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Database: PDB
Entry: 2XJL
LinkDB: 2XJL
Original site: 2XJL 
HEADER    OXIDOREDUCTASE                          07-JUL-10   2XJL              
TITLE     MONOMERIC HUMAN CU,ZN SUPEROXIDE DISMUTASE WITHOUT CU LIGANDS         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CU, ZN SUPEROXIDE DISMUTASE;                                
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    OXIDOREDUCTASE, CU/ZN SOD1, METAL-BINDING, NEURODEGENERATION          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.SARABOJI,L.LEINARTAITE,A.NORDLUND,M.OLIVEBERG,D.T.LOGAN             
REVDAT   3   17-JAN-18 2XJL    1       REMARK                                   
REVDAT   2   20-OCT-10 2XJL    1       JRNL   REMARK                            
REVDAT   1   01-SEP-10 2XJL    0                                                
JRNL        AUTH   L.LEINARTAITE,K.SARABOJI,A.NORDLUND,D.T.LOGAN,M.OLIVEBERG    
JRNL        TITL   FOLDING CATALYSIS BY TRANSIENT COORDINATION OF ZN2+ TO THE   
JRNL        TITL 2 CU LIGANDS OF THE ALS-ASSOCIATED ENZYME CU/ZN SUPEROXIDE     
JRNL        TITL 3 DISMUTASE 1.                                                 
JRNL        REF    J.AM.CHEM.SOC.                V. 132 13495 2010              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   20822138                                                     
JRNL        DOI    10.1021/JA1057136                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.NORDLUND,L.LEINARTAITE,K.SARABOJI,C.AISENBREY,G.GROBNER,   
REMARK   1  AUTH 2 P.ZETTERSTROM,J.DANIELSSON,D.T.LOGAN,M.OLIVEBERG             
REMARK   1  TITL   FUNCTIONAL FEATURES CAUSE MISFOLDING OF THE ALS-PROVOKING    
REMARK   1  TITL 2 ENZYME SOD1.                                                 
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V. 106  9667 2009              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1  PMID   19497878                                                     
REMARK   1  DOI    10.1073/PNAS.0812046106                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 19519                          
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) : 0.157                           
REMARK   3   R VALUE            (WORKING SET) : 0.156                           
REMARK   3   FREE R VALUE                     : 0.183                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1055                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.59                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1397                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.53                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2680                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 80                           
REMARK   3   BIN FREE R VALUE                    : 0.2880                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1099                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 17                                      
REMARK   3   SOLVENT ATOMS            : 145                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.06                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.28000                                             
REMARK   3    B22 (A**2) : 0.97000                                              
REMARK   3    B33 (A**2) : -0.69000                                             
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): 0.102         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.075         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.048         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.018         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.961                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1178 ; 0.010 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):   781 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1586 ; 1.258 ; 1.964       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  1939 ; 1.943 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   158 ; 6.001 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    51 ;36.599 ;26.275       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   202 ;13.273 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     5 ;14.931 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   177 ; 0.105 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1353 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   203 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):   776 ; 0.991 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   335 ; 0.249 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1238 ; 1.674 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   402 ; 2.455 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   348 ; 3.736 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  1959 ; 0.946 ; 3.000       
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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.4916  -3.4731  10.1206              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0058 T22:   0.0051                                     
REMARK   3      T33:   0.0056 T12:   0.0018                                     
REMARK   3      T13:   0.0026 T23:  -0.0007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9008 L22:   0.7031                                     
REMARK   3      L33:   1.2400 L12:  -0.1415                                     
REMARK   3      L13:  -0.2992 L23:   0.2801                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0109 S12:  -0.0480 S13:   0.0498                       
REMARK   3      S21:   0.0333 S22:   0.0093 S23:  -0.0114                       
REMARK   3      S31:   0.0119 S32:   0.0477 S33:  -0.0202                       
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. TLS ADDED WITH U VALUES. ATOM RECORD CONTAINS SUM OF     
REMARK   3  TLS AND RESIDUAL B FACTORS.                                         
REMARK   4                                                                      
REMARK   4 2XJL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-JUL-10.                  
