.4 106.2 110.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AA DA GA HA KA LA" IN EACH CHAIN ON         
REMARK 700 SHEET RECORDS BELOW IS ACTUALLY AN  9-STRANDED BARREL                
REMARK 700 THIS IS REPRESENTED BY A 10-STRANDED SHEET IN WHICH THE              
REMARK 700 FIRST AND LAST STRANDS ARE IDENTICAL.                                
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU A 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU B 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU C 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN C 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU D 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN D 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU E 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN E 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU F 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN F 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU G 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN G 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU H 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN H 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU I 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN I 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU J 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN J 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU K 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN K 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU L 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN L 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: 1UXL   RELATED DB: PDB                                   
REMARK 900  I113T 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  1UXM A    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1UXM B    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1UXM C    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1UXM D    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1UXM E    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1UXM F    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1UXM G    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1UXM H    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1UXM I    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1UXM J    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1UXM K    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1UXM L    1   153  UNP    P00441   SODC_HUMAN       1    153             
SEQADV 1UXM VAL A    4  UNP  P00441    ALA     4 ENGINEERED MUTATION            
SEQADV 1UXM VAL B    4  UNP  P00441    ALA     4 ENGINEERED MUTATION            
SEQADV 1UXM VAL C    4  UNP  P00441    ALA     4 ENGINEERED MUTATION            
SEQADV 1UXM VAL D    4  UNP  P00441    ALA     4 ENGINEERED MUTATION            
SEQADV 1UXM VAL E    4  UNP  P00441    ALA     4 ENGINEERED MUTATION            
SEQADV 1UXM VAL F    4  UNP  P00441    ALA     4 ENGINEERED MUTATION            
SEQADV 1UXM VAL G    4  UNP  P00441    ALA     4 ENGINEERED MUTATION            
SEQADV 1UXM VAL H    4  UNP  P00441    ALA     4 ENGINEERED MUTATION            
SEQADV 1UXM VAL I    4  UNP  P00441    ALA     4 ENGINEERED MUTATION            
SEQADV 1UXM VAL J    4  UNP  P00441    ALA     4 ENGINEERED MUTATION            
SEQADV 1UXM VAL K    4  UNP  P00441    ALA     4 ENGINEERED MUTATION            
SEQADV 1UXM VAL L    4  UNP  P00441    ALA     4 ENGINEERED MUTATION            
SEQRES   1 A  153  ALA THR LYS VAL VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 A  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 A  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 A  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 A  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 A  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 A  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 A  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 A  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 A  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 A  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 A  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 B  153  ALA THR LYS VAL VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 B  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 B  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 B  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 B  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 B  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 B  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 B  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 B  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 B  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 B  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 B  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 C  153  ALA THR LYS VAL VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 C  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 C  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 C  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 C  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 C  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 C  