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Database: PDB
Entry: 1OZT
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Original site: 1OZT 
HEADER    OXIDOREDUCTASE                          09-APR-03   1OZT              
TITLE     CRYSTAL STRUCTURE OF APO-H46R FAMILIAL ALS MUTANT HUMAN CU,           
TITLE    2 ZN SUPEROXIDE DISMUTASE (CUZNSOD) TO 2.5A RESOLUTION                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: M, N, G, H, K, L, I, J;                                       
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SOD1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SF21;                                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PVL1392                                   
KEYWDS    BETA BARREL, AMYLOID-LIKE LINEAR FILAMENTS, OXIDOREDUCTASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.S.ELAM,A.B.TAYLOR,R.STRANGE,S.ANTONYUK,P.A.DOUCETTE,                
AUTHOR   2 J.A.RODRIGUEZ,S.S.HASNAIN,L.J.HAYWARD,J.S.VALENTINE,                 
AUTHOR   3 T.O.YEATES,P.J.HART                                                  
REVDAT   2   24-FEB-09 1OZT    1       VERSN                                    
REVDAT   1   27-MAY-03 1OZT    0                                                
JRNL        AUTH   J.S.ELAM,A.B.TAYLOR,R.STRANGE,S.ANTONYUK,                    
JRNL        AUTH 2 P.A.DOUCETTE,J.A.RODRIGUEZ,S.S.HASNAIN,L.J.HAYWARD,          
JRNL        AUTH 3 J.S.VALENTINE,T.O.YEATES,P.J.HART                            
JRNL        TITL   AMYLOID-LIKE FILAMENTS AND WATER-FILLED NANOTUBES            
JRNL        TITL 2 FORMED BY SOD1 MUTANT PROTEINS LINKED TO FAMILIAL            
JRNL        TITL 3 ALS                                                          
JRNL        REF    NAT.STRUCT.BIOL.              V.  10   461 2003              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   12754496                                                     
JRNL        DOI    10.1038/NSB935                                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : MAXIMUM LIKELIHOOD                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.43                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2446069.400                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 40746                          
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 SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2064                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6307                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3430                       
REMARK   3   BIN FREE R VALUE                    : 0.3910                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 379                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7966                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 235                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -14.80000                                            
REMARK   3    B22 (A**2) : 29.52000                                             
REMARK   3    B33 (A**2) : -14.72000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.41000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.34                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.49                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.41                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.55                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.70                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.92                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : GROUP                                     
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.34                                                 
REMARK   3   BSOL        : 37.91                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1OZT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-APR-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB018849.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-NOV-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X8C                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.989                              
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40758                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 4.120                              
REMARK 200  R MERGE                    (I) : 0.08600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.4400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.320                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1AZV                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MAGNESIUM ACETATE, SODIUM                
REMARK 280  CACODYLATE, PEG 8000, PH 6.5, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 277K                                                    
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       34.99900            
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                                              
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HOMODIMER.                      
REMARK 300 THERE ARE 4 HOMODIMERS IN THE ASYMMETRIC UNIT.                       