REMARK 100 THE DEPOSITION ID IS D_1290044424.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-OCT-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I911-5                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9085                             
REMARK 200  MONOCHROMATOR                  : BENT SI (220) CRYSTAL              
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20574                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 8.300                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.62000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: MONOMERIC CU,ZN SOD1                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 6000, 0.1M SODIUM ACETATE (PH    
REMARK 280  5.0), 0.01M ZNCL2                                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   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       17.38000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.23000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.61000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.23000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       17.38000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       24.61000            
REMARK 290   SMTRY3   4  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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS   7 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, HIS  47 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, HIS  49 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, PHE  51 TO GLU                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLY  52 TO GLU                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 112 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, HIS 121 TO SER                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    VAL A 148   CG1 -  CB  -  CG2 ANGL. DEV. =  10.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  52      -77.57   -106.65                                   
REMARK 500    ALA A  55      -74.48    -73.89                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  63   ND1                                                    
REMARK 620 2 HIS A  80   ND1 113.2                                              
REMARK 620 3 ASP A  83   OD1 102.4 114.4                                        
REMARK 620 4 HIS A  71   ND1 104.5 122.1  97.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 156  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A   1   O                                                      
REMARK 620 2 GLU A  51   OE2  91.1                                              
REMARK 620 3 ASP A  96   OD2  86.1  96.5                                        
REMARK 620 4 HOH A2143   O   162.7 106.2  92.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 157  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  90   OD2                                                    
REMARK 620 2 ASP A  52   OD2 103.2                                              
REMARK 620 3 ASP A  52   OD2 102.8   3.3                                        
REMARK 620 4 ASP A  92   OD1 106.7 118.0 121.0                                  
REMARK 620 5 GLU A  50   OE2 110.6  99.7  96.9 117.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 158  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 153   O                                                      
REMARK 620 2 GLN A 153   OXT  55.1                                              
REMARK 620 3 HOH A2144   O   105.8 154.4                                        
REMARK 620 4 HIS A 110   NE2 137.4  93.2 111.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 160  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2131   O                                                      
REMARK 620 2 HOH A2130   O   136.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 161  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2057   O                                                      
REMARK 620 2 HOH A2007   O   128.8                                              
REMARK 620 3 CYS A 146   O   132.9  78.8                                        
REMARK 620 4 ALA A  55   O    85.3 131.1 103.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 156                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 157                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 158                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 159                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 160                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 161                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 162                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WZ6   RELATED DB: PDB                                   
REMARK 900 G93A SOD1 MUTANT COMPLEXED WITH QUINAZOLINE.                         
REMARK 900 RELATED ID: 1PTZ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CU, ZN SUPEROXIDE DISMUTASE,FAMILIAL  
REMARK 900 AMYOTROPHIC LATERAL SCLEROSIS (FALS) MUTANT H43R                     
REMARK 900 RELATED ID: 1OEZ   RELATED DB: PDB                                   
REMARK 900 ZN HIS46ARG MUTANT OF HUMAN CU, ZN SUPEROXIDE DISMUTASE              
REMARK 900 RELATED ID: 1AZV   RELATED DB: PDB                                   
REMARK 900 FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)                             
REMARK 900 RELATED ID: 1HL4   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF APO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE          
REMARK 900 RELATED ID: 2WYZ   RELATED DB: PDB                                   
REMARK 900 L38V SOD1 MUTANT COMPLEXED WITH UMP                                  
REMARK 900 RELATED ID: 2VR6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE       
REMARK 900 DISMUTASE (CUZNSOD) AT 1.3 A RESOLUTION                              
REMARK 900 RELATED ID: 1OZU   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FAMILIAL ALS MUTANT S134N OF HUMAN CU,ZN        
REMARK 900 SUPEROXIDE DISMUTASE ( CUZNSOD) TO 1.3A RESOLUTION                   
REMARK 900 RELATED ID: 2C9V   RELATED DB: PDB                                   
REMARK 900 ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN SUPEROXIDE DISMUTASE      
REMARK 900 RELATED ID: 2WZ5   RELATED DB: PDB                                   
REMARK 900 L38V SOD1 MUTANT COMPLEXED WITH L-METHIONINE .                       
