GenomeNet

Database: PDB
Entry: 3G4X
LinkDB: 3G4X
Original site: 3G4X 
HEADER    OXIDOREDUCTASE                          04-FEB-09   3G4X              
TITLE     CRYSTAL STRUCTURE OF NISOD Y9F MUTANT                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [NI];                                 
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: NISOD (UNP RESIDUES 15 TO 131);                            
COMPND   5 SYNONYM: NISOD, NICKEL-CONTAINING SUPEROXIDE DISMUTASE;              
COMPND   6 EC: 1.15.1.1;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES COELICOLOR;                        
SOURCE   3 ORGANISM_TAXID: 1902;                                                
SOURCE   4 GENE: 2SC7G11.16C, SCO5254, SOD1, SODN;                              
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PLYSS;                           
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET30                                     
KEYWDS    NICKEL, HEXAMER, SUPEROXIDE DISMUTASE, NISOD, SOD,, ANTIOXIDANT,      
KEYWDS   2 METAL-BINDING, OXIDOREDUCTASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.C.GARMAN,A.I.GUCE,R.W.HERBST,P.A.BRYNGELSON,D.E.CABELLI,            
AUTHOR   2 K.A.HIGGINS,K.C.RYAN,M.J.MARONEY                                     
REVDAT   2   13-JUL-11 3G4X    1       VERSN                                    
REVDAT   1   28-APR-09 3G4X    0                                                
JRNL        AUTH   R.W.HERBST,A.GUCE,P.A.BRYNGELSON,K.A.HIGGINS,K.C.RYAN,       
JRNL        AUTH 2 D.E.CABELLI,S.C.GARMAN,M.J.MARONEY                           
JRNL        TITL   ROLE OF CONSERVED TYROSINE RESIDUES IN NISOD CATALYSIS: A    
JRNL        TITL 2 CASE OF CONVERGENT EVOLUTION                                 
JRNL        REF    BIOCHEMISTRY                  V.  48  3354 2009              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   19183068                                                     
JRNL        DOI    10.1021/BI802029T                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.01 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0044                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.61                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 24113                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1300                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.01                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.06                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1709                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.77                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2620                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 86                           
REMARK   3   BIN FREE R VALUE                    : 0.3250                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2787                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 389                                     
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) : 26.79                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.03000                                              
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : -0.01000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.184         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.178         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.117         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.132         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.931                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2898 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3926 ; 1.479 ; 1.940       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   352 ; 4.759 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   139 ;36.560 ;24.892       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   504 ;14.881 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;18.297 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   417 ; 0.109 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2225 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1467 ; 0.229 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1964 ; 0.302 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   316 ; 0.173 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   135 ; 0.289 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    56 ; 0.227 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1773 ; 0.827 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2858 ; 1.423 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1125 ; 2.568 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1068 ; 3.968 ; 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  : 6                                          
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     7                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.0183  20.9258  28.6046              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .1143 T22:    .0699                                     
REMARK   3      T33:    .1712 T12:    .0260                                     
REMARK   3      T13:    .0353 T23:    .0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6648 L22:   1.1383                                     
REMARK   3      L33:   3.4384 L12:  -2.3041                                     
REMARK   3      L13:  -4.0033 L23:   1.9766                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.1103 S12:   -.0517 S13:   -.0249                       
REMARK   3      S21:    .0707 S22:    .0523 S23:    .0108                       
REMARK   3      S31:    .1039 S32:    .0407 S33:    .0580                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     8        A   116                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.0128  24.3996  16.2163              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0766 T22:    .0328                                     
REMARK   3      T33:    .0369 T12:   -.0042                                     
REMARK   3      T13:    .0402 T23:    .0150                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4796 L22:    .6742                                     
REMARK   3      L33:    .2642 L12:   -.3305                                     
REMARK   3      L13:    .0148 L23:    .0374                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:    .0189 S12:   -.0016 S13:    .0590                       
REMARK   3      S21:   -.1159 S22:    .0227 S23:   -.0252                       
REMARK   3      S31:   -.0964 S32:    .0086 S33:   -.0416                       
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 :   B     1        B     7                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.8784  -3.9164  27.8616              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0748 T22:    .1411                                     
REMARK   3      T33:    .2415 T12:   -.0453                                     
REMARK   3      T13:   -.0063 T23:    .1122                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5649 L22:   8.5571                                     
REMARK   3      L33:   2.8403 L12:   1.0430                                     
REMARK   3      L13:   -.6254 L23:   4.4210                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.2013 S12:    .5371 S13:    .6544                       
REMARK   3      S21:    .2851 S22:   -.0335 S23:    .9039                       