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: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
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                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
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 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     SER G    68                                                      
REMARK 465     ARG G    69                                                      
REMARK 465     LYS G    70                                                      
REMARK 465     HIS G    71                                                      
REMARK 465     GLY G    72                                                      
REMARK 465     GLY G    73                                                      
REMARK 465     PRO G    74                                                      
REMARK 465     LYS G    75                                                      
REMARK 465     ASP G    76                                                      
REMARK 465     GLU G    77                                                      
REMARK 465     LYS G   128                                                      
REMARK 465     GLY G   129                                                      
REMARK 465     GLY G   130                                                      
REMARK 465     ASN G   131                                                      
REMARK 465     GLU G   132                                                      
REMARK 465     GLU G   133                                                      
REMARK 465     SER G   134                                                      
REMARK 465     THR G   135                                                      
REMARK 465     LYS G   136                                                      
REMARK 465     THR G   137                                                      
REMARK 465     GLY G   138                                                      
REMARK 465     ASN G   139                                                      
REMARK 465     ALA G   140                                                      
REMARK 465     SER H    68                                                      
REMARK 465     ARG H    69                                                      
REMARK 465     LYS H    70                                                      
REMARK 465     HIS H    71                                                      
REMARK 465     GLY H    72                                                      
REMARK 465     GLY H    73                                                      
REMARK 465     PRO H    74                                                      
REMARK 465     LYS H    75                                                      
REMARK 465     ASP H    76                                                      
REMARK 465     GLU H    77                                                      
REMARK 465     GLU H    78                                                      
REMARK 465     GLU H   133                                                      
REMARK 465     SER H   134                                                      
REMARK 465     THR H   135                                                      
REMARK 465     LYS H   136                                                      
REMARK 465     THR H   137                                                      
REMARK 465     GLY H   138                                                      
REMARK 465     ASN H   139                                                      
REMARK 465     SER K    68                                                      
REMARK 465     ARG K    69                                                      
REMARK 465     LYS K    70                                                      
REMARK 465     HIS K    71                                                      
REMARK 465     GLY K    72                                                      
REMARK 465     GLY K    73                                                      
REMARK 465     PRO K    74                                                      
REMARK 465     LYS K    75                                                      
REMARK 465     ASP K    76                                                      
REMARK 465     GLU K    77                                                      
REMARK 465     ASP K   125                                                      
REMARK 465     LEU K   126                                                      
REMARK 465     GLY K   127                                                      
REMARK 465     LYS K   128                                                      
REMARK 465     GLY K   129                                                      
REMARK 465     GLY K   130                                                      
REMARK 465     ASN K   131                                                      
REMARK 465     GLU K   132                                                      
REMARK 465     GLU K   133                                                      
REMARK 465     SER K   134                                                      
REMARK 465     THR K   135                                                      
REMARK 465     LYS K   136                                                      