REMARK 900 RELATED ID: 1PU0   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN CU,ZN SUPEROXIDE DISMUTASE                        
REMARK 900 RELATED ID: 1FUN   RELATED DB: PDB                                   
REMARK 900 SUPEROXIDE DISMUTASE MUTANT WITH LYS 136 REPLACED BY GLU, CYS 6      
REMARK 900 REPLACED BY ALA AND CYS 111 REPLACED BY SER (K136E, C6A, C111S)      
REMARK 900 RELATED ID: 1SOS   RELATED DB: PDB                                   
REMARK 900 SUPEROXIDE DISMUTASE MUTANT WITH CYS 6 REPLACED BY ALA AND CYS 111   
REMARK 900 REPLACED BY SER (C6A, C111S)                                         
REMARK 900 RELATED ID: 1N19   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE HSOD A4V MUTANT                                     
REMARK 900 RELATED ID: 1P1V   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FALS-ASSOCIATED HUMAN COPPER-ZINCSUPEROXIDE     
REMARK 900 DISMUTASE (CUZNSOD) MUTANT D125H TO 1.4A                             
REMARK 900 RELATED ID: 2WZ0   RELATED DB: PDB                                   
REMARK 900 L38V SOD1 MUTANT COMPLEXED WITH ANILINE.                             
REMARK 900 RELATED ID: 2WKO   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF METAL LOADED PATHOGENIC SOD1 MUTANT G93A.               
REMARK 900 RELATED ID: 1L3N   RELATED DB: PDB                                   
REMARK 900 THE SOLUTION STRUCTURE OF REDUCED DIMERIC COPPER ZINC SOD:THE        
REMARK 900 STRUCTURAL EFFECTS OF DIMERIZATION                                   
REMARK 900 RELATED ID: 1UXL   RELATED DB: PDB                                   
REMARK 900 I113T MUTANT OF HUMAN SOD1                                           
REMARK 900 RELATED ID: 2AF2   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF DISULFIDE REDUCED AND COPPER DEPLETEDHUMAN     
REMARK 900 SUPEROXIDE DISMUTASE                                                 
REMARK 900 RELATED ID: 2VR8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE       
REMARK 900 DISMUTASE (CUZNSOD) AT 1.36 A RESOLUTION                             
REMARK 900 RELATED ID: 1RK7   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF APO CU,ZN SUPEROXIDE DISMUTASE: ROLEOF METAL   
REMARK 900 IONS IN PROTEIN FOLDING                                              
REMARK 900 RELATED ID: 2VR7   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE       
REMARK 900 DISMUTASE (CUZNSOD) AT 1.58 A RESOLUTION                             
REMARK 900 RELATED ID: 2C9S   RELATED DB: PDB                                   
REMARK 900 1.24 ANGSTROMS RESOLUTION STRUCTURE OF ZN- ZN HUMAN SUPEROXIDE       
REMARK 900 DISMUTASE                                                            
REMARK 900 RELATED ID: 2V0A   RELATED DB: PDB                                   
REMARK 900 ATOMIC RESOLUTION CRYSTAL STRUCTURE OF HUMAN SUPEROXIDE DISMUTASE    
REMARK 900 RELATED ID: 4SOD   RELATED DB: PDB                                   
REMARK 900 CU,ZN SUPEROXIDE DISMUTASE MUTANT WITH CYS 6 REPLACED BY ALA AND     
REMARK 900 CYS 111 REPLACED BY SER (C6A,C111S) WITH AN 18-RESIDUE HEPARIN-      
REMARK 900 BINDING PEPTIDE FUSED TO THE C- TERMINUS (THEORETICAL MODEL)         
REMARK 900 RELATED ID: 1MFM   RELATED DB: PDB                                   
REMARK 900 MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q AT ATOMIC RESOLUTION      
REMARK 900 RELATED ID: 2WYT   RELATED DB: PDB                                   
REMARK 900 1.0 A RESOLUTION STRUCTURE OF L38V SOD1 MUTANT                       
REMARK 900 RELATED ID: 1DSW   RELATED DB: PDB                                   
REMARK 900 THE SOLUTION STRUCTURE OF A MONOMERIC, REDUCED FORM OFHUMAN COPPER,  
REMARK 900 ZINC SUPEROXIDE DISMUTASE BEARING THE SAMECHARGE AS THE NATIVE       
REMARK 900 PROTEIN                                                              
REMARK 900 RELATED ID: 1KMG   RELATED DB: PDB                                   
REMARK 900 THE SOLUTION STRUCTURE OF MONOMERIC COPPER- FREE SUPEROXIDEDISMUTASE 