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 C  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 C  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 C  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 C  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 C  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 D  153  ALA THR LYS VAL VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 D  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 D  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 D  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 D  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 D  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 D  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 D  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 D  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 D  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 D  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 D  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 E  153  ALA THR LYS VAL VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 E  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 E  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 E  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 E  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 E  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 E  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 E  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 E  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 E  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 E  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 E  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 F  153  ALA THR LYS VAL VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 F  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 F  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 F  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 F  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 F  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 F  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 F  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 F  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 F  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 F  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 F  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 G  153  ALA THR LYS VAL VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 G  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 G  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 G  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 G  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 G  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 G  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 G  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 G  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 G  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 G  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 G  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 H  153  ALA THR LYS VAL VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 H  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 H  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 H  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 H  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 H  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 H  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 H  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 H  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 H  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 H  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 H  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 I  153  ALA THR LYS VAL VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 I  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 I  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 I  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 I  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 I  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 I  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 I  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 I  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 I  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 I  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 I  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 J  153  ALA THR LYS VAL VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 J  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 J  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 J  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 J  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 J  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 J  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 J  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 J  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 J  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 J  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 J  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 K  153  ALA THR LYS VAL VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 K  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 K  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 K  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 K  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 K  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 K  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 K  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 K  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 K  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 K  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 K  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 L  153  ALA THR LYS VAL VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 L  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 L  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 L  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 L  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 L  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 L  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 L  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 L  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 L  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 L  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 L  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
HET     CU  A 154       1                                                       
HET     ZN  A 155       1                                                       
HET     CU  B 154       1                                                       
HET     ZN  B 155       1                                                       
HET     CU  C 154       1                                                       
HET     ZN  C 155       1                                                       
HET     CU  D 154       1                                                       
HET     ZN  D 155       1                                                       
HET     CU  E 154       1                                                       
HET     ZN  E 155       1                                                       
HET     CU  F 154       1                                                       
HET     ZN  F 155       1                                                       
HET     CU  G 154       1                                                       
HET     ZN  G 155       1                                                       
HET     CU  H 154       1                                                       
HET     ZN  H 155       1                                                       
HET     CU  I 154       1                                                       
HET     ZN  I 155       1                                                       
HET     CU  J 154       1                                                       
HET     ZN  J 155       1                                                       
HET     CU  K 154       1                                                       
HET     ZN  K 155       1                                                       
HET     CU  L 154       1                                                       
HET     ZN  L 155       1                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
FORMUL  13   CU    12(CU 2+)                                                    
FORMUL  14   ZN    12(ZN 2+)                                                    
FORMUL  37  HOH   *1096(H2 O)                                                   
HELIX    1   1 CYS A   57  GLY A   61  5                                   5    
HELIX    2   2 GLU A  133  GLY A  138  1                                   6    
HELIX    3   3 CYS B   57  GLY B   61  5                                   5    
HELIX    4   4 SER B  107  HIS B  110  5                                   4    
HELIX    5   5 GLU B  133  GLY B  138  1                                   6    
HELIX    6   6 ALA C   55  GLY C   61  5                                   7    
HELIX    7   7 GLU C  133  GLY C  138  1                                   6    
HELIX    8   8 CYS D   57  GLY D   61  5                                   5    
HELIX    9   9 SER D  107  HIS D  110  5                                   4    
HELIX   10  10 GLU D  133  GLY D  138  1                                   6    
HELIX   11  11 ALA E   55  GLY E   61  5                                   7    
HELIX   12  12 SER E  107  HIS E  110  5                                   4    
HELIX   13  13 GLU E  133  GLY E  138  1                                   6    
HELIX   14  14 ALA F   55  GLY F   61  5                                   7    
HELIX   15  15 SER F  107  HIS F  110  5                                   4    
HELIX   16  16 GLU F  133  GLY F  138  1                                   6    
HELIX   17  17 ALA G   55  GLY G   61  5                                   7    
HELIX   18  18 GLU G  133  GLY G  138  1                                   6    
HELIX   19  19 CYS H   57  GLY H   61  5                                   5    
HELIX   20  20 GLU H  133  GLY H  138  1                                   6    
HELIX   21  21 ALA I   55  GLY I   61  5                                   7    
HELIX   22  22 SER I  107  HIS I  110  5                                   4    