REMARK 465     THR K   137                                                      
REMARK 465     GLY K   138                                                      
REMARK 465     ASN K   139                                                      
REMARK 465     ALA K   140                                                      
REMARK 465     GLY K   141                                                      
REMARK 465     LEU L    67                                                      
REMARK 465     SER L    68                                                      
REMARK 465     ARG L    69                                                      
REMARK 465     LYS L    70                                                      
REMARK 465     HIS L    71                                                      
REMARK 465     GLY L    72                                                      
REMARK 465     GLY L    73                                                      
REMARK 465     PRO L    74                                                      
REMARK 465     LYS L    75                                                      
REMARK 465     ASP L    76                                                      
REMARK 465     GLU L    77                                                      
REMARK 465     GLU L    78                                                      
REMARK 465     GLY L   127                                                      
REMARK 465     LYS L   128                                                      
REMARK 465     GLY L   129                                                      
REMARK 465     GLY L   130                                                      
REMARK 465     ASN L   131                                                      
REMARK 465     GLU L   132                                                      
REMARK 465     GLU L   133                                                      
REMARK 465     SER L   134                                                      
REMARK 465     THR L   135                                                      
REMARK 465     LYS L   136                                                      
REMARK 465     THR L   137                                                      
REMARK 465     SER I    68                                                      
REMARK 465     ARG I    69                                                      
REMARK 465     LYS I    70                                                      
REMARK 465     HIS I    71                                                      
REMARK 465     GLY I    72                                                      
REMARK 465     GLY I    73                                                      
REMARK 465     PRO I    74                                                      
REMARK 465     LYS I    75                                                      
REMARK 465     ASP I    76                                                      
REMARK 465     GLU I    77                                                      
REMARK 465     GLU I   133                                                      
REMARK 465     SER I   134                                                      
REMARK 465     THR I   135                                                      
REMARK 465     LYS I   136                                                      
REMARK 465     THR I   137                                                      
REMARK 465     GLY I   138                                                      
REMARK 465     ASN I   139                                                      
REMARK 465     ALA I   140                                                      
REMARK 465     LYS J    70                                                      
REMARK 465     HIS J    71                                                      
REMARK 465     GLY J    72                                                      
REMARK 465     GLY J    73                                                      
REMARK 465     PRO J    74                                                      
REMARK 465     LYS J    75                                                      
REMARK 465     ASP J    76                                                      
REMARK 465     GLU J    77                                                      
REMARK 465     GLU J   132                                                      
REMARK 465     GLU J   133                                                      
REMARK 465     SER J   134                                                      
REMARK 465     THR J   135                                                      
REMARK 465     LYS J   136                                                      
REMARK 465     THR J   137                                                      
REMARK 465     GLY J   138                                                      
REMARK 465     ASN J   139                                                      
REMARK 465     ALA J   140                                                      
REMARK 465     GLY J   141                                                      
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    SER M  68       93.93      2.13                                   
REMARK 500    SER M  98      111.44   -160.25                                   