REMARK 900 RELATED ID: 1OZT   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF APO-H46R FAMILIAL ALS MUTANT HUMAN CU,ZN        
REMARK 900 SUPEROXIDE DISMUTASE ( CUZNSOD) TO 2.5A RESOLUTION                   
REMARK 900 RELATED ID: 1N18   RELATED DB: PDB                                   
REMARK 900 THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE DISMUTASE, C6A,C111S         
REMARK 900 RELATED ID: 1BA9   RELATED DB: PDB                                   
REMARK 900 THE SOLUTION STRUCTURE OF REDUCED MONOMERIC SUPEROXIDE DISMUTASE,    
REMARK 900 NMR, 36 STRUCTURES                                                   
REMARK 900 RELATED ID: 2C9U   RELATED DB: PDB                                   
REMARK 900 1.24 ANGSTROMS RESOLUTION STRUCTURE OF AS- ISOLATED CU-ZN HUMAN      
REMARK 900 SUPEROXIDE DISMUTASE                                                 
REMARK 900 RELATED ID: 1HL5   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE         
REMARK 900 RELATED ID: 1SPD   RELATED DB: PDB                                   
REMARK 900 SUPEROXIDE DISMUTASE                                                 
REMARK 900 RELATED ID: 1UXM   RELATED DB: PDB                                   
REMARK 900 A4V MUTANT OF HUMAN SOD1                                             
REMARK 900 RELATED ID: 2XJK   RELATED DB: PDB                                   
REMARK 900 MONOMERIC HUMAN CU,ZN SUPEROXIDE DISMUTASE                           
DBREF  2XJL A    1   153  UNP    P00441   SODC_HUMAN       2    154             
SEQADV 2XJL ALA A    6  UNP  P00441    CYS     7 ENGINEERED MUTATION            
SEQADV 2XJL SER A   46  UNP  P00441    HIS    47 ENGINEERED MUTATION            
SEQADV 2XJL SER A   48  UNP  P00441    HIS    49 ENGINEERED MUTATION            
SEQADV 2XJL GLU A   50  UNP  P00441    PHE    51 ENGINEERED MUTATION            
SEQADV 2XJL GLU A   51  UNP  P00441    GLY    52 ENGINEERED MUTATION            
SEQADV 2XJL ALA A  111  UNP  P00441    CYS   112 ENGINEERED MUTATION            
SEQADV 2XJL SER A  120  UNP  P00441    HIS   121 ENGINEERED MUTATION            
SEQRES   1 A  153  ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 A  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 A  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 A  153  GLU GLY LEU HIS GLY PHE SER VAL SER GLU GLU GLU ASP          
SEQRES   5 A  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 A  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 A  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 A  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 A  153  SER LEU SER GLY ASP HIS ALA ILE ILE GLY ARG THR LEU          
SEQRES  10 A  153  VAL VAL SER GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 A  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 A  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
HET     ZN  A 155       1                                                       
HET     ZN  A 156       1                                                       
HET     ZN  A 157       1                                                       
HET     ZN  A 158       1                                                       
HET    PEG  A 159       7                                                       
HET     NA  A 160       1                                                       
HET     NA  A 161       1                                                       
HET    ACT  A 162       4                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM      NA SODIUM ION                                                       
HETNAM     ACT ACETATE ION                                                      
FORMUL   2   ZN    4(ZN 2+)                                                     
FORMUL   6  PEG    C4 H10 O3                                                    
FORMUL   7   NA    2(NA 1+)                                                     
FORMUL   9  ACT    C2 H3 O2 1-                                                  