REMARK   3      S31:    .2754 S32:   -.2894 S33:    .2348                       
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 :   B     8        B   116                          
REMARK   3    ORIGIN FOR THE GROUP (A):    .8616  -8.0308  16.3168              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0741 T22:    .0564                                     
REMARK   3      T33:    .0111 T12:    .0024                                     
REMARK   3      T13:    .0168 T23:   -.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3753 L22:   1.0003                                     
REMARK   3      L33:   1.2129 L12:   1.0482                                     
REMARK   3      L13:   -.9276 L23:   -.4973                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0811 S12:    .0936 S13:    .0239                       
REMARK   3      S21:   -.0889 S22:    .0520 S23:    .0430                       
REMARK   3      S31:    .1206 S32:   -.0468 S33:    .0291                       
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 :   C     1        C     7                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.1233   7.9842  46.3197              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0896 T22:    .0477                                     
REMARK   3      T33:    .0882 T12:    .0082                                     
REMARK   3      T13:    .0532 T23:   -.0213                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7206 L22:    .0018                                     
REMARK   3      L33:   3.5409 L12:   -.0368                                     
REMARK   3      L13:   1.1018 L23:   -.0761                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.2478 S12:   -.2314 S13:    .0534                       
REMARK   3      S21:   -.0046 S22:    .0347 S23:   -.0062                       
REMARK   3      S31:    .1497 S32:   -.0386 S33:    .2132                       
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 :   C     8        C   116                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.1785   8.5195  39.8301              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:    .0211 T22:    .0589                                     
REMARK   3      T33:    .0583 T12:   -.0024                                     
REMARK   3      T13:   -.0268 T23:   -.0085                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:    .4625 L22:    .8229                                     
REMARK   3      L33:   1.3240 L12:   -.2078                                     
REMARK   3      L13:   -.5634 L23:    .3519                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   -.0061 S12:   -.0210 S13:    .0323                       
REMARK   3      S21:    .1149 S22:    .0074 S23:   -.1279                       
REMARK   3      S31:    .0311 S32:    .0789 S33:   -.0013                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3G4X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-FEB-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB051427.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-NOV-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : OSMIC BLUE                         
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25440                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.010                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.51500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
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 1T6U                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 550 MME, CACL2, BIS-TRIS, PH 6.5,    
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 293K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.93300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.93300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       30.04450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       56.28400            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       30.04450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       56.28400            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       55.93300            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       30.04450            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       56.28400            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       55.93300            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       30.04450            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       56.28400            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14260 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 26560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       55.93300            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH C 347  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C 299  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C 208  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA C   117                                                      
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   O    HOH B   129     O    HOH B   275              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B   213     O    HOH B   213     3555     1.63            
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    ASP B   3       20.74     85.89                                   
REMARK 500    ASP B  10      116.91   -163.11                                   
REMARK 500    ASP C   3       12.57     82.65                                   
REMARK 500    ASP C  10      119.40   -160.61                                   
REMARK 500    PRO C  11       -7.00    -59.28                                   
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 C   8        23.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 272        DISTANCE =  6.37 ANGSTROMS                       
REMARK 525    HOH A 284        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH A 381        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH B 244        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH C 292        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH C 326        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH C 348        DISTANCE =  5.20 ANGSTROMS                       
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                              NI A 201N NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A   1   N                                                      
REMARK 620 2 HIS A   1   ND1  67.3                                              
REMARK 620 3 CYS A   2   N    84.3  81.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI B 202N NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B   1   N                                                      
REMARK 620 2 CYS B   2   N    83.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI C 203N NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C   1   N                                                      
REMARK 620 2 HIS C   1   ND1  72.4                                              
REMARK 620 3 CYS C   2   N    82.2  75.8                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 201N                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 301C                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 202N                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 302C                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI C 203N                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 303C                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1T6U   RELATED DB: PDB                                   