REMARK 500    LYS M 136      -67.24    -99.06                                   
REMARK 500    PRO N  66        3.50    -67.76                                   
REMARK 500    SER N  68       58.01     36.94                                   
REMARK 500    ASN G  65       98.86   -173.12                                   
REMARK 500    PRO G  66     -100.74    -82.82                                   
REMARK 500    LEU G 126      -46.00     76.57                                   
REMARK 500    ASN H  65       85.32   -158.90                                   
REMARK 500    PRO H  66     -153.44    -72.66                                   
REMARK 500    ASN K  65       97.77    178.63                                   
REMARK 500    ASN L  65       76.68   -163.82                                   
REMARK 500    ASP L 125      -61.32   -132.56                                   
REMARK 500    ALA L 140       56.85   -108.60                                   
REMARK 500    ASN I  65       95.03   -161.51                                   
REMARK 500    PRO I  66      -71.15    -40.14                                   
REMARK 500    LYS I 128       45.81    -68.70                                   
REMARK 500    ASN I 131     -143.52   -149.83                                   
REMARK 500    ASN J  65       67.52   -160.12                                   
REMARK 500    SER J  68     -112.01   -149.73                                   
REMARK 500    LEU J 126       30.01    -70.89                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1OZU   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF S134N MUTANT OF HUMAN CU,ZN SUPEROXIDE          
REMARK 900 DISMUTASE (CUZNSOD)                                                  
REMARK 900 RELATED ID: 1OEZ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ZN-LOADED H46R MUTANT OF HUMAN CU,ZN            
REMARK 900 SUPEROXIDE DISMUTASE (CUZNSOD)                                       
DBREF  1OZT M    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1OZT N    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1OZT G    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1OZT H    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1OZT K    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1OZT L    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1OZT I    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1OZT J    1   153  UNP    P00441   SODC_HUMAN       1    153             
SEQADV 1OZT ARG M   46  UNP  P00441    HIS    46 ENGINEERED                     
SEQADV 1OZT ARG N   46  UNP  P00441    HIS    46 ENGINEERED                     
SEQADV 1OZT ARG G   46  UNP  P00441    HIS    46 ENGINEERED                     
SEQADV 1OZT ARG H   46  UNP  P00441    HIS    46 ENGINEERED                     
SEQADV 1OZT ARG K   46  UNP  P00441    HIS    46 ENGINEERED                     
SEQADV 1OZT ARG L   46  UNP  P00441    HIS    46 ENGINEERED                     
SEQADV 1OZT ARG I   46  UNP  P00441    HIS    46 ENGINEERED                     
SEQADV 1OZT ARG J   46  UNP  P00441    HIS    46 ENGINEERED                     
SEQRES   1 M  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 M  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 M  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 M  153  GLU GLY LEU HIS GLY PHE ARG VAL HIS GLU PHE GLY ASP          
SEQRES   5 M  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 M  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 M  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 M  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 M  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 M  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 M  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 M  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 N  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 N  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 N  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 N  153  GLU GLY LEU HIS GLY PHE ARG VAL HIS GLU PHE GLY ASP          
SEQRES   5 N  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 N  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 N  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 N  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 N  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 N  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 N  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 N  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 G  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 G  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 G  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 G  153  GLU GLY LEU HIS GLY PHE ARG VAL HIS GLU PHE GLY ASP          
SEQRES   5 G  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 G  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 G  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 G  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 G  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 G  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 G  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 G  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 H  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 H  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 H  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 H  153  GLU GLY LEU HIS GLY PHE ARG 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 K  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 K  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 K  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 K  153  GLU GLY LEU HIS GLY PHE ARG VAL HIS GLU PHE GLY ASP          