HELIX   23  23 ALA J   55  GLY J   61  5                                   7    
HELIX   24  24 ALA K   55  GLY K   61  5                                   7    
HELIX   25  25 SER K  107  HIS K  110  5                                   4    
HELIX   26  26 ASN K  131  GLY K  138  1                                   8    
HELIX   27  27 CYS L   57  GLY L   61  5                                   5    
HELIX   28  28 SER L  107  HIS L  110  5                                   4    
HELIX   29  29 GLU L  133  GLY L  138  1                                   6    
SHEET    1  AA10 LYS A   3  LEU A   8  0                                        
SHEET    2  AA10 GLN A  15  GLN A  22 -1  O  GLY A  16   N  LEU A   8           
SHEET    3  AA10 VAL A  29  LYS A  36 -1  O  LYS A  30   N  GLU A  21           
SHEET    4  AA10 ALA A  95  ASP A 101 -1  O  ALA A  95   N  ILE A  35           
SHEET    5  AA10 ASP A  83  ALA A  89 -1  O  THR A  88   N  ASP A  96           
SHEET    6  AA10 GLY A  41  HIS A  48 -1  O  GLY A  41   N  ALA A  89           
SHEET    7  AA10 THR A 116  HIS A 120 -1  O  THR A 116   N  HIS A  48           
SHEET    8  AA10 ARG A 143  ILE A 151 -1  N  LEU A 144   O  VAL A 119           
SHEET    9  AA10 LYS A   3  LEU A   8 -1  O  VAL A   5   N  GLY A 150           
SHEET   10  AA10 LYS A   3  LEU A   8                                           
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  GLU B  21 -1  O  GLN B  15   N  LYS B  36           
SHEET    4  BA 5 LYS B   3  LEU B   8 -1  O  VAL B   4   N  PHE B  20           
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 LYS C   3  LEU C   8 -1  O  VAL C   4   N  PHE C  20           
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 9 LYS D   3  LYS D   9  0                                        
SHEET    2  DA 9 GLN D  15  GLN D  22 -1  O  GLY D  16   N  LEU D   8           
SHEET    3  DA 9 VAL D  29  LYS D  36 -1  O  LYS D  30   N  GLU D  21           
SHEET    4  DA 9 ALA D  95  ASP D 101 -1  O  ALA D  95   N  ILE D  35           
SHEET    5  DA 9 ASP D  83  ALA D  89 -1  O  THR D  88   N  ASP D  96           
SHEET    6  DA 9 GLY D  41  HIS D  48 -1  O  GLY D  41   N  ALA D  89           
SHEET    7  DA 9 THR D 116  HIS D 120 -1  O  THR D 116   N  HIS D  48           
SHEET    8  DA 9 ARG D 143  ILE D 151 -1  N  LEU D 144   O  VAL D 119           
SHEET    9  DA 9 LYS D   3  LYS D   9 -1  O  VAL D   5   N  GLY D 150           
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  GLU E  21 -1  O  GLN E  15   N  LYS E  36           
SHEET    4  EA 5 LYS E   3  LEU E   8 -1  O  VAL E   4   N  PHE E  20           
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 LYS F   3  LEU F   8 -1  O  VAL F   4   N  PHE F  20           
SHEET    5  FA 5 GLY F 150  ILE F 151 -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  GA24 LYS G   3  LEU G   8  0                                        
SHEET    2  GA24 GLN G  15  GLU G  21 -1  O  GLY G  16   N  LEU G   8           
SHEET    3  GA24 VAL G  29  LYS G  36 -1  O  LYS G  30   N  GLU G  21           
SHEET    4  GA24 VAL G  94  ALA G  95 -1  O  ALA G  95   N  ILE G  35           
SHEET    5  GA24 ASP G  83  ALA G  89                                           
SHEET    6  GA24 GLY G  41  HIS G  48 -1  O  GLY G  41   N  ALA G  89           
SHEET    7  GA24 THR G 116  HIS G 120 -1  O  THR G 116   N  HIS G  48           
SHEET    8  GA24 ARG G 143  ILE G 151 -1  N  LEU G 144   O  VAL G 119           
SHEET    9  GA24 GLN G  15  GLU G  21                                           
SHEET   10  GA24 LYS G   3  LEU G   8 -1  O  VAL G   4   N  PHE G  20           
SHEET   11  GA24 VAL G  29  LYS G  36                                           
SHEET   12  GA24 GLN G  15  GLU G  21 -1  O  GLN G  15   N  LYS G  36           
SHEET   13  GA24 GLY G  41  HIS G  48                                           
SHEET   14  GA24 ASP G  83  ALA G  89 -1  O  GLY G  85   N  PHE G  45           
SHEET   15  GA24 ASP G  83  ALA G  89                                           
SHEET   16  GA24 GLY G  41  HIS G  48 -1  O  GLY G  41   N  ALA G  89           
SHEET   17  GA24 VAL G  94  ALA G  95                                           
SHEET   18  GA24 VAL G  29  LYS G  36 -1  O  ILE G  35   N  ALA G  95           
SHEET   19  GA24 SER G  98  ASP G 101 -1  O  ILE G  99   N  VAL G  31           
SHEET   20  GA24 VAL G  29  LYS G  36 59  O  VAL G  29   N  ASP G 101           
SHEET   21  GA24 THR G 116  HIS G 120                                           
SHEET   22  GA24 GLY G  41  HIS G  48 -1  O  GLY G  44   N  HIS G 120           
SHEET   23  GA24 ARG G 143  ILE G 151                                           
SHEET   24  GA24 LYS G   3  LEU G   8 -1  O  VAL G   5   N  GLY G 150           
SHEET    1  HA16 LYS H   3  LYS H   9  0                                        
SHEET    2  HA16 GLN H  15  GLU H  21 -1  O  GLY H  16   N  LEU H   8           
SHEET    3  HA16 GLN H  15  GLU H  21                                           
SHEET    4  HA16 LYS H   3  LYS H   9 -1  O  VAL H   4   N  PHE H  20           
SHEET    5  HA16 VAL H  29  LYS H  36                                           
SHEET    6  HA16 GLN H  15  GLU H  21 -1  O  GLN H  15   N  LYS H  36           
SHEET    7  HA16 GLY H  41  HIS H  48                                           