FORMUL  10  HOH   *145(H2 O)                                                    
HELIX    1   1 GLU A  133  GLY A  138  1                                   6    
SHEET    1  AA 9 THR A   2  LYS A   9  0                                        
SHEET    2  AA 9 GLN A  15  GLN A  22 -1  O  GLY A  16   N  LEU A   8           
SHEET    3  AA 9 VAL A  29  LYS A  36 -1  O  LYS A  30   N  GLU A  21           
SHEET    4  AA 9 ALA A  95  ASP A 101 -1  O  ALA A  95   N  ILE A  35           
SHEET    5  AA 9 ASP A  83  ALA A  89 -1  O  THR A  88   N  ASP A  96           
SHEET    6  AA 9 GLY A  41  SER A  48 -1  O  GLY A  41   N  ALA A  89           
SHEET    7  AA 9 THR A 116  SER A 120 -1  O  THR A 116   N  SER A  48           
SHEET    8  AA 9 ARG A 143  ILE A 151 -1  N  LEU A 144   O  VAL A 119           
SHEET    9  AA 9 THR A   2  LYS A   9 -1  O  VAL A   5   N  GLY A 150           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.97  
LINK        ZN    ZN A 155                 ND1 HIS A  63     1555   1555  2.03  
LINK        ZN    ZN A 155                 ND1 HIS A  80     1555   1555  2.05  
LINK        ZN    ZN A 155                 OD1 ASP A  83     1555   1555  1.94  
LINK        ZN    ZN A 155                 ND1 HIS A  71     1555   1555  2.04  
LINK        ZN    ZN A 156                 O   ALA A   1     1555   4445  2.29  
LINK        ZN    ZN A 156                 OE2 GLU A  51     1555   1555  1.97  
LINK        ZN    ZN A 156                 OD2 ASP A  96     1555   1455  1.93  
LINK        ZN    ZN A 156                 O   HOH A2143     1555   1555  2.07  
LINK        ZN    ZN A 157                 OD2 ASP A  90     1555   1455  1.98  
LINK        ZN    ZN A 157                 OD2BASP A  52     1555   1555  1.89  
LINK        ZN    ZN A 157                 OD2AASP A  52     1555   1555  2.01  
LINK        ZN    ZN A 157                 OD1 ASP A  92     1555   1455  1.88  
LINK        ZN    ZN A 157                 OE2 GLU A  50     1555   1555  1.92  
LINK        ZN    ZN A 158                 O   GLN A 153     1555   4445  1.93  
LINK        ZN    ZN A 158                 OXT GLN A 153     1555   4445  2.51  
LINK        ZN    ZN A 158                 O   HOH A2144     1555   1555  2.16  
LINK        ZN    ZN A 158                 NE2 HIS A 110     1555   1555  1.96  
LINK        NA    NA A 160                 O   HOH A2131     1555   1555  2.96  
LINK        NA    NA A 160                 O   HOH A2130     1555   1555  2.84  
LINK        NA    NA A 161                 O   HOH A2057     1555   1555  3.03  
LINK        NA    NA A 161                 O   HOH A2007     1555   1555  3.00  
LINK        NA    NA A 161                 O   CYS A 146     1555   1555  2.68  
LINK        NA    NA A 161                 O  AALA A  55     1555   1555  2.22  
SITE     1 AC1  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC2  4 ALA A   1  GLU A  51  ASP A  96  HOH A2143                    
SITE     1 AC3  4 GLU A  50  ASP A  52  ASP A  90  ASP A  92                    
SITE     1 AC4  3 HIS A 110  GLN A 153  HOH A2144                               
SITE     1 AC5  8 LEU A  67  ASP A  76  GLU A  77  ARG A  79                    
SITE     2 AC5  8 VAL A 103  HOH A2074  HOH A2078  HOH A2145                    
SITE     1 AC6  2 HOH A2130  HOH A2131                                          
SITE     1 AC7  5 LYS A   9  ALA A  55  CYS A 146  HOH A2007                    
SITE     2 AC7  5 HOH A2057                                                     
SITE     1 AC8  6 LYS A  30  ILE A 113  VAL A 148  GLY A 150                    
SITE     2 AC8  6 ILE A 151  HOH A2032                                          
CRYST1   34.760   49.220   80.460  90.00  90.00  90.00 P 21 21 21    4          
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      0.028769  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.020317  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012429        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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