SEQRES   5 K  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 K  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 K  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 K  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 K  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 K  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 K  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 K  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 L  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 L  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 L  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 L  153  GLU GLY LEU HIS GLY PHE ARG VAL HIS GLU PHE GLY ASP          
SEQRES   5 L  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 L  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 L  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 L  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 L  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 L  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 L  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 L  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 I  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 I  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 I  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 I  153  GLU GLY LEU HIS GLY PHE ARG VAL HIS GLU PHE GLY ASP          
SEQRES   5 I  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 I  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 I  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 I  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 I  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 I  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 I  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 I  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 J  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 J  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 J  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 J  153  GLU GLY LEU HIS GLY PHE ARG 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                      
FORMUL   9  HOH   *235(H2 O)                                                    
HELIX    1   1 ALA M   55  GLY M   61  5                                   7    
HELIX    2   2 SER M  107  CYS M  111  5                                   5    
HELIX    3   3 ASN M  131  GLY M  138  1                                   8    
HELIX    4   4 ALA N   55  GLY N   61  5                                   7    
HELIX    5   5 SER N  107  CYS N  111  5                                   5    
HELIX    6   6 GLU N  133  GLY N  138  1                                   6    
HELIX    7   7 ALA G   55  GLY G   61  5                                   7    
HELIX    8   8 SER G  107  CYS G  111  5                                   5    
HELIX    9   9 ALA H   55  GLY H   61  5                                   7    
HELIX   10  10 SER H  107  CYS H  111  5                                   5    
HELIX   11  11 ALA K   55  GLY K   61  5                                   7    
HELIX   12  12 SER K  107  CYS K  111  5                                   5    
HELIX   13  13 ALA L   55  GLY L   61  5                                   7    
HELIX   14  14 SER L  107  CYS L  111  5                                   5    
HELIX   15  15 ALA I   55  GLY I   61  5                                   7    
HELIX   16  16 SER I  107  CYS I  111  5                                   5    
HELIX   17  17 ALA J   55  GLY J   61  5                                   7    
HELIX   18  18 SER J  107  CYS J  111  5                                   5    
SHEET    1   A 5 ALA M  95  ASP M 101  0                                        
SHEET    2   A 5 VAL M  29  LYS M  36 -1  N  GLY M  33   O  VAL M  97           
SHEET    3   A 5 GLN M  15  GLN M  22 -1  N  ASN M  19   O  TRP M  32           
SHEET    4   A 5 THR M   2  LEU M   8 -1  N  LEU M   8   O  GLY M  16           
SHEET    5   A 5 GLY M 150  ILE M 151 -1  O  GLY M 150   N  VAL M   5           
SHEET    1   B 4 ASP M  83  ALA M  89  0                                        
SHEET    2   B 4 GLY M  41  HIS M  48 -1  N  GLY M  41   O  ALA M  89           
SHEET    3   B 4 THR M 116  HIS M 120 -1  O  THR M 116   N  HIS M  48           
SHEET    4   B 4 ARG M 143  VAL M 148 -1  O  GLY M 147   N  LEU M 117           
SHEET    1   C 5 ALA N  95  ASP N 101  0                                        
SHEET    2   C 5 VAL N  29  LYS N  36 -1  N  GLY N  33   O  VAL N  97           
SHEET    3   C 5 GLN N  15  GLN N  22 -1  N  GLN N  15   O  LYS N  36           
SHEET    4   C 5 THR N   2  LEU N   8 -1  N  ALA N   4   O  PHE N  20           
SHEET    5   C 5 GLY N 150  ILE N 151 -1  O  GLY N 150   N  VAL N   5           
SHEET    1   D 4 ASP N  83  ALA N  89  0                                        
SHEET    2   D 4 GLY N  41  HIS N  48 -1  N  GLY N  41   O  ALA N  89           
SHEET    3   D 4 THR N 116  HIS N 120 -1  O  THR N 116   N  HIS N  48           