SHEET    8  HA16 ASP H  83  ALA H  89 -1  O  GLY H  85   N  PHE H  45           
SHEET    9  HA16 ASP H  83  ALA H  89                                           
SHEET   10  HA16 GLY H  41  HIS H  48 -1  O  GLY H  41   N  ALA H  89           
SHEET   11  HA16 VAL H  94  ASP H 101                                           
SHEET   12  HA16 VAL H  29  LYS H  36 -1  O  VAL H  29   N  ASP H 101           
SHEET   13  HA16 THR H 116  HIS H 120                                           
SHEET   14  HA16 GLY H  41  HIS H  48 -1  O  GLY H  44   N  HIS H 120           
SHEET   15  HA16 ARG H 143  GLY H 150                                           
SHEET   16  HA16 LYS H   3  LYS H   9 -1  O  VAL H   5   N  GLY H 150           
SHEET    1  IA 5 ALA I  95  ASP I 101  0                                        
SHEET    2  IA 5 VAL I  29  LYS I  36 -1  O  VAL I  29   N  ASP I 101           
SHEET    3  IA 5 GLN I  15  GLN I  22 -1  O  GLN I  15   N  LYS I  36           
SHEET    4  IA 5 LYS I   3  LEU I   8 -1  O  VAL I   4   N  PHE I  20           
SHEET    5  IA 5 GLY I 150  ILE I 151 -1  O  GLY I 150   N  VAL I   5           
SHEET    1  IB 4 ASP I  83  ALA I  89  0                                        
SHEET    2  IB 4 GLY I  41  HIS I  48 -1  O  GLY I  41   N  ALA I  89           
SHEET    3  IB 4 THR I 116  HIS I 120 -1  O  THR I 116   N  HIS I  48           
SHEET    4  IB 4 ARG I 143  VAL I 148 -1  N  LEU I 144   O  VAL I 119           
SHEET    1  JA 8 ASP J  83  ALA J  89  0                                        
SHEET    2  JA 8 GLY J  41  HIS J  48 -1  O  GLY J  41   N  ALA J  89           
SHEET    3  JA 8 THR J 116  HIS J 120 -1  O  THR J 116   N  HIS J  48           
SHEET    4  JA 8 ARG J 143  ILE J 151 -1  N  LEU J 144   O  VAL J 119           
SHEET    5  JA 8 LYS J   3  GLY J  10 -1  O  VAL J   5   N  GLY J 150           
SHEET    6  JA 8 GLN J  15  GLN J  22 -1  O  GLY J  16   N  LEU J   8           
SHEET    7  JA 8 VAL J  29  LYS J  36 -1  O  LYS J  30   N  GLU J  21           
SHEET    8  JA 8 ALA J  95  ASP J 101 -1  O  ALA J  95   N  ILE J  35           
SHEET    1  KA16 LYS K   3  LEU K   8  0                                        
SHEET    2  KA16 GLN K  15  GLN K  22 -1  O  GLY K  16   N  LEU K   8           
SHEET    3  KA16 GLN K  15  GLN K  22                                           
SHEET    4  KA16 LYS K   3  LEU K   8 -1  O  VAL K   4   N  PHE K  20           
SHEET    5  KA16 VAL K  29  LYS K  36                                           
SHEET    6  KA16 GLN K  15  GLN K  22 -1  O  GLN K  15   N  LYS K  36           
SHEET    7  KA16 GLY K  41  HIS K  48                                           
SHEET    8  KA16 ASP K  83  ALA K  89 -1  O  GLY K  85   N  PHE K  45           
SHEET    9  KA16 ASP K  83  ALA K  89                                           
SHEET   10  KA16 GLY K  41  HIS K  48 -1  O  GLY K  41   N  ALA K  89           
SHEET   11  KA16 VAL K  94  ASP K 101                                           
SHEET   12  KA16 VAL K  29  LYS K  36 -1  O  VAL K  29   N  ASP K 101           
SHEET   13  KA16 THR K 116  HIS K 120                                           
SHEET   14  KA16 GLY K  41  HIS K  48 -1  O  GLY K  44   N  HIS K 120           
SHEET   15  KA16 ARG K 143  ILE K 151                                           
SHEET   16  KA16 LYS K   3  LEU K   8 -1  O  VAL K   5   N  GLY K 150           
SHEET    1  LA16 LYS L   3  LEU L   8  0                                        
SHEET    2  LA16 GLN L  15  GLU L  21 -1  O  GLY L  16   N  LEU L   8           
SHEET    3  LA16 GLN L  15  GLU L  21                                           
SHEET    4  LA16 LYS L   3  LEU L   8 -1  O  VAL L   4   N  PHE L  20           
SHEET    5  LA16 VAL L  29  LYS L  36                                           
SHEET    6  LA16 GLN L  15  GLU L  21 -1  O  GLN L  15   N  LYS L  36           
SHEET    7  LA16 GLY L  41  HIS L  48                                           
SHEET    8  LA16 ASP L  83  ALA L  89 -1  O  GLY L  85   N  PHE L  45           
SHEET    9  LA16 ASP L  83  ALA L  89                                           
SHEET   10  LA16 GLY L  41  HIS L  48 -1  O  GLY L  41   N  ALA L  89           
SHEET   11  LA16 ALA L  95  ASP L 101                                           
SHEET   12  LA16 VAL L  29  LYS L  36 -1  O  VAL L  29   N  ASP L 101           
SHEET   13  LA16 THR L 116  HIS L 120                                           
SHEET   14  LA16 GLY L  41  HIS L  48 -1  O  GLY L  44   N  HIS L 120           
SHEET   15  LA16 ARG L 143  ILE L 151                                           
SHEET   16  LA16 LYS L   3  LEU L   8 -1  O  VAL L   5   N  GLY L 150           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.16  
SSBOND   2 CYS B   57    CYS B  146                          1555   1555  2.17  
SSBOND   3 CYS C   57    CYS C  146                          1555   1555  2.16  
SSBOND   4 CYS D   57    CYS D  146                          1555   1555  2.18  
SSBOND   5 CYS E   57    CYS E  146                          1555   1555  2.10  
SSBOND   6 CYS F   57    CYS F  146                          1555   1555  2.10  
SSBOND   7 CYS G   57    CYS G  146                          1555   1555  2.05  
SSBOND   8 CYS H   57    CYS H  146                          1555   1555  2.08  