REMARK 900 NICKEL SUPEROXIDE DISMUTASE (NISOD) NATIVE AT 1.30 A                 
REMARK 900 RELATED ID: 3G4Z   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF NISOD Y9F MUTANT                                
REMARK 900 RELATED ID: 3G50   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF NISOD D3A MUTANT                                
DBREF  3G4X A    1   117  UNP    P80735   SODN_STRCO      15    131             
DBREF  3G4X B    1   117  UNP    P80735   SODN_STRCO      15    131             
DBREF  3G4X C    1   117  UNP    P80735   SODN_STRCO      15    131             
SEQADV 3G4X PHE A    9  UNP  P80735    TYR    23 ENGINEERED                     
SEQADV 3G4X PHE B    9  UNP  P80735    TYR    23 ENGINEERED                     
SEQADV 3G4X PHE C    9  UNP  P80735    TYR    23 ENGINEERED                     
SEQRES   1 A  117  HIS CYS ASP LEU PRO CYS GLY VAL PHE ASP PRO ALA GLN          
SEQRES   2 A  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN GLU          
SEQRES   3 A  117  LYS MET ALA GLY ASN ASP ASP PRO HIS PHE GLN THR ARG          
SEQRES   4 A  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS          
SEQRES   5 A  117  HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS PRO          
SEQRES   6 A  117  PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU VAL          
SEQRES   7 A  117  ASN ASP THR LEU LYS ALA LEU SER ALA ALA LYS GLY SER          
SEQRES   8 A  117  LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE          
SEQRES   9 A  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA          
SEQRES   1 B  117  HIS CYS ASP LEU PRO CYS GLY VAL PHE ASP PRO ALA GLN          
SEQRES   2 B  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN GLU          
SEQRES   3 B  117  LYS MET ALA GLY ASN ASP ASP PRO HIS PHE GLN THR ARG          
SEQRES   4 B  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS          
SEQRES   5 B  117  HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS PRO          
SEQRES   6 B  117  PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU VAL          
SEQRES   7 B  117  ASN ASP THR LEU LYS ALA LEU SER ALA ALA LYS GLY SER          
SEQRES   8 B  117  LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE          
SEQRES   9 B  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA          
SEQRES   1 C  117  HIS CYS ASP LEU PRO CYS GLY VAL PHE ASP PRO ALA GLN          
SEQRES   2 C  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN GLU          
SEQRES   3 C  117  LYS MET ALA GLY ASN ASP ASP PRO HIS PHE GLN THR ARG          
SEQRES   4 C  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS          
SEQRES   5 C  117  HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS PRO          
SEQRES   6 C  117  PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU VAL          
SEQRES   7 C  117  ASN ASP THR LEU LYS ALA LEU SER ALA ALA LYS GLY SER          
SEQRES   8 C  117  LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE          
SEQRES   9 C  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA          
HET     NI  A 201N      1                                                       
HET     CL  A 301C      1                                                       
HET     NI  B 202N      1                                                       
HET     CL  B 302C      1                                                       
HET     NI  C 203N      1                                                       
HET     CL  C 303C      1                                                       
HETNAM      NI NICKEL (II) ION                                                  
HETNAM      CL CHLORIDE ION                                                     
FORMUL   4   NI    3(NI 2+)                                                     
FORMUL   5   CL    3(CL 1-)                                                     
FORMUL  10  HOH   *389(H2 O)                                                    
HELIX    1   1 PRO A   11  ALA A   29  1                                  19    
HELIX    2   2 ASP A   33  TYR A   62  1                                  30    
HELIX    3   3 LYS A   64  TYR A   71  1                                   8    
HELIX    4   4 GLU A   73  GLY A   90  1                                  18    
HELIX    5   5 ASP A   93  ALA A  117  1                                  25    
HELIX    6   6 PRO B   11  ALA B   29  1                                  19    
HELIX    7   7 ASP B   33  TYR B   62  1                                  30    
HELIX    8   8 LYS B   64  TYR B   71  1                                   8    
HELIX    9   9 GLU B   73  GLY B   90  1                                  18    
HELIX   10  10 ASP B   93  LYS B  116  1                                  24    
HELIX   11  11 PRO C   11  ALA C   29  1                                  19    
HELIX   12  12 ASP C   33  TYR C   62  1                                  30    
HELIX   13  13 LYS C   64  TYR C   71  1                                   8    
HELIX   14  14 GLU C   73  GLY C   90  1                                  18    
HELIX   15  15 ASP C   93  LYS C  116  1                                  24    
LINK         N  AHIS A   1                NI    NI A 201N    1555   1555  2.04  
LINK         N  BHIS A   1                NI    NI A 201N    1555   1555  2.12  
LINK         ND1BHIS A   1                NI    NI A 201N    1555   1555  2.23  
LINK         N   CYS A   2                NI    NI A 201N    1555   1555  2.02  
LINK         N  AHIS B   1                NI    NI B 202N    1555   1555  2.01  
LINK         N  BHIS B   1                NI    NI B 202N    1555   1555  2.03  
LINK         N   CYS B   2                NI    NI B 202N    1555   1555  2.06  
LINK         N  AHIS C   1                NI    NI C 203N    1555   1555  1.91  
LINK         N  BHIS C   1                NI    NI C 203N    1555   1555  2.01  
LINK         ND1BHIS C   1                NI    NI C 203N    1555   1555  2.58  
LINK         N   CYS C   2                NI    NI C 203N    1555   1555  2.08  
CISPEP   1 LEU A    4    PRO A    5          0         2.65                     
CISPEP   2 LEU B    4    PRO B    5          0        -0.29                     
CISPEP   3 LEU C    4    PRO C    5          0         7.60                     
SITE     1 AC1  4 HIS A   1  CYS A   2  CYS A   6   CL A 301C                   
SITE     1 AC2  7 HIS A   1  ASP A   3  PRO A   5  CYS A   6                    
SITE     2 AC2  7 PHE A   9  HOH A 123   NI A 201N                              
SITE     1 AC3  5 HIS B   1  CYS B   2  ASP B   3  CYS B   6                    
SITE     2 AC3  5  CL B 302C                                                    
SITE     1 AC4  7 HIS B   1  ASP B   3  PRO B   5  CYS B   6                    
SITE     2 AC4  7 PHE B   9   NI B 202N HOH B 349                               
SITE     1 AC5  4 HIS C   1  CYS C   2  CYS C   6   CL C 303C                   
SITE     1 AC6  8 HIS C   1  ASP C   3  PRO C   5  CYS C   6                    
SITE     2 AC6  8 PHE C   9   NI C 203N HOH C 340  HOH C 393                    
CRYST1   60.089  112.568  111.866  90.00  90.00  90.00 C 2 2 21     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      0.016642  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008884  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008939        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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