SHEET    4   D 4 ARG N 143  VAL N 148 -1  O  GLY N 147   N  LEU N 117           
SHEET    1   E 5 ALA G  95  ASP G 101  0                                        
SHEET    2   E 5 VAL G  29  LYS G  36 -1  N  ILE G  35   O  ALA G  95           
SHEET    3   E 5 GLN G  15  GLN G  22 -1  N  GLN G  15   O  LYS G  36           
SHEET    4   E 5 THR G   2  LEU G   8 -1  N  LEU G   8   O  GLY G  16           
SHEET    5   E 5 GLY G 150  ILE G 151 -1  O  GLY G 150   N  VAL G   5           
SHEET    1   F 4 ASP G  83  ALA G  89  0                                        
SHEET    2   F 4 GLY G  41  HIS G  48 -1  N  GLY G  41   O  ALA G  89           
SHEET    3   F 4 THR G 116  HIS G 120 -1  O  VAL G 118   N  ARG G  46           
SHEET    4   F 4 ARG G 143  VAL G 148 -1  O  GLY G 147   N  LEU G 117           
SHEET    1   G 5 ALA H  95  ASP H 101  0                                        
SHEET    2   G 5 VAL H  29  LYS H  36 -1  N  ILE H  35   O  ALA H  95           
SHEET    3   G 5 GLN H  15  GLN H  22 -1  N  GLU H  21   O  LYS H  30           
SHEET    4   G 5 THR H   2  LEU H   8 -1  N  ALA H   4   O  PHE H  20           
SHEET    5   G 5 GLY H 150  ILE H 151 -1  O  GLY H 150   N  VAL H   5           
SHEET    1   H 4 ASP H  83  ALA H  89  0                                        
SHEET    2   H 4 GLY H  41  HIS H  48 -1  N  GLY H  41   O  ALA H  89           
SHEET    3   H 4 THR H 116  HIS H 120 -1  O  VAL H 118   N  ARG H  46           
SHEET    4   H 4 ARG H 143  VAL H 148 -1  O  GLY H 147   N  LEU H 117           
SHEET    1   I 5 ALA K  95  ASP K 101  0                                        
SHEET    2   I 5 VAL K  29  LYS K  36 -1  N  ILE K  35   O  ALA K  95           
SHEET    3   I 5 GLN K  15  GLN K  22 -1  N  GLU K  21   O  LYS K  30           
SHEET    4   I 5 THR K   2  LEU K   8 -1  N  ALA K   4   O  PHE K  20           
SHEET    5   I 5 GLY K 150  ILE K 151 -1  O  GLY K 150   N  VAL K   5           
SHEET    1   J 4 ASP K  83  ALA K  89  0                                        
SHEET    2   J 4 GLY K  41  HIS K  48 -1  N  GLY K  41   O  ALA K  89           
SHEET    3   J 4 THR K 116  HIS K 120 -1  O  VAL K 118   N  ARG K  46           
SHEET    4   J 4 ARG K 143  VAL K 148 -1  O  GLY K 147   N  LEU K 117           
SHEET    1   K 8 ASP L  83  ALA L  89  0                                        
SHEET    2   K 8 GLY L  41  HIS L  48 -1  N  GLY L  41   O  ALA L  89           
SHEET    3   K 8 THR L 116  HIS L 120 -1  O  VAL L 118   N  ARG L  46           
SHEET    4   K 8 ARG L 143  ILE L 151 -1  O  GLY L 147   N  LEU L 117           
SHEET    5   K 8 THR L   2  LEU L   8 -1  N  VAL L   5   O  GLY L 150           
SHEET    6   K 8 GLN L  15  GLN L  22 -1  O  PHE L  20   N  ALA L   4           
SHEET    7   K 8 VAL L  29  LYS L  36 -1  O  LYS L  30   N  GLU L  21           
SHEET    8   K 8 ALA L  95  ASP L 101 -1  O  ALA L  95   N  ILE L  35           
SHEET    1   L 5 ALA I  95  ASP I 101  0                                        
SHEET    2   L 5 VAL I  29  LYS I  36 -1  N  ILE I  35   O  ALA I  95           
SHEET    3   L 5 GLN I  15  GLN I  22 -1  N  GLU I  21   O  LYS I  30           
SHEET    4   L 5 THR I   2  LEU I   8 -1  N  ALA I   4   O  PHE I  20           
SHEET    5   L 5 GLY I 150  ILE I 151 -1  O  GLY I 150   N  VAL I   5           
SHEET    1   M 4 ASP I  83  ALA I  89  0                                        
SHEET    2   M 4 GLY I  41  HIS I  48 -1  N  GLY I  41   O  ALA I  89           
SHEET    3   M 4 THR I 116  HIS I 120 -1  O  VAL I 118   N  ARG I  46           
SHEET    4   M 4 ARG I 143  VAL I 148 -1  O  GLY I 147   N  LEU I 117           
SHEET    1   N 5 ALA J  95  ASP J 101  0                                        
SHEET    2   N 5 VAL J  29  LYS J  36 -1  N  ILE J  35   O  ALA J  95           
SHEET    3   N 5 GLN J  15  GLN J  22 -1  N  GLU J  21   O  LYS J  30           
SHEET    4   N 5 THR J   2  LEU J   8 -1  N  ALA J   4   O  PHE J  20           
SHEET    5   N 5 GLY J 150  ILE J 151 -1  O  GLY J 150   N  VAL J   5           
SHEET    1   O 4 ASP J  83  ALA J  89  0                                        
SHEET    2   O 4 GLY J  41  HIS J  48 -1  N  GLY J  41   O  ALA J  89           
SHEET    3   O 4 THR J 116  HIS J 120 -1  O  THR J 116   N  HIS J  48           
SHEET    4   O 4 ARG J 143  VAL J 148 -1  O  GLY J 147   N  LEU J 117           
SSBOND   1 CYS M   57    CYS M  146                          1555   1555  2.06  
SSBOND   2 CYS N   57    CYS N  146                          1555   1555  2.05  
SSBOND   3 CYS G   57    CYS G  146                          1555   1555  2.04  
SSBOND   4 CYS H   57    CYS H  146                          1555   1555  2.05  
SSBOND   5 CYS K   57    CYS K  146                          1555   1555  2.06  
SSBOND   6 CYS L   57    CYS L  146                          1555   1555  2.06  
SSBOND   7 CYS I   57    CYS I  146                          1555   1555  2.04  
SSBOND   8 CYS J   57    CYS J  146                          1555   1555  2.04  
CRYST1   79.617   69.998  113.787  90.00 110.37  90.00 P 1 21 1     16          
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      0.012560  0.000000  0.004664        0.00000                         
SCALE2      0.000000  0.014286  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009375        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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