SSBOND   9 CYS I   57    CYS I  146                          1555   1555  2.09  
SSBOND  10 CYS J   57    CYS J  146                          1555   1555  2.10  
SSBOND  11 CYS K   57    CYS K  146                          1555   1555  2.08  
SSBOND  12 CYS L   57    CYS L  146                          1555   1555  2.04  
LINK        CU    CU A 154                 ND1 HIS A  46     1555   1555  2.18  
LINK        CU    CU A 154                 NE2 HIS A  48     1555   1555  2.13  
LINK        CU    CU A 154                 NE2 HIS A 120     1555   1555  2.08  
LINK        CU    CU A 154                 O   HOH A2060     1555   1555  1.86  
LINK        CU    CU A 154                 NE2 HIS A  63     1555   1555  2.36  
LINK        ZN    ZN A 155                 ND1 HIS A  71     1555   1555  2.08  
LINK        ZN    ZN A 155                 OD1 ASP A  83     1555   1555  1.91  
LINK        ZN    ZN A 155                 ND1 HIS A  63     1555   1555  2.01  
LINK        ZN    ZN A 155                 ND1 HIS A  80     1555   1555  1.91  
LINK        CU    CU B 154                 NE2 HIS B  63     1555   1555  2.22  
LINK        CU    CU B 154                 NE2 HIS B  48     1555   1555  2.15  
LINK        CU    CU B 154                 O   HOH B2062     1555   1555  2.21  
LINK        CU    CU B 154                 ND1 HIS B  46     1555   1555  2.12  
LINK        CU    CU B 154                 NE2 HIS B 120     1555   1555  2.19  
LINK        ZN    ZN B 155                 ND1 HIS B  63     1555   1555  2.05  
LINK        ZN    ZN B 155                 ND1 HIS B  71     1555   1555  2.02  
LINK        ZN    ZN B 155                 OD1 ASP B  83     1555   1555  1.95  
LINK        ZN    ZN B 155                 ND1 HIS B  80     1555   1555  1.97  
LINK        CU    CU C 154                 ND1 HIS C  46     1555   1555  2.22  
LINK        CU    CU C 154                 NE2 HIS C  48     1555   1555  2.09  
LINK        CU    CU C 154                 NE2 HIS C  63     1555   1555  2.29  
LINK        CU    CU C 154                 NE2 HIS C 120     1555   1555  2.09  
LINK        CU    CU C 154                 O   HOH C2063     1555   1555  2.44  
LINK        ZN    ZN C 155                 ND1 HIS C  71     1555   1555  2.04  
LINK        ZN    ZN C 155                 OD1 ASP C  83     1555   1555  1.98  
LINK        ZN    ZN C 155                 ND1 HIS C  80     1555   1555  1.96  
LINK        ZN    ZN C 155                 ND1 HIS C  63     1555   1555  2.02  
LINK        CU    CU D 154                 O   HOH D2063     1555   1555  2.14  
LINK        CU    CU D 154                 ND1 HIS D  46     1555   1555  2.09  
LINK        CU    CU D 154                 NE2 HIS D  63     1555   1555  2.36  
LINK        CU    CU D 154                 NE2 HIS D  48     1555   1555  2.12  
LINK        CU    CU D 154                 NE2 HIS D 120     1555   1555  2.05  
LINK        ZN    ZN D 155                 ND1 HIS D  63     1555   1555  1.95  
LINK        ZN    ZN D 155                 ND1 HIS D  80     1555   1555  1.94  
LINK        ZN    ZN D 155                 ND1 HIS D  71     1555   1555  2.02  
LINK        ZN    ZN D 155                 OD1 ASP D  83     1555   1555  1.90  
LINK        CU    CU E 154                 O   HOH E2032     1555   1555  2.35  
LINK        CU    CU E 154                 ND1 HIS E  46     1555   1555  2.08  
LINK        CU    CU E 154                 NE2 HIS E  48     1555   1555  2.21  
LINK        CU    CU E 154                 NE2 HIS E  63     1555   1555  2.20  
LINK        CU    CU E 154                 NE2 HIS E 120     1555   1555  2.02  
LINK        ZN    ZN E 155                 OD1 ASP E  83     1555   1555  1.99  
LINK        ZN    ZN E 155                 ND1 HIS E  71     1555   1555  2.12  
LINK        ZN    ZN E 155                 ND1 HIS E  63     1555   1555  2.03  
LINK        ZN    ZN E 155                 ND1 HIS E  80     1555   1555  1.90  
LINK        CU    CU F 154                 ND1 HIS F  46     1555   1555  2.17  
LINK        CU    CU F 154                 NE2 HIS F  63     1555   1555  2.43  
LINK        CU    CU F 154                 O   HOH F2018     1555   1555  2.03  
LINK        CU    CU F 154                 NE2 HIS F 120     1555   1555  1.99  
LINK        CU    CU F 154                 NE2 HIS F  48     1555   1555  2.14  
LINK        ZN    ZN F 155                 ND1 HIS F  71     1555   1555  1.95  
LINK        ZN    ZN F 155                 OD1 ASP F  83     1555   1555  1.91  
LINK        ZN    ZN F 155                 ND1 HIS F  63     1555   1555  1.94  
LINK        ZN    ZN F 155                 ND1 HIS F  80     1555   1555  2.13  
LINK        CU    CU G 154                 NE2 HIS G  48     1555   1555  2.17  
LINK        CU    CU G 154                 NE2 HIS G  63     1555   1555  2.36  
LINK        CU    CU G 154                 O   HOH G2030     1555   1555  2.43  
LINK        CU    CU G 154                 ND1 HIS G  46     1555   1555  2.07  
LINK        CU    CU G 154                 NE2 HIS G 120     1555   1555  2.15  
LINK        ZN    ZN G 155                 ND1 HIS G  80     1555   1555  1.91  
LINK        ZN    ZN G 155                 OD1 ASP G  83     1555   1555  1.93  
LINK        ZN    ZN G 155                 ND1 HIS G  71     1555   1555  2.03  
LINK        ZN    ZN G 155                 ND1 HIS G  63     1555   1555  1.92  
LINK        CU    CU H 154                 NE2 HIS H 120     1555   1555  2.05  
LINK        CU    CU H 154                 NE2 HIS H  63     1555   1555  2.22  
LINK        CU    CU H 154                 NE2 HIS H  48     1555   1555  2.26  
LINK        CU    CU H 154                 O   HOH H2065     1555   1555  2.62  
LINK        CU    CU H 154                 ND1 HIS H  46     1555   1555  2.05  
LINK        ZN    ZN H 155                 ND1 HIS H  63     1555   1555  2.02  
LINK        ZN    ZN H 155                 ND1 HIS H  71     1555   1555  2.17  
LINK        ZN    ZN H 155                 ND1 HIS H  80     1555   1555  1.82  
LINK        ZN    ZN H 155                 OD1 ASP H  83     1555   1555  2.07  
LINK        CU    CU I 154                 NE2 HIS I  63     1555   1555  1.97  
LINK        CU    CU I 154                 NE2 HIS I  48     1555   1555  2.28  
LINK        CU    CU I 154                 ND1 HIS I  46     1555   1555  2.34  
LINK        CU    CU I 154                 O   HOH I2031     1555   1555  2.28  
LINK        CU    CU I 154                 NE2 HIS I 120     1555   1555  2.17  
LINK        ZN    ZN I 155                 ND1 HIS I  63     1555   1555  2.29  
LINK        ZN    ZN I 155                 ND1 HIS I  71     1555   1555  2.07  
LINK        ZN    ZN I 155                 ND1 HIS I  80     1555   1555  1.74  
LINK        ZN    ZN I 155                 OD1 ASP I  83     1555   1555  2.12  
LINK        CU    CU J 154                 NE2 HIS J  48     1555   1555  2.24  
LINK        CU    CU J 154                 O   HOH J2030     1555   1555  2.28  
LINK        CU    CU J 154                 NE2 HIS J  63     1555   1555  2.15  
LINK        CU    CU J 154                 ND1 HIS J  46     1555   1555  2.01  
LINK        CU    CU J 154                 NE2 HIS J 120     1555   1555  2.04  
LINK        ZN    ZN J 155                 OD2 ASP J  83     1555   1555  2.77  
LINK        ZN    ZN J 155                 ND1 HIS J  63     1555   1555  2.06  
LINK        ZN    ZN J 155                 ND1 HIS J  71     1555   1555  1.98  
LINK        ZN    ZN J 155                 ND1 HIS J  80     1555   1555  1.85  
LINK        ZN    ZN J 155                 OD1 ASP J  83     1555   1555  1.84  
LINK        CU    CU K 154                 NE2 HIS K  63     1555   1555  2.26  
LINK        CU    CU K 154                 O   HOH K2021     1555   1555  2.35  
LINK        CU    CU K 154                 NE2 HIS K  48     1555   1555  2.18  
LINK        CU    CU K 154                 NE2 HIS K 120     1555   1555  2.13  
LINK        CU    CU K 154                 ND1 HIS K  46     1555   1555  2.07  
LINK        ZN    ZN K 155                 OD1 ASP K  83     1555   1555  1.95  
LINK        ZN    ZN K 155                 ND1 HIS K  63     1555   1555  1.92  
LINK        ZN    ZN K 155                 ND1 HIS K  71     1555   1555  2.11  
LINK        ZN    ZN K 155                 ND1 HIS K  80     1555   1555  2.03  
LINK        CU    CU L 154                 ND1 HIS L  46     1555   1555  2.11  
LINK        CU    CU L 154                 NE2 HIS L 120     1555   1555  2.23  
LINK        CU    CU L 154                 NE2 HIS L  63     1555   1555  1.96  
LINK        CU    CU L 154                 O   HOH L2023     1555   1555  2.47  
LINK        CU    CU L 154                 NE2 HIS L  48     1555   1555  2.16  
LINK        ZN    ZN L 155                 ND1 HIS L  63     1555   1555  2.28  
LINK        ZN    ZN L 155                 ND1 HIS L  80     1555   1555  1.63  
LINK        ZN    ZN L 155                 OD1 ASP L  83     1555   1555  1.99  
LINK        ZN    ZN L 155                 ND1 HIS L  71     1555   1555  2.14  
CISPEP   1 ASN A   26    GLY A   27          0        -0.81                     
SITE     1 AC1  5 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC1  5 HOH A2060                                                     
SITE     1 AC2  5 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     2 AC2  5 LYS A 136                                                     
SITE     1 AC3  5 HIS B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     2 AC3  5 HOH B2062                                                     
SITE     1 AC4  5 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     2 AC4  5 LYS B 136                                                     
SITE     1 AC5  5 HIS C  46  HIS C  48  HIS C  63  HIS C 120                    
SITE     2 AC5  5 HOH C2063                                                     
SITE     1 AC6  5 HIS C  63  HIS C  71  HIS C  80  ASP C  83                    
SITE     2 AC6  5 LYS C 136                                                     
SITE     1 AC7  5 HIS D  46  HIS D  48  HIS D  63  HIS D 120                    
SITE     2 AC7  5 HOH D2063                                                     
SITE     1 AC8  5 HIS D  63  HIS D  71  HIS D  80  ASP D  83                    
SITE     2 AC8  5 LYS D 136                                                     
SITE     1 AC9  5 HIS E  46  HIS E  48  HIS E  63  HIS E 120                    
SITE     2 AC9  5 HOH E2032                                                     
SITE     1 BC1  5 HIS E  63  HIS E  71  HIS E  80  ASP E  83                    
SITE     2 BC1  5 LYS E 136                                                     
SITE     1 BC2  5 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     2 BC2  5 HOH F2018                                                     
SITE     1 BC3  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 BC4  5 HIS G  46  HIS G  48  HIS G  63  HIS G 120                    
SITE     2 BC4  5 HOH G2030                                                     
SITE     1 BC5  5 HIS G  63  HIS G  71  HIS G  80  ASP G  83                    
SITE     2 BC5  5 LYS G 136                                                     
SITE     1 BC6  5 HIS H  46  HIS H  48  HIS H  63  HIS H 120                    
SITE     2 BC6  5 HOH H2065                                                     
SITE     1 BC7  5 HIS H  63  HIS H  71  HIS H  80  ASP H  83                    
SITE     2 BC7  5 LYS H 136                                                     
SITE     1 BC8  5 HIS I  46  HIS I  48  HIS I  63  HIS I 120                    
SITE     2 BC8  5 HOH I2031                                                     
SITE     1 BC9  5 HIS I  63  HIS I  71  HIS I  80  ASP I  83                    
SITE     2 BC9  5 LYS I 136                                                     
SITE     1 CC1  5 HIS J  46  HIS J  48  HIS J  63  HIS J 120                    
SITE     2 CC1  5 HOH J2030                                                     
SITE     1 CC2  4 HIS J  63  HIS J  71  HIS J  80  ASP J  83                    
SITE     1 CC3  5 HIS K  46  HIS K  48  HIS K  63  HIS K 120                    
SITE     2 CC3  5 HOH K2021                                                     
SITE     1 CC4  5 HIS K  63  HIS K  71  HIS K  80  ASP K  83                    
SITE     2 CC4  5 LYS K 136                                                     
SITE     1 CC5  5 HIS L  46  HIS L  48  HIS L  63  HIS L 120                    
SITE     2 CC5  5 HOH L2023                                                     
SITE     1 CC6  5 HIS L  63  HIS L  71  HIS L  80  ASP L  83                    
SITE     2 CC6  5 LYS L 136                                                     
CRYST1  112.374  145.582  112.497  90.00 120.05  90.00 P 1 21 1     24          
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      0.008899  0.000000  0.005148        0.00000                         
SCALE2      0.000000  0.006869  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010269        0.00000                         
MTRIX1   1 -0.998090 -0.061730 -0.001080       22.19083    1                    
MTRIX2   1 -0.061340  0.989390  0.131680       -0.27397    1                    
MTRIX3   1 -0.007060  0.131500 -0.991290       14.30155    1                    
MTRIX1   2  0.500080 -0.001140  0.865980        5.53139    1                    
MTRIX2   2  0.008610 -0.999940 -0.006290      -96.49535    1                    
MTRIX3   2  0.865940  0.010600 -0.500040        3.50316    1                    
MTRIX1   3  0.500080 -0.001140  0.865980        5.53139    1                    
MTRIX2   3  0.008610 -0.999940 -0.006290      -96.49535    1                    
MTRIX3   3  0.865940  0.010600 -0.500040        3.50316    1                    
MTRIX1   4  0.497670  0.043040 -0.866300       11.47130    1                    
MTRIX2   4 -0.011810 -0.998340 -0.056390      -24.22828    1                    
MTRIX3   4 -0.867290  0.038300 -0.496330       51.82755    1                    
MTRIX1   5 -0.496760 -0.103430  0.861700       10.20352    1                    
MTRIX2   5  0.037170 -0.994500 -0.097940      -24.47743    1                    
MTRIX3   5  0.867090 -0.016620  0.497870       24.20590    1                    
MTRIX1   6  0.999310  0.037140 -0.000220       29.20916    1                    
MTRIX2   6  0.037050 -0.997330 -0.062990      -24.06009    1                    
MTRIX3   6 -0.002560  0.062930 -0.998010       -3.92607    1                    
MTRIX1   7 -0.999750  0.022480  0.001970       52.84855    1                    
MTRIX2   7 -0.022540 -0.998820 -0.043060      -23.35865    1                    
MTRIX3   7  0.001000 -0.043100  0.999070      -17.47200    1                    
MTRIX1   8 -0.505140  0.036020 -0.862290       55.65426    1                    
MTRIX2   8  0.029500  0.999270  0.024460       73.59691    1                    
MTRIX3   8  0.862540 -0.013080 -0.505830      -13.55712    1                    
MTRIX1   9  0.505200 -0.100660  0.857110       30.64955    1                    
MTRIX2   9 -0.022250  0.991320  0.129540       73.32990    1                    
MTRIX3   9 -0.862710 -0.084510  0.498580        0.01541    1                    
MTRIX1  10 -0.489450 -0.071680  0.869080       15.39836    1                    
MTRIX2  10  0.001270  0.996560  0.082900       72.11509    1                    
MTRIX3  10 -0.872030  0.041680 -0.487670       57.78385    1                    
MTRIX1  11  0.494860  0.066130 -0.866450       16.56118    1                    
MTRIX2  11 -0.033700  0.997810  0.056910       72.75935    1                    
MTRIX3  11  0.868320  0.001040  0.496000       30.56594    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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